DJB11_RAT
ID DJB11_RAT Reviewed; 358 AA.
AC Q6TUG0;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=DnaJ homolog subfamily B member 11;
DE AltName: Full=ER-associated DNAJ;
DE AltName: Full=ER-associated Hsp40 co-chaperone;
DE AltName: Full=Endoplasmic reticulum DNA J domain-containing protein 3;
DE Short=ER-resident protein ERdj3;
DE Short=ERdj3;
DE Short=ERj3p;
DE AltName: Full=Liver regeneration-related protein LRRGT00084;
DE Flags: Precursor;
GN Name=Dnajb11;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RA Xu C.S., Chang C.F., Han H.P., Wang G.P., Chai L.Q., Yuan J.Y., Yang K.J.,
RA Zhao L.F., Ma H., Wang L., Wang S.F., Xing X.K., Shen G.M., Shi J.B.,
RA Rahman S., Wang Q.N., Zhang J.B.;
RT "Liver regeneration after PH.";
RL Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Thymus;
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 [3]
RP COMPONENT OF A CHAPERONE COMPLEX.
RX PubMed=12475965; DOI=10.1091/mbc.e02-05-0311;
RA Meunier L., Usherwood Y.-K., Chung K.T., Hendershot L.M.;
RT "A subset of chaperones and folding enzymes form multiprotein complexes in
RT endoplasmic reticulum to bind nascent proteins.";
RL Mol. Biol. Cell 13:4456-4469(2002).
CC -!- FUNCTION: As a co-chaperone for HSPA5 it is required for proper
CC folding, trafficking or degradation of proteins. Binds directly to both
CC unfolded proteins that are substrates for ERAD and nascent unfolded
CC peptide chains, but dissociates from the HSPA5-unfolded protein complex
CC before folding is completed. May help recruiting HSPA5 and other
CC chaperones to the substrate. Stimulates HSPA5 ATPase activity. It is
CC necessary for maturation and correct trafficking of PKD1.
CC {ECO:0000250|UniProtKB:Q9UBS4}.
CC -!- SUBUNIT: Part of a large chaperone multiprotein complex comprising
CC DNAJB11, HSP90B1, HSPA5, HYOU, PDIA2, PDIA4, PDIA6, PPIB, SDF2L1, UGGT1
CC and very small amounts of ERP29, but not, or at very low levels, CALR
CC nor CANX. Binds to denatured substrates in an ATP-independent manner.
CC Interacts via the J domain with HSPA5 in an ATP-dependent manner (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000250}.
CC -!- PTM: Contains high-mannose Endo H-sensitive carbohydrates.
CC {ECO:0000250}.
CC -!- PTM: Cys-169, Cys-171, Cys-193 and Cys-196 form intramolecular
CC disulfide bonds. The preferential partner for each Cys is not known (By
CC similarity). {ECO:0000250}.
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DR EMBL; AY387070; AAQ91040.1; -; mRNA.
DR EMBL; BC093384; AAH93384.1; -; mRNA.
DR RefSeq; NP_001015021.1; NM_001015021.1.
DR AlphaFoldDB; Q6TUG0; -.
DR SMR; Q6TUG0; -.
DR BioGRID; 262164; 1.
DR IntAct; Q6TUG0; 10.
DR MINT; Q6TUG0; -.
DR STRING; 10116.ENSRNOP00000002462; -.
DR GlyGen; Q6TUG0; 1 site.
DR jPOST; Q6TUG0; -.
DR PaxDb; Q6TUG0; -.
DR PRIDE; Q6TUG0; -.
DR Ensembl; ENSRNOT00000116132; ENSRNOP00000084615; ENSRNOG00000001803.
DR GeneID; 360734; -.
DR KEGG; rno:360734; -.
DR UCSC; RGD:1307373; rat.
DR CTD; 51726; -.
DR RGD; 1307373; Dnajb11.
DR eggNOG; KOG0713; Eukaryota.
DR GeneTree; ENSGT00940000155792; -.
DR HOGENOM; CLU_017633_0_0_1; -.
DR InParanoid; Q6TUG0; -.
DR OMA; WDAGFEF; -.
DR OrthoDB; 687505at2759; -.
DR PhylomeDB; Q6TUG0; -.
DR TreeFam; TF105144; -.
DR PRO; PR:Q6TUG0; -.
DR Proteomes; UP000002494; Chromosome 11.
DR Bgee; ENSRNOG00000001803; Expressed in pancreas and 20 other tissues.
DR Genevisible; Q6TUG0; RN.
DR GO; GO:0101031; C:chaperone complex; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0034663; C:endoplasmic reticulum chaperone complex; IDA:ParkinsonsUK-UCL.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0005615; C:extracellular space; ISO:RGD.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0051787; F:misfolded protein binding; ISO:RGD.
DR GO; GO:0005102; F:signaling receptor binding; ISO:RGD.
DR GO; GO:0051082; F:unfolded protein binding; ISO:RGD.
DR GO; GO:0016556; P:mRNA modification; ISO:RGD.
DR GO; GO:0050768; P:negative regulation of neurogenesis; ISO:RGD.
DR GO; GO:0032781; P:positive regulation of ATP-dependent activity; ISO:RGD.
DR GO; GO:0006457; P:protein folding; IEA:InterPro.
DR GO; GO:0051604; P:protein maturation; ISS:UniProtKB.
DR CDD; cd06257; DnaJ; 1.
DR Gene3D; 1.10.287.110; -; 1.
DR InterPro; IPR002939; DnaJ_C.
DR InterPro; IPR001623; DnaJ_domain.
DR InterPro; IPR018253; DnaJ_domain_CS.
DR InterPro; IPR008971; HSP40/DnaJ_pept-bd.
DR InterPro; IPR036869; J_dom_sf.
DR Pfam; PF00226; DnaJ; 1.
DR Pfam; PF01556; DnaJ_C; 1.
DR PRINTS; PR00625; JDOMAIN.
DR SMART; SM00271; DnaJ; 1.
DR SUPFAM; SSF46565; SSF46565; 1.
DR SUPFAM; SSF49493; SSF49493; 2.
DR PROSITE; PS00636; DNAJ_1; 1.
DR PROSITE; PS50076; DNAJ_2; 1.
PE 2: Evidence at transcript level;
KW Chaperone; Disulfide bond; Endoplasmic reticulum; Glycoprotein;
KW Phosphoprotein; Reference proteome; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000250"
FT CHAIN 23..358
FT /note="DnaJ homolog subfamily B member 11"
FT /id="PRO_0000324183"
FT DOMAIN 25..90
FT /note="J"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00286"
FT MOD_RES 188
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9UBS4"
FT CARBOHYD 261
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
SQ SEQUENCE 358 AA; 40495 MW; 25BBB32B17460C67 CRC64;
MAPQNLSTFC LLLLYLIGAV IAGRDFYKIL GVPRSASIKD IKKAYRKLAL QLHPDRNPDD
PQAQEKFQDL GAAYEVLSDS EKRKQYDTYG EEGLKDGHQS SHGDIFSHFF GDFGFMFGGA
PRQQDRNIPR GSDIIVDLEV TLEEVYAGNF VEVVRNKPVA RQAPGKRKCN CRQEMRTTQL
GPGRFQMTQE VVCDECPNVK LVNEERTLEV EIEPGVRDGM EYPFIGEGEP HVDGEPGDLR
FRIKVVKHRI FERRGDDLYT NVTVSLVEAL VGFEMDITHL DGHKVHISRD KITRPGAKLW
KKGEGLPNFD NNNIKGSLII TFDVDFPKEQ LTEEAKEGIK QLLKQGPVQK VYNGLQGY
