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 24-JAN-2024, entry version 163. 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, RC 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: 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}. 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; 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; 39. DR DIP; DIP-32350N; -. DR IntAct; P63037; 15. DR MINT; P63037; -. DR STRING; 10090.ENSMUSP00000129730; -. DR GlyGen; P63037; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P63037; -. DR PhosphoSitePlus; P63037; -. DR SwissPalm; P63037; -. DR EPD; P63037; -. DR jPOST; P63037; -. DR PaxDb; 10090-ENSMUSP00000030118; -. DR PeptideAtlas; P63037; -. DR ProteomicsDB; 279741; -. DR Pumba; P63037; -. DR Antibodypedia; 675; 336 antibodies from 32 providers. DR DNASU; 15502; -. DR Ensembl; ENSMUST00000030118.10; ENSMUSP00000030118.4; ENSMUSG00000028410.14. DR Ensembl; ENSMUST00000164233.8; ENSMUSP00000129730.2; ENSMUSG00000028410.14. DR GeneID; 15502; -. DR KEGG; mmu:15502; -. DR UCSC; uc008sht.2; mouse. DR AGR; MGI:1270129; -. 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; QHYNGEA; -. DR OrthoDB; 2785358at2759; -. 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 81 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 281 other cell types or tissues. DR ExpressionAtlas; P63037; baseline and differential. 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: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:0051087; F:protein-folding chaperone binding; ISS:UniProtKB. 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 CDD; cd06257; DnaJ; 1. DR CDD; cd10747; DnaJ_C; 1. DR CDD; cd10719; DnaJ_zf; 1. DR Gene3D; 1.10.287.110; DnaJ domain; 1. DR Gene3D; 2.10.230.10; Heat shock protein DnaJ, cysteine-rich domain; 1. DR Gene3D; 2.60.260.20; Urease metallochaperone UreE, N-terminal domain; 2. 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:SF8; DNAJ HOMOLOG SUBFAMILY A MEMBER 1; 1. DR PANTHER; PTHR43888; DNAJ-LIKE-2, ISOFORM A-RELATED; 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; Chaperone J-domain; 1. DR SUPFAM; SSF57938; DnaJ/Hsp40 cysteine-rich domain; 1. DR SUPFAM; SSF49493; HSP40/DnaJ peptide-binding domain; 2. DR PROSITE; PS00636; DNAJ_1; 1. DR PROSITE; PS50076; DNAJ_2; 1. DR PROSITE; PS51188; ZF_CR; 1. DR Genevisible; P63037; MM. 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 //