ID   PCDB5_PANTR             Reviewed;         795 AA.
AC   Q5DRC9;
DT   12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   29-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Protocadherin beta-5;
DE            Short=PCDH-beta-5;
DE   Flags: Precursor;
GN   Name=PCDHB5;
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; Q5DRC9; -.
DR   SMR; Q5DRC9; -.
DR   STRING; 9598.ENSPTRP00000029634; -.
DR   PaxDb; Q5DRC9; -.
DR   eggNOG; KOG3594; Eukaryota.
DR   InParanoid; Q5DRC9; -.
DR   Proteomes; UP000002277; Unplaced.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
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; IPR030730; PCDHB5/6/8.
DR   PANTHER; PTHR24028:SF90; PTHR24028:SF90; 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; 5.
DR   SUPFAM; SSF49313; SSF49313; 6.
DR   PROSITE; PS00232; CADHERIN_1; 4.
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..795
FT                   /note="Protocadherin beta-5"
FT                   /id="PRO_0000003923"
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..795
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          35..133
FT                   /note="Cadherin 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          138..242
FT                   /note="Cadherin 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          247..346
FT                   /note="Cadherin 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          351..450
FT                   /note="Cadherin 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          455..560
FT                   /note="Cadherin 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          567..670
FT                   /note="Cadherin 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   MOD_RES         296
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y5E7"
FT   CARBOHYD        169
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        417
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        435
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        566
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   795 AA;  86393 MW;  2131BCFC4D856D5A CRC64;
     METALAKTPQ KRQVMFLAIL LLLWEAGSEA VRYSIPEETE SGYSVANLAK DLGLGVGELA
     TRGARMHYKG NKELLQLDIK TGNLLLYEKL DREVICGATE PCILHFQLLL ENPVQFFQTD
     LQLTDINDHS PEFPEKEMLL KIPESTQPGT VFPLKVAQDF DIGSNAVQNY TISPNSHFHV
     ATHNRGDGRK YPELVLDKAL DREERPELSL TLTALDGGAP PRSGTTTIRI VVLDNNDNAP
     EFLQSLYEVQ VPENSPLNSL VVVVSARDLD AGAYGSVAYA LFQGDEVTQP FVIDEKTGEI
     RLKRALDFEA TPYYNVEIVA TDGGGLSGKC TVAMEVVDVN DNAPELTMST LSSPIPENAP
     ETVVAVFSVS DPDSGDNGRM ICSIQNDLPF LLKPTLKNFY TLVTQRTLDR ESQAEYNITI
     TVTDMGTPRL KTEHNITVLV SDVNDNAPAF TQTSYTLFVR ENNSPALQIG SVSATDRDSG
     TNAQVTYSLL PPQNPHLRLA SLVSINADNG HLFALRSLDY EALQAFEFRV GATDRGSPAL
     SSEALVRVLV LDANDNSPFV LYPLQNGSAP CTELVPRAAE PGYLVTKVVA VDGDSGQNAW
     LSYQLLKATE PGLFSMWAHN GEVRTARLLS ERDAAKHRLV VLVKDNGEPP RSATATLHVL
     LVDGFSQPYL PLPEAAPAQA QADSLTVYLV VALASVSSLF LFSVLLFVAV RLCRRSRAAP
     VGRCSVPEGP FPGHLVDVSG TGILSQSYQY EVCLTGDSGA GEFKFLKPII PNLLPQGASE
     EIGKTAAFRN SFGLN