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PCDBA_PANTR
ID   PCDBA_PANTR             Reviewed;         798 AA.
AC   Q5DRD9;
DT   12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   29-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Protocadherin beta-10;
DE            Short=PCDH-beta-10;
DE   Flags: Precursor;
GN   Name=PCDHB10;
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   RefSeq; NP_001013039.1; NM_001013021.2.
DR   AlphaFoldDB; Q5DRD9; -.
DR   SMR; Q5DRD9; -.
DR   STRING; 9598.ENSPTRP00000047955; -.
DR   PaxDb; Q5DRD9; -.
DR   GeneID; 503665; -.
DR   KEGG; ptr:503665; -.
DR   CTD; 56126; -.
DR   eggNOG; KOG3594; Eukaryota.
DR   HOGENOM; CLU_006480_3_0_1; -.
DR   InParanoid; Q5DRD9; -.
DR   OrthoDB; 300321at2759; -.
DR   TreeFam; TF332299; -.
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; 5.
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:0000250"
FT   CHAIN           27..798
FT                   /note="Protocadherin beta-10"
FT                   /id="PRO_0000003933"
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..798
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        169
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
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;  87239 MW;  01E51377E61E8346 CRC64;
     MAVRELCFSR QRQVLFLFLF WGVSLAGSGF GRYSVTEETE KGSFVVNLAK DLGLAEGKLA
     ARGTRVVSDD NKQYLLLDSH TGNLLTNEKL DREKLCGPKE PCMLYFQILM DDPFQIYRAE
     LRVRDINDHA PVFQDKETVL KISENTAEGT AFRLERAQDP DGGLNGIQNY TISPNSFFHI
     KISGSDEGMI YPELVLDKAL DREEQEELSL TLTALDGGSP SRSGTSTVRI VVLDVNDNAP
     QFAQALYETQ APENSPIGFL IVKVSAEDVD SGVNAEVSYS FFDASENIRT TFQINPFSGE
     IFLRELLDYE LVNSYKINIQ AMDGGGLSAR CRVLVEVLDT NDNPPELIVS SFSNSVAENS
     PETPLAVFKI NDRDSGENGK MVCYIQENLP FLLKPSVENF YILITEGALD RELRAEYNIT
     ITVTDLGTPR LKTEHNITVL VSDVNDNAPA FTQTSYTLFV RENNSPALHI GSVSATDGDS
     GTNAQVTYSL LPPQDLHLPL ASLVSINADN GHLFALRSLD YEALQAFEFR VGATDRGSPA
     LSSEALVRVL VLDANDNSPF VLYPLQNGSA PCTELVPRAA EPGYLVTKVV AVDGDSGQNA
     WLSYQLLKAT EPGLFGVWAH NGEVRTARLL SERDAAKHRL VVLVKDNGEP PRSATATLHL
     LLVDGFSQPY LPLPEAAPAQ AQADLLTVYL VVALASVSSL FLFSVLLFVA VRLCRRSRAA
     SVGRCSVPEG PFPGHLVDVS GAETLSQSYQ YEVCLTGGPG TSEFKFLKPV ISDIQAQGPG
     RKGEENSTFR NSFGFNIQ
 
 
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