PCDGB_PANTR
ID PCDGB_PANTR Reviewed; 935 AA.
AC Q5DRC0;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Protocadherin gamma-A11;
DE Short=PCDH-gamma-A11;
DE Flags: Precursor;
GN Name=PCDHGA11;
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_001076028.1; NM_001082559.2.
DR AlphaFoldDB; Q5DRC0; -.
DR SMR; Q5DRC0; -.
DR Ensembl; ENSPTRT00000061822; ENSPTRP00000054365; ENSPTRG00000017346.
DR GeneID; 100034693; -.
DR KEGG; ptr:100034693; -.
DR CTD; 56105; -.
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: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; 4.
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..935
FT /note="Protocadherin gamma-A11"
FT /id="PRO_0000003969"
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..935
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 30..134
FT /note="Cadherin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 135..243
FT /note="Cadherin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 244..348
FT /note="Cadherin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 349..453
FT /note="Cadherin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 454..563
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 805..844
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 905..935
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 48
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 255
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 266
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 420
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 546
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 935 AA; 101526 MW; 6CAB1DCC20E49C08 CRC64;
MANRLQRGDR SRLLLLLCIF LGTLRGFRAR QIRYSVPEET EKGSFVGNIS KDLGLEPREL
AKRGVRIVSR GKTQLFAVNP RSGSLITAGR IDREELCETV SSCFLNMELL VEDTLKIYGV
EVEIIDINDN APSFQEDEVE IKVSEHAIPG ARFALPNARD PDVGVNSLQS YQLSPNNYFS
LQLRGRTDGA KNPELVLEGS LDREKEAAHL LLLTALDGGD PIRKGAVPIR VVVLDVNDHI
PMFTQSVYRV SVPENISSGT RVLMVNATDP DEGINGEVMY SFRNMESKAS EIFQLDSQTG
EVQVRGSLDF EKYRFYEMEI QGQDGGGLFT TTTMLITVVD VNDNAPEITI TSSINSILEN
SPPGTVIALL NVQDQDSGEN GQVSCFIPNH LPFKLEKTYG NYYKLITSRV LDRELVQSYN
ITLTATDQGS PPLSAETHIW LNVADDNDNP PVFPHSSYSA YIPENNPRGA SIFSVTALDP
DSKQNALVTY SLTDDTVQGV PLSSYVSINS NTGVLYALQS FDYEQFRDLQ LRVIARDSGD
PPLSSNVSLS LFVLDQNDNA PEILYPALPT DGSTGVELAP RSAEPGYLVT KVVAVDKDSG
QNAWLSYRLL KASEPGLFAV GEHTGEVRTA RALLDRDALK QSLVVAVQDH GQPPLSATVT
LTVAVADSIP EVLADLGSLE SLANSEASDL SLYLVVAVAA VSCIFLVFVI VLLALRLWRW
HKSRLLQASE GGLAGMPTSH FVGVDGVQAF LQTYSHEVSL IADSQKSHLI FPQPNYGDTL
ISQESCEKSE PLLIAEDSAI ILGKCDPTSN QQAPPNTDWR FSQAQRPGTS GSQNGDDTGT
WPNNQFDTEM LQAMILASAS EAADGSSTLG GGAGTMGLSA RYGPQFTLQH VPDYRQNVYI
PGSNATLTNA AGKRDGKAPA GGNGNKKKSG KKEKK
