PCDGM_PANTR
ID PCDGM_PANTR Reviewed; 944 AA.
AC Q5DRA2;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Protocadherin gamma-C5;
DE Short=PCDH-gamma-C5;
DE Flags: Precursor;
GN Name=PCDHGC5;
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_001076027.1; NM_001082558.2.
DR AlphaFoldDB; Q5DRA2; -.
DR SMR; Q5DRA2; -.
DR Ensembl; ENSPTRT00000032094; ENSPTRP00000029648; ENSPTRG00000017346.
DR GeneID; 100034697; -.
DR KEGG; ptr:100034697; -.
DR CTD; 56097; -.
DR GeneTree; ENSGT00940000162232; -.
DR HOGENOM; CLU_006480_0_0_1; -.
DR InParanoid; Q5DRA2; -.
DR OrthoDB; 385992at2759; -.
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:0043524; P:negative regulation of neuron apoptotic process; IEA:Ensembl.
DR GO; GO:0007399; P:nervous system development; IEA:UniProt.
DR GO; GO:0050808; P:synapse organization; IEA:Ensembl.
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 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..29
FT /evidence="ECO:0000255"
FT CHAIN 30..944
FT /note="Protocadherin gamma-C5"
FT /id="PRO_0000003990"
FT TOPO_DOM 30..693
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 694..714
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 715..944
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..454
FT /note="Cadherin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 455..564
FT /note="Cadherin 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 571..677
FT /note="Cadherin 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT REGION 722..747
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 812..853
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 914..944
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 814..853
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 443
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 547
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 944 AA; 101849 MW; ADD38EE9FE14EFA8 CRC64;
MGPKTLPQLA GKWQVLCMLS LCCWGWVSGQ LRYSVVEESE PGTLVGNVAQ DLGLKMTDLL
SRRLQLGSEE NGRYFSLSLM SGALAVNQKI DRESLCGAST SCLLPVQVVT EHPLELIRVE
VEILDLNDNS PSFATPEREM RISESAASGA RFPLDSAQDP DVGTNTVSFY TLSPNSHFSL
NVKTLKDGKP FPELVLEQQL DREAQARHQL VLTAVDGGTP ARSGTTLISV IVLDINDNAP
TFQSSVLRVG IPENAPIGTL LLRLNATDPD EGTNGQLDYS FGDHTSEAVR NLFGLDPSSG
AIHVLGPIDF EESRFYEIHA RARDQGQPAM EGHCVIQVEV GDVNDNAPEV LLASLANPVL
ESTPVGTVVG LFNVRDRDSG RNGEVSLDIS PDLPFQIKPS ENHYSLLTSQ PLDREATSHY
IIELLASDAG SPSLHKHLTI RLNISDVNDN APRFNQQLYT AYILENRPPG SLLCTVAASD
PDTGDNARLT YSVVGNQVQG APASSFVYVN PEDGRVFAQR TFDYELLQML QIVVGVRDSG
SPPLHANTSL HVFVLDENDN APAVLHPRPG WEHSAPQRLP RSAPPGSLVT KVTAVDADAG
HNAWLSYSLL PQSTAPGLFL VSTHTGEVRT ARALLEDDSD TQQVVVLVRD NGDPSLSSTA
TVLLVLEDED PEEMPKSSDF LIHPPERSDL TLYLIVALAT VSLLSLVTFT FLSAKCLQGN
ADGDGGGGQC CRRQDSPSPD FYKQSSPNLQ VSSDGTLKYM EVTLRPTDSQ SHCYRTCFSP
ASDGSDFTFL RPLSVQQPTA LALEPDAIRS RSNTLRERSQ QAPPNTDWRF SQAQRPGTSG
SQNGDDTGTW PNNQFDTEML QAMILASASE AADGSSTLGG GAGTMGLSAR YGPQFTLQHV
PDYRQNVYIP GSNATLTNAA GKRDGKAPAG GNGNKKKSGK KEKK
