DNJB9_MOUSE
ID DNJB9_MOUSE Reviewed; 222 AA.
AC Q9QYI6; Q5D0C3; Q9DAW1;
DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 2.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=DnaJ homolog subfamily B member 9 {ECO:0000305};
DE AltName: Full=Endoplasmic reticulum DNA J domain-containing protein 4 {ECO:0000303|PubMed:11836248};
DE Short=ER-resident protein ERdj4 {ECO:0000303|PubMed:11836248};
DE Short=ERdj4 {ECO:0000303|PubMed:11836248};
DE AltName: Full=mDj7 {ECO:0000303|PubMed:11147971};
DE Flags: Precursor;
GN Name=Dnajb9 {ECO:0000312|MGI:MGI:1351618};
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=C57BL/6J;
RX PubMed=11147971; DOI=10.1379/1466-1268(2000)005<0098:mhdhco>2.0.co;2;
RA Ohtsuka K., Hata M.;
RT "Mammalian HSP40/DNAJ homologs: cloning of novel cDNAs and a proposal for
RT their classification and nomenclature.";
RL Cell Stress Chaperones 5:98-112(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Placenta;
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 MRNA].
RA Ebert L., Muenstermann E., Schatten R., Henze S., Bohn E., Mollenhauer J.,
RA Wiemann S., Schick M., Korn B.;
RT "Cloning of mouse full open reading frames in Gateway(R) system entry
RT vector (pDONR201).";
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Mammary gland, 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 [6]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH HSPA5, AND MUTAGENESIS OF
RP HIS-54.
RX PubMed=11836248; DOI=10.1074/jbc.m112214200;
RA Shen Y., Meunier L., Hendershot L.M.;
RT "Identification and characterization of a novel endoplasmic reticulum (ER)
RT DnaJ homologue, which stimulates ATPase activity of BiP in vitro and is
RT induced by ER stress.";
RL J. Biol. Chem. 277:15947-15956(2002).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver, 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).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH DERL1.
RX PubMed=22267725; DOI=10.1074/jbc.m111.311290;
RA Lai C.W., Otero J.H., Hendershot L.M., Snapp E.;
RT "ERdj4 protein is a soluble endoplasmic reticulum (ER) DnaJ family protein
RT that interacts with ER-associated degradation machinery.";
RL J. Biol. Chem. 287:7969-7978(2012).
RN [9]
RP DISRUPTION PHENOTYPE.
RX PubMed=24336520; DOI=10.1091/mbc.e13-06-0319;
RA Fritz J.M., Dong M., Apsley K.S., Martin E.P., Na C.L., Sitaraman S.,
RA Weaver T.E.;
RT "Deficiency of the BiP cochaperone ERdj4 causes constitutive endoplasmic
RT reticulum stress and metabolic defects.";
RL Mol. Biol. Cell 25:431-440(2014).
RN [10]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=25222125; DOI=10.1371/journal.pone.0107473;
RA Fritz J.M., Weaver T.E.;
RT "The BiP cochaperone ERdj4 is required for B cell development and
RT function.";
RL PLoS ONE 9:E107473-E107473(2014).
RN [11]
RP DOMAIN.
RX PubMed=27546788; DOI=10.1016/j.molcel.2016.07.012;
RA Behnke J., Mann M.J., Scruggs F.L., Feige M.J., Hendershot L.M.;
RT "Members of the Hsp70 family recognize distinct types of sequences to
RT execute er quality control.";
RL Mol. Cell 63:739-752(2016).
CC -!- FUNCTION: Co-chaperone for Hsp70 protein HSPA5/BiP that acts as a key
CC repressor of the ERN1/IRE1-mediated unfolded protein response (UPR) (By
CC similarity). J domain-containing co-chaperones stimulate the ATPase
CC activity of Hsp70 proteins and are required for efficient substrate
CC recognition by Hsp70 proteins (PubMed:11836248). In the unstressed
CC endoplasmic reticulum, interacts with the luminal region of ERN1/IRE1
CC and selectively recruits HSPA5/BiP: HSPA5/BiP disrupts the dimerization
CC of the active ERN1/IRE1 luminal region, thereby inactivating ERN1/IRE1
CC (By similarity). Also involved in endoplasmic reticulum-associated
CC degradation (ERAD) of misfolded proteins (PubMed:22267725). Required
CC for survival of B-cell progenitors and normal antibody production
CC (PubMed:25222125). {ECO:0000250|UniProtKB:G3H0N9,
CC ECO:0000269|PubMed:11836248, ECO:0000269|PubMed:22267725,
CC ECO:0000269|PubMed:25222125}.
CC -!- SUBUNIT: Interacts with HSPA5/BiP; interaction is direct
CC (PubMed:11836248). Interacts with ERN1/IRE1 (via the luminal region)
CC (By similarity). Interacts with DERL1 (PubMed:22267725).
CC {ECO:0000250|UniProtKB:G3H0N9, ECO:0000269|PubMed:11836248,
CC ECO:0000269|PubMed:22267725}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
CC {ECO:0000269|PubMed:22267725, ECO:0000305|PubMed:11836248}.
CC -!- DOMAIN: The J domain stimulates the ATPase activity of HSPA5/BiP, while
CC the divergent targeting domain is required for efficient substrate
CC recognition by HSPA5/BiP. The divergent targeting domain specifically
CC recognizes and binds to aggregation-prone sequences.
CC {ECO:0000269|PubMed:27546788}.
CC -!- PTM: Not N-glycosylated. {ECO:0000269|PubMed:11836248}.
CC -!- DISRUPTION PHENOTYPE: Perinatal death in approximately half of knockout
CC mice (PubMed:24336520). Death is caused by fetal growth restriction,
CC reduced hepatic glycogen stores and hypoglycemia (PubMed:24336520).
CC Surviving adult mice display constitutive endoplasmic reticulum stress
CC in multiple cells and tissues (PubMed:24336520). Elevated endoplasmic
CC reticulum stress in pancreatic beta cells is associated with beta cell
CC loss, hypoinsulinemia and glucose intolerance (PubMed:24336520)
CC Conditional knockout mice lacking Dnajb9 in bone marrow show impaired
CC hematopoiesis: the number of myeloid cells is increased, while the
CC number of erythroid and B lymphoid cells is reduced (PubMed:25222125).
CC B-cell defects cause decreased survival of B-cell precursors, including
CC large and small pre-B, and immature B-cells (PubMed:25222125).
CC {ECO:0000269|PubMed:24336520, ECO:0000269|PubMed:25222125}.
CC -!- CAUTION: Was initially thought to be an integral membrane protein
CC (PubMed:11836248). However, it was later shown that it is a soluble
CC luminal protein localized in the endoplasmic reticulum lumen.
CC {ECO:0000269|PubMed:11836248, ECO:0000269|PubMed:22267725}.
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DR EMBL; AB028857; BAA88305.1; -; mRNA.
DR EMBL; AK005475; BAB24065.1; -; mRNA.
DR EMBL; CT010304; CAJ18512.1; -; mRNA.
DR EMBL; CT010444; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC042713; AAH42713.1; -; mRNA.
DR EMBL; BC096676; AAH96676.1; -; mRNA.
DR CCDS; CCDS25897.1; -.
DR RefSeq; NP_038788.2; NM_013760.4.
DR AlphaFoldDB; Q9QYI6; -.
DR SMR; Q9QYI6; -.
DR BioGRID; 205171; 3.
DR STRING; 10090.ENSMUSP00000015049; -.
DR iPTMnet; Q9QYI6; -.
DR PhosphoSitePlus; Q9QYI6; -.
DR EPD; Q9QYI6; -.
DR MaxQB; Q9QYI6; -.
DR PaxDb; Q9QYI6; -.
DR PeptideAtlas; Q9QYI6; -.
DR PRIDE; Q9QYI6; -.
DR ProteomicsDB; 277351; -.
DR Antibodypedia; 31469; 238 antibodies from 32 providers.
DR DNASU; 27362; -.
DR Ensembl; ENSMUST00000015049; ENSMUSP00000015049; ENSMUSG00000014905.
DR GeneID; 27362; -.
DR KEGG; mmu:27362; -.
DR UCSC; uc007nlo.1; mouse.
DR CTD; 4189; -.
DR MGI; MGI:1351618; Dnajb9.
DR VEuPathDB; HostDB:ENSMUSG00000014905; -.
DR eggNOG; KOG0714; Eukaryota.
DR GeneTree; ENSGT00940000156246; -.
DR HOGENOM; CLU_077239_0_0_1; -.
DR InParanoid; Q9QYI6; -.
DR OMA; HFDSHFQ; -.
DR OrthoDB; 1173544at2759; -.
DR PhylomeDB; Q9QYI6; -.
DR TreeFam; TF105143; -.
DR BioGRID-ORCS; 27362; 6 hits in 74 CRISPR screens.
DR ChiTaRS; Dnajb9; mouse.
DR PRO; PR:Q9QYI6; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q9QYI6; protein.
DR Bgee; ENSMUSG00000014905; Expressed in seminal vesicle and 262 other tissues.
DR ExpressionAtlas; Q9QYI6; baseline and differential.
DR Genevisible; Q9QYI6; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0051087; F:chaperone binding; IDA:UniProtKB.
DR GO; GO:0030544; F:Hsp70 protein binding; IPI:UniProtKB.
DR GO; GO:0051787; F:misfolded protein binding; ISO:MGI.
DR GO; GO:0030183; P:B cell differentiation; IMP:UniProtKB.
DR GO; GO:1903895; P:negative regulation of IRE1-mediated unfolded protein response; ISS:UniProtKB.
DR GO; GO:0002639; P:positive regulation of immunoglobulin production; IMP:UniProtKB.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; IDA:UniProtKB.
DR GO; GO:0006986; P:response to unfolded protein; IEA:UniProtKB-KW.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IDA:UniProtKB.
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; IPR036869; J_dom_sf.
DR Pfam; PF00226; DnaJ; 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 Chaperone; Endoplasmic reticulum; Phosphoprotein; Reference proteome;
KW Signal; Unfolded protein response.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..222
FT /note="DnaJ homolog subfamily B member 9"
FT /id="PRO_0000071032"
FT DOMAIN 26..90
FT /note="J"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00286"
FT REGION 91..222
FT /note="Divergent targeting domain"
FT /evidence="ECO:0000305"
FT MOD_RES 133
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UBS3"
FT MUTAGEN 54
FT /note="H->Q: Abolishes ability to stimulate ATPase activity
FT of HSPA5/BiP."
FT /evidence="ECO:0000269|PubMed:11836248"
FT CONFLICT 133
FT /note="S -> F (in Ref. 1; BAA88305)"
FT /evidence="ECO:0000305"
FT CONFLICT 148
FT /note="S -> F (in Ref. 1; BAA88305)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 222 AA; 25616 MW; 4A737D704E760069 CRC64;
MATPQSVFVF AICILMITEL ILASKSYYDI LGVPKSASER QIKKAFHKLA MKYHPDKNKS
PDAEAKFREI AEAYETLSDA NSRKEYDTIG HSAFTNGKGQ RGNGSPFEQS FNFNFDDLFK
DFNFFGQNQN TRSKKHFENH FHTRQDGSSR QRHHFQEFSF GGGLFDDMFE DMEKMFSFSG
FDTTNRHTVQ TENRFHGSSK HCRTVTQRRG NMVTTYTDCS GQ
