DNJA1_MOUSE
ID DNJA1_MOUSE Reviewed; 397 AA.
AC P63037; P54102;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 31-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=DnaJ homolog subfamily A member 1;
DE AltName: Full=DnaJ protein homolog 2;
DE AltName: Full=Heat shock 40 kDa protein 4;
DE AltName: Full=Heat shock protein J2;
DE Short=HSJ-2;
DE Flags: Precursor;
GN Name=Dnaja1; Synonyms=Dnaj2, Hsj2, Hspf4;
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].
RX PubMed=9799614; DOI=10.1006/geno.1998.5501;
RA Royaux I., Minner F., Goffinet A.M., de Rouvroit C.L.;
RT "A DnaJ-like gene, Hsj2, maps to mouse chromosome 5, at approximately 24 cM
RT from the centromere.";
RL Genomics 53:415-415(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Spinal cord;
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].
RC STRAIN=FVB/N; TISSUE=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 [4]
RP PROTEIN SEQUENCE OF 106-124 AND 375-389, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Hippocampus;
RA Lubec G., Klug S.;
RL Submitted (MAR-2007) to UniProtKB.
RN [5]
RP FUNCTION, SUBUNIT, AND IDENTIFICATION IN A COMPLEX WITH HSPA1B AND BAX.
RX PubMed=14752510; DOI=10.1038/sj.cdd.4401369;
RA Gotoh T., Terada K., Oyadomari S., Mori M.;
RT "hsp70-DnaJ chaperone pair prevents nitric oxide- and CHOP-induced
RT apoptosis by inhibiting translocation of Bax to mitochondria.";
RL Cell Death Differ. 11:390-402(2004).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-335, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC 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: Co-chaperone for HSPA8/Hsc70. Plays a role in protein
CC transport into mitochondria via its role as co-chaperone. Stimulates
CC ATP hydrolysis, but not the folding of unfolded proteins mediated by
CC HSPA1A (in vitro). Promotes apoptosis in response to cellular stress
CC mediated by exposure to anisomycin or UV (By similarity). Functions as
CC co-chaperone for HSPA1B and negatively regulates the translocation of
CC BAX from the cytosol to mitochondria in response to cellular stress,
CC thereby protecting cells against apoptosis. {ECO:0000250,
CC ECO:0000269|PubMed:14752510}.
CC -!- SUBUNIT: Identified in a complex with HSPA1B and BAX (PubMed:14752510).
CC Interacts with RNF207 (By similarity). {ECO:0000250|UniProtKB:P31689,
CC ECO:0000269|PubMed:14752510}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Lipid-anchor
CC {ECO:0000250}. Cytoplasm {ECO:0000250}. Microsome {ECO:0000250}.
CC Mitochondrion {ECO:0000250}. Nucleus {ECO:0000250}. Cytoplasm,
CC perinuclear region {ECO:0000250}. Note=Primarily cytoplasmic and
CC associated with microsomes. A minor proportion is associated with
CC nuclei and mitochondria (By similarity). {ECO:0000250}.
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DR EMBL; AF055664; AAC78597.1; -; mRNA.
DR EMBL; AK083046; BAC38744.1; -; mRNA.
DR EMBL; BC057876; AAH57876.1; -; mRNA.
DR CCDS; CCDS18049.1; -.
DR RefSeq; NP_001158143.1; NM_001164671.2.
DR RefSeq; NP_001158144.1; NM_001164672.2.
DR RefSeq; NP_032324.1; NM_008298.6.
DR AlphaFoldDB; P63037; -.
DR BMRB; P63037; -.
DR SMR; P63037; -.
DR BioGRID; 200446; 34.
DR DIP; DIP-32350N; -.
DR IntAct; P63037; 15.
DR MINT; P63037; -.
DR STRING; 10090.ENSMUSP00000030118; -.
DR iPTMnet; P63037; -.
DR PhosphoSitePlus; P63037; -.
DR EPD; P63037; -.
DR jPOST; P63037; -.
DR PaxDb; P63037; -.
DR PeptideAtlas; P63037; -.
DR PRIDE; P63037; -.
DR ProteomicsDB; 279741; -.
DR Antibodypedia; 675; 294 antibodies from 32 providers.
DR DNASU; 15502; -.
DR Ensembl; ENSMUST00000030118; ENSMUSP00000030118; ENSMUSG00000028410.
DR Ensembl; ENSMUST00000164233; ENSMUSP00000129730; ENSMUSG00000028410.
DR GeneID; 15502; -.
DR KEGG; mmu:15502; -.
DR UCSC; uc008sht.2; mouse.
DR CTD; 3301; -.
DR MGI; MGI:1270129; Dnaja1.
DR VEuPathDB; HostDB:ENSMUSG00000028410; -.
DR eggNOG; KOG0712; Eukaryota.
DR GeneTree; ENSGT00940000153558; -.
DR HOGENOM; CLU_017633_10_0_1; -.
DR InParanoid; P63037; -.
DR OMA; GMSAFNG; -.
DR OrthoDB; 1012379at2759; -.
DR PhylomeDB; P63037; -.
DR TreeFam; TF105141; -.
DR Reactome; R-MMU-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand.
DR BioGRID-ORCS; 15502; 12 hits in 76 CRISPR screens.
DR ChiTaRS; Dnaja1; mouse.
DR PRO; PR:P63037; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; P63037; protein.
DR Bgee; ENSMUSG00000028410; Expressed in undifferentiated genital tubercle and 277 other tissues.
DR ExpressionAtlas; P63037; baseline and differential.
DR Genevisible; P63037; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0015630; C:microtubule cytoskeleton; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0001671; F:ATPase activator activity; ISS:UniProtKB.
DR GO; GO:0055131; F:C3HC4-type RING finger domain binding; ISO:MGI.
DR GO; GO:0051087; F:chaperone binding; ISS:UniProtKB.
DR GO; GO:0001664; F:G protein-coupled receptor binding; ISO:MGI.
DR GO; GO:0030544; F:Hsp70 protein binding; ISS:UniProtKB.
DR GO; GO:0050750; F:low-density lipoprotein particle receptor binding; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030957; F:Tat protein binding; ISO:MGI.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
DR GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR GO; GO:0030521; P:androgen receptor signaling pathway; IMP:MGI.
DR GO; GO:0030317; P:flagellated sperm motility; IMP:MGI.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:1903748; P:negative regulation of establishment of protein localization to mitochondrion; ISO:MGI.
DR GO; GO:0043508; P:negative regulation of JUN kinase activity; ISS:UniProtKB.
DR GO; GO:1905259; P:negative regulation of nitrosative stress-induced intrinsic apoptotic signaling pathway; ISO:MGI.
DR GO; GO:0031397; P:negative regulation of protein ubiquitination; ISO:MGI.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0070585; P:protein localization to mitochondrion; ISS:UniProtKB.
DR GO; GO:0042026; P:protein refolding; IBA:GO_Central.
DR GO; GO:0051223; P:regulation of protein transport; ISS:UniProtKB.
DR GO; GO:0009408; P:response to heat; IEA:InterPro.
DR GO; GO:0007283; P:spermatogenesis; IMP:MGI.
DR GO; GO:1901998; P:toxin transport; IMP:MGI.
DR CDD; cd06257; DnaJ; 1.
DR CDD; cd10719; DnaJ_zf; 1.
DR Gene3D; 1.10.287.110; -; 1.
DR HAMAP; MF_01152; DnaJ; 1.
DR InterPro; IPR012724; DnaJ.
DR InterPro; IPR002939; DnaJ_C.
DR InterPro; IPR001623; DnaJ_domain.
DR InterPro; IPR018253; DnaJ_domain_CS.
DR InterPro; IPR044713; DNJA1/2-like.
DR InterPro; IPR008971; HSP40/DnaJ_pept-bd.
DR InterPro; IPR001305; HSP_DnaJ_Cys-rich_dom.
DR InterPro; IPR036410; HSP_DnaJ_Cys-rich_dom_sf.
DR InterPro; IPR036869; J_dom_sf.
DR PANTHER; PTHR43888; PTHR43888; 1.
DR Pfam; PF00226; DnaJ; 1.
DR Pfam; PF01556; DnaJ_C; 1.
DR Pfam; PF00684; DnaJ_CXXCXGXG; 1.
DR PRINTS; PR00625; JDOMAIN.
DR SMART; SM00271; DnaJ; 1.
DR SUPFAM; SSF46565; SSF46565; 1.
DR SUPFAM; SSF49493; SSF49493; 2.
DR SUPFAM; SSF57938; SSF57938; 1.
DR PROSITE; PS00636; DNAJ_1; 1.
DR PROSITE; PS50076; DNAJ_2; 1.
DR PROSITE; PS51188; ZF_CR; 1.
PE 1: Evidence at protein level;
KW Acetylation; Chaperone; Cytoplasm; Direct protein sequencing;
KW Endoplasmic reticulum; Lipoprotein; Membrane; Metal-binding; Methylation;
KW Microsome; Mitochondrion; Nucleus; Phosphoprotein; Prenylation;
KW Reference proteome; Repeat; Zinc; Zinc-finger.
FT CHAIN 1..394
FT /note="DnaJ homolog subfamily A member 1"
FT /id="PRO_0000071009"
FT PROPEP 395..397
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000396753"
FT DOMAIN 6..68
FT /note="J"
FT REPEAT 134..141
FT /note="CXXCXGXG motif"
FT REPEAT 150..157
FT /note="CXXCXGXG motif"
FT REPEAT 177..184
FT /note="CXXCXGXG motif"
FT REPEAT 193..200
FT /note="CXXCXGXG motif"
FT ZN_FING 121..205
FT /note="CR-type"
FT REGION 352..397
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 365..390
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 134
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 137
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 150
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 153
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 177
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 180
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 193
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 196
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT MOD_RES 66
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P31689"
FT MOD_RES 83
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P31689"
FT MOD_RES 335
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 381
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P31689"
FT MOD_RES 394
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250"
FT LIPID 394
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 397 AA; 44868 MW; 1783CE3D5C4CD558 CRC64;
MVKETTYYDV LGVKPNATQE ELKKAYRKLA LKYHPDKNPN EGEKFKQISQ AYEVLADSKK
RELYDKGGEQ AIKEGGAGGG FGSPMDIFDM FFGGGGRMQR ERRGKNVVHQ LSVTLEDLYN
GATRKLALQK NVICDKCEGR GGKKGAVECC PNCRGTGMQI RIHQIGPGMV QQIQSVCMEC
QGHGERISPK DRCKSCNGRK IVREKKILEV HIDKGMKDGQ KITFHGEGDQ EPGLEPGDII
IVLDQKDHAV FTRRGEDLFM CMDIQLVEAL CGFQKPISTL DNRTIVITSH PGQIVKHGDI
KCVLNEGMPI YRRPYEKGRL IIEFKVNFPE NGFLSPDKLS LLEKLLPERK EVEETDEMDQ
VELVDFDPNQ ERRRHYNGEA YEDDEHHPRG GVQCQTS
