ID   PCDB5_HUMAN             Reviewed;         795 AA.
AC   Q9Y5E4; Q549F4; Q9UFU9;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   23-FEB-2022, sequence version 2.
DT   24-JAN-2024, entry version 180.
DE   RecName: Full=Protocadherin beta-5;
DE            Short=PCDH-beta-5;
DE   Flags: Precursor;
GN   Name=PCDHB5;
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], AND VARIANT SER-720.
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], AND VARIANT SER-720.
RA   Ding J.B., Yu L., Zhao S.Y.;
RT   "Cloning and characterization of a new human cDNA homologous to Rattus
RT   norvegicus protocadherin-3 (pcdh3).";
RL   Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT SER-720.
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Muscle;
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 95-795.
RC   TISSUE=Uterus;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA   Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA   Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
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   EMBL; AF152498; AAD43759.1; -; mRNA.
DR   EMBL; AF134474; AAP97251.1; -; mRNA.
DR   EMBL; AF217753; AAK51620.1; -; mRNA.
DR   EMBL; BC001186; AAH01186.1; -; mRNA.
DR   EMBL; AL117449; CAB55933.1; -; mRNA.
DR   CCDS; CCDS4247.1; -.
DR   PIR; T17243; T17243.
DR   RefSeq; NP_056484.2; NM_015669.4.
DR   AlphaFoldDB; Q9Y5E4; -.
DR   SMR; Q9Y5E4; -.
DR   BioGRID; 117593; 56.
DR   IntAct; Q9Y5E4; 9.
DR   STRING; 9606.ENSP00000231134; -.
DR   GlyConnect; 1683; 1 N-Linked glycan (1 site).
DR   GlyCosmos; Q9Y5E4; 4 sites, 1 glycan.
DR   GlyGen; Q9Y5E4; 4 sites, 1 N-linked glycan (1 site).
DR   iPTMnet; Q9Y5E4; -.
DR   PhosphoSitePlus; Q9Y5E4; -.
DR   BioMuta; PCDHB5; -.
DR   DMDM; 13431375; -.
DR   EPD; Q9Y5E4; -.
DR   jPOST; Q9Y5E4; -.
DR   MassIVE; Q9Y5E4; -.
DR   PaxDb; 9606-ENSP00000231134; -.
DR   PeptideAtlas; Q9Y5E4; -.
DR   ProteomicsDB; 86343; -.
DR   Antibodypedia; 2351; 128 antibodies from 19 providers.
DR   DNASU; 26167; -.
DR   Ensembl; ENST00000231134.8; ENSP00000231134.5; ENSG00000113209.9.
DR   Ensembl; ENST00000708353.1; ENSP00000517187.1; ENSG00000291677.1.
DR   GeneID; 26167; -.
DR   KEGG; hsa:26167; -.
DR   MANE-Select; ENST00000231134.8; ENSP00000231134.5; NM_015669.5; NP_056484.2.
DR   UCSC; uc003liq.5; human.
DR   AGR; HGNC:8690; -.
DR   CTD; 26167; -.
DR   GeneCards; PCDHB5; -.
DR   HGNC; HGNC:8690; PCDHB5.
DR   HPA; ENSG00000113209; Low tissue specificity.
DR   MIM; 604967; gene.
DR   MIM; 606331; gene.
DR   neXtProt; NX_Q9Y5E4; -.
DR   OpenTargets; ENSG00000113209; -.
DR   PharmGKB; PA33039; -.
DR   VEuPathDB; HostDB:ENSG00000113209; -.
DR   eggNOG; KOG3594; Eukaryota.
DR   GeneTree; ENSGT00940000157793; -.
DR   HOGENOM; CLU_006480_3_0_1; -.
DR   InParanoid; Q9Y5E4; -.
DR   OMA; RIHYKGD; -.
DR   OrthoDB; 5402790at2759; -.
DR   PhylomeDB; Q9Y5E4; -.
DR   TreeFam; TF332299; -.
DR   PathwayCommons; Q9Y5E4; -.
DR   SignaLink; Q9Y5E4; -.
DR   BioGRID-ORCS; 26167; 9 hits in 1105 CRISPR screens.
DR   ChiTaRS; PCDHB5; human.
DR   GeneWiki; PCDHB5; -.
DR   GenomeRNAi; 26167; -.
DR   Pharos; Q9Y5E4; Tdark.
DR   PRO; PR:Q9Y5E4; -.
DR   Proteomes; UP000005640; Chromosome 5.
DR   RNAct; Q9Y5E4; Protein.
DR   Bgee; ENSG00000113209; Expressed in sperm and 117 other cell types or tissues.
DR   ExpressionAtlas; Q9Y5E4; baseline and differential.
DR   GO; GO:0016020; C:membrane; NAS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0045202; C:synapse; IEA:GOC.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0016339; P:calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules; NAS:UniProtKB.
DR   GO; GO:0007155; P:cell adhesion; IBA:GO_Central.
DR   GO; GO:0007268; P:chemical synaptic transmission; TAS:UniProtKB.
DR   GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro.
DR   GO; GO:0007416; P:synapse assembly; TAS:UniProtKB.
DR   CDD; cd11304; Cadherin_repeat; 5.
DR   Gene3D; 2.60.40.60; Cadherins; 6.
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   PANTHER; PTHR24028; CADHERIN-87A; 1.
DR   PANTHER; PTHR24028:SF90; PROTOCADHERIN BETA-5; 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; Cadherin-like; 6.
DR   PROSITE; PS00232; CADHERIN_1; 5.
DR   PROSITE; PS50268; CADHERIN_2; 6.
DR   Genevisible; Q9Y5E4; HS.
PE   2: Evidence at transcript level;
KW   Acetylation; Calcium; Cell adhesion; Cell membrane; Glycoprotein; Membrane;
KW   Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..30
FT                   /evidence="ECO:0000255"
FT   CHAIN           31..795
FT                   /note="Protocadherin beta-5"
FT                   /id="PRO_0000003922"
FT   TOPO_DOM        31..689
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        690..710
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        711..795
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..346
FT                   /note="Cadherin 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          351..450
FT                   /note="Cadherin 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          455..560
FT                   /note="Cadherin 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          567..670
FT                   /note="Cadherin 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   MOD_RES         296
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y5E7"
FT   CARBOHYD        169
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        417
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        435
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        566
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   VARIANT         156
FT                   /note="I -> T (in dbSNP:rs17096901)"
FT                   /id="VAR_033704"
FT   VARIANT         720
FT                   /note="P -> S (in dbSNP:rs400562)"
FT                   /evidence="ECO:0000269|PubMed:10380929,
FT                   ECO:0000269|PubMed:11322959, ECO:0000269|Ref.2"
FT                   /id="VAR_048552"
SQ   SEQUENCE   795 AA;  86433 MW;  BB67435BC10958A8 CRC64;
     METALAKTPQ KRQVMFLAIL LLLWEAGSEA VRYSIPEETE SGYSVANLAK DLGLGVGELA
     TRGARMHYKG NKELLQLDIK TGNLLLYEKL DREVMCGATE PCILHFQLLL ENPVQFFQTD
     LQLTDINDHA PEFPEKEMLL KIPESTQPGT VFPLKIAQDF DIGSNTVQNY TISPNSHFHV
     ATHNRGDGRK YPELVLDKAL DREERPELSL TLTALDGGAP PRSGTTTIRI VVLDNNDNAP
     EFLQSFYEVQ VPENSPLNSL VVVVSARDLD AGAYGSVAYA LFQGDEVTQP FVIDEKTAEI
     RLKRALDFEA TPYYNVEIVA TDGGGLSGKC TVAIEVVDVN DNAPELTMST LSSPTPENAP
     ETVVAVFSVS DPDSGDNGRM ICSIQNDLPF LLKPTLKNFY TLVTQRTLDR ESQAEYNITI
     TVTDMGTPRL KTEHNITVLV SDVNDNAPAF TQTSYTLFVR ENNSPALHIG SVSATDRDSG
     TNAQVTYSLL PPQNPHLRLA SLVSINADNG HLFALRSLDY EALQAFEFRV GATDRGSPAL
     SSEALVRVLV LDANDNSPFV LYPLQNGSAP CTELVPRAAE PGYLVTKVVA VDGDSGQNAW
     LSYQLLKATE PGLFSMWAHN GEVRTARLLS ERDAAKHRLV VLVKDNGEPP RSATATLHVL
     LVDGFSQPYL PLPEAAPAQA QADSLTVYLV VALASVSSLF LFSVLLFVAV RLCRRSRAAP
     VGRCSVPEGP FPGHLVDVSG TGTLSQSYHY EVCLTGDSGA GEFKFLKPII PNLLPQGAGE
     EIGKTAAFRN SFGLN
//