DJB11_MOUSE
ID DJB11_MOUSE Reviewed; 358 AA.
AC Q99KV1; A6X957; Q543I7; Q8BK79; Q8VCY1; Q8VHB1;
DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=DnaJ homolog subfamily B member 11;
DE AltName: Full=APOBEC1-binding protein 2;
DE Short=ABBP-2;
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ; TISSUE=Liver;
RX PubMed=11584023; DOI=10.1074/jbc.m109215200;
RA Lau P.P., Villanueva H., Kobayashi K., Nakamuta M., Chang B.H.-J., Chan L.;
RT "A DnaJ protein, apobec-1-binding protein-2, modulates apolipoprotein B
RT mRNA editing.";
RL J. Biol. Chem. 276:46445-46452(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Pancreas;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II, and FVB/N; TISSUE=Colon, and Mammary tumor;
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 [5]
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).
RN [6]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH DENATURED SUBSTRATES.
RX PubMed=15525676; DOI=10.1091/mbc.e04-05-0434;
RA Shen Y., Hendershot L.M.;
RT "ERdj3, a stress-inducible endoplasmic reticulum DnaJ homologue, serves as
RT a cofactor for BiP's interactions with unfolded substrates.";
RL Mol. Biol. Cell 16:40-50(2005).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Liver, Lung, Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 -!- INTERACTION:
CC Q99KV1; P20029: Hspa5; NbExp=4; IntAct=EBI-8328260, EBI-772325;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
CC {ECO:0000269|PubMed:15525676}.
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 -!- CAUTION: PubMed:11584023 reported a cytosolic, as well as nuclear
CC subcellular location. This result was obtained using an N-terminally
CC GFP-tagged construct which most probably affected signal peptide-driven
CC targeting to the ER. As a consequence, the in vivo revelance of the
CC observed interaction with APOBEC1, a nuclear protein, is dubious.
CC {ECO:0000305}.
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DR EMBL; AY054981; AAL17676.1; -; mRNA.
DR EMBL; AK050500; BAC34293.1; -; mRNA.
DR EMBL; AK075785; BAC35956.1; -; mRNA.
DR EMBL; AK075953; BAC36079.1; -; mRNA.
DR EMBL; AK148511; BAE28593.1; -; mRNA.
DR EMBL; AK166730; BAE38977.1; -; mRNA.
DR EMBL; CT027991; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC003999; AAH03999.1; -; mRNA.
DR EMBL; BC018282; AAH18282.1; -; mRNA.
DR EMBL; BC040747; AAH40747.1; -; mRNA.
DR CCDS; CCDS28070.1; -.
DR RefSeq; NP_001177733.1; NM_001190804.1.
DR RefSeq; NP_001177734.1; NM_001190805.1.
DR RefSeq; NP_080676.3; NM_026400.5.
DR AlphaFoldDB; Q99KV1; -.
DR SMR; Q99KV1; -.
DR BioGRID; 212468; 26.
DR CORUM; Q99KV1; -.
DR DIP; DIP-60531N; -.
DR IntAct; Q99KV1; 8.
DR MINT; Q99KV1; -.
DR STRING; 10090.ENSMUSP00000126828; -.
DR GlyGen; Q99KV1; 1 site.
DR iPTMnet; Q99KV1; -.
DR PhosphoSitePlus; Q99KV1; -.
DR REPRODUCTION-2DPAGE; Q99KV1; -.
DR EPD; Q99KV1; -.
DR jPOST; Q99KV1; -.
DR MaxQB; Q99KV1; -.
DR PaxDb; Q99KV1; -.
DR PeptideAtlas; Q99KV1; -.
DR PRIDE; Q99KV1; -.
DR ProteomicsDB; 277457; -.
DR DNASU; 67838; -.
DR Ensembl; ENSMUST00000004574; ENSMUSP00000004574; ENSMUSG00000004460.
DR Ensembl; ENSMUST00000166487; ENSMUSP00000126828; ENSMUSG00000004460.
DR Ensembl; ENSMUST00000178320; ENSMUSP00000137542; ENSMUSG00000004460.
DR GeneID; 67838; -.
DR KEGG; mmu:67838; -.
DR UCSC; uc007yso.2; mouse.
DR CTD; 51726; -.
DR MGI; MGI:1915088; Dnajb11.
DR VEuPathDB; HostDB:ENSMUSG00000004460; -.
DR eggNOG; KOG0713; Eukaryota.
DR GeneTree; ENSGT00940000155792; -.
DR HOGENOM; CLU_017633_0_0_1; -.
DR InParanoid; Q99KV1; -.
DR OMA; WDAGFEF; -.
DR OrthoDB; 687505at2759; -.
DR PhylomeDB; Q99KV1; -.
DR TreeFam; TF105144; -.
DR BioGRID-ORCS; 67838; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Dnajb11; mouse.
DR PRO; PR:Q99KV1; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q99KV1; protein.
DR Bgee; ENSMUSG00000004460; Expressed in ileal epithelium and 260 other tissues.
DR ExpressionAtlas; Q99KV1; baseline and differential.
DR Genevisible; Q99KV1; MM.
DR GO; GO:0101031; C:chaperone complex; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0034663; C:endoplasmic reticulum chaperone complex; ISO:MGI.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0005615; C:extracellular space; IDA:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0051787; F:misfolded protein binding; ISO:MGI.
DR GO; GO:0005102; F:signaling receptor binding; IPI:MGI.
DR GO; GO:0051082; F:unfolded protein binding; IDA:MGI.
DR GO; GO:0016556; P:mRNA modification; IDA:MGI.
DR GO; GO:0050768; P:negative regulation of neurogenesis; IMP:MGI.
DR GO; GO:0032781; P:positive regulation of ATP-dependent activity; ISO:MGI.
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 1: Evidence at protein 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_0000007261"
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"
FT CONFLICT 9
FT /note="F -> L (in Ref. 2; BAC35956)"
FT /evidence="ECO:0000305"
FT CONFLICT 88
FT /note="T -> A (in Ref. 4; AAH18282)"
FT /evidence="ECO:0000305"
FT CONFLICT 217
FT /note="R -> L (in Ref. 1; AAL17676)"
FT /evidence="ECO:0000305"
FT CONFLICT 240
FT /note="R -> P (in Ref. 1; AAL17676)"
FT /evidence="ECO:0000305"
FT CONFLICT 255
FT /note="G -> E (in Ref. 2; BAC35956)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 358 AA; 40555 MW; E53CE0B3DF7465B8 CRC64;
MAPQNLSTFC LLLLYLIGTV IAGRDFYKIL GVPRSASIKD IKKAYRKLAL QLHPDRNPDD
PQAQEKFQDL GAAYEVLSDS EKRKQYDTYG EEGLKDGHQS SHGDIFSHFF GDFGFMFGGT
PRQQDRNIPR GSDIIVDLEV TLEEVYAGNF VEVVRNKPVA RQAPGKRKCN CRQEMRTTQL
GPGRFQMTQE VVCDECPNVK LVNEERTLEV EIEPGVRDGM EYPFIGEGEP HVDGEPGDLR
FRIKVVKHRI FERRGDDLYT NVTVSLVEAL VGFEMDITHL DGHKVHISRD KITRPGAKLW
KKGEGLPNFD NNNIKGSLII TFDVDFPKEQ LTEEAKEGIK QLLKQGPVQK VYNGLQGY
