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DNJ1_CAEEL
ID   DNJ1_CAEEL              Reviewed;         401 AA.
AC   Q17438; K8ESE7;
DT   12-APR-2017, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 144.
DE   RecName: Full=DnaJ homolog subfamily B member 1 {ECO:0000305};
GN   Name=dnj-1 {ECO:0000312|WormBase:B0035.14a};
GN   ORFNames=B0035.14 {ECO:0000312|WormBase:B0035.14a};
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
RN   [2]
RP   FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, AND TISSUE SPECIFICITY.
RX   PubMed=27916661; DOI=10.1016/j.molcel.2016.10.027;
RA   Li K., Jiang Q., Bai X., Yang Y.F., Ruan M.Y., Cai S.Q.;
RT   "Tetrameric assembly of K(+) channels requires ER-located chaperone
RT   proteins.";
RL   Mol. Cell 65:52-65(2017).
CC   -!- FUNCTION: Acts as a co-chaperone with Hsp70 required to promote protein
CC       folding and trafficking, prevent aggregation of client proteins, and
CC       promote unfolded proteins to endoplasmic reticulum-associated
CC       degradation (ERAD) pathway (By similarity). Acts by determining Hsp70's
CC       ATPase and polypeptide-binding activities (By similarity). Can also act
CC       as a chaperone that promotes maturation of potassium channel unc-103 by
CC       stabilizing nascent channel subunits and assembling them into tetramers
CC       (PubMed:27916661). {ECO:0000250|UniProtKB:Q9NXW2,
CC       ECO:0000269|PubMed:27916661}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000269|PubMed:27916661}; Single-pass membrane protein
CC       {ECO:0000255}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q17438-1; Sequence=Displayed;
CC       Name=b;
CC         IsoId=Q17438-2; Sequence=VSP_058895;
CC   -!- TISSUE SPECIFICITY: Expressed in many head neurons, vulva muscles and
CC       some tail neurons. {ECO:0000269|PubMed:27916661}.
CC   -!- SIMILARITY: Belongs to the DnaJ family. DNAJB12/DNAJB14 subfamily.
CC       {ECO:0000305}.
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DR   EMBL; BX284604; CAA97416.1; -; Genomic_DNA.
DR   EMBL; BX284604; CCO25610.1; -; Genomic_DNA.
DR   PIR; T18661; T18661.
DR   RefSeq; NP_001263785.1; NM_001276856.1. [Q17438-2]
DR   RefSeq; NP_502122.1; NM_069721.6. [Q17438-1]
DR   AlphaFoldDB; Q17438; -.
DR   SMR; Q17438; -.
DR   STRING; 6239.B0035.14a.2; -.
DR   EPD; Q17438; -.
DR   PaxDb; Q17438; -.
DR   PeptideAtlas; Q17438; -.
DR   EnsemblMetazoa; B0035.14a.1; B0035.14a.1; WBGene00001019. [Q17438-1]
DR   EnsemblMetazoa; B0035.14b.1; B0035.14b.1; WBGene00001019. [Q17438-2]
DR   GeneID; 178040; -.
DR   KEGG; cel:CELE_B0035.14; -.
DR   UCSC; B0035.14.1; c. elegans. [Q17438-1]
DR   CTD; 178040; -.
DR   WormBase; B0035.14a; CE05169; WBGene00001019; dnj-1. [Q17438-1]
DR   WormBase; B0035.14b; CE47882; WBGene00001019; dnj-1. [Q17438-2]
DR   eggNOG; KOG0714; Eukaryota.
DR   GeneTree; ENSGT00940000168650; -.
DR   HOGENOM; CLU_043579_3_0_1; -.
DR   InParanoid; Q17438; -.
DR   OMA; VRVHQFG; -.
DR   OrthoDB; 1173544at2759; -.
DR   PhylomeDB; Q17438; -.
DR   PRO; PR:Q17438; -.
DR   Proteomes; UP000001940; Chromosome IV.
DR   Bgee; WBGene00001019; Expressed in germ line (C elegans) and 4 other tissues.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0030544; F:Hsp70 protein binding; IBA:GO_Central.
DR   GO; GO:0071218; P:cellular response to misfolded protein; IBA:GO_Central.
DR   GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; IBA:GO_Central.
DR   GO; GO:0065003; P:protein-containing complex assembly; IMP:UniProtKB.
DR   GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IBA:GO_Central.
DR   CDD; cd06257; DnaJ; 1.
DR   Gene3D; 1.10.287.110; -; 1.
DR   InterPro; IPR001623; DnaJ_domain.
DR   InterPro; IPR018253; DnaJ_domain_CS.
DR   InterPro; IPR015399; DUF1977_DnaJ-like.
DR   InterPro; IPR036869; J_dom_sf.
DR   Pfam; PF00226; DnaJ; 1.
DR   Pfam; PF09320; DUF1977; 1.
DR   PRINTS; PR00625; JDOMAIN.
DR   SMART; SM00271; DnaJ; 1.
DR   SUPFAM; SSF46565; SSF46565; 1.
DR   PROSITE; PS00636; DNAJ_1; 1.
DR   PROSITE; PS50076; DNAJ_2; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Chaperone; Endoplasmic reticulum; Membrane;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..401
FT                   /note="DnaJ homolog subfamily B member 1"
FT                   /id="PRO_0000439644"
FT   TOPO_DOM        1..278
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305|PubMed:27916661"
FT   TRANSMEM        279..299
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        300..401
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305|PubMed:27916661"
FT   DOMAIN          137..201
FT                   /note="J"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00286"
FT   REGION          50..122
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        50..71
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        72..110
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         1..355
FT                   /note="Missing (in isoform b)"
FT                   /id="VSP_058895"
SQ   SEQUENCE   401 AA;  46582 MW;  74E2170B3BADBD5A CRC64;
     MTADANKSES LLCMDKAREA IKSGDTDKAR RMLLKAKKLD PGQNIEFLTK KIDDMTNNTS
     SSSQTSSSRA SEERSYAHDD HYDDPNLRNR KARSPVKKNG KTEPEPKQRS ASRTPKLGVD
     YTSEQKELVE RIRHCKDYYE ILKIDKKASD DDIRKEYRKL ALKLHPDKCR APHATEAFKA
     LGNAYAVLSD TDKRRQYDQY GAEAANSHTP TTRRRGGGHG AFFEHDYAHG FEAEFTPEEI
     FNMFFGGGFP TEQVRRRARY AQQQQYHHYE QQQSPYGPLL QLLPLIAIMV IGLLAQLMVG
     EPAYSLHQTS KFTIKRLTAD LRVPYFVRTD FETSYRGRIR QVEQQVEDDY IQNLRMNCYK
     EQNLKETKLY RARWMRDEAM MRDAERTPLP SCIRLNEIYS H
 
 
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