PCDB1_HUMAN
ID PCDB1_HUMAN Reviewed; 818 AA.
AC Q9Y5F3; Q2M257;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 2.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Protocadherin beta-1;
DE Short=PCDH-beta-1;
DE Flags: Precursor;
GN Name=PCDHB1;
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 LEU-778.
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 [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
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).
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; AF152488; AAD43749.1; -; mRNA.
DR EMBL; CH471062; EAW61985.1; -; Genomic_DNA.
DR EMBL; BC112096; AAI12097.1; -; mRNA.
DR EMBL; BC112098; AAI12099.1; -; mRNA.
DR CCDS; CCDS4243.1; -.
DR RefSeq; NP_037472.2; NM_013340.3.
DR AlphaFoldDB; Q9Y5F3; -.
DR SMR; Q9Y5F3; -.
DR BioGRID; 118971; 20.
DR IntAct; Q9Y5F3; 1.
DR STRING; 9606.ENSP00000307234; -.
DR GlyGen; Q9Y5F3; 5 sites.
DR iPTMnet; Q9Y5F3; -.
DR PhosphoSitePlus; Q9Y5F3; -.
DR BioMuta; PCDHB1; -.
DR DMDM; 205371811; -.
DR jPOST; Q9Y5F3; -.
DR MassIVE; Q9Y5F3; -.
DR PaxDb; Q9Y5F3; -.
DR PeptideAtlas; Q9Y5F3; -.
DR PRIDE; Q9Y5F3; -.
DR ProteomicsDB; 86352; -.
DR Antibodypedia; 27174; 87 antibodies from 16 providers.
DR DNASU; 29930; -.
DR Ensembl; ENST00000306549.6; ENSP00000307234.4; ENSG00000171815.6.
DR GeneID; 29930; -.
DR KEGG; hsa:29930; -.
DR MANE-Select; ENST00000306549.6; ENSP00000307234.4; NM_013340.4; NP_037472.2.
DR UCSC; uc003lik.3; human.
DR CTD; 29930; -.
DR DisGeNET; 29930; -.
DR GeneCards; PCDHB1; -.
DR HGNC; HGNC:8680; PCDHB1.
DR HPA; ENSG00000171815; Tissue enhanced (skeletal).
DR MIM; 604967; gene.
DR MIM; 606327; gene.
DR neXtProt; NX_Q9Y5F3; -.
DR OpenTargets; ENSG00000171815; -.
DR PharmGKB; PA33025; -.
DR VEuPathDB; HostDB:ENSG00000171815; -.
DR eggNOG; KOG3594; Eukaryota.
DR GeneTree; ENSGT00940000162745; -.
DR HOGENOM; CLU_006480_3_2_1; -.
DR InParanoid; Q9Y5F3; -.
DR OMA; ERDPMMQ; -.
DR OrthoDB; 300321at2759; -.
DR PhylomeDB; Q9Y5F3; -.
DR TreeFam; TF332299; -.
DR PathwayCommons; Q9Y5F3; -.
DR BioGRID-ORCS; 29930; 7 hits in 1029 CRISPR screens.
DR GenomeRNAi; 29930; -.
DR Pharos; Q9Y5F3; Tdark.
DR PRO; PR:Q9Y5F3; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q9Y5F3; protein.
DR Bgee; ENSG00000171815; Expressed in upper leg skin and 5 other tissues.
DR Genevisible; Q9Y5F3; HS.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
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; IEA:UniProt.
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; IPR030723; PCDHB1.
DR PANTHER; PTHR24028:SF12; PTHR24028:SF12; 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; 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..28
FT /evidence="ECO:0000255"
FT CHAIN 29..818
FT /note="Protocadherin beta-1"
FT /id="PRO_0000003914"
FT TOPO_DOM 29..691
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 692..712
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 713..818
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 243..347
FT /note="Cadherin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 348..452
FT /note="Cadherin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 457..562
FT /note="Cadherin 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 577..672
FT /note="Cadherin 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT REGION 789..818
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 803..818
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 169
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 209
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 257
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 419
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 568
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VARIANT 385
FT /note="F -> L (in dbSNP:rs2233591)"
FT /id="VAR_048541"
FT VARIANT 390
FT /note="L -> F (in dbSNP:rs2233592)"
FT /id="VAR_048542"
FT VARIANT 524
FT /note="A -> V (in dbSNP:rs17208383)"
FT /id="VAR_048543"
FT VARIANT 611
FT /note="T -> I (in dbSNP:rs10476822)"
FT /id="VAR_048544"
FT VARIANT 712
FT /note="I -> T (in dbSNP:rs31738)"
FT /id="VAR_048545"
FT VARIANT 719
FT /note="K -> I (in dbSNP:rs2233595)"
FT /id="VAR_048546"
FT VARIANT 778
FT /note="F -> L (in dbSNP:rs246679)"
FT /evidence="ECO:0000269|PubMed:10380929"
FT /id="VAR_048547"
SQ SEQUENCE 818 AA; 90491 MW; 4697DC76EDB7D604 CRC64;
MAGTRRKSLQ NRQVGSLLIF LCISVGDATT IRYSVAEEME SGSFVANVAK DLGLEVGKLA
ARGARLVSEG NKMHFRLHRK TGDLFVKEKL DRESLCGKAD PCVLHFEVVL VEPLQSFRAE
VRVFDINDNA PVFLNKEPLL KIPESTPLGS RFPLQSAQDL DVGLNGLQNY TLSANGYFHL
HTRFCSHGPK YAELVLNKPL DREEQPEVNL TITAVDGGSP PKSGTAHIHV VVLDVNDHVP
QFSRLVYRAQ VSENSPNGSL VATVTAVDLD EGTNKAITYS LAQNPEAILK TFQIDPQNGE
VRLRGPLDFE AIETYDIDIQ ATDGGGLSAH SKVLVEVVDV NDNPPEVMVS SVSSPLPEDS
PPQTVVALFT IRDRDIRVGG KVTCFLREDL PFVIKPTFGN SYSLVTDRSL DREEVSGYNI
TIVAMDTGPP SLSAETMIEV LISDVNDNPP IFREDSYILT VRENNSPAVF IGKVHAEDLD
LGENAQITYS LLPPKNGDLS VFAYISINSG NGKLYALRTM DYEAIQDFQF VVKATDGGFL
SLSSQVTVRV VVLDDNDNRP MILYPLQNGT LPCNDLVPRS AEAGYLVTKV VAVDGDSGQN
SWLSYHLLKA TDLGLFSVQR QNGEIHTLRQ ISERDPMMQK LIILVQDHGQ PALSTTVSLN
ILLVDGFSEP YLQFQDPTKH SRKVNPSTKY LVISLVILSF LFLLSVIVIF IIHVYQKIKY
REKFTIQEHF YDDCNFSNNL VQGQGNGSLS RPCPYEMCSA TGTGNSEFRF LKRFMPNFPF
PHATGEIKME AGSSLPPNSD RNKSQRLEGH DQVSDDYM
