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Conserved domains on  [gi|20072318|gb|AAH26491|]
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Aplp2 protein, partial [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
JMTM_APLP2 cd21709
juxtamembrane and transmembrane (JMTM) domain found in amyloid-like protein 2 (APLP-2) and ...
125-205 6.32e-54

juxtamembrane and transmembrane (JMTM) domain found in amyloid-like protein 2 (APLP-2) and similar proteins; Amyloid-like protein 2 (APLP-2), also called amyloid protein homolog (APPH), or CDEI box-binding protein (CDEBP), may play a role in the regulation of hemostasis. Its soluble form may have inhibitory properties towards coagulation factors. APLP-2 may bind to the DNA 5'-GTCACATG-3'(CDEI box). It inhibits trypsin, chymotrypsin, plasmin, factor XIA, and plasma and glandular kallikrein. This model corresponds to juxtamembrane and transmembrane (JMTM) domain of APLP-2, which consists of the intact transmembrane (TM) domain with adjacent N-terminal juxtamembrane (JM) region.


:

Pssm-ID: 411992  Cd Length: 81  Bit Score: 167.03  E-value: 6.32e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20072318 125 SVGPLREDFSLSSNALIGLLVIAVAIATVIVISLVMLRKRQYGTISHGIVEVDPMLTPEERHLNKMQNHGYENPTYKYLE 204
Cdd:cd21709   1 SDGPLRDDFSFSSSALIGLLVIAVAIATVIVISLVLLRKRQYGTISHGIVEVDPMLTPEERHLNKMQNHGYENPTYKYLE 80

                .
gi 20072318 205 Q 205
Cdd:cd21709  81 Q 81
 
Name Accession Description Interval E-value
JMTM_APLP2 cd21709
juxtamembrane and transmembrane (JMTM) domain found in amyloid-like protein 2 (APLP-2) and ...
125-205 6.32e-54

juxtamembrane and transmembrane (JMTM) domain found in amyloid-like protein 2 (APLP-2) and similar proteins; Amyloid-like protein 2 (APLP-2), also called amyloid protein homolog (APPH), or CDEI box-binding protein (CDEBP), may play a role in the regulation of hemostasis. Its soluble form may have inhibitory properties towards coagulation factors. APLP-2 may bind to the DNA 5'-GTCACATG-3'(CDEI box). It inhibits trypsin, chymotrypsin, plasmin, factor XIA, and plasma and glandular kallikrein. This model corresponds to juxtamembrane and transmembrane (JMTM) domain of APLP-2, which consists of the intact transmembrane (TM) domain with adjacent N-terminal juxtamembrane (JM) region.


Pssm-ID: 411992  Cd Length: 81  Bit Score: 167.03  E-value: 6.32e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20072318 125 SVGPLREDFSLSSNALIGLLVIAVAIATVIVISLVMLRKRQYGTISHGIVEVDPMLTPEERHLNKMQNHGYENPTYKYLE 204
Cdd:cd21709   1 SDGPLRDDFSFSSSALIGLLVIAVAIATVIVISLVLLRKRQYGTISHGIVEVDPMLTPEERHLNKMQNHGYENPTYKYLE 80

                .
gi 20072318 205 Q 205
Cdd:cd21709  81 Q 81
APP_amyloid pfam10515
Beta-amyloid precursor protein C-terminus; This is the amyloid, C-terminal, protein of the ...
154-204 9.12e-27

Beta-amyloid precursor protein C-terminus; This is the amyloid, C-terminal, protein of the beta-Amyloid precursor protein (APP) which is a conserved and ubiquitous transmembrane glycoprotein strongly implicated in the pathogenesis of Alzheimer's disease but whose normal biological function is unknown. The C-terminal 100 residues are released and aggregate into amyloid deposits which are strongly implicated in the pathology of Alzheimer's disease plaque-formation. The domain is associated with family A4_EXTRA, pfam02177, further towards the N-terminus.


Pssm-ID: 463129  Cd Length: 52  Bit Score: 96.63  E-value: 9.12e-27
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 20072318   154 IVISLVMLRKR-QYGTISHGIVEVDPMLTPEERHLNKMQNHGYENPTYKYLE 204
Cdd:pfam10515   1 IVVGMALLRRRaARSPSAHGFVEVDPNVTPEERHVANMQVNGYENPTYKYFE 52
 
Name Accession Description Interval E-value
JMTM_APLP2 cd21709
juxtamembrane and transmembrane (JMTM) domain found in amyloid-like protein 2 (APLP-2) and ...
125-205 6.32e-54

juxtamembrane and transmembrane (JMTM) domain found in amyloid-like protein 2 (APLP-2) and similar proteins; Amyloid-like protein 2 (APLP-2), also called amyloid protein homolog (APPH), or CDEI box-binding protein (CDEBP), may play a role in the regulation of hemostasis. Its soluble form may have inhibitory properties towards coagulation factors. APLP-2 may bind to the DNA 5'-GTCACATG-3'(CDEI box). It inhibits trypsin, chymotrypsin, plasmin, factor XIA, and plasma and glandular kallikrein. This model corresponds to juxtamembrane and transmembrane (JMTM) domain of APLP-2, which consists of the intact transmembrane (TM) domain with adjacent N-terminal juxtamembrane (JM) region.


Pssm-ID: 411992  Cd Length: 81  Bit Score: 167.03  E-value: 6.32e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20072318 125 SVGPLREDFSLSSNALIGLLVIAVAIATVIVISLVMLRKRQYGTISHGIVEVDPMLTPEERHLNKMQNHGYENPTYKYLE 204
Cdd:cd21709   1 SDGPLRDDFSFSSSALIGLLVIAVAIATVIVISLVLLRKRQYGTISHGIVEVDPMLTPEERHLNKMQNHGYENPTYKYLE 80

                .
gi 20072318 205 Q 205
Cdd:cd21709  81 Q 81
JMTM_APLP1 cd21708
juxtamembrane and transmembrane (JMTM) domain found in amyloid-like protein 1 (APLP-1) and ...
134-205 2.41e-36

juxtamembrane and transmembrane (JMTM) domain found in amyloid-like protein 1 (APLP-1) and similar proteins; Amyloid-like protein 1 (APLP-1), also called APLP, may play a role in postsynaptic function. It couples to JIP signal transduction through C-terminal binding. APLP-1 may interact with cellular G-protein signaling pathways. It can regulate neurite outgrowth through binding to components of the extracellular matrix such as heparin and collagen I. This model corresponds to the juxtamembrane and transmembrane (JMTM) domain of APLP-1, which consists of the intact transmembrane (TM) domain with adjacent N-terminal juxtamembrane (JM) region.


Pssm-ID: 411991  Cd Length: 85  Bit Score: 122.24  E-value: 2.41e-36
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 20072318 134 SLSSNALIGLLVIAVAIATVIVISLVMLRKRQYGTISHGIVEVDPMLTPEERHLNKMQNHGYENPTYKYLEQ 205
Cdd:cd21708  14 TFNRGALIGLLVVAVAVAMVIVISLLLVRRKPYGTISHGIVEVDPMLTPEERQLSKMQNHGYENPTYRFLEE 85
APP_amyloid pfam10515
Beta-amyloid precursor protein C-terminus; This is the amyloid, C-terminal, protein of the ...
154-204 9.12e-27

Beta-amyloid precursor protein C-terminus; This is the amyloid, C-terminal, protein of the beta-Amyloid precursor protein (APP) which is a conserved and ubiquitous transmembrane glycoprotein strongly implicated in the pathogenesis of Alzheimer's disease but whose normal biological function is unknown. The C-terminal 100 residues are released and aggregate into amyloid deposits which are strongly implicated in the pathology of Alzheimer's disease plaque-formation. The domain is associated with family A4_EXTRA, pfam02177, further towards the N-terminus.


Pssm-ID: 463129  Cd Length: 52  Bit Score: 96.63  E-value: 9.12e-27
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 20072318   154 IVISLVMLRKR-QYGTISHGIVEVDPMLTPEERHLNKMQNHGYENPTYKYLE 204
Cdd:pfam10515   1 IVVGMALLRRRaARSPSAHGFVEVDPNVTPEERHVANMQVNGYENPTYKYFE 52
JMTM_APP_like cd21699
juxtamembrane and transmembrane (JMTM) domain found in the amyloid-beta precursor protein (APP) ...
125-164 1.94e-09

juxtamembrane and transmembrane (JMTM) domain found in the amyloid-beta precursor protein (APP) family; The amyloid-beta precursor protein (APP) family includes amyloid-like proteins APLP-1 and APLP-2. APP (also called ABPP, APPI, Alzheimer disease (AD) amyloid protein, amyloid precursor protein, amyloid-beta A4 protein, cerebral vascular amyloid peptide (CVAP), PreA4, or protease nexin-II (PN-II)) functions as a cell surface receptor and performs physiological functions on the surface of neurons relevant to neurite growth, neuronal adhesion and axonogenesis. Amyloid-beta peptides are lipophilic metal chelators with metal-reducing activity; they bind transient metals such as copper, zinc and iron. APLP-1, also called APLP, may play a role in postsynaptic function. It couples to JIP signal transduction through C-terminal binding. APLP-1 may interact with cellular G-protein signaling pathways. It can regulate neurite outgrowth through binding to components of the extracellular matrix such as heparin and collagen I. APLP-2 (also called amyloid protein homolog (APPH), or CDEI box-binding protein (CDEBP)) may play a role in the regulation of hemostasis. Its soluble form may have inhibitory properties towards coagulation factors. APLP-2 may bind to the DNA 5'-GTCACATG-3'(CDEI box). It inhibits trypsin, chymotrypsin, plasmin, factor XIA, and plasma and glandular kallikrein. This model corresponds to juxtamembrane and transmembrane (JMTM) domain of APP, which consists of the intact transmembrane (TM) domain with adjacent N-terminal juxtamembrane (JM) region. More than half of all familial APP mutations of Alzheimer's disease are seen in its JMTM domain region.


Pssm-ID: 411982  Cd Length: 41  Bit Score: 51.51  E-value: 1.94e-09
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 20072318 125 SVGPLREDFS-LSSNALIGLLVIAVAIATVIVISLVMLRKR 164
Cdd:cd21699   1 ERVFLAEDSSnSSFGAVIGLAVGGVAVAIVIVVAVVMLRRR 41
JMTM_APP cd21707
juxtamembrane and transmembrane (JMTM) domain found in amyloid-beta precursor protein (APP) ...
131-164 4.04e-04

juxtamembrane and transmembrane (JMTM) domain found in amyloid-beta precursor protein (APP) and similar proteins; Amyloid-beta precursor protein (APP), also called APPI, ABPP, Alzheimer disease amyloid protein, amyloid precursor protein, amyloid-beta A4 protein, cerebral vascular amyloid peptide (CVAP), PreA4, or protease nexin-II (PN-II), functions as a cell surface receptor and performs physiological functions on the surface of neurons relevant to neurite growth, neuronal adhesion and axonogenesis. Amyloid-beta peptides are lipophilic metal chelators with metal-reducing activity; they bind transient metals such as copper, zinc and iron. This model corresponds to juxtamembrane and transmembrane (JMTM) domain of APP, which consists of the intact transmembrane (TM) domain with adjacent N-terminal juxtamembrane (JM) region. More than half of all familial APP mutations of Alzheimer's disease are seen in its JMTM domain region.


Pssm-ID: 411990  Cd Length: 40  Bit Score: 36.85  E-value: 4.04e-04
                        10        20        30
                ....*....|....*....|....*....|....
gi 20072318 131 EDFSLSSNALIGLLVIAVAIATVIVISLVMLRKR 164
Cdd:cd21707   7 EDVGSNKGAIIGLMVGGVVIATVIVITLVMLKKK 40
 
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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