ID   DJB11_BOVIN             Reviewed;         358 AA.
AC   Q3ZBA6;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 106.
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   Flags: Precursor;
GN   Name=DNAJB11;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Uterus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BC103470; AAI03471.1; -; mRNA.
DR   RefSeq; NP_001029440.1; NM_001034268.1.
DR   RefSeq; XP_005201525.1; XM_005201468.2.
DR   AlphaFoldDB; Q3ZBA6; -.
DR   SMR; Q3ZBA6; -.
DR   STRING; 9913.ENSBTAP00000004094; -.
DR   PaxDb; Q3ZBA6; -.
DR   PeptideAtlas; Q3ZBA6; -.
DR   PRIDE; Q3ZBA6; -.
DR   Ensembl; ENSBTAT00000004094; ENSBTAP00000004094; ENSBTAG00000003151.
DR   GeneID; 506316; -.
DR   KEGG; bta:506316; -.
DR   CTD; 51726; -.
DR   VEuPathDB; HostDB:ENSBTAG00000003151; -.
DR   eggNOG; KOG0713; Eukaryota.
DR   GeneTree; ENSGT00940000155792; -.
DR   HOGENOM; CLU_017633_0_0_1; -.
DR   InParanoid; Q3ZBA6; -.
DR   OMA; WDAGFEF; -.
DR   OrthoDB; 687505at2759; -.
DR   TreeFam; TF105144; -.
DR   Proteomes; UP000009136; Chromosome 1.
DR   Bgee; ENSBTAG00000003151; Expressed in semen and 105 other tissues.
DR   GO; GO:0101031; C:chaperone complex; IEA:Ensembl.
DR   GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR   GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR   GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR   GO; GO:0051787; F:misfolded protein binding; IBA:GO_Central.
DR   GO; GO:0005102; F:signaling receptor binding; IEA:Ensembl.
DR   GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR   GO; GO:0016556; P:mRNA modification; IEA:Ensembl.
DR   GO; GO:0050768; P:negative regulation of neurogenesis; IEA:Ensembl.
DR   GO; GO:0032781; P:positive regulation of ATP-dependent activity; IEA:Ensembl.
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_0000284954"
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;  40504 MW;  DE20440D03A1197D CRC64;
     MAPQNLGTFC LLLLYLIGTV IAGRDFYKIL GVPRSASIKD IKKAYRKLAL QLHPDRNPDD
     PRAQEKFQDL GAAYEVLSDS EKRKQYDTYG EEGLKDGHQS SHGDIFSHFF GDFGFMFGGT
     PRQQDRNIPR GSDIIVDLEV TLEEVYAGNF VEVVRNKPVA RQAPGKRKCN CRQEMRTTQL
     GPGRFQMTQE VVCDECPNVK LVNEERTLEV EIEPGVRDGM EYPFIGEGEP HVDGEPGDLR
     FRIKVVKHSI FERRGDDLYT NVTISLVESL VGFDMDITHL DGHKVHISRD KITRPGAKLW
     KKGEGLPNFD NNNIKGSLII TFDVDFPKEQ LSEEAREGIK QLLKQGSVQK VYNGLQGY