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PCDGJ_HUMAN
ID   PCDGJ_HUMAN             Reviewed;         929 AA.
AC   Q9Y5F8; Q9UN63;
DT   24-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 167.
DE   RecName: Full=Protocadherin gamma-B7;
DE            Short=PCDH-gamma-B7;
DE   Flags: Precursor;
GN   Name=PCDHGB7;
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] (ISOFORMS 1 AND 2).
RC   TISSUE=Brain;
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 MRNA] (ISOFORM 1).
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}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9Y5F8-1; Sequence=Displayed;
CC       Name=2; Synonyms=Short;
CC         IsoId=Q9Y5F8-2; Sequence=VSP_008696, VSP_008697;
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DR   EMBL; AF152336; AAD43730.1; -; mRNA.
DR   EMBL; AF152523; AAD43783.1; -; mRNA.
DR   EMBL; BC051788; AAH51788.1; -; mRNA.
DR   CCDS; CCDS47293.1; -. [Q9Y5F8-1]
DR   CCDS; CCDS75344.1; -. [Q9Y5F8-2]
DR   RefSeq; NP_061750.1; NM_018927.3. [Q9Y5F8-1]
DR   RefSeq; NP_115272.1; NM_032101.2. [Q9Y5F8-2]
DR   AlphaFoldDB; Q9Y5F8; -.
DR   SMR; Q9Y5F8; -.
DR   BioGRID; 121039; 4.
DR   STRING; 9606.ENSP00000381594; -.
DR   GlyConnect; 1690; 4 N-Linked glycans (1 site).
DR   GlyGen; Q9Y5F8; 2 sites, 3 N-linked glycans (1 site).
DR   iPTMnet; Q9Y5F8; -.
DR   PhosphoSitePlus; Q9Y5F8; -.
DR   BioMuta; PCDHGB7; -.
DR   DMDM; 37999828; -.
DR   EPD; Q9Y5F8; -.
DR   jPOST; Q9Y5F8; -.
DR   MassIVE; Q9Y5F8; -.
DR   MaxQB; Q9Y5F8; -.
DR   PaxDb; Q9Y5F8; -.
DR   PeptideAtlas; Q9Y5F8; -.
DR   PRIDE; Q9Y5F8; -.
DR   ProteomicsDB; 86357; -. [Q9Y5F8-1]
DR   ProteomicsDB; 86358; -. [Q9Y5F8-2]
DR   Antibodypedia; 56135; 12 antibodies from 4 providers.
DR   DNASU; 56099; -.
DR   Ensembl; ENST00000398594.4; ENSP00000381594.3; ENSG00000254122.3. [Q9Y5F8-1]
DR   Ensembl; ENST00000612073.1; ENSP00000479132.1; ENSG00000254122.3. [Q9Y5F8-2]
DR   GeneID; 56099; -.
DR   KEGG; hsa:56099; -.
DR   MANE-Select; ENST00000398594.4; ENSP00000381594.3; NM_018927.4; NP_061750.1.
DR   UCSC; uc003lkm.4; human. [Q9Y5F8-1]
DR   CTD; 56099; -.
DR   DisGeNET; 56099; -.
DR   GeneCards; PCDHGB7; -.
DR   HGNC; HGNC:8714; PCDHGB7.
DR   HPA; ENSG00000254122; Low tissue specificity.
DR   MIM; 604968; gene.
DR   MIM; 606304; gene.
DR   neXtProt; NX_Q9Y5F8; -.
DR   OpenTargets; ENSG00000254122; -.
DR   PharmGKB; PA33062; -.
DR   VEuPathDB; HostDB:ENSG00000254122; -.
DR   eggNOG; KOG3594; Eukaryota.
DR   GeneTree; ENSGT00940000164848; -.
DR   HOGENOM; CLU_006480_3_0_1; -.
DR   InParanoid; Q9Y5F8; -.
DR   OMA; ICKERRI; -.
DR   OrthoDB; 305110at2759; -.
DR   PhylomeDB; Q9Y5F8; -.
DR   TreeFam; TF332299; -.
DR   PathwayCommons; Q9Y5F8; -.
DR   SIGNOR; Q9Y5F8; -.
DR   BioGRID-ORCS; 56099; 9 hits in 1020 CRISPR screens.
DR   GeneWiki; PCDHGB7; -.
DR   GenomeRNAi; 56099; -.
DR   Pharos; Q9Y5F8; Tdark.
DR   PRO; PR:Q9Y5F8; -.
DR   Proteomes; UP000005640; Chromosome 5.
DR   RNAct; Q9Y5F8; protein.
DR   Bgee; ENSG00000254122; Expressed in stromal cell of endometrium and 95 other tissues.
DR   Genevisible; Q9Y5F8; 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; IPR031904; Cadherin_CBD.
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   Pfam; PF15974; Cadherin_tail; 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   Alternative splicing; Calcium; Cell adhesion; Cell membrane; Glycoprotein;
KW   Membrane; Reference proteome; Repeat; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL          1..30
FT                   /evidence="ECO:0000255"
FT   CHAIN           31..929
FT                   /note="Protocadherin gamma-B7"
FT                   /id="PRO_0000003983"
FT   TOPO_DOM        31..691
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        692..712
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        713..929
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          31..133
FT                   /note="Cadherin 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          134..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          453..562
FT                   /note="Cadherin 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          570..675
FT                   /note="Cadherin 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   REGION          806..838
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          899..929
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        809..838
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        419
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        545
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         806..808
FT                   /note="QAP -> VSI (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:10380929"
FT                   /id="VSP_008696"
FT   VAR_SEQ         809..929
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:10380929"
FT                   /id="VSP_008697"
FT   VARIANT         405
FT                   /note="V -> L (in dbSNP:rs17208397)"
FT                   /id="VAR_048573"
SQ   SEQUENCE   929 AA;  100974 MW;  2AFDD977CE501F59 CRC64;
     MGGSCAQRRR AGPRQVLFPL LLPLFYPTLC EPIRYSIPEE LAKGSVVGNL AKDLGLSVLD
     VSARELRVSA EKLHFSVDAQ SGDLLVKDRI DREQICKERR RCELQLEAVV ENPLNIFHVI
     VVIEDVNDHA PQFRKDEINL EISESVSLGM GTILESAEDP DISMNSLSKY QLSPNEYFSL
     VEKDNPDGGK YPELVLQKTL DRETQSAHHL VLTALDGGDP PRSGTAQIRI LVIDANDNPP
     VFSQDVYRVS LREDVPPGTS ILRVKATDQD EGINSEITYS FFGVADKAQH VFSLDYTTGN
     ILTQQPLDFE EVERYTINIE AKDRGSLSTR CKVIVEVVDE NDNSPEIIIT SLSDQIMEDS
     PPGVVVALFK TRDQDSGENG EVRCSLSRGV PFKIHSSSNN YYKLVTDEAL DREQTPEYNV
     TIAATDRGKP PLSSSKTITL HITDVNDNAP VFGQSAYLVH VPENNQPGAS IAQVSASDPD
     FGLNGRVSYS LIASDLESRT LSSYVSVSAQ SGVVFAQRAF DHEQLRTFEL TLQARDQGSP
     ALSANVSLRV LVGDRNDNAP RVLYPALGPD GSALFDTVPR AAQPGYLVTK VVAVDADSGH
     NAWLSYHVVQ ASEPGLFSLG LRTGEVRMVR ALGDKDSVRQ RLLVAVRDGG QPPLSATATL
     HLVFADSLQE VLPDFSDHPT PSDSQAEMQF YLVVALALIS VLFLLAVILA IALRLRQSFS
     PTAGDCFESV LCSKSGPVGP PNYSEGTLPY AYNFCVPGDQ MNPEFNFFTS VDHCPATQDN
     LNKDSMLLAS ILTPSVEADK KILKQQAPPN TDWRFSQAQR PGTSGSQNGD DTGTWPNNQF
     DTEMLQAMIL ASASEAADGS STLGGGAGTM GLSARYGPQF TLQHVPDYRQ NVYIPGSNAT
     LTNAAGKRDG KAPAGGNGNK KKSGKKEKK
 
 
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