PCDGK_PANTR
ID PCDGK_PANTR Reviewed; 934 AA.
AC Q5DRA4;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Protocadherin gamma-C3;
DE Short=PCDH-gamma-C3;
DE Flags: Precursor;
GN Name=PCDHGC3;
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 RefSeq; NP_001076040.1; NM_001082571.2.
DR AlphaFoldDB; Q5DRA4; -.
DR SMR; Q5DRA4; -.
DR Ensembl; ENSPTRT00000032093; ENSPTRP00000029647; ENSPTRG00000017346.
DR GeneID; 100034695; -.
DR KEGG; ptr:100034695; -.
DR CTD; 5098; -.
DR GeneTree; ENSGT00940000162232; -.
DR OrthoDB; 213724at2759; -.
DR Proteomes; UP000002277; Chromosome 5.
DR Bgee; ENSPTRG00000017346; Expressed in dorsolateral prefrontal cortex and 21 other tissues.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
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; IPR032455; Cadherin_C.
DR InterPro; IPR031904; Cadherin_CBD.
DR InterPro; IPR020894; Cadherin_CS.
DR InterPro; IPR013164; Cadherin_N.
DR InterPro; IPR030728; PCDHGC3.
DR PANTHER; PTHR24028:SF70; PTHR24028:SF70; 1.
DR Pfam; PF00028; Cadherin; 5.
DR Pfam; PF08266; Cadherin_2; 1.
DR Pfam; PF16492; Cadherin_C_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..31
FT /evidence="ECO:0000255"
FT CHAIN 32..934
FT /note="Protocadherin gamma-C3"
FT /id="PRO_0000003986"
FT TOPO_DOM 32..693
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 694..714
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 715..934
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 32..135
FT /note="Cadherin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 136..244
FT /note="Cadherin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 245..352
FT /note="Cadherin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 353..457
FT /note="Cadherin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 458..567
FT /note="Cadherin 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 572..685
FT /note="Cadherin 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT REGION 804..843
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 904..934
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 809..843
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 245
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 424
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 478
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 550
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 615
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 689
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 934 AA; 101064 MW; 5FC8D07B78106B14 CRC64;
MVPEAWRSGL VSTGRVVGVL LLLGALNKAS TVIHYEIPEE REKGFAVGNV VANLGLDLGS
LSARRFRVVS GASRRFFEVN RETGEMFVND RLDREELCGT LPSCTVTLEL VVENPLELFS
VEVVIQDIND NNPAFPTQEM KLEISEAVAP GTRFPLESAH DPDVGSNSLQ TYELSRNEYF
ALRVQTREDS TKYAELVLER ALDREREPSL QLVLTALDGG TPALSASLPI HIKVLDANDN
APVFNQSLYR ARVLEDAPSG TRVVQVLATD LDEGPNGEII YSFGSHNRAG VRELFALDLV
TGMLTIKGRL DFEDTKLHEI YIQAKDKGAN PEGAHCKVLV EVVDVNDNAP EITVTSVYSP
VPEDAPLGTV IALLSVTDLD AGENGLVTCE VPPGLPFSLT SSLKNYFTLK TSADLDRETV
PEYNLSITAR DAGTPSLSAL TIVRVQVSDI NDNPPQSSQS SYDVYIEENN LPGAPILNLS
VWDPDAPQNA RLSFFLLEQG AETGLVGRYF TINRDNGIVS SLVPLDYEDR REFELTAHIS
DGGTPVLATN ISVNIFVTDR NDNAPQVLYP RPGGSSVEML PRGTSAGHLV SRVVGWDADA
GHNAWLSYSL LGSPNQSLFA IGLHTGQIST ARPVQDTDSP RQTLTVLIKD NGEPSLSTTA
TLTVSVTEDS PEARAEFPSG SAPREQNKNL TFYLLLSLIL VSVGFVVTVF GVIIFKVYKW
KQSRDLYRAP VSSLYRTPGP SLHADAVRGG LMSPHLYHQV YLTTDSRRSD PLLKKPGAAS
PLASRQNTLR SCDPVFYRQV LGAESAPPGQ QAPPNTDWRF SQAQRPGTSG SQNGDDTGTW
PNNQFDTEML QAMILASASE AADGSSTLGG GAGTMGLSAR YGPQFTLQHV PDYRQNVYIP
GSNATLTNAA GKRDGKAPAG GNGNKKKSGK KEKK
