ID   PCDB2_PANTR             Reviewed;         798 AA.
AC   Q5DRD2;
DT   12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   29-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Protocadherin beta-2;
DE            Short=PCDH-beta-2;
DE   Flags: Precursor;
GN   Name=PCDHB2;
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; Q5DRD2; -.
DR   SMR; Q5DRD2; -.
DR   STRING; 9598.ENSPTRP00000047958; -.
DR   PaxDb; Q5DRD2; -.
DR   eggNOG; KOG3594; Eukaryota.
DR   InParanoid; Q5DRD2; -.
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; IPR020894; Cadherin_CS.
DR   InterPro; IPR013164; Cadherin_N.
DR   InterPro; IPR030735; PCDHB2.
DR   PANTHER; PTHR24028:SF281; PTHR24028:SF281; 1.
DR   Pfam; PF00028; Cadherin; 5.
DR   Pfam; PF08266; Cadherin_2; 1.
DR   Pfam; PF16492; Cadherin_C_2; 1.
DR   PRINTS; PR00205; CADHERIN.
DR   SMART; SM00112; CA; 6.
DR   SUPFAM; SSF49313; SSF49313; 5.
DR   PROSITE; PS00232; CADHERIN_1; 5.
DR   PROSITE; PS50268; CADHERIN_2; 6.
PE   3: Inferred from homology;
KW   Acetylation; 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..798
FT                   /note="Protocadherin beta-2"
FT                   /id="PRO_0000003917"
FT   TOPO_DOM        31..692
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        693..713
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        714..798
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          37..135
FT                   /note="Cadherin 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          136..244
FT                   /note="Cadherin 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          249..349
FT                   /note="Cadherin 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          354..453
FT                   /note="Cadherin 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          458..563
FT                   /note="Cadherin 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          570..673
FT                   /note="Cadherin 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   MOD_RES         299
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y5E7"
FT   CARBOHYD        171
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        438
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        569
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   798 AA;  87110 MW;  F4AC842472390CE4 CRC64;
     MEAGEGKEPV PKQRQVLIFF VLLGIAQASC QPRHYSVAEE TESGSFVANL LKDLGLEIGE
     LAVRGARVVS KGKKMHLQFD RQTGDLLLNE KLDREELCGP TEPCVLPFQV LLENPLQFFQ
     AELRIRDIND HSPVFLDKEI LLKIPESITP GTTFLIERAQ DLDVGTNSLQ NYTISPNFHF
     HLNLQDSLDG IILPQLVLNR ALDREEQPEI RLTLTALDGG SPPRSGTALV RIEVVDINDN
     VPEFAKLLYE VQIPEDSPVG SQVAIVSARD LDIGTNGEIS YAFSQASEDI RKTFRLSAKS
     GELLLRQKLD FESIQTYTVN IQATDGGGLS GTCVVFVQVM DLNDNPPELT MSTLINQIPE
     NLQDTLIAVF SVSDPDSGDN GRMVCSIQDD LPFFLKPSVE NFYTLVISTA LDRETRSEYN
     ITITVTDFGT PRLKTEHNIT VLVSDVNDNA PAFTQTSYTL FVRENNSPAL HIGSVSATDR
     DSGTNAQVTY SLLPPQDPHL PLASLVSINA DNGHLFALQS LDYEALQAFE FRVGAADRGS
     PALSSEALVR VLVLDANDNS PFVLYPLQNG SAPCTELVPR AAEPGYLVTK VVAVDGDSGQ
     NAWLSYQLLK ATEPGLFGVW AHNGEVRTAR LLSERDAAKH RLVVLVKDNG EPPRSATATL
     HVLLVDGFSQ PYLPLPEAAP AQAQADLLTV YLVVALASVS SLFLFSVLLF VAVRLCRRSR
     AASVGRCSVP EGPFPGHLVD VSGTGTLSQS YQYEVCLTGG SGTNEFKFLK PIIPNFVAQG
     AERVSEANPS FRKSFEFS