PCDGD_PANTR
ID PCDGD_PANTR Reviewed; 927 AA.
AC Q5DRB0;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Protocadherin gamma-B1;
DE Short=PCDH-gamma-B1;
DE Flags: Precursor;
GN Name=PCDHGB1;
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_001076038.1; NM_001082569.1.
DR AlphaFoldDB; Q5DRB0; -.
DR SMR; Q5DRB0; -.
DR GeneID; 100034680; -.
DR KEGG; ptr:100034680; -.
DR CTD; 56104; -.
DR InParanoid; Q5DRB0; -.
DR OrthoDB; 385992at2759; -.
DR Proteomes; UP000002277; Unplaced.
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..28
FT /evidence="ECO:0000255"
FT CHAIN 29..927
FT /note="Protocadherin gamma-B1"
FT /id="PRO_0000003973"
FT TOPO_DOM 29..687
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 688..708
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 709..927
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 29..130
FT /note="Cadherin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 131..239
FT /note="Cadherin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 240..343
FT /note="Cadherin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 344..448
FT /note="Cadherin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 449..558
FT /note="Cadherin 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 566..671
FT /note="Cadherin 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT REGION 797..836
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 897..927
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 801..836
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 41
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 73
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 300
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 415
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 541
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 927 AA; 100460 MW; 6BF1E51C46588C07 CRC64;
MRRAREAEMM KSQVLFPFLL SLFCGAISQQ IRYTIPEELA NGSRVGNLAK DLGLSVRELP
TRKLRVSAED YFNVSLESGD LLVNGRIDRE KICGRKLECA LEFETVTENP MNVFHVVVVI
QDINDNAPRF VAKGIDLEIC ESALPGVKFS LDSAQDADVE GNSLKLYTIN PNQYFSLSTK
ESPDGSKYPE LLLEKPLDRE HQSSHRLILT AMDGGDPPLS GTTHIWIRVT DANDNAPVFS
QEVYRVSLQE NVPWGTSVLR VMATDQDEGI NAEITYAFLN SPISTSLFNL NPNTGDITTN
GTLDFEETSR YVLSVEAKDG GVHTAHCNVQ IEIVDENDNA PEVTFVSFSN QIPEDSDLGT
VIALIKVRDK DSGQNGMVTC YIQEEVPFKL ESTSKNYYKL VIAGALNREQ TADYNVTIIA
TDKGKPALSS RTSITLHISD INDNAPVFHQ ASYVVHVSEN NPPGASIAQV SASDPDLGPN
GRVSYSILAS DLEPRELLSY VSVSPQSGVV FAQRAFDHEQ LRAFELTLQA RDQGSPALSA
NVSLRVLVGD LNDNAPRVLY PALGPDGSAL FDMVPRAAEP GYLVTKVVAV DADSGHNAWL
SYHVLQASEP GLFSLGLRTG EVRTARALGD RDAARQRLLV AVRDGGQPPL SATATLHLIF
ADSLQEVLPD LSDRPEPSDP QTELQFYLVV ALALISVLFL LAVILAIALR LRRSSSLDTE
GCFQTGLCSK SGPGVPPNHS EGTLPYSYNL CVASHSAKTE FNFLNLTPEM APPQDLLCDD
PSMVVCASNE DHKIAYDPSL SSHQAPPNTD WRFSQAQRPG TSGSQNGDDT GTWPNNQFDT
EMLQAMILAS ASEAADGSST LGGGAGTMGL SARYGPQFTL QHVPDYRQNV YIPGSNATLT
NAAGKRDGKA PAGGNGNKKK SGKKEKK
