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Conserved domains on  [gi|30089932|ref|NP_821066|]
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ankyrin repeat and SOCS box protein 6 isoform 2 [Homo sapiens]

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];
17-160 3.41e-16

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 74.61  E-value: 3.41e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089932  17 LVDAILGSLGIQDPERQESLDRPSYVASEESRILVLTELLERKAHSPFYQEGVSNALLKMAELGLTRAADVLLRHGANLN 96
Cdd:COG0666  68 LVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVN 147

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30089932  97 FEDPvTYYTALHIAVLRNQPDMVELLVHHGADVNRRDREKLlcSMLWPAATGCRSTILRTFVSY 160
Cdd:COG0666 148 AQDN-DGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGE--TPLHLAAENGHLEIVKLLLEA 208
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
17-160 3.41e-16

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 74.61  E-value: 3.41e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089932  17 LVDAILGSLGIQDPERQESLDRPSYVASEESRILVLTELLERKAHSPFYQEGVSNALLKMAELGLTRAADVLLRHGANLN 96
Cdd:COG0666  68 LVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVN 147

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30089932  97 FEDPvTYYTALHIAVLRNQPDMVELLVHHGADVNRRDREKLlcSMLWPAATGCRSTILRTFVSY 160
Cdd:COG0666 148 AQDN-DGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGE--TPLHLAAENGHLEIVKLLLEA 208
Ank_2 pfam12796
Ankyrin repeats (3 copies);
42-133 1.14e-10

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 55.89  E-value: 1.14e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089932    42 VASEESRILVLTELLERKAHSPFYQEGVSNALLKMAELGLTRAADVLLRHgANLNFEDpvTYYTALHIAVLRNQPDMVEL 121
Cdd:pfam12796   3 LAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD--NGRTALHYAARSGHLEIVKL 79

                          90
                  ....*....|..
gi 30089932   122 LVHHGADVNRRD 133
Cdd:pfam12796  80 LLEKGADINVKD 91
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 104-130 2.26e-06

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: 42.57  E-value: 2.26e-06
                           10        20
                   ....*....|....*....|....*..
gi 30089932    104 YTALHIAVLRNQPDMVELLVHHGADVN 130
Cdd:smart00248   3 RTPLHLAAENGNLEVVKLLLDKGADIN 29
PHA03095 PHA03095
ankyrin-like protein; Provisional
 86-133 4.25e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 46.17  E-value: 4.25e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 30089932   86 DVLLRHGANLNFEDPVTYyTALHIAvLRNQ---PDMVELLVHHGADVNRRD 133
Cdd:PHA03095 101 KLLIKAGADVNAKDKVGR-TPLHVY-LSGFninPKVIRLLLRKGADVNALD 149
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
 102-132 3.50e-05

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: 43.64  E-value: 3.50e-05
                        10        20        30
                ....*....|....*....|....*....|....
gi 30089932 102 TYY---TALHIAVLRNQPDMVELLVHHGADVNRR 132
Cdd:cd22196  90 SYYkgqTALHIAIERRNMHLVELLVQNGADVHAR 123
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 14-132 2.09e-03

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: 38.14  E-value: 2.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089932    14 YQPLVDAILGSLGIQDPERQESLdrpsYVASEESRILVLTELLERKAHSPFyqegVSNALLKMAELGLTRAADVLLRH-- 91
Cdd:TIGR00870  34 YRDLEEPKKLNINCPDRLGRSAL----FVAAIENENLELTELLLNLSCRGA----VGDTLLHAISLEYVDAVEAILLHll 105

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 30089932    92 -----GANLNF---EDPVTYY---TALHIAVLRNQPDMVELLVHHGADVNRR 132
Cdd:TIGR00870 106 aafrkSGPLELandQYTSEFTpgiTALHLAAHRQNYEIVKLLLERGASVPAR 157
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
17-160 3.41e-16

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 74.61  E-value: 3.41e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089932  17 LVDAILGSLGIQDPERQESLDRPSYVASEESRILVLTELLERKAHSPFYQEGVSNALLKMAELGLTRAADVLLRHGANLN 96
Cdd:COG0666  68 LVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVN 147

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30089932  97 FEDPvTYYTALHIAVLRNQPDMVELLVHHGADVNRRDREKLlcSMLWPAATGCRSTILRTFVSY 160
Cdd:COG0666 148 AQDN-DGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGE--TPLHLAAENGHLEIVKLLLEA 208
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
17-135 3.34e-15

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 71.91  E-value: 3.34e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089932  17 LVDAILGSLGIQDPERQESLDRPSYVASEESRILVLTELLERKAHSPFYQEGVSNALLKMAELGLTRAADVLLRHGANLN 96
Cdd:COG0666  35 LLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVN 114

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 30089932  97 FEDPvTYYTALHIAVLRNQPDMVELLVHHGADVNRRDRE 135
Cdd:COG0666 115 ARDK-DGETPLHLAAYNGNLEIVKLLLEAGADVNAQDND 152
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
29-135 5.08e-15

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 71.52  E-value: 5.08e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089932  29 DPERQESLDR-PSYVASEESRILVLTELLERKAhSPFYQEGVSN-ALLKMAELGLTRAADVLLRHGANLNFEDPvTYYTA 106
Cdd:COG0666 112 DVNARDKDGEtPLHLAAYNGNLEIVKLLLEAGA-DVNAQDNDGNtPLHLAAANGNLEIVKLLLEAGADVNARDN-DGETP 189

                        90       100
                ....*....|....*....|....*....
gi 30089932 107 LHIAVLRNQPDMVELLVHHGADVNRRDRE 135
Cdd:COG0666 190 LHLAAENGHLEIVKLLLEAGADVNAKDND 218
Ank_2 pfam12796
Ankyrin repeats (3 copies);
42-133 1.14e-10

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 55.89  E-value: 1.14e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089932    42 VASEESRILVLTELLERKAHSPFYQEGVSNALLKMAELGLTRAADVLLRHgANLNFEDpvTYYTALHIAVLRNQPDMVEL 121
Cdd:pfam12796   3 LAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD--NGRTALHYAARSGHLEIVKL 79

                          90
                  ....*....|..
gi 30089932   122 LVHHGADVNRRD 133
Cdd:pfam12796  80 LLEKGADINVKD 91
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
43-135 1.63e-07

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 50.34  E-value: 1.63e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089932  43 ASEESRILVLTELLERKAHSPFYQEGVSNALLKMAELGLTRAADVLLRHGANLNFEDPVTYYTALHIAVLRNQPDMVELL 122
Cdd:COG0666  27 AAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLL 106

                        90
                ....*....|...
gi 30089932 123 VHHGADVNRRDRE 135
Cdd:COG0666 107 LEAGADVNARDKD 119
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 104-134 1.63e-07

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: 45.74  E-value: 1.63e-07
                          10        20        30
                  ....*....|....*....|....*....|..
gi 30089932   104 YTALHIAVLR-NQPDMVELLVHHGADVNRRDR 134
Cdd:pfam00023   3 NTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
41-146 2.06e-07

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 49.95  E-value: 2.06e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089932  41 YVASEESRILVLTELLERKAHSPFYQEGVSNALLKMAELGLTRAADVLLRHGANLNFEDPvTYYTALHIAVLRNQPDMVE 120
Cdd:COG0666 158 HLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDN-DGKTALDLAAENGNLEIVK 236

                        90       100
                ....*....|....*....|....*.
gi 30089932 121 LLVHHGADVNRRDREKLLCSMLWPAA 146
Cdd:COG0666 237 LLLEAGADLNAKDKDGLTALLLAAAA 262
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 104-130 2.26e-06

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: 42.57  E-value: 2.26e-06
                           10        20
                   ....*....|....*....|....*..
gi 30089932    104 YTALHIAVLRNQPDMVELLVHHGADVN 130
Cdd:smart00248   3 RTPLHLAAENGNLEVVKLLLDKGADIN 29
PHA03095 PHA03095
ankyrin-like protein; Provisional
 86-133 4.25e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 46.17  E-value: 4.25e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 30089932   86 DVLLRHGANLNFEDPVTYyTALHIAvLRNQ---PDMVELLVHHGADVNRRD 133
Cdd:PHA03095 101 KLLIKAGADVNAKDKVGR-TPLHVY-LSGFninPKVIRLLLRKGADVNALD 149
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 103-130 5.78e-06

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.


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 41.47  E-value: 5.78e-06
                          10        20
                  ....*....|....*....|....*...
gi 30089932   103 YYTALHIAVLRNQPDMVELLVHHGADVN 130
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENGADIN 29
Ank_5 pfam13857
Ankyrin repeats (many copies);
88-135 3.15e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 40.02  E-value: 3.15e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 30089932    88 LLRHGANLNFEDPVTYYTALHIAVLRNQPDMVELLVHHGADVNRRDRE 135
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEE 48
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
 102-132 3.50e-05

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: 43.64  E-value: 3.50e-05
                        10        20        30
                ....*....|....*....|....*....|....
gi 30089932 102 TYY---TALHIAVLRNQPDMVELLVHHGADVNRR 132
Cdd:cd22196  90 SYYkgqTALHIAIERRNMHLVELLVQNGADVHAR 123
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 74-133 5.32e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 42.73  E-value: 5.32e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30089932   74 LKMAELGLTRAADV--------LLRHGANLNFEDpVTYYTALHIAVLRNQPDMVELLVHHGADVNRRD 133
Cdd:PHA03100 156 LKILKLLIDKGVDInaknrvnyLLSYGVPINIKD-VYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVN 222
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 39-130 8.39e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 42.34  E-value: 8.39e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089932   39 PSYVASEESRILVLTELLERKAH-----SPFYQEGVSNALLKMAELGLTRAADVLLRHGANLNFEDPVTYyTALHIAVLR 113
Cdd:PHA03100  38 PLYLAKEARNIDVVKILLDNGADinsstKNNSTPLHYLSNIKYNLTDVKEIVKLLLEYGANVNAPDNNGI-TPLLYAISK 116

                         90
                 ....*....|....*....
gi 30089932  114 --NQPDMVELLVHHGADVN 130
Cdd:PHA03100 117 ksNSYSIVEYLLDNGANVN 135
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 87-137 1.32e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 41.79  E-value: 1.32e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 30089932   87 VLLRHGANLNFEDPVTYYTALHIAVlrNQPDMVELLVHHGADVNRRDREKL 137
Cdd:PHA02878 253 LLLEHGVDVNAKSYILGLTALHSSI--KSERKLKLLLEYGADINSLNSYKL 301
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 88-138 1.42e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 41.57  E-value: 1.42e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 30089932   88 LLRHGANLNfedPVTYY--TALHIAVLRNQPD--MVELLVHHGADVNRRDREKLL 138
Cdd:PHA03100 127 LLDNGANVN---IKNSDgeNLLHLYLESNKIDlkILKLLIDKGVDINAKNRVNYL 178
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 7-130 2.32e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 40.74  E-value: 2.32e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089932    7 FRRIIFEYQPLVDAILgSLGIqDPERQESLDRPSYVaseesrilvltellerkahspfyqegvsNALLKMAELGLTRAAD 86
Cdd:PHA02884  38 YSSIKFHYTDIIDAIL-KLGA-DPEAPFPLSENSKT----------------------------NPLIYAIDCDNDDAAK 87

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 30089932   87 VLLRHGANLNFEDPVTYYTALHIAVLRNQPDMVELLVHHGADVN 130
Cdd:PHA02884  88 LLIRYGADVNRYAEEAKITPLYISVLHGCLKCLEILLSYGADIN 131
Ank_4 pfam13637
Ankyrin repeats (many copies);
103-158 3.55e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 37.25  E-value: 3.55e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 30089932   103 YYTALHIAVLRNQPDMVELLVHHGADVNRRDREKllCSMLWPAATGCRSTILRTFV 158
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNG--ETALHFAASNGNVEVLKLLL 54
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 88-160 4.88e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 40.03  E-value: 4.88e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089932   88 LLRHGANLNFEDpVTYYTALHI-----AVLRNQPDMVELLVHHGADVNRRDREKllCSMLWPAATGCR--STILRTFVSY 160
Cdd:PHA03100  54 LLDNGADINSST-KNNSTPLHYlsnikYNLTDVKEIVKLLLEYGANVNAPDNNG--ITPLLYAISKKSnsYSIVEYLLDN 130
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 68-130 7.52e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 39.59  E-value: 7.52e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30089932   68 GVSNALLKMAElGLTRAADVLLRHGANLNFEDPVTYYTALHIAVLRNQPDMVELLVHHGADVN 130
Cdd:PHA02875 168 GCTPLIIAMAK-GDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNKIDIVRLFIKRGADCN 229
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 89-134 1.07e-03

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: 39.01  E-value: 1.07e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 30089932  89 LRHGANLNFEDpvTYY---TALHIAVLRNQPDMVELLVHHGADVNRRDR 134
Cdd:cd22193  61 LKRFINAEYTD--EYYegqTALHIAIERRQGDIVALLVENGADVHAHAK 107
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 83-130 1.38e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 38.89  E-value: 1.38e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 30089932   83 RAADVLLRHGANLNFEDpVTYYTALHIAVLRNQPDMVELLVHHGADVN 130
Cdd:PHA02876 159 LIAEMLLEGGADVNAKD-IYCITPIHYAAERGNAKMVNLLLSYGADVN 205
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 37-129 1.41e-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: 38.84  E-value: 1.41e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089932  37 DRPSYVASEESRILVLTELLERKAHSPFYQEGVSNALLKMAEL-GLTRAADVLLRHGANLNFEdPVT--YY---TALHIA 110
Cdd:cd22192  18 ESPLLLAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALyDNLEAAVVLMEAAPELVNE-PMTsdLYqgeTALHIA 96

                        90
                ....*....|....*....
gi 30089932 111 VLRNQPDMVELLVHHGADV 129
Cdd:cd22192  97 VVNQNLNLVRELIARGADV 115
PHA03095 PHA03095
ankyrin-like protein; Provisional
 82-134 1.42e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 38.85  E-value: 1.42e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 30089932   82 TRAADVLLRHGANLNfeDPVTY-YTALHIAVL-RNQPDMVELLVHHGADVNRRDR 134
Cdd:PHA03095  63 KDIVRLLLEAGADVN--APERCgFTPLHLYLYnATTLDVIKLLIKAGADVNAKDK 115
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 105-130 1.72e-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: 38.59  E-value: 1.72e-03
                        10        20
                ....*....|....*....|....*.
gi 30089932 105 TALHIAVLRNQPDMVELLVHHGADVN 130
Cdd:cd22194 143 TALNIAIERRQGDIVKLLIAKGADVN 168
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 14-132 2.09e-03

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: 38.14  E-value: 2.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089932    14 YQPLVDAILGSLGIQDPERQESLdrpsYVASEESRILVLTELLERKAHSPFyqegVSNALLKMAELGLTRAADVLLRH-- 91
Cdd:TIGR00870  34 YRDLEEPKKLNINCPDRLGRSAL----FVAAIENENLELTELLLNLSCRGA----VGDTLLHAISLEYVDAVEAILLHll 105

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 30089932    92 -----GANLNF---EDPVTYY---TALHIAVLRNQPDMVELLVHHGADVNRR 132
Cdd:TIGR00870 106 aafrkSGPLELandQYTSEFTpgiTALHLAAHRQNYEIVKLLLERGASVPAR 157
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 87-134 2.61e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 37.94  E-value: 2.61e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 30089932   87 VLLRHGANLNFEDPVTYYTALHIAVLRNQPDMVELLVHHGADVNRRDR 134
Cdd:PHA02878 152 LLLSYGADINMKDRHKGNTALHYATENKDQRLTELLLSYGANVNIPDK 199
TRPV4 cd22195
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 4; TRPV4 is expressed ...
 89-138 3.65e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 4; TRPV4 is expressed broadly in neuronal and non-neuronal cells. It is activated by various stimuli, including hypo-osmolarity, warm temperature, and chemical ligands. TRPV4 acts in physiological functions such as osmoregulation and thermoregulation. It also has a role in mechanosensation in the vascular endothelium and urinary tract, and in cell barrier formation in vascular and epidermal tissues. Knockout mice studies suggested the functional importance of TRPV4 in the central nervous system, nociception, and bone formation. TRPV4 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: 411979 [Multi-domain]  Cd Length: 733  Bit Score: 37.52  E-value: 3.65e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 30089932  89 LRHGANLNFEDpvTYY---TALHIAVLRNQPDMVELLVHHGADVNRRDREKLL 138
Cdd:cd22195 122 LREFINSPFRD--VYYrgqTALHIAIERRCKHYVELLVEKGADVHAQARGRFF 172
Ank_2 pfam12796
Ankyrin repeats (3 copies);
107-137 4.16e-03

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 35.09  E-value: 4.16e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 30089932   107 LHIAVLRNQPDMVELLVHHGADVNRRDREKL 137
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGR 31
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 32-135 6.09e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 36.80  E-value: 6.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089932   32 RQESLDRPSYVASEESRI---LVLTELLERKAHSPFY----QEGVSNALLKM--------AELGLTRAADVLLRHGANLN 96
Cdd:PTZ00322  30 KPISFERMAAIQEEIARIdthLEALEATENKDATPDHnlttEEVIDPVVAHMltvelcqlAASGDAVGARILLTGGADPN 109

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 30089932   97 FEDpvtYY--TALHIAVLRNQPDMVELLVHHGADVNRRDRE 135
Cdd:PTZ00322 110 CRD---YDgrTPLHIACANGHVQVVRVLLEFGADPTLLDKD 147
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 75-187 6.66e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 36.77  E-value: 6.66e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089932   75 KMAELGLTRAadvLLRHGANLNFEDPvTYYTALHIAVLRNQPDMVELLVHHGADVNRRDREKLLCS-----MLWPAATGC 149
Cdd:PLN03192 631 KRNDLTAMKE---LLKQGLNVDSEDH-QGATALQVAMAEDHVDMVRLLIMNGADVDKANTDDDFSPtelreLLQKRELGH 706

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 30089932  150 RSTILRTFVSYWKEGQTSRPPPKMGTQCSPASSSCLVR 187
Cdd:PLN03192 707 SITIVDSVPADEPDLGRDGGSRPGRLQGTSSDNQCRPR 744
 
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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