ID   PCDBB_PANTR             Reviewed;         797 AA.
AC   Q5DRD8;
DT   12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   29-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Protocadherin beta-11;
DE            Short=PCDH-beta-11;
DE   Flags: Precursor;
GN   Name=PCDHB11;
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   PaxDb; Q5DRD8; -.
DR   eggNOG; KOG3594; Eukaryota.
DR   InParanoid; Q5DRD8; -.
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; IPR030734; PCDHB11/12.
DR   PANTHER; PTHR24028:SF286; PTHR24028:SF286; 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; 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..26
FT                   /evidence="ECO:0000255"
FT   CHAIN           27..797
FT                   /note="Protocadherin beta-11"
FT                   /id="PRO_0000003935"
FT   TOPO_DOM        27..690
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        691..711
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        712..797
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..347
FT                   /note="Cadherin 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          352..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        487
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   797 AA;  87079 MW;  B2296F5E51F2A975 CRC64;
     MENGGTRTQQ IRQVLLLFVL LGMSQAGSET WSFSVAEEMQ SGSFVGNLAK DLGLKVRELS
     SRGARVVSND KKQRLQLDIN TGDVLLSETL DREELCGSIE PCVLHFQVLM QNPTQFLQIE
     LQVRDINDHS PIFLEKQMLL EIPENSPVGA VFLLESAKDL DVGINAVKSY TISPNSHFHI
     KMRVNPDNRK YPELVLDKAL DYEELPELSF ILTALDGGSP PRSGTALVRV VVVDINDNSP
     EFEQAFYEVK IPENSILGSL ILTVSAWDLD SGTNGEICYT LSHASEDIRK TFEINQKSGD
     ITLTAPLDFE TIESYSIIIQ ATDRGGLFGK STVRIQVIDV NDNAPEITVS SITSPIPENT
     PETVVMVFSI QDIDSGDNGR IVCSIPEDLP FVLKSSVENY YTLETERPLD RESTAEYNIT
     ITVTDLGIPR LKTEHNTTVL VSDVNDNAPT FTQTSYTLFV SENNSPALHI GSVSATDRDS
     GTNAQVNYSL LPPQDPHLPL ASLVSINADN GHLFALRSLD YEALQAFEFR VGATDRGSPA
     LSSEALVRVL VLDANDNSPF VLYPLQNGSA PCTELVPRAA EPGYLVTKVV AVDGDSGQNA
     WLSYQLLKAT EPGLFXVWAH NGEVRTARLL SERDAAKHRL VVLVKDNGEP PRSATATLHV
     LLVDGFSQPF LPLPEAAPAQ AQTDFLTVYL VVALASVSSL FFFSVLLFVA VRLCRRSRAA
     SVGSCSVPKG PFPGHLVDVS GTGTLSQSYQ YEVCLTGGSE TNEFKFLKPV IPNIQAKGLG
     KNSEENSTFQ NSFGFNF