ID   PCDBD_PANTR             Reviewed;         798 AA.
AC   Q5DRD6;
DT   12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   29-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Protocadherin beta-13;
DE            Short=PCDH-beta-13;
DE   Flags: Precursor;
GN   Name=PCDHB13;
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; Q5DRD6; -.
DR   SMR; Q5DRD6; -.
DR   STRING; 9598.ENSPTRP00000047956; -.
DR   PaxDb; Q5DRD6; -.
DR   eggNOG; KOG3594; Eukaryota.
DR   InParanoid; Q5DRD6; -.
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   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   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..798
FT                   /note="Protocadherin beta-13"
FT                   /id="PRO_0000003939"
FT   TOPO_DOM        29..690
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        691..711
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        712..798
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          36..134
FT                   /note="Cadherin 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          139..243
FT                   /note="Cadherin 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          248..348
FT                   /note="Cadherin 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          353..451
FT                   /note="Cadherin 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          456..561
FT                   /note="Cadherin 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          568..671
FT                   /note="Cadherin 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   CARBOHYD        418
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        436
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        567
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   798 AA;  87213 MW;  C486C5980644DE08 CRC64;
     MEASGKLICR QRQVLFSFLL LGLSLAGAAE PRSYSVVEET EGSSFVTNLA KDLGLEQREF
     SRRGVRVVSR GNKLHLQLNQ ETGDLLLNEK LDREDLCGHT EPCVLRFQVL LESPFEFFQA
     ELQVIDINDH SPVFLDKQML VKVSESSPPG TAFPLKNAED LDVGQNNIEN YIISPNSHFR
     VLTRKRSDGR KYPELVLDKA LDREEEAELR LTLTALDGGS PPRSGTAQVY IEVLDVNDNA
     PEFEQPFYRV QISEDSPVGF LVVKVSATDV DTGVNGEISY SLFQASEEIG KTFKINPLTG
     EIELKKQLDF EKLQSYEVNI EARDAGTFSG KCTVLIQVID VNDHAPEVTM SAFTSPIPEN
     APETVVALFS VSDLDSGENG KISCSIQEDL PFLLKSAENF YTLLTERPLD RESRAEYNIT
     ITVTDLGTPM LKTQLNMTVL IADVNDNAPA FTQTSYTLFV RENNSPALHI GSVSATDRDS
     GTNAQVTYSL LPPQDPHLPL TSLVSINADN GHLFALRSLD YEALQGFEFR VGASDHGSPA
     LSSEALVRVL VLDANDNSPF VLYPLQNGSA PCTELVPRAA EPGYLVTKVV AVDGDSGQNA
     WLSYQLLKAT EPGLFGVWAH NGEVRTARLL SERDAAKHRL AVLVKDNGEP PRSATATLHV
     LLVDGFSQPY LPLPEAAPTQ AQADSLTVYL VVALASVSSL FLFSVLLFVA VRLCRRSRAA
     SVGRCLVPEG PLPGHLVDMG GTGTLSQSYQ YEVCLAGGSG TNEFKFLKPI IPNFPPQCPG
     KEIQGNSTFP NNFGFNIQ