HARC1_ARATH
ID HARC1_ARATH Reviewed; 169 AA.
AC Q8RUD6; Q0WSX5; Q7Y234;
DT 18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Protein HIGH ARSENIC CONTENT 1, mitochondrial {ECO:0000303|PubMed:25464340};
DE Short=AtHAC1 {ECO:0000303|PubMed:25464340};
DE AltName: Full=Arsenate reductase {ECO:0000305};
DE EC=1.20.4.1 {ECO:0000269|PubMed:25464340};
DE AltName: Full=Arsenate tolerance QTL1 {ECO:0000303|PubMed:25099865};
DE Short=AtATQ1 {ECO:0000303|PubMed:25099865};
DE AltName: Full=Rhodanese-like domain-containing protein 19 {ECO:0000305};
DE AltName: Full=Sulfurtransferase 19 {ECO:0000303|PubMed:17408957};
DE Short=AtStr19 {ECO:0000303|PubMed:17408957};
DE Flags: Precursor;
GN Name=HAC1 {ECO:0000303|PubMed:25464340};
GN Synonyms=ATQ1 {ECO:0000303|PubMed:25099865},
GN STR19 {ECO:0000303|PubMed:17408957};
GN OrderedLocusNames=At2g21045 {ECO:0000312|Araport:AT2G21045};
GN ORFNames=F26H11 {ECO:0000312|EMBL:AAM15226.1},
GN F5H14 {ECO:0000312|EMBL:AAM15209.1};
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 13-169.
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 30-169.
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=17408957; DOI=10.1016/j.plaphy.2007.02.005;
RA Bartels A., Mock H.P., Papenbrock J.;
RT "Differential expression of Arabidopsis sulfurtransferases under various
RT growth conditions.";
RL Plant Physiol. Biochem. 45:178-187(2007).
RN [6]
RP FUNCTION, ACTIVITY REGULATION, MUTAGENESIS OF CYS-113, AND 3D-STRUCTURE
RP MODELING.
RX PubMed=25099865; DOI=10.1038/ncomms5617;
RA Sanchez-Bermejo E., Castrillo G., del Llano B., Navarro C.,
RA Zarco-Fernandez S., Martinez-Herrera D.J., Leo-del Puerto Y., Munoz R.,
RA Camara C., Paz-Ares J., Alonso-Blanco C., Leyva A.;
RT "Natural variation in arsenate tolerance identifies an arsenate reductase
RT in Arabidopsis thaliana.";
RL Nat. Commun. 5:4617-4617(2014).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND
RP INDUCTION.
RX PubMed=25464340; DOI=10.1371/journal.pbio.1002009;
RA Chao D.Y., Chen Y., Chen J., Shi S., Chen Z., Wang C., Danku J.M.,
RA Zhao F.J., Salt D.E.;
RT "Genome-wide association mapping identifies a new arsenate reductase enzyme
RT critical for limiting arsenic accumulation in plants.";
RL PLoS Biol. 12:E1002009-E1002009(2014).
CC -!- FUNCTION: Arsenate reductase critical for arsenic tolerance
CC (PubMed:25099865). Reduces arsenate to arsenite in the root,
CC facilitating efflux of arsenic back into the soil to limit both its
CC accumulation in the root and transport to the shoot (PubMed:25464340).
CC Essential for arsenite efflux from the root, but not necessary for
CC arsenate uptake (PubMed:25464340). {ECO:0000269|PubMed:25099865,
CC ECO:0000269|PubMed:25464340}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[glutaredoxin]-dithiol + arsenate + glutathione + H(+) =
CC arsenite + glutathionyl-S-S-[glutaredoxin] + H2O;
CC Xref=Rhea:RHEA:22016, Rhea:RHEA-COMP:10729, Rhea:RHEA-COMP:17668,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29242,
CC ChEBI:CHEBI:29950, ChEBI:CHEBI:48597, ChEBI:CHEBI:57925,
CC ChEBI:CHEBI:146199; EC=1.20.4.1;
CC Evidence={ECO:0000269|PubMed:25464340};
CC -!- ACTIVITY REGULATION: Inhibited by trobenzenesulphonic acid (TNBS).
CC {ECO:0000269|PubMed:25099865}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in root hairs, epidermal cells at the
CC surface of the root and in the pericycle within the stele.
CC {ECO:0000269|PubMed:25464340}.
CC -!- INDUCTION: Up-regulated by arsenate and down-regulated by arsenite.
CC {ECO:0000269|PubMed:25464340}.
CC -!- DISRUPTION PHENOTYPE: Reduced arsenate resistance and increased
CC accumulation of arsenic in shoots and roots.
CC {ECO:0000269|PubMed:25464340}.
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DR EMBL; AC006234; AAM15209.1; -; Genomic_DNA.
DR EMBL; AC006264; AAM15226.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC07115.1; -; Genomic_DNA.
DR EMBL; AK227791; BAE99773.1; -; mRNA.
DR EMBL; BT008306; AAP37665.1; -; mRNA.
DR RefSeq; NP_565497.3; NM_127674.5.
DR AlphaFoldDB; Q8RUD6; -.
DR SMR; Q8RUD6; -.
DR BioGRID; 1992; 1.
DR STRING; 3702.AT2G21045.1; -.
DR PaxDb; Q8RUD6; -.
DR PRIDE; Q8RUD6; -.
DR ProteomicsDB; 230306; -.
DR EnsemblPlants; AT2G21045.1; AT2G21045.1; AT2G21045.
DR GeneID; 816639; -.
DR Gramene; AT2G21045.1; AT2G21045.1; AT2G21045.
DR KEGG; ath:AT2G21045; -.
DR Araport; AT2G21045; -.
DR TAIR; locus:505006261; AT2G21045.
DR eggNOG; KOG1530; Eukaryota.
DR HOGENOM; CLU_089574_3_0_1; -.
DR OMA; HLVVGCN; -.
DR OrthoDB; 1478958at2759; -.
DR PhylomeDB; Q8RUD6; -.
DR BioCyc; MetaCyc:AT2G21045-MON; -.
DR PRO; PR:Q8RUD6; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q8RUD6; baseline and differential.
DR Genevisible; Q8RUD6; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0008794; F:arsenate reductase (glutaredoxin) activity; IEA:UniProtKB-EC.
DR GO; GO:0030611; F:arsenate reductase activity; IDA:TAIR.
DR GO; GO:0071722; P:detoxification of arsenic-containing substance; IMP:TAIR.
DR GO; GO:0046685; P:response to arsenic-containing substance; IMP:TAIR.
DR Gene3D; 3.40.250.10; -; 1.
DR InterPro; IPR001763; Rhodanese-like_dom.
DR InterPro; IPR036873; Rhodanese-like_dom_sf.
DR InterPro; IPR044684; STR17/STR18/HARC1-like.
DR PANTHER; PTHR44542; PTHR44542; 1.
DR Pfam; PF00581; Rhodanese; 1.
DR SMART; SM00450; RHOD; 1.
DR SUPFAM; SSF52821; SSF52821; 1.
DR PROSITE; PS50206; RHODANESE_3; 1.
PE 1: Evidence at protein level;
KW Mitochondrion; Oxidoreductase; Reference proteome; Repeat; Transit peptide.
FT TRANSIT 1..59
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 60..169
FT /note="Protein HIGH ARSENIC CONTENT 1, mitochondrial"
FT /id="PRO_0000416539"
FT DOMAIN 60..153
FT /note="Rhodanese"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT ACT_SITE 113
FT /note="Cysteine persulfide intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT MUTAGEN 113
FT /note="C->G: Loss of activity."
FT /evidence="ECO:0000269|PubMed:25099865"
SQ SEQUENCE 169 AA; 19039 MW; DC27623AC032F5B9 CRC64;
MYTYSLLNLS HCRRQTRKKR KTDHTEGFLM EETKPKTVED VETVDVYTAK GFLSTGHRYL
DVRTNEEFAK SHVEEALNIP YMFKTDEGRV INPDFLSQVA SVCKKDEHLI VACNAGGRGS
RACVDLLNEG YDHVANMGGG YSAWVDAGFA GDKPPEDLKI ACKFRPKEN
