PCDA7_PANTR
ID PCDA7_PANTR Reviewed; 937 AA.
AC Q5DRE5;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Protocadherin alpha-7 {ECO:0000305};
DE Short=PCDH-alpha-7 {ECO:0000305};
DE Flags: Precursor;
GN Name=PCDHA7 {ECO:0000250|UniProtKB:Q9UN72};
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16136131; DOI=10.1038/nature04072;
RG Chimpanzee sequencing and analysis consortium;
RT "Initial sequence of the chimpanzee genome and comparison with the human
RT genome.";
RL Nature 437:69-87(2005).
RN [2]
RP IDENTIFICATION.
RX PubMed=15744052; DOI=10.1534/genetics.104.037606;
RA Wu Q.;
RT "Comparative genomics and diversifying selection of the clustered
RT vertebrate protocadherin genes.";
RL Genetics 169:2179-2188(2005).
CC -!- FUNCTION: Calcium-dependent cell-adhesion protein involved in cells
CC self-recognition and non-self discrimination. Thereby, it is involved
CC in the establishment and maintenance of specific neuronal connections
CC in the brain. {ECO:0000250|UniProtKB:Q91Y13}.
CC -!- SUBUNIT: Forms homodimers in trans (molecules expressed by two
CC different cells). Forms promiscuous heterodimers in cis (at the plasma
CC membrane of the same cell) with other protocadherins.
CC {ECO:0000250|UniProtKB:Q91Y13}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q91Y13};
CC Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q91Y13}.
CC -!- DOMAIN: Cadherin 1 to cadherin 4 domains mediate homophilic trans-
CC interaction, the interaction with an identical protocadherin expressed
CC by a neighboring cell. This is a head-to-tail interaction, the cadherin
CC 1 domain interacting with the cadherin 4 domain and the cadherin 2
CC domain interacting the cadherin 3 domain of the other protocadherin.
CC The cadherin 6 domain mediates promiscuous interactions with
CC protocadherins on the same cell membrane. Each cadherin domain binds
CC three calcium ions. {ECO:0000250|UniProtKB:Q91Y13}.
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DR AlphaFoldDB; Q5DRE5; -.
DR SMR; Q5DRE5; -.
DR STRING; 9598.ENSPTRP00000056340; -.
DR PaxDb; Q5DRE5; -.
DR eggNOG; KOG3594; Eukaryota.
DR InParanoid; Q5DRE5; -.
DR Proteomes; UP000002277; Unplaced.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR GO; GO:0007155; P:cell adhesion; IBA:GO_Central.
DR GO; GO:0009988; P:cell-cell recognition; ISS:UniProtKB.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; ISS:UniProtKB.
DR GO; GO:0007399; P:nervous system development; IEA:UniProt.
DR InterPro; IPR002126; Cadherin-like_dom.
DR InterPro; IPR015919; Cadherin-like_sf.
DR InterPro; IPR031904; Cadherin_CBD.
DR InterPro; IPR020894; Cadherin_CS.
DR InterPro; IPR013164; Cadherin_N.
DR Pfam; PF00028; Cadherin; 5.
DR Pfam; PF08266; Cadherin_2; 1.
DR Pfam; PF15974; Cadherin_tail; 1.
DR PRINTS; PR00205; CADHERIN.
DR SMART; SM00112; CA; 6.
DR SUPFAM; SSF49313; SSF49313; 6.
DR PROSITE; PS00232; CADHERIN_1; 5.
DR PROSITE; PS50268; CADHERIN_2; 6.
PE 3: Inferred from homology;
KW Calcium; Cell adhesion; Cell membrane; Disulfide bond; Glycoprotein;
KW Membrane; Metal-binding; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..29
FT /evidence="ECO:0000255"
FT CHAIN 30..937
FT /note="Protocadherin alpha-7"
FT /id="PRO_0000003897"
FT TOPO_DOM 30..697
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q91Y13"
FT TRANSMEM 698..718
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 719..937
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q91Y13"
FT DOMAIN 30..133
FT /note="Cadherin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 134..242
FT /note="Cadherin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 243..350
FT /note="Cadherin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 351..455
FT /note="Cadherin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 456..565
FT /note="Cadherin 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 581..678
FT /note="Cadherin 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT REPEAT 774..777
FT /note="PXXP 1"
FT REPEAT 786..789
FT /note="PXXP 2"
FT REPEAT 819..822
FT /note="PXXP 3"
FT REPEAT 860..863
FT /note="PXXP 4"
FT REPEAT 878..881
FT /note="PXXP 5"
FT REGION 756..795
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 774..881
FT /note="5 X 4 AA repeats of P-X-X-P"
FT REGION 817..843
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 888..937
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 774..792
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 922..937
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 254
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 265
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 548
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 96..102
FT /evidence="ECO:0000250|UniProtKB:Q91Y13"
SQ SEQUENCE 937 AA; 101012 MW; C446ACCBF42C0988 CRC64;
MVCPNGYDPG GRHLLLFIII LAAWEAGRGQ LHYSVPEEAK HGNFVGRIAQ DLGLELAELV
PRLFRVVCKF RGDLLEVNLQ NGILFVNSRI DREELCGRSA ECSIHLEVIV ERPLQVFHVD
VEVKDINDNP PVFPATQRNL FIAESRPLDS RFPLEGASDA DIGENALLTY RLSPNEYFFL
DVPTSNQQVK PLGLVLRKLL DREETPELHL LLTATDGGKP ELTGTVQLLI TVLDNNDNAP
VFDRTLYTVK LPENVSIGTL VIHPNASDLD EGLNGDIIYS FSSDVSPDIK SKFHMDPLSG
AITVIGHMDF EESRAHKIPV EAVDKGFPPL AGHCTVLVEV VDVNDNAPQL TLTSLSLPIP
EDAQPGTVIT LISVFDRDFG VNGQVTCSLT PHVPFKLVST FKNYYSLVLD RALDRESVSA
YELVVTARDG GSPSLWATAS VSVEVADVND NAPAFAQPEY TVFVKENNPP GCHIFTVSAG
DADAQKNALV SYSLVERRVG ERALSSYISV HAESGKVYVL QPLDHEELEL LQFQVSARDA
GVPPLGSNVT LQVFVLDEND NAPALLAPRV GGTGGAVREL VPRSVGAGHV VAKVRAVDAD
SGYNAWLSYE LQPVAAGASI PFRVGLYTGE ISTTRALDET DAPRHRLLVL VKDHGEPSLT
ATATVLVSLV ESGQAPKASS RASLGIAGPE TELVDVNVYL IIAICAVSSL LVLTLLLYTA
LRCSAPSSEG ACSLIKPTLV CSSAVGSWSF SQQRRQRVCS GEGPPKTDLM AFSPSLPQGP
SSTDNPRQPN PDWRYSASLR AGMHSSVHLE EAGILRAGPG GPDQQWPTVS SATPEPEAGE
VSPPVGAGVN SNSWTFKYGP GNPKQSGPGE LPDKFIIPGS PAIISIRQEP ANSQIDKSDF
ITFGKKEETK KKKKKKKGNK TQEKKEKGNS TTDNSDQ
