PCDA4_PANTR
ID PCDA4_PANTR Reviewed; 947 AA.
AC Q5DRE8;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Protocadherin alpha-4 {ECO:0000305};
DE Short=PCDH-alpha-4 {ECO:0000305};
DE Flags: Precursor;
GN Name=PCDHA4 {ECO:0000250|UniProtKB:O88689};
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:O88689}.
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. Interacts with
CC FYN. {ECO:0000250|UniProtKB:O88689}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O88689};
CC Single-pass type I membrane protein {ECO:0000250|UniProtKB:O88689}.
CC Note=Detected in dendrites and synapses.
CC {ECO:0000250|UniProtKB:O88689}.
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:O88689}.
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DR AlphaFoldDB; Q5DRE8; -.
DR SMR; Q5DRE8; -.
DR PRIDE; Q5DRE8; -.
DR InParanoid; Q5DRE8; -.
DR Proteomes; UP000002277; Unplaced.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
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:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro.
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..947
FT /note="Protocadherin alpha-4"
FT /id="PRO_0000003891"
FT TOPO_DOM 30..697
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:O88689"
FT TRANSMEM 698..718
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 719..947
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:O88689"
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 588..678
FT /note="Cadherin 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT REPEAT 734..737
FT /note="PXXP 1"
FT REPEAT 774..777
FT /note="PXXP 2"
FT REPEAT 796..799
FT /note="PXXP 3"
FT REPEAT 829..832
FT /note="PXXP 4"
FT REPEAT 870..873
FT /note="PXXP 5"
FT REPEAT 888..891
FT /note="PXXP 6"
FT REGION 734..891
FT /note="6 X 4 AA repeats of P-X-X-P"
FT REGION 738..947
FT /note="Required for interaction with FYN"
FT /evidence="ECO:0000250|UniProtKB:O88689"
FT REGION 754..805
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 828..853
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 892..947
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 777..791
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 932..947
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 139
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 257
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:O88689"
SQ SEQUENCE 947 AA; 102366 MW; E0F2468542A95397 CRC64;
MEFSWGSGQE SRRLLLLLLL LSAWEAGNGQ LHYSVSEEAK HGTFVGRIAQ DLGLELAELV
PRLFRVASKG RGGLLEVNLQ NGILFVNSRI DREELCRRSA ECSIHLEVIV DRPLQVFHVD
VEVRDINDNP PVFPATQKNL SIAESRPLDS RFPLEGASDA DIGENALLTY RLSPNEYFSL
EKPSDDELVK GLGLILRKSL DREEAPEIFL VLTATDGGKP ELTGTVQLLI TVLDANDNAP
AFDRTIYKVR LLENVPNGTL VIKLNASDLD EGLNGDIIYS FSNDISPNVK SKFHIDPITG
QIIVKGYIDF EESKSYEIIV EGIDKGQLPL SGHCRVIVEV EDNNDNVPDL EFKSLSLPIR
EDAPLGTVIA LISVSDKDMG VNGLVTCSLT SHVPFKLVST FKNYYSLVLD SALDRESVSA
YELVVTARDG GSPSLWATAS VSVEVADVND NAPAFAQPEY TVFVKENNPP GCHIFTVSAW
DADAQENALV SYSLVERRVG ERALSSYVSV HAESGKVYAL QPLDHEELEL LQFQVTARDA
GVPPLGSNVT LQVFVLDEND NAPALLAHRA GGTGGAVSEL VPWSVGVDHV VAKVRAVDAD
SGYNAWLSYE LQPGTGGARI PFRVGLYTGE ISTTRALDET DAPRHRLLVL VKDHGEPALT
ATATVLVSLV ESGQAPKASS RALVGAVGPD AALVDVNVYL IIAICAVSSL LVLTLLLYTA
LRCSAPPTEG ACAPGKPTLV CSSAVGSWSY SQQRRPRVCS GEGPPKTDLM AFSPSLPDSR
DREDELQTTE ESFAKPRQPN PDWRYSASLR AGMHSSVHLE EAGILRAGPG GPDQQWPTVS
SATPEPEAGE VSPPVGAGVN SNSWTFKYGP GNPKQSGPGE LPDKFIIPGS PAIISIRQEP
ANSQIDKSDF ITFGKKEETK KKKKKKKGNK TQEKKEKGNS TTDNSDQ
