DNJA1_PONAB
ID DNJA1_PONAB Reviewed; 396 AA.
AC Q5NVI9;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=DnaJ homolog subfamily A member 1;
DE Flags: Precursor;
GN Name=DNAJA1;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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 -!- 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; CR926041; CAI29674.1; -; mRNA.
DR RefSeq; NP_001127102.1; NM_001133630.1.
DR AlphaFoldDB; Q5NVI9; -.
DR BMRB; Q5NVI9; -.
DR SMR; Q5NVI9; -.
DR STRING; 9601.ENSPPYP00000021446; -.
DR GeneID; 100174139; -.
DR KEGG; pon:100174139; -.
DR CTD; 3301; -.
DR eggNOG; KOG0712; Eukaryota.
DR HOGENOM; CLU_017633_10_0_1; -.
DR InParanoid; Q5NVI9; -.
DR Proteomes; UP000001595; Unplaced.
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; Reference proteome; Repeat; Zinc; Zinc-finger.
FT CHAIN 1..393
FT /note="DnaJ homolog subfamily A member 1"
FT /id="PRO_0000285807"
FT PROPEP 394..396
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000396754"
FT DOMAIN 6..68
FT /note="J"
FT REPEAT 133..140
FT /note="CXXCXGXG motif"
FT REPEAT 149..156
FT /note="CXXCXGXG motif"
FT REPEAT 176..183
FT /note="CXXCXGXG motif"
FT REPEAT 192..199
FT /note="CXXCXGXG motif"
FT ZN_FING 120..204
FT /note="CR-type"
FT REGION 351..396
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 364..389
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 133
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 136
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 149
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 152
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 176
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 179
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 192
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 195
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 334
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P31689"
FT MOD_RES 380
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P31689"
FT MOD_RES 393
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250"
FT LIPID 393
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 396 AA; 44811 MW; A20D2B5123894B6A CRC64;
MVKETTYYDV LGVKPNATQE ELKKAYRKLA LKYHPDKNPN EGEKFKQISQ AYEVLSDAKK
RELYDKGGEQ AIKEGGAGGG FGSPMDIFDM FFGGGRMQRE RRGKNVVHQL SVTLEDLYNG
ATRKLALQKN VICDKCEGRG GKKGAVECCP NCRGTGMQIR IHQIGPGMVQ QIQSVCMECQ
GHGERISPKD RCKSCNGRKI VREKKILEVH IDKGMKDGQK ITFHGEGDQE PGLEPGDIII
VLDQKDHAVF TRRGEDLFMC MDIQLVEALC GFQKPISTLD NRTIVITSHP GQIVKHGDIK
CVLNEGMPIY RRPYEKGRLI IEFKVNFPEN GFLSPDKLSL LEKLLPERKE VEETDEMDQV
ELVDFDPNQE RRRHYNGEAY EDDEHHPRGG VQCQTS
