PCDBF_HUMAN
ID PCDBF_HUMAN Reviewed; 787 AA.
AC Q9Y5E8; Q8IUX5;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Protocadherin beta-15;
DE Short=PCDH-beta-15;
DE Flags: Precursor;
GN Name=PCDHB15;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10380929; DOI=10.1016/s0092-8674(00)80789-8;
RA Wu Q., Maniatis T.;
RT "A striking organization of a large family of human neural cadherin-like
RT cell adhesion genes.";
RL Cell 97:779-790(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=11322959; DOI=10.1016/s0014-5793(01)02372-9;
RA Vanhalst K., Kools P., Vanden Eynde E., van Roy F.;
RT "The human and murine protocadherin-beta one-exon gene families show high
RT evolutionary conservation, despite the difference in gene number.";
RL FEBS Lett. 495:120-125(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS ARG-474 AND GLN-494.
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP VARIANTS [LARGE SCALE ANALYSIS] VAL-719 AND VAL-758.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF152494; AAD43755.1; -; mRNA.
DR EMBL; AF217742; AAK51610.1; -; mRNA.
DR EMBL; BC038797; AAH38797.1; -; mRNA.
DR CCDS; CCDS4257.1; -.
DR RefSeq; NP_061758.1; NM_018935.3.
DR AlphaFoldDB; Q9Y5E8; -.
DR SMR; Q9Y5E8; -.
DR BioGRID; 121061; 25.
DR IntAct; Q9Y5E8; 25.
DR STRING; 9606.ENSP00000231173; -.
DR GlyConnect; 1679; 1 N-Linked glycan (1 site).
DR GlyGen; Q9Y5E8; 2 sites, 1 N-linked glycan (1 site).
DR iPTMnet; Q9Y5E8; -.
DR PhosphoSitePlus; Q9Y5E8; -.
DR BioMuta; PCDHB15; -.
DR DMDM; 13431379; -.
DR EPD; Q9Y5E8; -.
DR jPOST; Q9Y5E8; -.
DR MassIVE; Q9Y5E8; -.
DR PaxDb; Q9Y5E8; -.
DR PeptideAtlas; Q9Y5E8; -.
DR PRIDE; Q9Y5E8; -.
DR ProteomicsDB; 86347; -.
DR Antibodypedia; 2352; 160 antibodies from 23 providers.
DR DNASU; 56121; -.
DR Ensembl; ENST00000231173.6; ENSP00000231173.3; ENSG00000113248.6.
DR GeneID; 56121; -.
DR KEGG; hsa:56121; -.
DR MANE-Select; ENST00000231173.6; ENSP00000231173.3; NM_018935.4; NP_061758.1.
DR UCSC; uc003lje.5; human.
DR CTD; 56121; -.
DR DisGeNET; 56121; -.
DR GeneCards; PCDHB15; -.
DR HGNC; HGNC:8686; PCDHB15.
DR HPA; ENSG00000113248; Low tissue specificity.
DR MIM; 604967; gene.
DR MIM; 606341; gene.
DR neXtProt; NX_Q9Y5E8; -.
DR OpenTargets; ENSG00000113248; -.
DR PharmGKB; PA33031; -.
DR VEuPathDB; HostDB:ENSG00000113248; -.
DR eggNOG; KOG3594; Eukaryota.
DR GeneTree; ENSGT00940000162842; -.
DR HOGENOM; CLU_006480_3_0_1; -.
DR InParanoid; Q9Y5E8; -.
DR OMA; TDPCVMH; -.
DR OrthoDB; 300321at2759; -.
DR PhylomeDB; Q9Y5E8; -.
DR TreeFam; TF332299; -.
DR PathwayCommons; Q9Y5E8; -.
DR SignaLink; Q9Y5E8; -.
DR BioGRID-ORCS; 56121; 9 hits in 1024 CRISPR screens.
DR GeneWiki; PCDHB15; -.
DR GenomeRNAi; 56121; -.
DR Pharos; Q9Y5E8; Tdark.
DR PRO; PR:Q9Y5E8; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q9Y5E8; protein.
DR Bgee; ENSG00000113248; Expressed in cortical plate and 99 other tissues.
DR ExpressionAtlas; Q9Y5E8; baseline and differential.
DR Genevisible; Q9Y5E8; HS.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0032391; C:photoreceptor connecting cilium; IEA:Ensembl.
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; TAS:ProtInc.
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; IPR030733; PCDHB15.
DR PANTHER; PTHR24028:SF97; PTHR24028:SF97; 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; 5.
DR PROSITE; PS50268; CADHERIN_2; 6.
PE 2: Evidence at transcript level;
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..787
FT /note="Protocadherin beta-15"
FT /id="PRO_0000003942"
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..787
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 567
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VARIANT 474
FT /note="S -> R (in dbSNP:rs618506)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_019633"
FT VARIANT 494
FT /note="R -> Q (in dbSNP:rs618096)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_019634"
FT VARIANT 719
FT /note="A -> V (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036106"
FT VARIANT 758
FT /note="G -> V (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036107"
SQ SEQUENCE 787 AA; 86329 MW; 8DE8D3A07B0B6A56 CRC64;
MEPAGERFPE QRQVLILLLL LEVTLAGWEP RRYSVMEETE RGSFVANLAN DLGLGVGELA
ERGARVVSED NEQGLQLDLQ TGQLILNEKL DREKLCGPTE PCIMHFQVLL KKPLEVFRAE
LLVTDINDHS PEFPEREMTL KIPETSSLGT VFPLKKARDL DVGSNNVQNY NISPNSHFHV
STRTRGDGRK YPELVLDTEL DREEQAELRL TLTAVDGGSP PRSGTVQILI LVLDANDNAP
EFVQALYEVQ VPENSPVGSL VVKVSARDLD TGTNGEISYS LYYSSQEIDK PFELSSLSGE
IRLIKKLDFE TMSSYDLDIE ASDGGGLSGK CSVSVKVLDV NDNFPELSIS SLTSPIPENS
PETEVALFRI RDRDSGENGK MICSIQDDVP FKLKPSVENF YRLVTEGALD RETRAEYNIT
ITITDLGTPR LKTEQSITVL VSDVNDNAPA FTQTSYTLFV RENNSPALHI GSVSATDRDS
GTNAQVTYSL LPPRDPHLPL TSLVSINTDN GHLFALQSLD YEALQAFEFR VGATDRGFPA
LSSEALVRVL VLDANDNSPF VLYPLQNGSA PCTELVPRAA EPGYLVTKVV AVDGDSGQNA
WLSYQLLKAT EPGLFGVWAH NGEVRTARLL SERDVAKHRL VVLVKDNGEP PRSATATLQV
LLVDGFSQPY LPLPEAAPAQ AQADSLTVYL VVALASVSSL FLFSVFLFVA VRLCRRSRAA
SVGRCSVPEG PFPGHLVDVS GTGTLSQSYQ YEVCLTGGSE SNDFKFLKPI FPNIVSQDSR
RKSEFLE
