PCDB8_HUMAN
ID PCDB8_HUMAN Reviewed; 801 AA.
AC Q9UN66; B9EGV1;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2020, sequence version 4.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Protocadherin beta-8 {ECO:0000305};
DE Short=PCDH-beta-8 {ECO:0000305};
DE AltName: Full=Protocadherin-3I;
DE Flags: Precursor;
GN Name=PCDHB8 {ECO:0000312|HGNC:HGNC:8693}; Synonyms=PCDH3I;
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 VARIANTS ASN-199; GLN-244; LEU-661 AND
RP PHE-767.
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 SEQUENCE REVISION.
RA Wu Q., Maniatis T.;
RL Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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 [GENOMIC DNA] OF 192-801, AND VARIANT HIS-639.
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).
CC -!- FUNCTION: Calcium-dependent cell-adhesion protein involved in cells
CC self-recognition and non-self discrimination. Thereby, it is involved
CC in the establishment and maintenance of specific neuronal connections
CC in the brain. {ECO:0000250|UniProtKB:Q91XZ2}.
CC -!- SUBUNIT: Forms homodimers in trans (molecules expressed by two
CC different cells). Forms promiscuous heterodimers in cis (at the plasma
CC membrane of the same cell) with other protocadherins.
CC {ECO:0000250|UniProtKB:Q91XZ2}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q91XZ2};
CC Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q91XZ2}.
CC -!- DOMAIN: Cadherin 1 to cadherin 4 domains mediate homophilic trans-
CC interaction, the interaction with an identical protocadherin expressed
CC by a neighboring cell. This is a head-to-tail interaction, the cadherin
CC 1 domain interacting with the cadherin 4 domain and the cadherin 2
CC domain interacting the cadherin 3 domain of the other protocadherin.
CC The cadherin 6 domain mediates promiscuous interactions with
CC protocadherins on the same cell membrane. Each cadherin domain binds
CC three calcium ions. {ECO:0000250|UniProtKB:Q91XZ2}.
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DR EMBL; AF152501; AAD43762.2; -; mRNA.
DR EMBL; AC244517; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC136801; AAI36802.1; -; mRNA.
DR EMBL; AF282973; AAG10031.1; -; Genomic_DNA.
DR CCDS; CCDS4250.1; -.
DR RefSeq; NP_061993.3; NM_019120.4.
DR AlphaFoldDB; Q9UN66; -.
DR SMR; Q9UN66; -.
DR BioGRID; 121068; 4.
DR GlyConnect; 1684; 1 N-Linked glycan (1 site).
DR GlyGen; Q9UN66; 3 sites, 1 N-linked glycan (1 site).
DR iPTMnet; Q9UN66; -.
DR PhosphoSitePlus; Q9UN66; -.
DR BioMuta; PCDHB8; -.
DR DMDM; 145559514; -.
DR jPOST; Q9UN66; -.
DR MassIVE; Q9UN66; -.
DR MaxQB; Q9UN66; -.
DR PaxDb; Q9UN66; -.
DR PeptideAtlas; Q9UN66; -.
DR PRIDE; Q9UN66; -.
DR ProteomicsDB; 85251; -.
DR Antibodypedia; 72031; 26 antibodies from 7 providers.
DR DNASU; 56128; -.
DR Ensembl; ENST00000239444.4; ENSP00000239444.2; ENSG00000120322.4.
DR GeneID; 56128; -.
DR KEGG; hsa:56128; -.
DR MANE-Select; ENST00000239444.4; ENSP00000239444.2; NM_019120.5; NP_061993.3.
DR UCSC; uc011dai.3; human.
DR CTD; 56128; -.
DR DisGeNET; 56128; -.
DR GeneCards; PCDHB8; -.
DR HGNC; HGNC:8693; PCDHB8.
DR HPA; ENSG00000120322; Low tissue specificity.
DR MIM; 604967; gene.
DR MIM; 606334; gene.
DR neXtProt; NX_Q9UN66; -.
DR OpenTargets; ENSG00000120322; -.
DR PharmGKB; PA33042; -.
DR VEuPathDB; HostDB:ENSG00000120322; -.
DR eggNOG; KOG3594; Eukaryota.
DR GeneTree; ENSGT00940000165899; -.
DR HOGENOM; CLU_006480_3_0_1; -.
DR InParanoid; Q9UN66; -.
DR OMA; QVYIEVV; -.
DR OrthoDB; 300321at2759; -.
DR PhylomeDB; Q9UN66; -.
DR TreeFam; TF332299; -.
DR PathwayCommons; Q9UN66; -.
DR BioGRID-ORCS; 56128; 10 hits in 997 CRISPR screens.
DR GenomeRNAi; 56128; -.
DR Pharos; Q9UN66; Tdark.
DR PRO; PR:Q9UN66; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q9UN66; protein.
DR Bgee; ENSG00000120322; Expressed in cortical plate and 89 other tissues.
DR Genevisible; Q9UN66; HS.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
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 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; 5.
PE 2: Evidence at transcript level;
KW Calcium; Cell adhesion; Cell membrane; Disulfide bond; Glycoprotein;
KW Membrane; Metal-binding; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..29
FT /evidence="ECO:0000250|UniProtKB:Q91XZ2"
FT CHAIN 30..801
FT /note="Protocadherin beta-8"
FT /id="PRO_0000003928"
FT TOPO_DOM 30..691
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q91XZ2"
FT TRANSMEM 692..710
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 711..801
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q91XZ2"
FT DOMAIN 36..134
FT /note="Cadherin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 139..243
FT /note="Cadherin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 248..348
FT /note="Cadherin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 353..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 569..672
FT /note="Cadherin 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT CARBOHYD 419
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 437
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 568
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 97..103
FT /evidence="ECO:0000250|UniProtKB:Q91XZ2"
FT VARIANT 199
FT /note="K -> N (in dbSNP:rs2950845)"
FT /evidence="ECO:0000269|PubMed:10380929"
FT /id="VAR_031619"
FT VARIANT 232
FT /note="E -> G (in dbSNP:rs17096954)"
FT /id="VAR_055581"
FT VARIANT 244
FT /note="E -> Q (in dbSNP:rs2950844)"
FT /evidence="ECO:0000269|PubMed:10380929"
FT /id="VAR_031620"
FT VARIANT 305
FT /note="K -> E (in dbSNP:rs3733694)"
FT /id="VAR_021880"
FT VARIANT 322
FT /note="A -> V (in dbSNP:rs7700833)"
FT /id="VAR_024392"
FT VARIANT 382
FT /note="I -> T (in dbSNP:rs3733693)"
FT /id="VAR_055582"
FT VARIANT 639
FT /note="Q -> H (in dbSNP:rs2740582)"
FT /evidence="ECO:0000269|PubMed:11322959"
FT /id="VAR_055583"
FT VARIANT 661
FT /note="V -> L (in dbSNP:rs2697541)"
FT /evidence="ECO:0000269|PubMed:10380929"
FT /id="VAR_055584"
FT VARIANT 745
FT /note="S -> N (in dbSNP:rs17096961)"
FT /id="VAR_055585"
FT VARIANT 759
FT /note="G -> V (in dbSNP:rs35245446)"
FT /id="VAR_055586"
FT VARIANT 767
FT /note="L -> F (in dbSNP:rs2740583)"
FT /evidence="ECO:0000269|PubMed:10380929"
FT /id="VAR_024393"
FT CONFLICT 234
FT /note="V -> L (in Ref. 5; AAG10031)"
FT /evidence="ECO:0000305"
FT CONFLICT 569
FT /note="G -> S (in Ref. 5; AAG10031)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 801 AA; 87591 MW; 5BFB22B63D56E010 CRC64;
MEASGKLICR QRQVLFSFLL LGLSLAGAAE PRSYSVVEET EGSSFVTNLA KDLGLEQREF
SRRGVRVVSR GNKLHLQLNQ ETADLLLNEK LDREDLCGHT EPCVLRFQVL LESPFEFFQA
ELQVIDINDH SPVFLDKQML VKVSESSPPG TAFPLKNAED LDIGQNNIEN YIISPNSYFR
VLTRKRSDGR KYPELVLDKA LDREEEAELR LTLTALDGGS PPRSGTAQVY IEVVDVNDNA
PEFEQPFYRV QISEDSPISF LVVKVSATDV DTGVNGEISY SLFQASDEIS KTFKVDFLTG
EIRLKKQLDF EKFQSYEVNI EARDAGGFSG KCTVLIQVID VNDHAPEVTM SAFTSPIPEN
APETVVALFS VSDLDSGENG KISCSIQEDL PFLLKSSVGN FYTLLTETPL DRESRAEYNV
TITVTDLGTP RLTTHLNMTV LVSDVNDNAP AFTQTSYTLF VRENNSPALH IGSVSATDRD
SGTNAQVTYS LLPPQDPHLP LASLVSINTD NGHLFALRSL DYEALQAFEF RVGASDRGSP
ALSSEALVRV LVLDANDNSP FVLYPLQNGS APCTELVPRA AEPGYLVTKV VAVDGDSGQN
AWLSYQLLKA TEPGLFGVWA HNGEVRTARL LSERDAAKQR LVVLVKDNGE PPCSATATLH
VLLVDGFSQP YLPLPEAAPA QGQADSLTVY LVVALASVSS LFLFSVLLFV AVLLCRRSRA
ASVGRCSVPE GPFPGHLVDV RGTGSLSQNY QYEVCLAGGS GTNEFQLLKP VLPNIQGHSF
GPEMEQNSNF RNGFGFSLQL K
