DNAJ1_CHLAE
ID DNAJ1_CHLAE Reviewed; 397 AA.
AC Q95JF4;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=DnaJ homolog subfamily A member 1;
DE AltName: Full=DnaJ protein homolog 2;
DE Short=DJ-2;
DE AltName: Full=Mydj2;
DE Flags: Precursor;
GN Name=DNAJA1;
OS Chlorocebus aethiops (Green monkey) (Cercopithecus aethiops).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Chlorocebus.
OX NCBI_TaxID=9534;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC TISSUE=Kidney;
RX PubMed=11874471; DOI=10.1046/j.1432-1033.2002.02807.x;
RA Bozidis P., Lazaridis I., Pagoulatos G.N., Angelidis C.E.;
RT "Mydj2 as a potent partner of hsc70 in mammalian cells.";
RL Eur. J. Biochem. 269:1553-1560(2002).
CC -!- FUNCTION: Co-chaperone for HSPA8/Hsc70. Plays a role in protein
CC transport into mitochondria via its role as co-chaperone. 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. Stimulates ATP hydrolysis,
CC but not the folding of unfolded proteins mediated by HSPA1A (in vitro).
CC Promotes apoptosis in response to cellular stress mediated by exposure
CC to anisomycin or UV (By similarity). {ECO:0000250,
CC ECO:0000269|PubMed:11874471}.
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: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; AF395203; AAK81721.1; -; mRNA.
DR AlphaFoldDB; Q95JF4; -.
DR SMR; Q95JF4; -.
DR CORUM; Q95JF4; -.
DR PRIDE; Q95JF4; -.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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:0051087; F:chaperone binding; ISS:UniProtKB.
DR GO; GO:0030544; F:Hsp70 protein binding; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0043508; P:negative regulation of JUN kinase activity; ISS:UniProtKB.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0006457; P:protein folding; IEA:InterPro.
DR GO; GO:0070585; P:protein localization to mitochondrion; ISS:UniProtKB.
DR GO; GO:0051223; P:regulation of protein transport; ISS:UniProtKB.
DR GO; GO:0009408; P:response to heat; IEA:InterPro.
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 2: Evidence at transcript level;
KW Acetylation; Chaperone; Cytoplasm; Endoplasmic reticulum; Lipoprotein;
KW Membrane; Metal-binding; Methylation; Microsome; Mitochondrion; Nucleus;
KW Phosphoprotein; Prenylation; Repeat; Zinc; Zinc-finger.
FT CHAIN 1..394
FT /note="DnaJ homolog subfamily A member 1"
FT /id="PRO_0000328580"
FT PROPEP 395..397
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000396752"
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:0000250|UniProtKB:P31689"
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; 44882 MW; 733AD8D4C8B32792 CRC64;
MVKETTYYDV LGVKPNATQE ELKKAYRKLA LKYHPDKNPN EGEKFKQISQ AYEVLSDAKK
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 IIEFKINFPE NGFLSPDKLS LLEKLLPERK EVEETDEMDQ
VELVDFDPNQ ERRRHYNGEA YEDDEHHPRG GVQCQTS
