PCDBA_HUMAN
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 03-AUG-2022, entry version 182.
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}.
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; 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 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; Q9UN67; -.
DR PeptideAtlas; Q9UN67; -.
DR PRIDE; Q9UN67; -.
DR Antibodypedia; 2995; 109 antibodies from 22 providers.
DR DNASU; 56126; -.
DR Ensembl; ENST00000239446.6; ENSP00000239446.4; ENSG00000120324.9.
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 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; NLNSFFH; -.
DR OrthoDB; 300321at2759; -.
DR PhylomeDB; Q9UN67; -.
DR TreeFam; TF332299; -.
DR PathwayCommons; Q9UN67; -.
DR SignaLink; Q9UN67; -.
DR BioGRID-ORCS; 56126; 11 hits in 1026 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 tissues.
DR Genevisible; Q9UN67; HS.
DR GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
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 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 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