GFA2_ARATH
ID GFA2_ARATH Reviewed; 456 AA.
AC Q8GWW8; Q8L8A1; Q8LEU4; Q9FI35;
DT 16-MAR-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Chaperone protein dnaJ GFA2, mitochondrial {ECO:0000305};
DE AltName: Full=Chaperone protein dnaJ A30 {ECO:0000303|PubMed:11599562};
DE Short=AtDjA30 {ECO:0000303|PubMed:11599562};
DE AltName: Full=Gametophytic factor 2 {ECO:0000303|PubMed:12215516};
DE Flags: Precursor;
GN Name=GFA2 {ECO:0000303|PubMed:12215516};
GN OrderedLocusNames=At5g48030 {ECO:0000312|Araport:AT5G48030};
GN ORFNames=MDN11.11 {ECO:0000312|EMBL:BAB11067.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=12215516; DOI=10.1105/tpc.002170;
RA Christensen C.A., Gorsich S.W., Brown R.H., Jones L.G., Brown J.,
RA Shaw J.M., Drews G.N.;
RT "Mitochondrial GFA2 is required for synergid cell death in Arabidopsis.";
RL Plant Cell 14:2215-2232(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10470850; DOI=10.1093/dnares/6.3.183;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Kotani H.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. IX. Sequence
RT features of the regions of 1,011,550 bp covered by seventeen P1 and TAC
RT clones.";
RL DNA Res. 6:183-195(1999).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=11599562; DOI=10.1379/1466-1268(2001)006<0209:tjdpoa>2.0.co;2;
RA Miernyk J.A.;
RT "The J-domain proteins of Arabidopsis thaliana: an unexpectedly large and
RT diverse family of chaperones.";
RL Cell Stress Chaperones 6:209-218(2001).
CC -!- FUNCTION: Chaperone that may play a role in mitochondrial protein
CC folding. Involved in female gametophyte development. Required for cell
CC death of the synergid cells during fertilization process, and fusion of
CC the polar nuclei during megagametogenesis.
CC {ECO:0000269|PubMed:12215516}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:12215516}.
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:12215516}.
CC -!- DISRUPTION PHENOTYPE: Defect in fusion of polar nuclei and in synergid
CC cell death.
CC -!- SIMILARITY: Belongs to the DnaJ family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB11067.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AY103490; AAM49801.1; -; mRNA.
DR EMBL; AB017064; BAB11067.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED95612.1; -; Genomic_DNA.
DR EMBL; AK118588; BAC43188.1; -; mRNA.
DR EMBL; AY085227; AAM62460.1; -; mRNA.
DR RefSeq; NP_568690.1; NM_124177.4.
DR AlphaFoldDB; Q8GWW8; -.
DR SMR; Q8GWW8; -.
DR STRING; 3702.AT5G48030.1; -.
DR SwissPalm; Q8GWW8; -.
DR PaxDb; Q8GWW8; -.
DR PRIDE; Q8GWW8; -.
DR ProteomicsDB; 220736; -.
DR EnsemblPlants; AT5G48030.1; AT5G48030.1; AT5G48030.
DR GeneID; 834854; -.
DR Gramene; AT5G48030.1; AT5G48030.1; AT5G48030.
DR KEGG; ath:AT5G48030; -.
DR Araport; AT5G48030; -.
DR TAIR; locus:2162692; AT5G48030.
DR eggNOG; KOG0715; Eukaryota.
DR HOGENOM; CLU_017633_0_3_1; -.
DR InParanoid; Q8GWW8; -.
DR OMA; IIITPCA; -.
DR OrthoDB; 894595at2759; -.
DR PhylomeDB; Q8GWW8; -.
DR PRO; PR:Q8GWW8; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q8GWW8; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0031072; F:heat shock protein binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; IGI:TAIR.
DR GO; GO:0009558; P:embryo sac cellularization; IMP:TAIR.
DR GO; GO:0009553; P:embryo sac development; IMP:TAIR.
DR GO; GO:0000740; P:nuclear membrane fusion; IMP:TAIR.
DR GO; GO:0010197; P:polar nucleus fusion; IMP:TAIR.
DR GO; GO:0042026; P:protein refolding; IBA:GO_Central.
DR GO; GO:0009408; P:response to heat; IEA:InterPro.
DR GO; GO:0010198; P:synergid death; IMP:TAIR.
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; 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 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 Apoptosis; Chaperone; Metal-binding; Mitochondrion; Reference proteome;
KW Repeat; Transit peptide; Zinc; Zinc-finger.
FT TRANSIT 1..89
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 90..456
FT /note="Chaperone protein dnaJ GFA2, mitochondrial"
FT /evidence="ECO:0000255"
FT /id="PRO_0000435728"
FT DOMAIN 94..159
FT /note="J"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00286"
FT REPEAT 238..245
FT /note="CXXCXGXG motif"
FT /evidence="ECO:0000305"
FT REPEAT 255..262
FT /note="CXXCXGXG motif"
FT /evidence="ECO:0000305"
FT REPEAT 277..284
FT /note="CXXCXGXG motif"
FT /evidence="ECO:0000305"
FT REPEAT 291..298
FT /note="CXXCXGXG motif"
FT /evidence="ECO:0000305"
FT ZN_FING 225..303
FT /note="CR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00546"
FT BINDING 238
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q96EY1"
FT BINDING 241
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q96EY1"
FT BINDING 255
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q96EY1"
FT BINDING 258
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q96EY1"
FT BINDING 277
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q96EY1"
FT BINDING 280
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q96EY1"
FT BINDING 291
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q96EY1"
FT BINDING 294
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q96EY1"
FT CONFLICT 30
FT /note="K -> R (in Ref. 5; AAM62460)"
FT /evidence="ECO:0000305"
FT CONFLICT 63
FT /note="D -> H (in Ref. 5; AAM62460)"
FT /evidence="ECO:0000305"
FT CONFLICT 158
FT /note="V -> F (in Ref. 5; AAM62460)"
FT /evidence="ECO:0000305"
FT CONFLICT 174
FT /note="D -> Y (in Ref. 5; AAM62460)"
FT /evidence="ECO:0000305"
FT CONFLICT 235
FT /note="E -> Q (in Ref. 1; AAM49801)"
FT /evidence="ECO:0000305"
FT CONFLICT 309
FT /note="T -> N (in Ref. 5; AAM62460)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 456 AA; 49438 MW; AD571ED32BE33D2F CRC64;
MVPSNGAKVL RLLSRRCLSS SLIQDLANQK LRGVCIGSYR RLNTSVGNHA NVIGDYASKS
GHDRKWINFG GFNTNFGSTR SFHGTGSSFM SAKDYYSVLG VSKNAQEGEI KKAYYGLAKK
LHPDMNKDDP EAETKFQEVS KAYEILKDKE KRDLYDQVGH EAFEQNASGG FPNDQGFGGG
GGGGFNPFDI FGSFNGDIFN MYRQDIGGQD VKVLLDLSFM EAVQGCSKTV TFQTEMACNT
CGGQGVPPGT KREKCKACNG SGMTSLRRGM LSIQTTCQKC GGAGQTFSSI CKSCRGARVV
RGQKSVKVTI DPGVDNSDTL KVARVGGADP EGDQPGDLYV TLKVREDPVF RREGSDIHVD
AVLSVTQAIL GGTIQVPTLT GDVVVKVRPG TQPGHKVVLR NKGIRARKST KFGDQYVHFN
VSIPANITQR QRELLEEFSK AEQGEYEQRT ATGSSQ
