ID   PCDGG_PANTR             Reviewed;         923 AA.
AC   Q5DRA8;
DT   12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   29-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=Protocadherin gamma-B4;
DE            Short=PCDH-gamma-B4;
DE   Flags: Precursor;
GN   Name=PCDHGB4;
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   AlphaFoldDB; Q5DRA8; -.
DR   SMR; Q5DRA8; -.
DR   STRING; 9598.ENSPTRP00000058450; -.
DR   PaxDb; Q5DRA8; -.
DR   eggNOG; KOG3594; Eukaryota.
DR   InParanoid; Q5DRA8; -.
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-B4"
FT                   /id="PRO_0000003978"
FT   TOPO_DOM        31..689
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        690..710
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        711..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..345
FT                   /note="Cadherin 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          346..450
FT                   /note="Cadherin 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          451..560
FT                   /note="Cadherin 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          568..673
FT                   /note="Cadherin 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   REGION          797..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        417
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        543
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   923 AA;  99956 MW;  2777339C4ECA6A75 CRC64;
     MGSGAGELGR AERLPVLFLF LLSLFCPALC EQIRYRIPEE MPKGSVVGNL ATDLGFSVQE
     LPTRKLRVSS EKPYFTVSAE SGELLVSSRL DREEICGKKP ACALEFEAVA ENPLNFYHVN
     VEIEDINDHT PKFTQNSFEL QISESAQPGT RFILGSAHDA DIGSNTLQNY QLSPSDHFSL
     INKEKSDGSK YPEMVLKTPL DREKQKSYHL TLTALDFGAP PLSSTAQIHV LVTDANDNAP
     VFSQDIYRVS LSENVYPGTT VLQVTATDQD EGVNAEITFS FSEASQITQF DLNSNTGEIT
     VLNTLDFEEV KEYSIVLEAR DGGGMIAQCT VEVEVIDEND NAPEVIFQSL PNLIMEDAEL
     GTHIALLKVR DKDSRHNGEV TCKLEGDVPF KILTSSRNTY KLVTDAVLDR EQNPEYNITV
     TARDRGKPPL SSSSSITLHI GDVNDNAPVF SQSSYIVHVA ENNPPGASIS QVSASDPDLG
     PNGQVSYCII ASDLEQRELS SYVSISAESG VVFAQRAFDH EQLRAFELTL QARDQGSPAL
     SANVSLRVLV DDRNDNAPRV LYPALGPDGS ALFDMVPRAA EPGYLVTKVV AVDADSGHNA
     WLSYHVLQAS EPGLFSLGLR TGEVRTARAL GDRDAVRQRL LVAVRDGGQP PLSATATLHL
     VFADSLQEVL PDITDRPDPS DLEAELQFYL VVALALISVL FLVAMILAIA LRLRRSSSPA
     SWSCFQPGLC VKSESVVPPN YSEGTLPYSY NLCVAHTGKT EFNFLKCNEQ LSSGQDILCG
     DSSGALFPLC NSSELTSHQQ APPNTDWRFS QAQRPGTSGS QNGDDTGTWP NNQFDTEMLQ
     AMILASASEA ADGSSTLGGG AGTMGLSARY GPQFTLQHVP DYRQNVYIPG SNATLTNAAG
     KRDGKAPAGG NGNKKKSGKK EKK