ID   PCDGH_PANTR             Reviewed;         923 AA.
AC   Q5DRA7;
DT   12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   29-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Protocadherin gamma-B5;
DE            Short=PCDH-gamma-B5;
DE   Flags: Precursor;
GN   Name=PCDHGB5;
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_001076034.1; NM_001082565.1.
DR   AlphaFoldDB; Q5DRA7; -.
DR   SMR; Q5DRA7; -.
DR   GeneID; 100034688; -.
DR   KEGG; ptr:100034688; -.
DR   CTD; 56101; -.
DR   InParanoid; Q5DRA7; -.
DR   OrthoDB; 305110at2759; -.
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..30
FT                   /evidence="ECO:0000255"
FT   CHAIN           31..923
FT                   /note="Protocadherin gamma-B5"
FT                   /id="PRO_0000003980"
FT   TOPO_DOM        31..687
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        688..708
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        709..923
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..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          794..832
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          893..923
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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   923 AA;  100047 MW;  90298C5351CC7AAD CRC64;
     MGRGTGELGR AERLPVLFLF LLSLFCPALC EQIRYRIPEE MPKGSVVGNL ATDLGFSVQE
     LPTRKLRVSS EKPYFTVSAE SGELLVSSRL DREEICGKKP ACALEFEAVA ENPLNFYHVN
     VEIEDINDHT PKFTQNSFEL QISESAQPGT RFILEVAEDA DIGLNSLQKY KLSLNPSFSL
     IIKEKQDGSK YPELALEKTL DREQQSYHRL VLTALDGGNP PLSGTTELRI QVTDANDNPP
     VFNRDVYRVS LRENVPPGTT VLQVSATDQD EGINSEITYS FYRTGQIFSL NSKSGEITTQ
     KKLDFEETKE YSMVVEGRDG GGLVAQCTVE INIQDENDNS PEVTFHSLLE MILENAVPGT
     LIALIKIHDQ DSGENGEVNC QLQGEVPFKI ISSSKNSYKL VTDGTLDREQ TPEYNVTITA
     TDRGKPPLSS SISVILHIRD VNDNAPVFHQ ASYLVSVPEN NPPGASIAQV CASDLDLGLN
     GQVSYSIMAS DLEPLALASY VSMSAQSGVV FAQRAFDYEQ LRTFELTLQA RDQGSPALSA
     NVSLRVLVGD RNDNAPRVLY PALGPDGSAL FDMVPRAAEP GYLVTKVVAV DADSGHNAWL
     SYHVLHASEP GLFSLGLRTG EVRTARALGD RDAARQRLLV AVRDGGQPPL SATATLHLVF
     ADSLQEVLPD ITDRPVPSDP QAELQFYLVV ALALISVLFL LAVILAIALR LRRSSSPAAW
     SCFQPGLCVK SGPVVPPNYS EGTLPYSYNL CVAHTGKTEF NFLKCSEQLS SEQDILCGDS
     SGALFPLCNS SESTSHPELQ APPNTDWRFS QAQRPGTSGS QNGDDTGTWP NNQFDTEMLQ
     AMILASASEA ADGSSTLGGG AGTMGLSARY GPQFTLQHVP DYRQNVYIPG SNATLTNAAG
     KRDGKAPAGG NGNKKKSGKK EKK