PCDGL_PANTR
ID PCDGL_PANTR Reviewed; 938 AA.
AC Q5DRA3;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Protocadherin gamma-C4;
DE Short=PCDH-gamma-C4;
DE Flags: Precursor;
GN Name=PCDHGC4;
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: Potential calcium-dependent cell-adhesion protein. May be
CC involved in the establishment and maintenance of specific neuronal
CC connections in the brain.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}.
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DR AlphaFoldDB; Q5DRA3; -.
DR SMR; Q5DRA3; -.
DR Ensembl; ENSPTRT00000032092; ENSPTRP00000047948; ENSPTRG00000017346.
DR GeneTree; ENSGT00940000162232; -.
DR InParanoid; Q5DRA3; -.
DR Proteomes; UP000002277; Chromosome 5.
DR Bgee; ENSPTRG00000017346; Expressed in dorsolateral prefrontal cortex and 21 other tissues.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
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; Glycoprotein; Membrane;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..29
FT /evidence="ECO:0000255"
FT CHAIN 30..938
FT /note="Protocadherin gamma-C4"
FT /id="PRO_0000003988"
FT TOPO_DOM 30..692
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 693..713
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 714..938
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
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 572..676
FT /note="Cadherin 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT REGION 791..847
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 908..938
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 819..847
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 265
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 276
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 444
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 938 AA; 101214 MW; 99820B82A2F18ECC CRC64;
MLRKVRSWTE IWRWATLLFL FYHLGYVCGQ IRYPVPEESQ EGTFVGNVAQ DFLLDTDSLS
ARRLQVAGEV NQRHFRVDLD SGALLIKNPI DREALCGLSA SCIVPLEFVT EGPLEMYRAE
VEIVDVNDHA PRFPRQQLDL EIGEAAPPGQ RFPLEKAQDA DVGSNSISSY RLSSNEHFAL
DVKKRSDGSL VPELLLEKPL DREKQSDYRL VLTAVDGGNP PRSGTAELRV SVLDVNDNAP
AFQQSSYRIS VLESAPAGMV LIQLNASDPD LGPSGNVTFY FSGHTPDRVR NLFSLHPTTG
KLTLLGPLDF ESENYYEFDV RARDGGSPAM EQHCSLRVDL LDVNDNAPYI TVTSELGTLP
ESAEPGTVVA LISVQDPDSG SNGDVSLRIP DHLPFALKSA FRNQFSLVTA GPLDREAKSS
YDIMVTASDA GNPPLSTHRT IFLNISDVND NPPSFFQRSH EVFVPENNRP GDLLCSLAAS
DPDSGLNALI SYSLLEPRNR DVSASSFISL NPQTGAVHAT RSFDYEQTQT LQFEVQARDR
GNPPLSSTVT VRLFVLDLND NAPAVLRPRA RPGSLCPQAL PPSVGAGHLI TKVTAVDLDS
GYNAWVSYQL LEAPDPSLFA VSRYAGEVRT AVPIPADLPP QKLVIVVKDS GSPPLSTSVT
LLVSLEEDTH PVVPDLRESS APREGESRLT LYLAVSLVAI CFVSFGSFVA LLSKCLRGAA
CGVTCFPAGT CACLTRSRRR EGLPPSNGIL RIQLGSDDPI KFVDVGGHSH GCTPLASAPT
RSDSFMMVKS PSAPMAGEPV RPSCPPSDLL YGLEQAPPNT DWRFSQAQRP GTSGSQNGDD
TGTWPNNQFD TEMLQAMILA SASEAADGSS TLGGGAGTMG LSARYGPQFT LQHVPDYRQN
VYIPGSNATL TNAAGKRDGK APAGGNGNKK KSGKKEKK
