PCDGC_PANTR
ID PCDGC_PANTR Reviewed; 932 AA.
AC Q5DRB9;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Protocadherin gamma-A12;
DE Short=PCDH-gamma-A12;
DE Flags: Precursor;
GN Name=PCDHGA12;
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; Q5DRB9; -.
DR SMR; Q5DRB9; -.
DR Ensembl; ENSPTRT00000032096; ENSPTRP00000029650; ENSPTRG00000017346.
DR GeneTree; ENSGT00940000162232; -.
DR InParanoid; Q5DRB9; -.
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; 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..932
FT /note="Protocadherin gamma-A12"
FT /id="PRO_0000003971"
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..932
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..347
FT /note="Cadherin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 348..452
FT /note="Cadherin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 453..562
FT /note="Cadherin 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 570..683
FT /note="Cadherin 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT REGION 803..841
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 902..932
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 813..841
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 419
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 545
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 932 AA; 100906 MW; 7851E8A79E3AF2B6 CRC64;
MIPARLHRDY KGLVLLGILL GTLWETGCTQ IRYSVPEELE KGSRVGDISR DLGLEPRELA
ERGVRIIPRG RTQLFALNPR SGSLVTAGRI DREELCMGAI KCQLNLDILM EDKVKIYGVE
VEVRDINDNA PYFRESELEI KISENAATEM RFPLPHAWDP DIGKNSLQSY ELSPNTHFSL
IVQNGADGSK YPELVLKRAL DREEKAAHHL VLTASDGGDP VRTGTARIRV MVLDANDNAP
AFAQPEYRAS VPENLALGTQ LLVVNATDPD EGVNAEVRYS FRSVDDKAAQ VFKLDCNSGT
ISTIGELDHE ESGFYQMEVQ AMDNAGYSAR AKVLITVLDV NDNAPEVVLT SLASSVPENS
PRGTLIALLN VNDQDSEENG QVICFIQGNL PFKLEKSYGN YYSLVTDIVL DREQVPSYNI
TVTATDRGTP PLSTETHISL NVADTNDNPP VFPQASYSAY IPENNPRGVS LVSVTAHDPD
CEENAQITYS LAENTIQGAS LSSYVSINSD TGVLYALSSF DYEQFRDLQV KVMARDNGHP
PLSSNVSLSL FVLDQNDNAP EILYPALPTD GSTSVELAPR SAEPGYLVTK VVAVDRDSGQ
NAWLSYRLLK ASEPGLFSVG LHTGEVRTAR ALLDRDALKQ SLVVAVQDHG QPPLSATVTL
TVAVANSIPQ VLADLGSLES PANSETSDLT LYLVVAVAAV SCVFLAFVIL LLALRLRRWH
KSRLLQASGG GLTGAPASHF VGVDGVQAFL QTYSHEVSLT TDSRRSHLIF PQPNYADMLV
SQESFEKSEP LLLSGDSVFS KDGHGLIEQA PPNTDWRFSQ AQRPGTSGSQ NGDDTGTWPN
NQFDTEMLQA MILASASEAA DGSSTLGGGA GTMGLSARYG PQFTLQHVPD YRQNVYIPGS
NATLTNAAGK RDGKAPAGGN GNKKKSGKKE KK
