ID DNJA1_RAT Reviewed; 397 AA.
AC P63036; P54102;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 31-AUG-2004, sequence version 1.
DT 24-JAN-2024, entry version 146.
DE RecName: Full=DnaJ homolog subfamily A member 1;
DE AltName: Full=DnaJ-like protein 1;
DE AltName: Full=Heat shock protein J2;
DE Short=HSJ-2;
DE Flags: Precursor;
GN Name=Dnaja1; Synonyms=Hsj2, Rdj1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RX PubMed=9605323; DOI=10.1002/pro.5560070513;
RA Leng C.H., Brodsky J.L., Wang C.;
RT "Isolation and characterization of a DnaJ-like protein in rats: the C-
RT terminal 10-kDa domain of hsc70 is not essential for stimulating the ATP-
RT hydrolytic activity of hsc70 by a DnaJ-like protein.";
RL Protein Sci. 7:1186-1194(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate;
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 [3]
RP FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, AND TISSUE SPECIFICITY.
RX PubMed=10816573; DOI=10.1074/jbc.m002021200;
RA Terada K., Mori M.;
RT "Human DnaJ homologs dj2 and dj3, and bag-1 are positive cochaperones of
RT hsc70.";
RL J. Biol. Chem. 275:24728-24734(2000).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83 AND SER-335, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Functions as a co-chaperone for HSPA1B and negatively
CC regulates the translocation of BAX from the cytosol to mitochondria in
CC response to cellular stress, thereby protecting cells against
CC apoptosis. Promotes apoptosis in response to cellular stress mediated
CC by exposure to anisomycin or UV. Stimulates ATP hydrolysis, but not the
CC folding of unfolded proteins mediated by HSPA1A (in vitro) (By
CC similarity). Co-chaperone for HSPA8/Hsc70. Plays a role in protein
CC transport into mitochondria via its role as co-chaperone
CC (PubMed:10816573). {ECO:0000250, ECO:0000269|PubMed:10816573,
CC ECO:0000269|PubMed:9605323}.
CC -!- SUBUNIT: Identified in a complex with HSPA1B and BAX. Interacts with
CC RNF207. {ECO:0000250|UniProtKB:P31689}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Lipid-anchor
CC {ECO:0000250}. Cytoplasm {ECO:0000269|PubMed:10816573}. Microsome
CC {ECO:0000269|PubMed:10816573}. Mitochondrion
CC {ECO:0000269|PubMed:10816573}. Nucleus {ECO:0000269|PubMed:10816573}.
CC Cytoplasm, perinuclear region {ECO:0000250}. Note=Primarily cytoplasmic
CC and associated with microsomes. A minor proportion is associated with
CC nuclei and mitochondria.
CC -!- TISSUE SPECIFICITY: Detected in liver (at protein level).
CC {ECO:0000269|PubMed:10816573}.
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DR EMBL; U53922; AAA98855.1; -; mRNA.
DR EMBL; BC062009; AAH62009.1; -; mRNA.
DR RefSeq; NP_075223.1; NM_022934.1.
DR RefSeq; XP_006238161.1; XM_006238099.2.
DR AlphaFoldDB; P63036; -.
DR BMRB; P63036; -.
DR SMR; P63036; -.
DR BioGRID; 249221; 6.
DR CORUM; P63036; -.
DR IntAct; P63036; 2.
DR STRING; 10116.ENSRNOP00000010061; -.
DR iPTMnet; P63036; -.
DR PhosphoSitePlus; P63036; -.
DR jPOST; P63036; -.
DR PaxDb; 10116-ENSRNOP00000010061; -.
DR Ensembl; ENSRNOT00000010061.4; ENSRNOP00000010061.2; ENSRNOG00000007029.4.
DR Ensembl; ENSRNOT00055027767; ENSRNOP00055022299; ENSRNOG00055016378.
DR Ensembl; ENSRNOT00060006030; ENSRNOP00060004449; ENSRNOG00060003657.
DR Ensembl; ENSRNOT00065006743; ENSRNOP00065004642; ENSRNOG00065004655.
DR GeneID; 65028; -.
DR KEGG; rno:65028; -.
DR UCSC; RGD:620942; rat.
DR AGR; RGD:620942; -.
DR CTD; 3301; -.
DR RGD; 620942; Dnaja1.
DR eggNOG; KOG0712; Eukaryota.
DR GeneTree; ENSGT00940000153558; -.
DR HOGENOM; CLU_017633_10_0_1; -.
DR InParanoid; P63036; -.
DR OMA; QHYNGEA; -.
DR OrthoDB; 2785358at2759; -.
DR PhylomeDB; P63036; -.
DR TreeFam; TF105141; -.
DR Reactome; R-RNO-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand.
DR PRO; PR:P63036; -.
DR Proteomes; UP000002494; Chromosome 5.
DR Bgee; ENSRNOG00000007029; Expressed in cerebellum and 20 other cell types or tissues.
DR Genevisible; P63036; RN.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISO:RGD.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0015630; C:microtubule cytoskeleton; IEA:Ensembl.
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; IDA:RGD.
DR GO; GO:0055131; F:C3HC4-type RING finger domain binding; ISO:RGD.
DR GO; GO:0001664; F:G protein-coupled receptor binding; ISO:RGD.
DR GO; GO:0030544; F:Hsp70 protein binding; ISS:UniProtKB.
DR GO; GO:0050750; F:low-density lipoprotein particle receptor binding; ISO:RGD.
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:RGD.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:RGD.
DR GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR GO; GO:0030521; P:androgen receptor signaling pathway; ISO:RGD.
DR GO; GO:0030317; P:flagellated sperm motility; ISO:RGD.
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:RGD.
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:RGD.
DR GO; GO:0031397; P:negative regulation of protein ubiquitination; ISO:RGD.
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; ISO:RGD.
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.
PE 1: Evidence at protein level;
KW Acetylation; Chaperone; Cytoplasm; Endoplasmic reticulum; Lipoprotein;
KW Membrane; Metal-binding; Methylation; Microsome; Mitochondrion; Nucleus;
KW Phosphoprotein; Prenylation; Reference proteome; Repeat; Zinc; Zinc-finger.
FT CHAIN 1..394
FT /note="DnaJ homolog subfamily A member 1"
FT /id="PRO_0000071010"
FT PROPEP 395..397
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000396755"
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:0007744|PubMed:22673903"
FT MOD_RES 335
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
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
//
