ID PCDGE_PANTR Reviewed; 931 AA.
AC Q5DRA9;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2005, sequence version 1.
DT 03-MAY-2023, entry version 81.
DE RecName: Full=Protocadherin gamma-B2;
DE Short=PCDH-gamma-B2;
DE Flags: Precursor;
GN Name=PCDHGB2;
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; Q5DRA9; -.
DR SMR; Q5DRA9; -.
DR GlyCosmos; Q5DRA9; 2 sites, No reported glycans.
DR InParanoid; Q5DRA9; -.
DR Proteomes; UP000002277; Unplaced.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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 CDD; cd11304; Cadherin_repeat; 6.
DR Gene3D; 2.60.40.60; Cadherins; 6.
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 PANTHER; PTHR24028; CADHERIN-87A; 1.
DR PANTHER; PTHR24028:SF144; PROTOCADHERIN GAMMA-B2; 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; Cadherin-like; 6.
DR PROSITE; PS00232; CADHERIN_1; 4.
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..30
FT /evidence="ECO:0000255"
FT CHAIN 31..931
FT /note="Protocadherin gamma-B2"
FT /id="PRO_0000003975"
FT TOPO_DOM 31..691
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 692..712
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 713..931
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 31..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..675
FT /note="Cadherin 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT REGION 814..840
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 901..931
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 931 AA; 100910 MW; 8138B9D3F127CD36 CRC64;
MKASSGRCGL VRWLQVLLPF LLSLFPGALP VQIRYSIPEE LAKNSVVGNL AKDLGLSVRD
LPARKLRVSA EKEYFTVNPE SGDLLVSDRI DREQICGKQP LCVLDFDTVA ENPLNIFYIA
VIVQDINDNT PLFKQTKINL KIGESTKPGT TFPLDPALDS DVGPNSLQRY HLNDNEYFDL
AEKQTPDGRK YPELILQHSL DREEHSLHQL VLTAVDGGDP PQSGTTQIRV KVTDANDNPP
VFSQDVYRVT LREDVPPGFF VLQVTATDRD EGVNAEITYS FHNVDEQVKH FFNLNEKTGE
ITTKDDLDFE IASSYTLSIE AKDPGDLAAH CSIQVEILDD NDCAPEVIVT SVFTPLPEDS
PPGTVIALIK TRDRDSGENG EVYCQVLGNA KFILKSSSKN YYKLVTDGAL DREEIPEYNL
TITATDGGKP PLSSSIIVTL HISDVNDNAP VFQQTSYMVH VAENNPPGAS IAQISASDPD
LGPNGQVSYS IVASDLKPRE ILSYVSVSAQ SGVVFAQRAF DHEQLRAFEL TLQARDQGSP
ALSANVSLRV LVGDLNDNAP RVLYPALGSD GSALFDMVPR AAEPGYLVTK VVAVDADSGH
NAWLSYHVLQ ASEPGLFSLG LRTGEVRTAR ALGDRDAARQ RLLVAVRDGG QPPLSATATL
HLIFADSLQE VLPDLSDRPE PSDPQAELQF YLVVALALIS VLFFLAVILA ISLRLRRSSR
SDAWDCFQPG LSSKPGPGVL PSYSEGTLPY SYNLCVASQS AKTEFNFLNI TPELIPAQDL
LCDNASWEQN TNHGAAGVPF ASDTILKQAP PNTDWRFSQA QRPGTSGSQN GDDTGTWPNN
QFDTEMLQAM ILASASEAAD GSSTLGGGAG TMGLSARYGP QFTLQHVPDY RQNVYIPGSN
ATLTNAAGKR DGKAPAGGNG NKKKSGKKEK K
//
