PCDB2_HUMAN
ID PCDB2_HUMAN Reviewed; 798 AA.
AC Q9Y5E7; Q4KMU1;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Protocadherin beta-2;
DE Short=PCDH-beta-2;
DE Flags: Precursor;
GN Name=PCDHB2;
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=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 ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-299, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
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; AF152495; AAD43756.1; -; mRNA.
DR EMBL; AF217756; AAK51623.1; -; mRNA.
DR EMBL; BC098347; AAH98347.1; -; mRNA.
DR CCDS; CCDS4244.1; -.
DR RefSeq; NP_061759.1; NM_018936.3.
DR AlphaFoldDB; Q9Y5E7; -.
DR SMR; Q9Y5E7; -.
DR BioGRID; 121073; 12.
DR IntAct; Q9Y5E7; 1.
DR GlyConnect; 1681; 1 N-Linked glycan (1 site).
DR GlyGen; Q9Y5E7; 4 sites, 1 N-linked glycan (1 site).
DR iPTMnet; Q9Y5E7; -.
DR PhosphoSitePlus; Q9Y5E7; -.
DR BioMuta; PCDHB2; -.
DR DMDM; 13431378; -.
DR EPD; Q9Y5E7; -.
DR jPOST; Q9Y5E7; -.
DR MassIVE; Q9Y5E7; -.
DR PaxDb; Q9Y5E7; -.
DR PeptideAtlas; Q9Y5E7; -.
DR PRIDE; Q9Y5E7; -.
DR ProteomicsDB; 86346; -.
DR Antibodypedia; 27181; 55 antibodies from 10 providers.
DR DNASU; 56133; -.
DR Ensembl; ENST00000194155.7; ENSP00000194155.4; ENSG00000112852.7.
DR GeneID; 56133; -.
DR KEGG; hsa:56133; -.
DR MANE-Select; ENST00000194155.7; ENSP00000194155.4; NM_018936.4; NP_061759.1.
DR UCSC; uc003lil.5; human.
DR CTD; 56133; -.
DR GeneCards; PCDHB2; -.
DR HGNC; HGNC:8687; PCDHB2.
DR HPA; ENSG00000112852; Low tissue specificity.
DR MIM; 604967; gene.
DR MIM; 606328; gene.
DR neXtProt; NX_Q9Y5E7; -.
DR OpenTargets; ENSG00000112852; -.
DR PharmGKB; PA33036; -.
DR VEuPathDB; HostDB:ENSG00000112852; -.
DR eggNOG; KOG3594; Eukaryota.
DR GeneTree; ENSGT00940000163333; -.
DR HOGENOM; CLU_006480_3_0_1; -.
DR InParanoid; Q9Y5E7; -.
DR OMA; FRLNQNT; -.
DR OrthoDB; 300321at2759; -.
DR PhylomeDB; Q9Y5E7; -.
DR TreeFam; TF332299; -.
DR PathwayCommons; Q9Y5E7; -.
DR SignaLink; Q9Y5E7; -.
DR BioGRID-ORCS; 56133; 11 hits in 1032 CRISPR screens.
DR GeneWiki; PCDHB2; -.
DR GenomeRNAi; 56133; -.
DR Pharos; Q9Y5E7; Tdark.
DR PRO; PR:Q9Y5E7; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q9Y5E7; protein.
DR Bgee; ENSG00000112852; Expressed in sperm and 103 other tissues.
DR ExpressionAtlas; Q9Y5E7; baseline and differential.
DR Genevisible; Q9Y5E7; 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:0007399; P:nervous system development; TAS:ProtInc.
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 InterPro; IPR030735; PCDHB2.
DR PANTHER; PTHR24028:SF281; PTHR24028:SF281; 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; 6.
DR SUPFAM; SSF49313; SSF49313; 5.
DR PROSITE; PS00232; CADHERIN_1; 5.
DR PROSITE; PS50268; CADHERIN_2; 6.
PE 1: Evidence at protein 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..798
FT /note="Protocadherin beta-2"
FT /id="PRO_0000003916"
FT TOPO_DOM 31..692
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 693..713
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 714..798
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 37..135
FT /note="Cadherin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 136..244
FT /note="Cadherin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 249..349
FT /note="Cadherin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 354..453
FT /note="Cadherin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 458..563
FT /note="Cadherin 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 570..673
FT /note="Cadherin 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT MOD_RES 299
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT CARBOHYD 171
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 420
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 438
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 569
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VARIANT 128
FT /note="V -> I (in dbSNP:rs31853)"
FT /id="VAR_020365"
FT VARIANT 674
FT /note="L -> P (in dbSNP:rs384081)"
FT /id="VAR_033701"
FT VARIANT 760
FT /note="G -> D (in dbSNP:rs1047372)"
FT /id="VAR_033702"
SQ SEQUENCE 798 AA; 87254 MW; B2602E865378CB27 CRC64;
MEAGEGKERV PKQRQVLIFF VLLGIAQASC QPRHYSVAEE TESGSFVANL LKDLGLEIGE
LAVRGARVVS KGKKMHLQFD RQTGDLLLNE KLDREELCGP TEPCVLPFQV LLENPLQFFQ
AELRIRDVND HSPVFLDKEI LLKIPESITP GTTFLIERAQ DLDVGTNSLQ NYTISPNFHF
HLNLQDSLDG IILPQLVLNR ALDREEQPEI RLTLTALDGG SPPRSGTALV RIEVVDINDN
VPEFAKLLYE VQIPEDSPVG SQVAIVSARD LDIGTNGEIS YAFSQASEDI RKTFRLSAKS
GELLLRQKLD FESIQTYTVN IQATDGGGLS GTCVVFVQVM DLNDNPPELT MSTLINQIPE
NLQDTLIAVF SVSDPDSGDN GRMVCSIQDD LPFFLKPSVE NFYTLVISTA LDRETRSEYN
ITITVTDFGT PRLKTEHNIT VLVSDVNDNA PAFTQTSYTL FVRENNSPAL HIGSVSATDR
DSGTNAQVTY SLLPPQDPHL PLASLVSINA DNGHLFALQS LDYEALQAFE FRVGAADRGS
PALSSEALVR VLVLDANDNS PFVLYPLQNG SAPCTELVPR AAEPGYLVTK VVAVDGDSGQ
NAWLSYQLLK ATEPGLFGVW AHNGEVRTAR LLRERDAAKQ RLVVLVKDNG EPPRSATATL
HVLLVDGFSQ PYLLLPEAAP AQAQADLLTV YLVVALASVS SLFLFSVLLF VAVRLCRRSR
AASVGRCSVP EGPFPGQMVD VSGTGTLSQS YQYEVCLTGG SGTNEFKFLK PIIPNFVAQG
AERVSEANPS FRKSFEFT
