ID   DJB11_PONAB             Reviewed;         358 AA.
AC   Q5RAJ6;
DT   12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 97.
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   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) 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,
CC       UGT1A1 and very small amounts of ERP29, but not, or at very low levels,
CC       CALR nor CANX. Binds to denatured substrates in an ATP-independent
CC       manner. Interacts via the J domain with HSPA5 in an ATP-dependent
CC       manner (By 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; CR859019; CAH91214.1; -; mRNA.
DR   RefSeq; XP_002814428.1; XM_002814382.3.
DR   AlphaFoldDB; Q5RAJ6; -.
DR   SMR; Q5RAJ6; -.
DR   STRING; 9601.ENSPPYP00000016085; -.
DR   GeneID; 100462077; -.
DR   KEGG; pon:100462077; -.
DR   CTD; 51726; -.
DR   eggNOG; KOG0713; Eukaryota.
DR   HOGENOM; CLU_017633_0_0_1; -.
DR   InParanoid; Q5RAJ6; -.
DR   OMA; WDAGFEF; -.
DR   OrthoDB; 687505at2759; -.
DR   TreeFam; TF105144; -.
DR   Proteomes; UP000001595; Chromosome 3.
DR   GO; GO:0101031; C:chaperone complex; IEA:Ensembl.
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; IEA:Ensembl.
DR   GO; GO:0005102; F:signaling receptor binding; IEA:Ensembl.
DR   GO; GO:0051082; F:unfolded protein binding; IEA:Ensembl.
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_0000290020"
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;  40514 MW;  580CC4D66A06B734 CRC64;
     MAPQNLSTFC LLLLYLIGAV IAGRDFYKIL GVPRSASIKD IKKAYRKLAL QLHPDRNPDD
     PQAQEKFQDL GAAYEVLSDS EKRKQYDTYG EEGLKDGHQS SHGDIFSHFF GDFGFMFGGT
     PRQQDRNIPR GSDIIVDLEV TLEEVYAGNF VEVVRNKPVA RQAPGKRKCN CRQEMRTTQL
     GPGRFQMTQE VVCDECPNVK LVNEERTLEV EIEPGVRDGM EYPFIGEGEP HVDGEPGDLR
     FRIKVVKHPI FERRGDDLYT NVTISLVESL VGFEMDITHL DGHKVHISRD KITRPGAKLW
     KKGEGLPNFD NNNIKGSLII TFDVDFPKEQ LTEEAREGIK QLLKQGSVQK VYNGLQGY