ID DNJA2_RAT Reviewed; 412 AA.
AC O35824;
DT 11-JUL-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 08-NOV-2023, entry version 138.
DE RecName: Full=DnaJ homolog subfamily A member 2;
DE AltName: Full=RDJ2;
DE Flags: Precursor;
GN Name=Dnaja2;
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].
RX PubMed=9328291; DOI=10.1006/abbi.1997.0296;
RA Andres D.A., Shao H., Crick D.C., Finlin B.S.;
RT "Expression cloning of a novel farnesylated protein, RDJ2, encoding a DnaJ
RT protein homologue.";
RL Arch. Biochem. Biophys. 346:113-124(1997).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-123, AND IDENTIFICATION BY
RP 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: Co-chaperone of Hsc70. Stimulates ATP hydrolysis and the
CC folding of unfolded proteins mediated by HSPA1A/B (in vitro).
CC {ECO:0000250|UniProtKB:O60884}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}.
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DR EMBL; U95727; AAB64094.1; -; mRNA.
DR AlphaFoldDB; O35824; -.
DR SMR; O35824; -.
DR IntAct; O35824; 3.
DR MINT; O35824; -.
DR STRING; 10116.ENSRNOP00000022573; -.
DR iPTMnet; O35824; -.
DR PhosphoSitePlus; O35824; -.
DR SwissPalm; O35824; -.
DR jPOST; O35824; -.
DR PaxDb; 10116-ENSRNOP00000022573; -.
DR AGR; RGD:71001; -.
DR RGD; 71001; Dnaja2.
DR eggNOG; KOG0712; Eukaryota.
DR InParanoid; O35824; -.
DR PhylomeDB; O35824; -.
DR Reactome; R-RNO-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand.
DR PRO; PR:O35824; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISO:RGD.
DR GO; GO:0016020; C:membrane; 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:0030544; F:Hsp70 protein binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051087; F:protein-folding chaperone binding; ISO:RGD.
DR GO; GO:0051082; F:unfolded protein binding; ISO:RGD.
DR GO; GO:0018885; P:carbon tetrachloride metabolic process; IEP:RGD.
DR GO; GO:0042026; P:protein refolding; ISO:RGD.
DR GO; GO:0009408; P:response to heat; IEA:InterPro.
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:SF31; DNAJ HOMOLOG SUBFAMILY A MEMBER 2; 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; Isopeptide bond; Lipoprotein; Membrane;
KW Metal-binding; Methylation; Phosphoprotein; Prenylation;
KW Reference proteome; Repeat; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..409
FT /note="DnaJ homolog subfamily A member 2"
FT /id="PRO_0000071013"
FT PROPEP 410..412
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000396759"
FT DOMAIN 8..70
FT /note="J"
FT REPEAT 143..150
FT /note="CXXCXGXG motif"
FT REPEAT 159..166
FT /note="CXXCXGXG motif"
FT REPEAT 186..193
FT /note="CXXCXGXG motif"
FT REPEAT 202..209
FT /note="CXXCXGXG motif"
FT ZN_FING 130..214
FT /note="CR-type"
FT REGION 365..412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 143
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 146
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 159
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 162
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 186
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 189
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 202
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 205
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT MOD_RES 39
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYJ0"
FT MOD_RES 78
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60884"
FT MOD_RES 123
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 152
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYJ0"
FT MOD_RES 391
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O60884"
FT MOD_RES 394
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60884"
FT MOD_RES 395
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60884"
FT MOD_RES 409
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250|UniProtKB:O60884"
FT LIPID 409
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:O60884"
FT CROSSLNK 134
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O60884"
SQ SEQUENCE 412 AA; 45766 MW; FAE60601B55C409F CRC64;
MANVADTKLY DILGVPPGAS ENELKKAYRK LAKEYHPDKN PNAGDKFKEI SFAYEVLSNP
EKRELYDRYG EQGLREGSGG GGGMDDIFSH IFGGGLFGFM GNQSRSRNGR RRGEDMMHPL
KVSLEDLYNG KTTKLQLSKN VLCSACSGQG GKSGAVQKCS ACRGRGVRIM IRQLAPGMVQ
QMQSVCSDCN GEGEVINEKD RCKKCEGKKV IKEVKILEVH VDKGMKHGQR ITFTGEADQA
PGVEPGDIVL FVQEKEHEVF QRDGNDLHMT YKIGLVEALC GFQFTFKHLD ARQIVVKYPP
GKVIEPGCVR VVRGEGMPQY RNPFEKGDLY IKFDVQFPEN NWINPDKLSE LEDLLPSRPE
VPNVIGETEE VELQEFDSTR GSGGGQRREA YNDSSDEESS SHHGPGVQCA HQ
//
