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Conserved domains on  [gi|31543321|ref|NP_032716|]
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NF-kappa-B inhibitor epsilon isoform 1 [Mus musculus]

Protein Classification

ankyrin repeat domain-containing protein( domain architecture ID 11429852)

ankyrin repeat (ANK) domain-containing protein is involved in mediating protein-protein interactions

Gene Ontology:  GO:0005515
PubMed:  33435370|17176038

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
121-358 7.59e-34

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 126.61  E-value: 7.59e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543321 121 EDGDTLLHLAVIHEAPSVLFccLAFLPQEVLDIQNNLYQTALHLAVHLDQPDVVRALVLKGASRILQDQHGDTALHVACR 200
Cdd:COG0666  52 ALGALLLLAAALAGDLLVAL--LLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAY 129

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543321 201 RQNLACACCLLEeqpepgrqlsHPLDLQLKNWQGLACLHIATLQRNQPLIELLLQNGADIDVQEGtSGKTALHLAVETQE 280
Cdd:COG0666 130 NGNLEIVKLLLE----------AGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDN-DGETPLHLAAENGH 198

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 31543321 281 RSLVQFLLQAGARVDARMLNGCTPLHLAAGRGLNSISSTLCEAGADSLLLNVEDETPQDLAEDLLSYLPFDDLKISGK 358
Cdd:COG0666 199 LEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALL 276
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
121-358 7.59e-34

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 126.61  E-value: 7.59e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543321 121 EDGDTLLHLAVIHEAPSVLFccLAFLPQEVLDIQNNLYQTALHLAVHLDQPDVVRALVLKGASRILQDQHGDTALHVACR 200
Cdd:COG0666  52 ALGALLLLAAALAGDLLVAL--LLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAY 129

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543321 201 RQNLACACCLLEeqpepgrqlsHPLDLQLKNWQGLACLHIATLQRNQPLIELLLQNGADIDVQEGtSGKTALHLAVETQE 280
Cdd:COG0666 130 NGNLEIVKLLLE----------AGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDN-DGETPLHLAAENGH 198

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 31543321 281 RSLVQFLLQAGARVDARMLNGCTPLHLAAGRGLNSISSTLCEAGADSLLLNVEDETPQDLAEDLLSYLPFDDLKISGK 358
Cdd:COG0666 199 LEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALL 276
Ank_2 pfam12796
Ankyrin repeats (3 copies);
238-326 5.51e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 67.06  E-value: 5.51e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543321   238 LHIATLQRNQPLIELLLQNGADIDVQEgTSGKTALHLAVETQERSLVQFLLQaGARVDARMlNGCTPLHLAAGRGLNSIS 317
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQD-KNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIV 77


                  ....*....
gi 31543321   318 STLCEAGAD 326
Cdd:pfam12796  78 KLLLEKGAD 86
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 221-326 9.43e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 62.98  E-value: 9.43e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543321  221 LSHPLDLQLKNWQGL-ACLHIATLQRNQPLIELLLQNGADIDVQEGTSgKTALHLAVETQERSLVQFLLQAGARVDARML 299
Cdd:PHA02878 154 LSYGADINMKDRHKGnTALHYATENKDQRLTELLLSYGANVNIPDKTN-NSPLHHAVKHYNKPIVHILLENGASTDARDK 232

                         90       100
                 ....*....|....*....|....*...
gi 31543321  300 NGCTPLHLAAGRGLN-SISSTLCEAGAD 326
Cdd:PHA02878 233 CGNTPLHISVGYCKDyDILKLLLEHGVD 260
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 123-317 1.92e-09

transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 59.32  E-value: 1.92e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543321   123 GDTLLHLAVIHEAPSVLFCCLAFL--------PQEVLDIQNNLY---QTALHLAVHLDQPDVVRALVLKGASrilqdqhg 191
Cdd:TIGR00870  82 GDTLLHAISLEYVDAVEAILLHLLaafrksgpLELANDQYTSEFtpgITALHLAAHRQNYEIVKLLLERGAS-------- 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543321   192 dtaLHVACrrqnlACACCLLEEQPEPGRQLSHPLDLqlknwqgLACLhiatlqrNQP-LIELLLQNGADIDVQEgTSGKT 270
Cdd:TIGR00870 154 ---VPARA-----CGDFFVKSQGVDSFYHGESPLNA-------AACL-------GSPsIVALLSEDPADILTAD-SLGNT 210

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 31543321   271 ALHLAVETQE---------RSLVQFLLQAGARVDAR-----MLN--GCTPLHLAAGRGLNSIS 317
Cdd:TIGR00870 211 LLHLLVMENEfkaeyeelsCQMYNFALSLLDKLRDSkelevILNhqGLTPLKLAAKEGRIVLF 273
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 190-307 2.24e-09

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 58.87  E-value: 2.24e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543321 190 HGDTALHVACRRQNLACACCLLEEQPEpgrQLSHPLDLQLknWQGLACLHIATLQRNQPLIELLLQNGADIDVQEGTS-- 267
Cdd:cd22192  50 LGETALHVAALYDNLEAAVVLMEAAPE---LVNEPMTSDL--YQGETALHIAVVNQNLNLVRELIARGADVVSPRATGtf 124

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 31543321 268 -----------GKTALHLAVETQERSLVQFLLQAGARVDARMLNGCTPLHL 307
Cdd:cd22192 125 frpgpknliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHI 175
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 268-296 6.80e-03

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 33.72  E-value: 6.80e-03
                           10        20
                   ....*....|....*....|....*....
gi 31543321    268 GKTALHLAVETQERSLVQFLLQAGARVDA 296
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
121-358 7.59e-34

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 126.61  E-value: 7.59e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543321 121 EDGDTLLHLAVIHEAPSVLFccLAFLPQEVLDIQNNLYQTALHLAVHLDQPDVVRALVLKGASRILQDQHGDTALHVACR 200
Cdd:COG0666  52 ALGALLLLAAALAGDLLVAL--LLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAY 129

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543321 201 RQNLACACCLLEeqpepgrqlsHPLDLQLKNWQGLACLHIATLQRNQPLIELLLQNGADIDVQEGtSGKTALHLAVETQE 280
Cdd:COG0666 130 NGNLEIVKLLLE----------AGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDN-DGETPLHLAAENGH 198

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 31543321 281 RSLVQFLLQAGARVDARMLNGCTPLHLAAGRGLNSISSTLCEAGADSLLLNVEDETPQDLAEDLLSYLPFDDLKISGK 358
Cdd:COG0666 199 LEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALL 276
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
113-341 8.79e-30

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 115.82  E-value: 8.79e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543321 113 LEALTYISEDGDTLLHLAVIHEAPSVLFCCLAFLPQEVLDIQNNLYQTALHLAVHLDQPDVVRALVLKGASRILQDQHGD 192
Cdd:COG0666   9 LLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGN 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543321 193 TALHVACRRQNLACACCLLEeqpepgrqlsHPLDLQLKNWQGLACLHIATLQRNQPLIELLLQNGADIDVQeGTSGKTAL 272
Cdd:COG0666  89 TLLHAAARNGDLEIVKLLLE----------AGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQ-DNDGNTPL 157

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 31543321 273 HLAVETQERSLVQFLLQAGARVDARMLNGCTPLHLAAGRGLNSISSTLCEAGADSLLLNVEDETPQDLA 341
Cdd:COG0666 158 HLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLA 226
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
115-336 9.68e-28

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 110.43  E-value: 9.68e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543321 115 ALTYISEDGDTLLHLAVIHEAPSVLfccLAFLPQEV-LDIQNNLYQTALHLAVHLDQPDVVRALVLKGASRILQDQHGDT 193
Cdd:COG0666  79 DINAKDDGGNTLLHAAARNGDLEIV---KLLLEAGAdVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNT 155

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543321 194 ALHVACRRQNLACACCLLEeqpepgrqlsHPLDLQLKNWQGLACLHIATLQRNQPLIELLLQNGADIDVQEgTSGKTALH 273
Cdd:COG0666 156 PLHLAAANGNLEIVKLLLE----------AGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKD-NDGKTALD 224

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 31543321 274 LAVETQERSLVQFLLQAGARVDARMLNGCTPLHLAAGRGLNSISSTLCEAGADSLLLNVEDET 336
Cdd:COG0666 225 LAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLT 287
Ank_2 pfam12796
Ankyrin repeats (3 copies);
238-326 5.51e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 67.06  E-value: 5.51e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543321   238 LHIATLQRNQPLIELLLQNGADIDVQEgTSGKTALHLAVETQERSLVQFLLQaGARVDARMlNGCTPLHLAAGRGLNSIS 317
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQD-KNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIV 77


                  ....*....
gi 31543321   318 STLCEAGAD 326
Cdd:pfam12796  78 KLLLEKGAD 86
Ank_2 pfam12796
Ankyrin repeats (3 copies);
162-263 4.35e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 64.37  E-value: 4.35e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543321   162 LHLAVHLDQPDVVRALVLKGASRILQDQHGDTALHVACRRQNLACACCLLEEqpepgrqlshpLDLQLKNwQGLACLHIA 241
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-----------ADVNLKD-NGRTALHYA 68

                          90       100
                  ....*....|....*....|..
gi 31543321   242 TLQRNQPLIELLLQNGADIDVQ 263
Cdd:pfam12796  69 ARSGHLEIVKLLLEKGADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
195-297 6.87e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 60.90  E-value: 6.87e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543321   195 LHVACRRQNLACACCLLEEQPEPGrqlshpldlqLKNWQGLACLHIATLQRNQPLIELLLQNgadIDVQEGTSGKTALHL 274
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADAN----------LQDKNGRTALHLAAKNGHLEIVKLLLEH---ADVNLKDNGRTALHY 67

                          90       100
                  ....*....|....*....|...
gi 31543321   275 AVETQERSLVQFLLQAGARVDAR 297
Cdd:pfam12796  68 AARSGHLEIVKLLLEKGADINVK 90
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 221-326 9.43e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 62.98  E-value: 9.43e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543321  221 LSHPLDLQLKNWQGL-ACLHIATLQRNQPLIELLLQNGADIDVQEGTSgKTALHLAVETQERSLVQFLLQAGARVDARML 299
Cdd:PHA02878 154 LSYGADINMKDRHKGnTALHYATENKDQRLTELLLSYGANVNIPDKTN-NSPLHHAVKHYNKPIVHILLENGASTDARDK 232

                         90       100
                 ....*....|....*....|....*...
gi 31543321  300 NGCTPLHLAAGRGLN-SISSTLCEAGAD 326
Cdd:PHA02878 233 CGNTPLHISVGYCKDyDILKLLLEHGVD 260
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 170-341 2.48e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 61.43  E-value: 2.48e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543321  170 QPDVVRALVLKGASRILQDQH-GDTALHVACRRQNLACACCLLEEQPE---PGRQLSHPLdlqlknwqglaclHIATLQR 245
Cdd:PHA02878 146 EAEITKLLLSYGADINMKDRHkGNTALHYATENKDQRLTELLLSYGANvniPDKTNNSPL-------------HHAVKHY 212

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543321  246 NQPLIELLLQNGADIDVQEgTSGKTALHLAV-ETQERSLVQFLLQAGARVDAR-MLNGCTPLHLA--AGRGLNsissTLC 321
Cdd:PHA02878 213 NKPIVHILLENGASTDARD-KCGNTPLHISVgYCKDYDILKLLLEHGVDVNAKsYILGLTALHSSikSERKLK----LLL 287

                        170       180
                 ....*....|....*....|
gi 31543321  322 EAGADSLLLNVEDETPQDLA 341
Cdd:PHA02878 288 EYGADINSLNSYKLTPLSSA 307
PHA03095 PHA03095
ankyrin-like protein; Provisional
 160-326 1.24e-09

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 59.27  E-value: 1.24e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543321  160 TALHLAVHL---DQPDVVRALVLKGASRILQDQHGDTALHvacrrqnlacacCLLEEQPEPgrqlshpldlqlknwqgla 236
Cdd:PHA03095  49 TPLHLYLHYsseKVKDIVRLLLEAGADVNAPERCGFTPLH------------LYLYNATTL------------------- 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543321  237 clhiatlqrnqPLIELLLQNGADIDVqEGTSGKTALH--LAVETQERSLVQFLLQAGARVDARMLNGCTPLH-LAAGRGL 313
Cdd:PHA03095  98 -----------DVIKLLIKAGADVNA-KDKVGRTPLHvyLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAvLLKSRNA 165

                        170
                 ....*....|....
gi 31543321  314 N-SISSTLCEAGAD 326
Cdd:PHA03095 166 NvELLRLLIDAGAD 179
Ank_2 pfam12796
Ankyrin repeats (3 copies);
127-220 1.59e-09

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 54.35  E-value: 1.59e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543321   127 LHLAVIHEAPSvlfCCLAFLPQEV-LDIQNNLYQTALHLAVHLDQPDVVRALVLKGASRIlqDQHGDTALHVACRRQNLA 205
Cdd:pfam12796   1 LHLAAKNGNLE---LVKLLLENGAdANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL--KDNGRTALHYAARSGHLE 75

                          90
                  ....*....|....*
gi 31543321   206 CACCLLEEQPEPGRQ 220
Cdd:pfam12796  76 IVKLLLEKGADINVK 90
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 123-317 1.92e-09

transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 59.32  E-value: 1.92e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543321   123 GDTLLHLAVIHEAPSVLFCCLAFL--------PQEVLDIQNNLY---QTALHLAVHLDQPDVVRALVLKGASrilqdqhg 191
Cdd:TIGR00870  82 GDTLLHAISLEYVDAVEAILLHLLaafrksgpLELANDQYTSEFtpgITALHLAAHRQNYEIVKLLLERGAS-------- 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543321   192 dtaLHVACrrqnlACACCLLEEQPEPGRQLSHPLDLqlknwqgLACLhiatlqrNQP-LIELLLQNGADIDVQEgTSGKT 270
Cdd:TIGR00870 154 ---VPARA-----CGDFFVKSQGVDSFYHGESPLNA-------AACL-------GSPsIVALLSEDPADILTAD-SLGNT 210

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 31543321   271 ALHLAVETQE---------RSLVQFLLQAGARVDAR-----MLN--GCTPLHLAAGRGLNSIS 317
Cdd:TIGR00870 211 LLHLLVMENEfkaeyeelsCQMYNFALSLLDKLRDSkelevILNhqGLTPLKLAAKEGRIVLF 273
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 190-307 2.24e-09

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 58.87  E-value: 2.24e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543321 190 HGDTALHVACRRQNLACACCLLEEQPEpgrQLSHPLDLQLknWQGLACLHIATLQRNQPLIELLLQNGADIDVQEGTS-- 267
Cdd:cd22192  50 LGETALHVAALYDNLEAAVVLMEAAPE---LVNEPMTSDL--YQGETALHIAVVNQNLNLVRELIARGADVVSPRATGtf 124

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 31543321 268 -----------GKTALHLAVETQERSLVQFLLQAGARVDARMLNGCTPLHL 307
Cdd:cd22192 125 frpgpknliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHI 175
PHA03095 PHA03095
ankyrin-like protein; Provisional
 250-339 4.64e-09

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 57.73  E-value: 4.64e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543321  250 IELLLQNGADIDVQEgTSGKTALHLAVETQ-ERSLVQFLLQAGARVDARMLNGCTPLHLAAgRGLN---SISSTLCEAGA 325
Cdd:PHA03095  66 VRLLLEAGADVNAPE-RCGFTPLHLYLYNAtTLDVIKLLIKAGADVNAKDKVGRTPLHVYL-SGFNinpKVIRLLLRKGA 143

                         90
                 ....*....|....
gi 31543321  326 DSLLLNVEDETPQD 339
Cdd:PHA03095 144 DVNALDLYGMTPLA 157
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 233-326 1.54e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 55.77  E-value: 1.54e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543321  233 QGLACLHIATLQRNQPLIELLLQNGADIDVQEgTSGKTALHLAVETQERSLVQFLLQAGARVDARMLNGCTPLHLAAGRG 312
Cdd:PHA02875 101 DGMTPLHLATILKKLDIMKLLIARGADPDIPN-TDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKG 179

                         90
                 ....*....|....
gi 31543321  313 LNSISSTLCEAGAD 326
Cdd:PHA02875 180 DIAICKMLLDSGAN 193
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 221-356 2.58e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 55.06  E-value: 2.58e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543321  221 LSHPLDLQLKNWQGLACLHIATLQRNQPLIELLLQNGADIDvQEGTSGKTALHL-----AVETQERSLVQFLLQAGARVD 295
Cdd:PHA03100  22 IMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADIN-SSTKNNSTPLHYlsnikYNLTDVKEIVKLLLEYGANVN 100

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 31543321  296 ARMLNGCTPLHLAAGRGLNSIS--STLCEAGADSLLLNVEDETPQDLAedlLSYlPFDDLKIS 356
Cdd:PHA03100 101 APDNNGITPLLYAISKKSNSYSivEYLLDNGANVNIKNSDGENLLHLY---LES-NKIDLKIL 159
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 172-308 3.44e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 54.97  E-value: 3.44e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543321  172 DVVRALVLKGASRILQDQHGDTALHVACRRQNLACACCLLEeqpepgrqlsHPLDLQLKNWQGLACLHIATLQRNQPLIE 251
Cdd:PHA02874 105 DMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFE----------YGADVNIEDDNGCYPIHIAIKHNFFDIIK 174

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 31543321  252 LLLQNGADIDVQEgTSGKTALHLAVETQERSLVQFLLQAGARVDARMLNGCTPLHLA 308
Cdd:PHA02874 175 LLLEKGAYANVKD-NNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNA 230
PHA03095 PHA03095
ankyrin-like protein; Provisional
 160-341 5.56e-08

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 54.26  E-value: 5.56e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543321  160 TALHlaVHLD----QPDVVRALVLKGASRILQDQHGDTALHVACRRQNlacaCC-----LLeeqpepgrqLSHPLDLQLK 230
Cdd:PHA03095 119 TPLH--VYLSgfniNPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRN----ANvellrLL---------IDAGADVYAV 183

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543321  231 NWQGLACLHI--ATLQRNQPLIELLLQNGADiDVQEGTSGKTALHLAV--ETQERSLVQFLLQAGARVDARMLNGCTPLH 306
Cdd:PHA03095 184 DDRFRSLLHHhlQSFKPRARIVRELIRAGCD-PAATDMLGNTPLHSMAtgSSCKRSLVLPLLIAGISINARNRYGQTPLH 262

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 31543321  307 LAAGRGLNSISSTLCEAGADSLLLNVEDETPQDLA 341
Cdd:PHA03095 263 YAAVFNNPRACRRLIALGADINAVSSDGNTPLSLM 297
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 151-326 1.25e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 53.13  E-value: 1.25e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543321  151 LDIQNNLYQTALHL-----AVHLDQPDVVRALVLKGASRILQDQHGDTALHVacrrqnlaCACCLLEEQPEPGRQLSHPL 225
Cdd:PHA03100  61 INSSTKNNSTPLHYlsnikYNLTDVKEIVKLLLEYGANVNAPDNNGITPLLY--------AISKKSNSYSIVEYLLDNGA 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543321  226 DLQLKNWQGLACLHIATLQ--RNQPLIELLLQNGADIDVQE--------GTS-------GKTALHLAVETQERSLVQFLL 288
Cdd:PHA03100 133 NVNIKNSDGENLLHLYLESnkIDLKILKLLIDKGVDINAKNrvnyllsyGVPinikdvyGFTPLHYAVYNNNPEFVKYLL 212

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 31543321  289 QAGARVDARMLNGCTPLHLAAGRGLNSISSTLCEAGAD 326
Cdd:PHA03100 213 DLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPS 250
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 160-308 1.81e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 52.57  E-value: 1.81e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543321  160 TALHLAVHLDQPDVVRALVLKGASRILQDQHGDTALHVACRRQNLACACCLLEEqpepGRQLSHpldlqlKNWQGLACLH 239
Cdd:PHA02878 170 TALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLEN----GASTDA------RDKCGNTPLH 239

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543321  240 IATLQ-RNQPLIELLLQNGADIDVQEGTSGKTALHLAVETQERslVQFLLQAGARVDARMLNGCTPLHLA 308
Cdd:PHA02878 240 ISVGYcKDYDILKLLLEHGVDVNAKSYILGLTALHSSIKSERK--LKLLLEYGADINSLNSYKLTPLSSA 307
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 231-325 3.10e-07

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 49.49  E-value: 3.10e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543321  231 NWQGLACLHIATLQRN---QPLIELLLQNGADIDVQEGTSGKTALHLAVETQERSLVQFLLQAgARVDARMLNGC--TPL 305
Cdd:PHA02736  52 NRHGKQCVHIVSNPDKadpQEKLKLLMEWGADINGKERVFGNTPLHIAVYTQNYELATWLCNQ-PGVNMEILNYAfkTPY 130

                         90       100
                 ....*....|....*....|
gi 31543321  306 HLAAGRGLNSISSTLCEAGA 325
Cdd:PHA02736 131 YVACERHDAKMMNILRAKGA 150
PHA03095 PHA03095
ankyrin-like protein; Provisional
 250-335 4.63e-07

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 51.56  E-value: 4.63e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543321  250 IELLLQNGADIDvQEGTSGKTALHLAVET---QERSLVQFLLQAGARVDARMLNGCTPLHLAAgrgLNSIS----STLCE 322
Cdd:PHA03095  30 VRRLLAAGADVN-FRGEYGKTPLHLYLHYsseKVKDIVRLLLEAGADVNAPERCGFTPLHLYL---YNATTldviKLLIK 105

                         90
                 ....*....|...
gi 31543321  323 AGADsllLNVEDE 335
Cdd:PHA03095 106 AGAD---VNAKDK 115
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 246-337 6.41e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 50.73  E-value: 6.41e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543321  246 NQPLIELLLQNGADIDVQEGTSgKTALHLAVETQERSLVQFLLQAGARVDARMLNGCTPLHLAAGRGLNSISSTLCEAGA 325
Cdd:PHA02874 103 EKDMIKTILDCGIDVNIKDAEL-KTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGA 181

                         90
                 ....*....|....*
gi 31543321  326 dslLLNVED---ETP 337
Cdd:PHA02874 182 ---YANVKDnngESP 193
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 151-308 6.47e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 50.73  E-value: 6.47e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543321  151 LDIQNNLYQTALHLAVHLDQPDVVRALVLKGASRILQDQHGDTALHVACRRQNLACACCLLEEQPEpgrqlshpldLQLK 230
Cdd:PHA02874 117 VNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAY----------ANVK 186

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 31543321  231 NWQGLACLHIATLQRNQPLIELLLQNGADIDVQeGTSGKTALHLAVeTQERSLVQFLLQaGARVDARMLNGCTPLHLA 308
Cdd:PHA02874 187 DNNGESPLHNAAEYGDYACIKLLIDHGNHIMNK-CKNGFTPLHNAI-IHNRSAIELLIN-NASINDQDIDGSTPLHHA 261
PHA02741 PHA02741
hypothetical protein; Provisional
 222-308 7.99e-07

hypothetical protein; Provisional


Pssm-ID: 165108 [Multi-domain]  Cd Length: 169  Bit Score: 48.50  E-value: 7.99e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543321  222 SHPLDLQLKNWQGLACLHIATLQRNQ----PLIELLLQNGADIDVQEGTSGKTALHLAVETQERSLVQFLL-QAGARVDA 296
Cdd:PHA02741  48 CHAAALNATDDAGQMCIHIAAEKHEAqlaaEIIDHLIELGADINAQEMLEGDTALHLAAHRRDHDLAEWLCcQPGIDLHF 127

                         90
                 ....*....|..
gi 31543321  297 RMLNGCTPLHLA 308
Cdd:PHA02741 128 CNADNKSPFELA 139
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 162-337 8.75e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 50.35  E-value: 8.75e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543321  162 LHLAVHLDQPDVVRALVLKGASRILQDQHGDTALHVACRRQNLACACCLleeqpepgrqLSHPLDLQLKNWQGLACLHIA 241
Cdd:PHA02874 161 IHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLL----------IDHGNHIMNKCKNGFTPLHNA 230

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543321  242 TLQrNQPLIELLLQNgADIDVQEgTSGKTALHLAVETQ-ERSLVQFLLQAGARVDARMLNGCTPLHLAAgRGLNSIsSTL 320
Cdd:PHA02874 231 IIH-NRSAIELLINN-ASINDQD-IDGSTPLHHAINPPcDIDIIDILLYHKADISIKDNKGENPIDTAF-KYINKD-PVI 305

                        170
                 ....*....|....*..
gi 31543321  321 CEAGADSLLLNVEDETP 337
Cdd:PHA02874 306 KDIIANAVLIKEADKLK 322
PHA02741 PHA02741
hypothetical protein; Provisional
 267-343 9.48e-07

hypothetical protein; Provisional


Pssm-ID: 165108 [Multi-domain]  Cd Length: 169  Bit Score: 48.50  E-value: 9.48e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543321  267 SGKTALHLAVETQER----SLVQFLLQAGARVDAR-MLNGCTPLHLAAGRGLNSISSTLC-EAGADSLLLNVEDETPQDL 340
Cdd:PHA02741  59 AGQMCIHIAAEKHEAqlaaEIIDHLIELGADINAQeMLEGDTALHLAAHRRDHDLAEWLCcQPGIDLHFCNADNKSPFEL 138


                 ...
gi 31543321  341 AED 343
Cdd:PHA02741 139 AID 141
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 284-343 1.27e-06

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 50.28  E-value: 1.27e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543321  284 VQFLLQAGARVDARMLNGCTPLHLAAGRGLNSISSTLCEAGADSLLLNVEDETPQDLAED 343
Cdd:PTZ00322  98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEE 157
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 159-335 1.72e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 49.60  E-value: 1.72e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543321  159 QTALHLAVhlDQPDVVRALVLKGASRILQD---QHGDTALHVACRRQNLACACCLLEEQPEPgrqlshpldlQLKNWQGL 235
Cdd:PHA02875  69 ESELHDAV--EEGDVKAVEELLDLGKFADDvfyKDGMTPLHLATILKKLDIMKLLIARGADP----------DIPNTDKF 136

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543321  236 ACLHIATLQRNQPLIELLLQNGADIDVQEGTsGKTALHLAVETQERSLVQFLLQAGARVDARMLNGC-TPLHLAAGRGLN 314
Cdd:PHA02875 137 SPLHLAVMMGDIKGIELLIDHKACLDIEDCC-GCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCvAALCYAIENNKI 215

                        170       180
                 ....*....|....*....|..
gi 31543321  315 SISSTLCEAGADS-LLLNVEDE 335
Cdd:PHA02875 216 DIVRLFIKRGADCnIMFMIEGE 237
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 191-306 2.90e-06

Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily (TRPV), named after the vanilloid receptor 1 (TRPV1), consists of six members: four thermo-sensing channels (TRPV1, TRPV2, TRPV3, and TRPV4) and two Ca2+ selective channels (TRPV5 and TRPV6). The calcium-selective channels TRPV5 and TRPV6 can be heterotetramers and are important for general Ca2+ homeostasis. All four channels within the TRPV1-4 group show temperature-invoked currents when expressed in heterologous cell systems, ranging from activation at ~25C for TRPV4 to ~52C for TRPV2. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains. The TRP family consists of membrane proteins that function as ion channels that communicate between the cell and its environment, by a vast array of physical or chemical stimuli, including radiation (in the form of temperature, infrared ,or light) and pressure (osmotic or mechanical). TRP channels are formed by a tetrameric complex of channel subunits. Based on sequence identity, the mammalian TRP channel family is classified into six subfamilies, with significant sequence similarity within the transmembrane domains, but very low similarity in their N- and C-terminal cytoplasmic regions. The six subfamilies are named based on their first member: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin), TRPA (ankyrin), TRPML (mucolipin), and TRPP (polycystic).


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 49.11  E-value: 2.90e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543321 191 GDTALHVACRRQN---LACACCLLEEQPEPGRQLshpldlQLKN-------WQGLACLHIATLQRNQPLIELLLQNGADI 260
Cdd:cd21882  26 GKTCLHKAALNLNdgvNEAIMLLLEAAPDSGNPK------ELVNapctdefYQGQTALHIAIENRNLNLVRLLVENGADV 99

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 31543321 261 DVQE-GTS-----------GKTALHLAVETQERSLVQFLLQAGAR---VDARMLNGCTPLH 306
Cdd:cd21882 100 SARAtGRFfrkspgnlfyfGELPLSLAACTNQEEIVRLLLENGAQpaaLEAQDSLGNTVLH 160
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
 232-306 4.96e-06

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 (TRPV1), a capsaicin (vanilloid) receptor, is the founding member of the vanilloid TRP subfamily (TRPV). In humans, it is expressed in the brain, kidney, pancreas, testis, uterus, spleen, stomach, small intestine, lung and liver. TRPV1 has been implicated to have function in thermo-sensation (heat), autonomic thermoregulation, nociception, food intake regulation, and multiple functions in the gastrointestinal (GI) tract. The receptor has also been involved in growth cone guidance, long-term depression, endocannabinoid signaling and osmosensing in the central nervous system. TRPV1 is up regulated in several human pathological conditions including vulvodynia, GI inflammation, Crohn's disease and ulcerative colitis. TRPV1 knock-out mice exhibit impaired sensation to thermal-mechanical acute pain. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411980 [Multi-domain]  Cd Length: 649  Bit Score: 48.26  E-value: 4.96e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543321 232 WQGLACLHIATLQRNQPLIELLLQNGADID----------VQEGTS---GKTALHLAVETQERSLVQFLLQ---AGARVD 295
Cdd:cd22196  92 YKGQTALHIAIERRNMHLVELLVQNGADVHarasgeffkkKKGGPGfyfGELPLSLAACTNQLDIVKFLLEnphSPADIS 171

                        90
                ....*....|.
gi 31543321 296 ARMLNGCTPLH 306
Cdd:cd22196 172 ARDSMGNTVLH 182
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 188-329 7.09e-06

transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 47.77  E-value: 7.09e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543321   188 DQHGDTAL-HVACRRQNLACACCLLEEQPEP--GRQLSHPLDLQLKNWQGLACLHIATLQRNQPLIELLLqngaDIDVQE 264
Cdd:TIGR00870  49 DRLGRSALfVAAIENENLELTELLLNLSCRGavGDTLLHAISLEYVDAVEAILLHLLAAFRKSGPLELAN----DQYTSE 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543321   265 GTSGKTALHLAVETQERSLVQFLLQAGARVDARmlngCT------------------PLHLAAGRGLNSISSTLCEAGAD 326
Cdd:TIGR00870 125 FTPGITALHLAAHRQNYEIVKLLLERGASVPAR----ACgdffvksqgvdsfyhgesPLNAAACLGSPSIVALLSEDPAD 200


                  ...
gi 31543321   327 SLL 329
Cdd:TIGR00870 201 ILT 203
Ank_2 pfam12796
Ankyrin repeats (3 copies);
121-183 8.53e-06

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 43.57  E-value: 8.53e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 31543321   121 EDGDTLLHLAVIHeapSVLFCCLAFLPQEVLDIQNNlYQTALHLAVHLDQPDVVRALVLKGAS 183
Cdd:pfam12796  28 KNGRTALHLAAKN---GHLEIVKLLLEHADVNLKDN-GRTALHYAARSGHLEIVKLLLEKGAD 86
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 234-334 1.36e-05

Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily (TRPV), named after the vanilloid receptor 1 (TRPV1), consists of six members: four thermo-sensing channels (TRPV1, TRPV2, TRPV3, and TRPV4) and two Ca2+ selective channels (TRPV5 and TRPV6). The calcium-selective channels TRPV5 and TRPV6 can be heterotetramers and are important for general Ca2+ homeostasis. All four channels within the TRPV1-4 group show temperature-invoked currents when expressed in heterologous cell systems, ranging from activation at ~25C for TRPV4 to ~52C for TRPV2. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains. The TRP family consists of membrane proteins that function as ion channels that communicate between the cell and its environment, by a vast array of physical or chemical stimuli, including radiation (in the form of temperature, infrared ,or light) and pressure (osmotic or mechanical). TRP channels are formed by a tetrameric complex of channel subunits. Based on sequence identity, the mammalian TRP channel family is classified into six subfamilies, with significant sequence similarity within the transmembrane domains, but very low similarity in their N- and C-terminal cytoplasmic regions. The six subfamilies are named based on their first member: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin), TRPA (ankyrin), TRPML (mucolipin), and TRPP (polycystic).


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 46.80  E-value: 1.36e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543321 234 GLACLHIATLQRNQPLIE---LLLQNGADID----------VQEGTSGKTALHLAVETQERSLVQFLLQAGARVDARML- 299
Cdd:cd21882  26 GKTCLHKAALNLNDGVNEaimLLLEAAPDSGnpkelvnapcTDEFYQGQTALHIAIENRNLNLVRLLVENGADVSARATg 105

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 31543321 300 -----NGCT-------PLHLAAGRGLNSISSTLCEAGADSLLLNVED 334
Cdd:cd21882 106 rffrkSPGNlfyfgelPLSLAACTNQEEIVRLLLENGAQPAALEAQD 152
Ank_4 pfam13637
Ankyrin repeats (many copies);
160-211 1.87e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 41.49  E-value: 1.87e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 31543321   160 TALHLAVHLDQPDVVRALVLKGASRILQDQHGDTALHVACRRQNLACACCLL 211
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 160-343 2.25e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 46.21  E-value: 2.25e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543321  160 TALHLAVHLDQPDVVRALVLKGASRI-LQDQHGDTALHVACRRQNLACACCLLEEQPEPGRQLSHPLDLQLKNWQGLACL 238
Cdd:PHA02876  43 TAIHQALQLRQIDIVEEIIQQNPELIyITDHKCHSTLHTICIIPNVMDIVISLTLDCDIILDIKYASIILNKHKLDEACI 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543321  239 HIatlqrnqpLIELLLQNGADID-VQEGTSGKTALHLAVETQERSLVQFLLQAGARVDARMLNGCTPLHLAAGRGLNSIS 317
Cdd:PHA02876 123 HI--------LKEAISGNDIHYDkINESIEYMKLIKERIQQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMV 194

                        170       180
                 ....*....|....*....|....*.
gi 31543321  318 STLCEAGADSLLLNVEDETPQDLAED 343
Cdd:PHA02876 195 NLLLSYGADVNIIALDDLSVLECAVD 220
Ank_4 pfam13637
Ankyrin repeats (many copies);
234-288 4.24e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 40.72  E-value: 4.24e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 31543321   234 GLACLHIATLQRNQPLIELLLQNGADIDVQEGtSGKTALHLAVETQERSLVQFLL 288
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDG-NGETALHFAASNGNVEVLKLLL 54
PHA02743 PHA02743
Viral ankyrin protein; Provisional
 233-308 5.65e-05

Viral ankyrin protein; Provisional


Pssm-ID: 222925 [Multi-domain]  Cd Length: 166  Bit Score: 43.27  E-value: 5.65e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543321  233 QGLACLHIATL-QRNQPL--IELLLQNGADIDVQEGTSGKTALHLAVETQERSLVQFLLQA-GARVDARMLNGCTPLHLA 308
Cdd:PHA02743  56 HGRQCTHMVAWyDRANAVmkIELLVNMGADINARELGTGNTLLHIAASTKNYELAEWLCRQlGVNLGAINYQHETAYHIA 135
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 174-337 6.16e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 45.05  E-value: 6.16e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543321  174 VRALVLKGASRILQDQHGDTALHVACR-RQNLACACCLLEEQPepgrqlshplDLQLKNWQGLACLHIATLQRNQPLIEL 252
Cdd:PHA02876 324 IRTLIMLGADVNAADRLYITPLHQASTlDRNKDIVITLLELGA----------NVNARDYCDKTPIHYAAVRNNVVIINT 393

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543321  253 LLQNGADIDVQEGTSGkTALHLAV-ETQERSLVQFLLQAGARVDARMLNGCTPLHLAAGRGLN-SISSTLCEAGADSLLL 330
Cdd:PHA02876 394 LLDYGADIEALSQKIG-TALHFALcGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNCKlDVIEMLLDNGADVNAI 472


                 ....*..
gi 31543321  331 NVEDETP 337
Cdd:PHA02876 473 NIQNQYP 479
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 225-312 6.84e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 44.57  E-value: 6.84e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543321  225 LDLQLKNWQGLACLHIATLQRNQPLIELLLQNGADIDVQEgTSGKTALHLAVETQERSLVQFLLQAGARVDARMLNGCTP 304
Cdd:PHA02874 115 IDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIED-DNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESP 193


                 ....*...
gi 31543321  305 LHLAAGRG 312
Cdd:PHA02874 194 LHNAAEYG 201
PHA03095 PHA03095
ankyrin-like protein; Provisional
 155-276 7.17e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 44.63  E-value: 7.17e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543321  155 NNLYQTALHlaVHLD----QPDVVRALVLKGASRILQDQHGDTALHVA-----CRRQNLACaccLLEEQpepgrqlshpL 225
Cdd:PHA03095 184 DDRFRSLLH--HHLQsfkpRARIVRELIRAGCDPAATDMLGNTPLHSMatgssCKRSLVLP---LLIAG----------I 248

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 31543321  226 DLQLKNWQGLACLHIATLQRNQPLIELLLQNGADIDVQEGTsGKTALHLAV 276
Cdd:PHA03095 249 SINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSD-GNTPLSLMV 298
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 232-306 1.82e-04

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are thermo-sensing channels that function directly in temperature-sensing and nociception; they share substantial structural and functional properties. Transient Receptor Potential (TRP) ion channels activated by temperature (thermo TRPs) are important molecular players in acute, inflammatory, and chronic pain states. So far, 11 TRP channels in mammalian cells have been identified as thermosensitive TRP (thermo-TRP) channels. TRPV1-4 channels are activated by different heat temperatures, for example, TRPV1 and TRPV2 are activated by high temperatures (>43C and >55C, respectively). TRPV1-4 belong to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411977 [Multi-domain]  Cd Length: 607  Bit Score: 43.25  E-value: 1.82e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543321 232 WQGLACLHIATLQRNQPLIELLLQNGADIDVQ----------EGTS---GKTALHLAVETQERSLVQFLLQ---AGARVD 295
Cdd:cd22193  74 YEGQTALHIAIERRQGDIVALLVENGADVHAHakgrffqpkyQGEGfyfGELPLSLAACTNQPDIVQYLLEnehQPADIE 153

                        90
                ....*....|.
gi 31543321 296 ARMLNGCTPLH 306
Cdd:cd22193 154 AQDSRGNTVLH 164
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 230-327 1.84e-04

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a temperature-sensitive Transient Receptor Potential (TRP) ion channel that is activated by warm temperatures, synthetic small-molecule chemicals, and natural compounds from plants. TRPV3 function is regulated by physiological factors such as extracellular divalent cations and acidic pH, intracellular adenosine triphosphate, membrane voltage, and arachidonic acid. It is expressed in both neuronal and non-neuronal tissues including epidermal keratinocytes, epithelial cells in the gut, endothelial cells in blood vessels, and neurons in dorsal root ganglia and CNS. TRPV3 null mice have abnormal hair morphogenesis and compromised skin barrier function. It may play roles in inflammatory skin disorders, such as itch and pain sensation. TRPV3 is also expressed by many neuronal and non-neuronal tissues, showing that TRPV3 might play roles in other unknown cellular and physiological functions. TRPV3 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 43.59  E-value: 1.84e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543321 230 KNWQGLACLHIATLQRNQPLIELLLQNGADIDVQ-EGT------------SGKTALHLAVETQERSLVQFLLQagarvda 296
Cdd:cd22194 137 EAYEGQTALNIAIERRQGDIVKLLIAKGADVNAHaKGVffnpkykhegfyFGETPLALAACTNQPEIVQLLME------- 209

                        90       100       110
                ....*....|....*....|....*....|.
gi 31543321 297 rmlNGCTPLHLAAGRGlNSISSTLCEAGADS 327
Cdd:cd22194 210 ---KESTDITSQDSRG-NTVLHALVTVAEDS 236
Ank_4 pfam13637
Ankyrin repeats (many copies);
270-312 2.30e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 38.79  E-value: 2.30e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 31543321   270 TALHLAVETQERSLVQFLLQAGARVDARMLNGCTPLHLAAGRG 312
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNG 45
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 148-326 2.36e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 43.13  E-value: 2.36e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543321  148 QEVLDIQNNLYQTALHLAVHLDQPDVVRALVL--KGASRILQDQHGDTALHVACRRQNLACaccLLEEQPEPGrqlshpL 225
Cdd:PHA02876 228 KAIIDNRSNINKNDLSLLKAIRNEDLETSLLLydAGFSVNSIDDCKNTPLHHASQAPSLSR---LVPKLLERG------A 298

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543321  226 DLQLKNWQGLACLHI-ATLQRNQPLIELLLQNGADIDVQEGTSgKTALHLAVE-TQERSLVQFLLQAGARVDARMLNGCT 303
Cdd:PHA02876 299 DVNAKNIKGETPLYLmAKNGYDTENIRTLIMLGADVNAADRLY-ITPLHQASTlDRNKDIVITLLELGANVNARDYCDKT 377

                        170       180
                 ....*....|....*....|...
gi 31543321  304 PLHLAAGRGLNSISSTLCEAGAD 326
Cdd:PHA02876 378 PIHYAAVRNNVVIINTLLDYGAD 400
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 232-341 3.40e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 42.29  E-value: 3.40e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543321  232 WQGLACLHIATLQRNQPLIELLLQNGADIDVQEgTSGKTALHLAVETQERSLVQFLLQAGARVDARML-NGCTPLHLAAG 310
Cdd:PHA02875  33 YDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKY-PDIESELHDAVEEGDVKAVEELLDLGKFADDVFYkDGMTPLHLATI 111

                         90       100       110
                 ....*....|....*....|....*....|.
gi 31543321  311 RGLNSISSTLCEAGADSLLLNVEDETPQDLA 341
Cdd:PHA02875 112 LKKLDIMKLLIARGADPDIPNTDKFSPLHLA 142
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
 205-306 4.37e-04

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely related to TRPV1, sharing high sequence identity (>50%), but TRPV2 shows a higher temperature threshold and sensitivity for activation than TRPV1. TRPV2 can be stimulated by ligands or lipids, and is involved in osmosensation and mechanosensation. TRPV2 is expressed in both neuronal and non-neuronal tissues, and it has been implicated in diverse physiological and pathophysiological processes, including cardiac-structure maintenance, innate immunity, and cancer. TRPV2 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411981 [Multi-domain]  Cd Length: 640  Bit Score: 42.15  E-value: 4.37e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543321 205 ACACCLLEEQPEPGRqlSHPL-DLQLKN--WQGLACLHIATLQRNQPLIELLLQNGADIDV---------QEGTS---GK 269
Cdd:cd22197  64 ACIMPLLEIDKDSGN--PKPLvNAQCTDeyYRGHSALHIAIEKRSLQCVKLLVENGADVHAracgrffqkKQGTCfyfGE 141

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 31543321 270 TALHLAVETQERSLVQFLLQAG---ARVDARMLNGCTPLH 306
Cdd:cd22197 142 LPLSLAACTKQWDVVNYLLENPhqpASLQAQDSLGNTVLH 181
Ank_5 pfam13857
Ankyrin repeats (many copies);
151-198 4.57e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 37.71  E-value: 4.57e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 31543321   151 LDIQNNLYQTALHLAVHLDQPDVVRALVLKGASRILQDQHGDTALHVA 198
Cdd:pfam13857   9 LNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 123-256 6.73e-04

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 41.54  E-value: 6.73e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543321 123 GDTLLHLAVIH---EAPSVLFCC---LAFLPqevldIQNNLYQ--TALHLAVHLDQPDVVRALVLKGAS----------- 183
Cdd:cd22192  51 GETALHVAALYdnlEAAVVLMEAapeLVNEP-----MTSDLYQgeTALHIAVVNQNLNLVRELIARGADvvspratgtff 125

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543321 184 ---------------------------RIL---------QDQHGDTALHVACRRQNLACAC----CLLEEQPEPGrqlSH 223
Cdd:cd22192 126 rpgpknliyygehplsfaacvgneeivRLLiehgadiraQDSLGNTVLHILVLQPNKTFACqmydLILSYDKEDD---LQ 202

                       170       180       190
                ....*....|....*....|....*....|...
gi 31543321 224 PLDlQLKNWQGLACLHIATLQRNQPLIELLLQN 256
Cdd:cd22192 203 PLD-LVPNNQGLTPFKLAAKEGNIVMFQHLVQK 234
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 159-312 1.21e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a temperature-sensitive Transient Receptor Potential (TRP) ion channel that is activated by warm temperatures, synthetic small-molecule chemicals, and natural compounds from plants. TRPV3 function is regulated by physiological factors such as extracellular divalent cations and acidic pH, intracellular adenosine triphosphate, membrane voltage, and arachidonic acid. It is expressed in both neuronal and non-neuronal tissues including epidermal keratinocytes, epithelial cells in the gut, endothelial cells in blood vessels, and neurons in dorsal root ganglia and CNS. TRPV3 null mice have abnormal hair morphogenesis and compromised skin barrier function. It may play roles in inflammatory skin disorders, such as itch and pain sensation. TRPV3 is also expressed by many neuronal and non-neuronal tissues, showing that TRPV3 might play roles in other unknown cellular and physiological functions. TRPV3 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 40.90  E-value: 1.21e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543321 159 QTALHLAVHLDQPDVVRALVLKGASRILQ---------DQH-----GDTALHVAcrrqnlACAcclleeqpepgrqlshp 224
Cdd:cd22194 142 QTALNIAIERRQGDIVKLLIAKGADVNAHakgvffnpkYKHegfyfGETPLALA------ACT----------------- 198

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543321 225 ldlqlknwqglaclhiatlqrNQP-LIELLLQNGADIDVQEGTSGKTALHLAVETQERSLVQ----------FLLQAGAR 293
Cdd:cd22194 199 ---------------------NQPeIVQLLMEKESTDITSQDSRGNTVLHALVTVAEDSKTQndfvkrmydmILLKSENK 257

                       170       180
                ....*....|....*....|.
gi 31543321 294 VDARMLN--GCTPLHLAAGRG 312
Cdd:cd22194 258 NLETIRNneGLTPLQLAAKMG 278
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 247-326 1.54e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 40.38  E-value: 1.54e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543321 247 QPLIELLLQNGADIdVQEGTSGKTALHLAVETQERSLVQFLLQAGAR-----VDARMLNGCTPLHLAAGRGLNSISSTLC 321
Cdd:cd22192  31 QAIKKLLKCPSCDL-FQRGALGETALHVAALYDNLEAAVVLMEAAPElvnepMTSDLYQGETALHIAVVNQNLNLVRELI 109


                ....*
gi 31543321 322 EAGAD 326
Cdd:cd22192 110 ARGAD 114
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 119-262 1.72e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 39.97  E-value: 1.72e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543321  119 ISEDGDTLLHLAVIHEAPSVLFCCLAFLPQEvlDIQNNLYQTALHLAVHLDQPDVVRALVLKGASRILQDQHGDTALHVA 198
Cdd:PHA02875  98 FYKDGMTPLHLATILKKLDIMKLLIARGADP--DIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIA 175

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 31543321  199 CRRQNLACACCLLEEQPEPgrqlshplDLQLKNwqGLACLHIATLQRNQP-LIELLLQNGADIDV 262
Cdd:PHA02875 176 MAKGDIAICKMLLDSGANI--------DYFGKN--GCVAALCYAIENNKIdIVRLFIKRGADCNI 230
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 122-266 1.73e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 40.03  E-value: 1.73e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543321  122 DGDTLLHLAVIheapsvlfCClaflpqevlDIQNNLYQTALHLAVHLDQPDVVRALVLKGASRILQDQHGDTALHVACRR 201
Cdd:PHA03100 140 DGENLLHLYLE--------SN---------KIDLKILKLLIDKGVDINAKNRVNYLLSYGVPINIKDVYGFTPLHYAVYN 202

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 31543321  202 QNLACACCLLEEQPepgrqlshplDLQLKNWQGLACLHIATLQRNQPLIELLLQNGADIDVQEGT 266
Cdd:PHA03100 203 NNPEFVKYLLDLGA----------NPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIET 257
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 268-297 1.95e-03

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 35.34  E-value: 1.95e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 31543321   268 GKTALHLAVETQER-SLVQFLLQAGARVDAR 297
Cdd:pfam00023   2 GNTPLHLAAGRRGNlEIVKLLLSKGADVNAR 32
Ank_5 pfam13857
Ankyrin repeats (many copies);
253-308 1.98e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.17  E-value: 1.98e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 31543321   253 LLQNGADIDVQEGTSGKTALHLAVETQERSLVQFLLQAGARVDARMLNGCTPLHLA 308
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 263-309 3.44e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a temperature-sensitive Transient Receptor Potential (TRP) ion channel that is activated by warm temperatures, synthetic small-molecule chemicals, and natural compounds from plants. TRPV3 function is regulated by physiological factors such as extracellular divalent cations and acidic pH, intracellular adenosine triphosphate, membrane voltage, and arachidonic acid. It is expressed in both neuronal and non-neuronal tissues including epidermal keratinocytes, epithelial cells in the gut, endothelial cells in blood vessels, and neurons in dorsal root ganglia and CNS. TRPV3 null mice have abnormal hair morphogenesis and compromised skin barrier function. It may play roles in inflammatory skin disorders, such as itch and pain sensation. TRPV3 is also expressed by many neuronal and non-neuronal tissues, showing that TRPV3 might play roles in other unknown cellular and physiological functions. TRPV3 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 39.36  E-value: 3.44e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 31543321 263 QEGTSGKTALHLAVETQERSLVQFLLQAGARVDAR----MLN----------GCTPLHLAA 309
Cdd:cd22194 136 EEAYEGQTALNIAIERRQGDIVKLLIAKGADVNAHakgvFFNpkykhegfyfGETPLALAA 196
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 188-344 5.95e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 38.70  E-value: 5.95e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543321  188 DQHGDTALHVACRRQNLACACCLLEeqpepgrqlsHPLDLQLKNWQGLACLHIATLQRNQPLIELLLQNGADIDVQegtS 267
Cdd:PLN03192 555 DSKGRTPLHIAASKGYEDCVLVLLK----------HACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPH---A 621

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 31543321  268 GKTALHLAVETQERSLVQFLLQAGARVDARMLNGCTPLHLAAGRGLNSISSTLCEAGADSLLLNVEDE-TPQDLAEDL 344
Cdd:PLN03192 622 AGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTDDDfSPTELRELL 699
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 246-316 6.27e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 38.70  E-value: 6.27e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 31543321  246 NQPLIELLLQNGADIDVQEGTsGKTALHLAVETQERSLVQFLLQAGARVDARMLNGCTPLHLAAGRGLNSI 316
Cdd:PLN03192 537 NAALLEELLKAKLDPDIGDSK-GRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKI 606
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 268-296 6.80e-03

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 33.72  E-value: 6.80e-03
                           10        20
                   ....*....|....*....|....*....
gi 31543321    268 GKTALHLAVETQERSLVQFLLQAGARVDA 296
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 190-217 9.13e-03

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 33.33  E-value: 9.13e-03
                           10        20
                   ....*....|....*....|....*...
gi 31543321    190 HGDTALHVACRRQNLACACCLLEEQPEP 217
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADI 28
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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