DNJA1_BOVIN
ID DNJA1_BOVIN Reviewed; 397 AA.
AC Q5E954; Q3SZU2;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 17-APR-2007, sequence version 2.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=DnaJ homolog subfamily A member 1;
DE Flags: Precursor;
GN Name=DNAJA1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) 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; BT021066; AAX09083.1; -; mRNA.
DR EMBL; BC102711; AAI02712.1; -; mRNA.
DR RefSeq; NP_001015637.1; NM_001015637.1.
DR AlphaFoldDB; Q5E954; -.
DR BMRB; Q5E954; -.
DR SMR; Q5E954; -.
DR STRING; 9913.ENSBTAP00000021637; -.
DR PaxDb; Q5E954; -.
DR PeptideAtlas; Q5E954; -.
DR PRIDE; Q5E954; -.
DR Ensembl; ENSBTAT00000021637; ENSBTAP00000021637; ENSBTAG00000016265.
DR GeneID; 528862; -.
DR KEGG; bta:528862; -.
DR CTD; 3301; -.
DR VEuPathDB; HostDB:ENSBTAG00000016265; -.
DR VGNC; VGNC:56944; DNAJA1.
DR eggNOG; KOG0712; Eukaryota.
DR GeneTree; ENSGT00940000153558; -.
DR HOGENOM; CLU_017633_10_0_1; -.
DR InParanoid; Q5E954; -.
DR OMA; GMSAFNG; -.
DR OrthoDB; 1012379at2759; -.
DR TreeFam; TF105141; -.
DR Reactome; R-BTA-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand.
DR Proteomes; UP000009136; Chromosome 8.
DR Bgee; ENSBTAG00000016265; Expressed in spermatid and 104 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
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:0050750; F:low-density lipoprotein particle receptor binding; ISS:AgBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR GO; GO:0030521; P:androgen receptor signaling pathway; ISS:AgBase.
DR GO; GO:0030317; P:flagellated sperm motility; ISS:AgBase.
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: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; ISS:AgBase.
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..394
FT /note="DnaJ homolog subfamily A member 1"
FT /id="PRO_0000239805"
FT PROPEP 395..397
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000396751"
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"
FT CONFLICT 99
FT /note="Q -> H (in Ref. 1; AAX09083)"
FT /evidence="ECO:0000305"
FT CONFLICT 181..182
FT /note="QG -> HC (in Ref. 1; AAX09083)"
FT /evidence="ECO:0000305"
FT CONFLICT 188
FT /note="S -> T (in Ref. 1; AAX09083)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 397 AA; 44882 MW; FDCB27F110B2E12C CRC64;
MVKETTYYDV LGVKPNATQE ELKKAYRKLA LKYHPDKNPN EGEKFKQISQ AYEVLSDAKK
RELYDKGGEQ AIKEGGAGGG FGSPMDIFDM FFGGGGRMQR ERRGKNVVHQ LTVTLEDLYN
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
