ID   PCDBI_PANTR             Reviewed;         788 AA.
AC   Q5DRD4;
DT   12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   29-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Protocadherin beta-18;
DE            Short=PCDH-beta-18;
DE   AltName: Full=Protocadherin beta-17;
DE   Flags: Precursor;
GN   Name=PCDHB18; Synonyms=PCDHB17;
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.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I
CC       membrane protein {ECO:0000250}.
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DR   EMBL; GL386549; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; Q5DRD4; -.
DR   SMR; Q5DRD4; -.
DR   InParanoid; Q5DRD4; -.
DR   OrthoDB; 300321at2759; -.
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..28
FT                   /evidence="ECO:0000255"
FT   CHAIN           29..788
FT                   /note="Protocadherin beta-18"
FT                   /id="PRO_0000003946"
FT   TOPO_DOM        29..691
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        692..712
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        713..788
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          29..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..452
FT                   /note="Cadherin 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          453..562
FT                   /note="Cadherin 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          569..672
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        419
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        437
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        568
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   788 AA;  86204 MW;  75295794BEEEAE37 CRC64;
     MEPGKGRAQP TRQVLLFFVF LGGSLVYSET WSYSIAEEME VGTFIANVVK DMGLDVEDLV
     ARGARVIFDD YKPYLRLDPQ NGDLLLNEQL DREALCDLTE PCILHFQVLF ENPLQFFRAE
     LLVKDINDHT PTFLNNHILL KISEGATLGT LFQIDSAQDL DVGKNGVQNY TISPNPHFHL
     KLRDGDEGRK YPELVLDQSL DREKESQLSL TLTAVDGGSP PRSGTTLINV VVLDINDNAP
     EFEKPVYEVH VPESSPLDSL IIKASATDLD AGINGELSYS FSHVSRDVRK TFEIHPISGE
     VYLKAPLDFE IIQSYIINIQ AIDGGSLSGK SSILVRVVDV NDNPPEIAMT SLTSPIPENS
     SPEMVVAVFS IRDQDAGDNG RMVGSIQDNL PFVLKPTFKN FYALVTEHPL DREVRNEYNI
     TITVTDLGTP RLKTQHNITV LVSDVNDNAP AFTQTSYTLF VRENNSPALH IGSVSATDRD
     SGTNAQVTYS LLPPQDPHLP LASLVSINTD NGHLFALRSL DYEALQAFEF HVGATDRGSP
     ALSSEALVRV LVLDANDNSP FVLYPLQNGS APCTELVPRA AEPGYLVTKV VAVDGDSGQN
     AWLSYQLLKA TEPGLFGVWA HNGEVRTARL LSERDVAKHR LVVLVKDNGE PPRSATATLQ
     VLLVDGFSQP YLPLPEAAPS QAQADSLTVY LVVALASVSS LFLFSVFLFV AVRLCRRSRA
     ASVGRCSVPE GPFPGHLLDV SGTGTLSQSY QYEVCLTGGS GANEFKFLKP VIPNLLSRDS
     DMEKAPPF