ID   PCDBA_HUMAN             Reviewed;         800 AA.
AC   Q9UN67; Q96T99;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   24-JAN-2024, entry version 189.
DE   RecName: Full=Protocadherin beta-10;
DE            Short=PCDH-beta-10;
DE   Flags: Precursor;
GN   Name=PCDHB10; ORFNames=UNQ1906/PRO4352;
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].
RX   PubMed=12975309; DOI=10.1101/gr.1293003;
RA   Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA   Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA   Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA   Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA   Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA   Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA   Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA   Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT   "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT   identify novel human secreted and transmembrane proteins: a bioinformatics
RT   assessment.";
RL   Genome Res. 13:2265-2270(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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   [5]
RP   PROTEIN SEQUENCE OF 27-41.
RX   PubMed=15340161; DOI=10.1110/ps.04682504;
RA   Zhang Z., Henzel W.J.;
RT   "Signal peptide prediction based on analysis of experimentally verified
RT   cleavage sites.";
RL   Protein Sci. 13:2819-2824(2004).
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; AF152489; AAD43750.1; -; mRNA.
DR   EMBL; AF217748; AAK51616.1; -; mRNA.
DR   EMBL; AY358720; AAQ89082.1; -; mRNA.
DR   EMBL; BC031837; AAH31837.1; -; mRNA.
DR   CCDS; CCDS4252.1; -.
DR   RefSeq; NP_061753.1; NM_018930.3.
DR   AlphaFoldDB; Q9UN67; -.
DR   SMR; Q9UN67; -.
DR   BioGRID; 121066; 6.
DR   IntAct; Q9UN67; 5.
DR   STRING; 9606.ENSP00000239446; -.
DR   GlyConnect; 1676; 1 N-Linked glycan (1 site).
DR   GlyCosmos; Q9UN67; 5 sites, 1 glycan.
DR   GlyGen; Q9UN67; 5 sites, 1 N-linked glycan (1 site).
DR   iPTMnet; Q9UN67; -.
DR   PhosphoSitePlus; Q9UN67; -.
DR   BioMuta; PCDHB10; -.
DR   DMDM; 13431371; -.
DR   jPOST; Q9UN67; -.
DR   MassIVE; Q9UN67; -.
DR   PaxDb; 9606-ENSP00000239446; -.
DR   PeptideAtlas; Q9UN67; -.
DR   Antibodypedia; 2995; 121 antibodies from 22 providers.
DR   DNASU; 56126; -.
DR   Ensembl; ENST00000239446.6; ENSP00000239446.4; ENSG00000120324.9.
DR   Ensembl; ENST00000708377.1; ENSP00000517197.1; ENSG00000291689.1.
DR   GeneID; 56126; -.
DR   KEGG; hsa:56126; -.
DR   MANE-Select; ENST00000239446.6; ENSP00000239446.4; NM_018930.4; NP_061753.1.
DR   UCSC; uc003lix.4; human.
DR   AGR; HGNC:8681; -.
DR   CTD; 56126; -.
DR   GeneCards; PCDHB10; -.
DR   HGNC; HGNC:8681; PCDHB10.
DR   HPA; ENSG00000120324; Low tissue specificity.
DR   MIM; 604967; gene.
DR   MIM; 606336; gene.
DR   neXtProt; NX_Q9UN67; -.
DR   OpenTargets; ENSG00000120324; -.
DR   PharmGKB; PA33026; -.
DR   VEuPathDB; HostDB:ENSG00000120324; -.
DR   eggNOG; KOG3594; Eukaryota.
DR   GeneTree; ENSGT00940000163508; -.
DR   HOGENOM; CLU_006480_3_0_1; -.
DR   InParanoid; Q9UN67; -.
DR   OMA; VCYIQEN; -.
DR   OrthoDB; 5402790at2759; -.
DR   PhylomeDB; Q9UN67; -.
DR   TreeFam; TF332299; -.
DR   PathwayCommons; Q9UN67; -.
DR   SignaLink; Q9UN67; -.
DR   BioGRID-ORCS; 56126; 11 hits in 1104 CRISPR screens.
DR   GeneWiki; PCDHB10; -.
DR   GenomeRNAi; 56126; -.
DR   Pharos; Q9UN67; Tdark.
DR   PRO; PR:Q9UN67; -.
DR   Proteomes; UP000005640; Chromosome 5.
DR   RNAct; Q9UN67; Protein.
DR   Bgee; ENSG00000120324; Expressed in cortical plate and 131 other cell types or tissues.
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:SF54; PROTOCADHERIN BETA-10; 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; Q9UN67; HS.
PE   1: Evidence at protein level;
KW   Calcium; Cell adhesion; Cell membrane; Direct protein sequencing;
KW   Glycoprotein; Membrane; Reference proteome; Repeat; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000269|PubMed:15340161"
FT   CHAIN           27..800
FT                   /note="Protocadherin beta-10"
FT                   /id="PRO_0000003932"
FT   TOPO_DOM        27..692
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        693..713
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        714..800
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        181
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"
FT   CONFLICT        543
FT                   /note="R -> S (in Ref. 2; AAK51616)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        660
FT                   /note="L -> V (in Ref. 2; AAK51616)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   800 AA;  87621 MW;  7DF4CE8467502B91 CRC64;
     MAVRELCFPR QRQVLFLFLF WGVSLAGSGF GRYSVTEETE KGSFVVNLAK DLGLAEGELA
     ARGTRVVSDD NKQYLLLDSH TGNLLTNEKL DREKLCGPKE PCMLYFQILM DDPFQIYRAE
     LRVRDINDHA PVFQDKETVL KISENTAEGT AFRLERAQDP DGGLNGIQNY TISPNSFFHI
     NISGGDEGMI YPELVLDKAL DREEQGELSL TLTALDGGSP SRSGTSTVRI VVLDVNDNAP
     QFAQALYETQ APENSPIGFL IVKVWAEDVD SGVNAEVSYS FFDASENIRT TFQINPFSGE
     IFLRELLDYE LVNSYKINIQ AMDGGGLSAR CRVLVEVLDT NDNPPELIVS SFSNSVAENS
     PETPLAVFKI NDRDSGENGK MVCYIQENLP FLLKPSVENF YILITEGALD REIRAEYNIT
     ITVTDLGTPR LKTEHNITVL VSDVNDNAPA FTQTSYTLFV RENNSPALHI GSVSATDRDS
     GTNAQVTYSL LPPQDPHLPL ASLVSINADN GHLFALRSLD YEALQAFEFR VGATDRGSPA
     LSREALVRVL VLDANDNSPF VLYPLQNGSA PCTELVPRAA EPGYLVTKVV AVDGDSGQNA
     WLSYQLLKAT EPGLFGVWAH NGEVRTARLL SERDAAKHRL VVLVKDNGEP PRSATATLHL
     LLVDGFSQPY LPLPEAAPAQ AQAEADLLTV YLVVALASVS SLFLLSVLLF VAVRLCRRSR
     AASVGRCSVP EGPFPGHLVD VRGAETLSQS YQYEVCLTGG PGTSEFKFLK PVISDIQAQG
     PGRKGEENST FRNSFGFNIQ
//