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PCDBH_PANTR
ID   PCDBH_PANTR             Reviewed;         795 AA.
AC   Q5DRC3;
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-17;
DE            Short=PCDH-beta-17;
DE   AltName: Full=Protocadherin beta-16;
DE   Flags: Precursor;
GN   Name=PCDHB17; Synonyms=PCDHB16;
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; Q5DRC3; -.
DR   SMR; Q5DRC3; -.
DR   STRING; 9598.ENSPTRP00000054381; -.
DR   PaxDb; Q5DRC3; -.
DR   eggNOG; KOG3594; Eukaryota.
DR   HOGENOM; CLU_006480_3_0_1; -.
DR   InParanoid; Q5DRC3; -.
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..29
FT                   /evidence="ECO:0000255"
FT   CHAIN           30..795
FT                   /note="Protocadherin beta-17"
FT                   /id="PRO_0000003945"
FT   TOPO_DOM        30..690
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        691..711
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        712..795
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          30..133
FT                   /note="Cadherin 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          134..242
FT                   /note="Cadherin 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          243..347
FT                   /note="Cadherin 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          348..451
FT                   /note="Cadherin 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          452..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   REGION          776..795
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        778..795
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        169
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        184
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   795 AA;  87073 MW;  919ADEDC4787A930 CRC64;
     METPLPKAPE KRQVTAIIFL LLLWEAGSAT IKYSVLEERD SGSFVANLAK DLGLGVGELA
     ARGARILSKG NKQYLQLERK SGNLLLKEKL DREELCGDID PCILHFQMLL KNPVQFIQGE
     LQLQDVNDHA PEFLENEILL KISEGSHPGT SFPLKIAQDL DVGSNTVQNY SISTNSYFHL
     FTRNHSDGKK YPELVLDQAL DREEQPQLRL TLTALDGGSP PRIGTSQVLI VIVDINDNVP
     EFAQRRYEVQ VPENTPIGSL VITVSARDLD AGTHGELSYS FFQYSNQIIQ AFEINSITGE
     IRLKKALDFE EIQSYHMEVE ASDGGGLSGK CTVAIEVMDI NDNAPELTMS LLISDILENS
     PETVVAVFGI SDPDSGNNGK MMCSIQDHLP FLLKPTLENF YTLLTEGALD RESRAEYNIT
     ITVTDLGTPR LKTEYNITVL VSDVNDNAPA FTQTSYTLFV RENNSPALHI GSVSATDRDS
     GTNAQVTYSL LPPQNPHLPL ASLVSINTDN GHLFALRSLD YEALQEFEFR VGATDRGSPA
     LSSEALVRVL VLDANDNSPF VLYPLQNGSA PCTELVPRAA EPGYLVTKVV AVDGDSGQNA
     WLSYQLLKAT EPGLFGVWAH NGEVRTARLL SERDAAKHRL VVLVKDNGEP PRSATATLHV
     LLVDGFSQPY LPLPEAAPAQ AQADSLTVYL VVALASVSSL FLFSVLLFVA VRLCRRSRAA
     SVGRYSVPEG PFPGHLVDVS GTRTLSQNYQ YEVYLAESSE SQFKFLKPVL PNFLGEGTGG
     DSETNSNSRN HFGFN
 
 
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