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Dual specificity phosphatase Cdc25 (EC 3.1.3.48) (Arath;CDC25) (Arsenate reductase) (AtASR) (Arsenate reductase 2) (EC 1.20.4.1) (Sulfurtransferase 5) (AtStr5)

 CDC25_ARATH             Reviewed;         146 AA.
Q8GY31; Q8LC90; Q9LZE1;
29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
01-MAR-2003, sequence version 1.
25-OCT-2017, entry version 111.
RecName: Full=Dual specificity phosphatase Cdc25 {ECO:0000303|PubMed:15329414};
EC=3.1.3.48 {ECO:0000269|PubMed:15329414};
AltName: Full=Arath;CDC25 {ECO:0000303|PubMed:15329414};
AltName: Full=Arsenate reductase {ECO:0000303|PubMed:16507083};
Short=AtASR {ECO:0000303|PubMed:16507083};
AltName: Full=Arsenate reductase 2 {ECO:0000303|PubMed:16567632};
EC=1.20.4.1 {ECO:0000269|PubMed:16766666};
AltName: Full=Sulfurtransferase 5 {ECO:0000303|PubMed:17408957};
Short=AtStr5 {ECO:0000303|PubMed:17408957};
Name=CDC25 {ECO:0000303|PubMed:15329414};
Synonyms=ACR2 {ECO:0000303|PubMed:16567632},
ASR {ECO:0000303|PubMed:16507083}, STR5 {ECO:0000303|PubMed:17408957};
OrderedLocusNames=At5g03455 {ECO:0000312|Araport:AT5G03455};
ORFNames=F12E4_220 {ECO:0000312|EMBL:CAB83305.1};
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130714; DOI=10.1038/35048507;
Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K.,
Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S.,
Nakazaki N., Naruo K., Okumura S., Shinpo S., Takeuchi C., Wada T.,
Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M.,
Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R.,
Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J.,
Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M.,
Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M.,
Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P.,
Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C.,
Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N.,
Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J.,
Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S.,
Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W.,
Ramsperger U., Wedler H., Balke K., Wedler E., Peters S.,
van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R.,
Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S.,
Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W.,
Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H.,
Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.;
"Sequence and analysis of chromosome 5 of the plant Arabidopsis
thaliana.";
Nature 408:823-826(2000).
[2]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=11910074; DOI=10.1126/science.1071006;
Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M.,
Hayashizaki Y., Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T.,
Shibata K., Shinagawa A., Shinozaki K.;
"Functional annotation of a full-length Arabidopsis cDNA collection.";
Science 296:141-145(2002).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
Feldmann K.A.;
"Full-length cDNA from Arabidopsis thaliana.";
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
[6]
TISSUE SPECIFICITY.
PubMed=15720653; DOI=10.1111/j.1469-8137.2004.01288.x;
Sorrell D.A., Chrimes D., Dickinson J.R., Rogers H.J., Francis D.;
"The Arabidopsis CDC25 induces a short cell length when overexpressed
in fission yeast: evidence for cell cycle function.";
New Phytol. 165:425-428(2005).
[7]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=16507083; DOI=10.1111/j.1365-313X.2005.02651.x;
Bleeker P.M., Hakvoort H.W., Bliek M., Souer E., Schat H.;
"Enhanced arsenate reduction by a CDC25-like tyrosine phosphatase
explains increased phytochelatin accumulation in arsenate-tolerant
Holcus lanatus.";
Plant J. 45:917-929(2006).
[8]
FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=16766666; DOI=10.1104/pp.106.084079;
Ellis D.R., Gumaelius L., Indriolo E., Pickering I.J., Banks J.A.,
Salt D.E.;
"A novel arsenate reductase from the arsenic hyperaccumulating fern
Pteris vittata.";
Plant Physiol. 141:1544-1554(2006).
[9]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=16567632; DOI=10.1073/pnas.0509770102;
Dhankher O.P., Rosen B.P., McKinney E.C., Meagher R.B.;
"Hyperaccumulation of arsenic in the shoots of Arabidopsis silenced
for arsenate reductase (ACR2).";
Proc. Natl. Acad. Sci. U.S.A. 103:5413-5418(2006).
[10]
GENE FAMILY.
PubMed=17408957; DOI=10.1016/j.plaphy.2007.02.005;
Bartels A., Mock H.P., Papenbrock J.;
"Differential expression of Arabidopsis sulfurtransferases under
various growth conditions.";
Plant Physiol. Biochem. 45:178-187(2007).
[11]
DISRUPTION PHENOTYPE.
PubMed=20647223; DOI=10.1093/aob/mcq142;
Spadafora N.D., Doonan J.H., Herbert R.J., Bitonti M.B., Wallace E.,
Rogers H.J., Francis D.;
"Arabidopsis T-DNA insertional lines for CDC25 are hypersensitive to
hydroxyurea but not to zeocin or salt stress.";
Ann. Bot. 107:1183-1192(2011).
[12]
3D-STRUCTURE MODELING, AND FUNCTION.
PubMed=22562211; DOI=10.1007/s00894-012-1419-y;
Nahar N., Rahman A., Mos M., Warzecha T., Algerin M., Ghosh S.,
Johnson-Brousseau S., Mandal A.;
"In silico and in vivo studies of an Arabidopsis thaliana gene, ACR2,
putatively involved in arsenic accumulation in plants.";
J. Mol. Model. 18:4249-4262(2012).
[13]
FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
PubMed=22879969; DOI=10.1371/journal.pone.0042408;
Liu W., Schat H., Bliek M., Chen Y., McGrath S.P., George G.,
Salt D.E., Zhao F.J.;
"Knocking out ACR2 does not affect arsenic redox status in Arabidopsis
thaliana: implications for as detoxification and accumulation in
plants.";
PLoS ONE 7:E42408-E42408(2012).
[14]
DISRUPTION PHENOTYPE.
PubMed=25099865; DOI=10.1038/ncomms5617;
Sanchez-Bermejo E., Castrillo G., del Llano B., Navarro C.,
Zarco-Fernandez S., Martinez-Herrera D.J., Leo-del Puerto Y.,
Munoz R., Camara C., Paz-Ares J., Alonso-Blanco C., Leyva A.;
"Natural variation in arsenate tolerance identifies an arsenate
reductase in Arabidopsis thaliana.";
Nat. Commun. 5:4617-4617(2014).
[15]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=25464340; DOI=10.1371/journal.pbio.1002009;
Chao D.Y., Chen Y., Chen J., Shi S., Chen Z., Wang C., Danku J.M.,
Zhao F.J., Salt D.E.;
"Genome-wide association mapping identifies a new arsenate reductase
enzyme critical for limiting arsenic accumulation in plants.";
PLoS Biol. 12:E1002009-E1002009(2014).
[16]
STRUCTURE BY NMR OF 15-146 OF CYS-145 IN COMPLEX WITH ZINC,
BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF CYS-145.
PubMed=15336525; DOI=10.1016/j.bbrc.2004.07.182;
Landrieu I., Hassan S., Sauty M., Dewitte F., Wieruszeski J.-M.,
Inze D., de Veylder L., Lippens G.;
"Characterization of the Arabidopsis thaliana Arath;CDC25 dual-
specificity tyrosine phosphatase.";
Biochem. Biophys. Res. Commun. 322:734-739(2004).
[17]
STRUCTURE BY NMR OF 15-146 OF CYS-86 MUTANT IN COMPLEX WITH ZINC,
FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL
PROPERTIES, AND MUTAGENESIS OF CYS-86.
PubMed=15329414; DOI=10.1073/pnas.0405248101;
Landrieu I., da Costa M., de Veylder L., Dewitte F., Vandepoele K.,
Hassan S., Wieruszeski J.-M., Corellou F., Faure J.-D.,
Van Montagu M., Inze D., Lippens G.;
"A small CDC25 dual-specificity tyrosine-phosphatase isoform in
Arabidopsis thaliana.";
Proc. Natl. Acad. Sci. U.S.A. 101:13380-13385(2004).
[18]
ERRATUM.
DOI=10.1073/pnas.0407263101;
Landrieu I., da Costa M., de Veylder L., Dewitte F., Vandepoele K.,
Hassan S., Wieruszeski J.M., Corellou F., Faure J.D., Van Montagu M.,
Inze D., Lippens G.;
Proc. Natl. Acad. Sci. U.S.A. 101:16391-16391(2004).
-!- FUNCTION: Tyrosine protein phosphatase that dephosphorylates CDK
complex and activate its kinase activity in vitro.
{ECO:0000269|PubMed:15329414, ECO:0000269|PubMed:16766666}.
-!- FUNCTION: Arsenate reductase that plays a major role in the
reduction of arsenate to arsenite and arsenic retention in roots
(PubMed:16567632). Has an in vitro and in vivo arsenate reductase
activity (PubMed:16507083, PubMed:16766666, PubMed:22562211).
Plays no role in arsenic metabolism (PubMed:22879969,
PubMed:25464340). {ECO:0000269|PubMed:16507083,
ECO:0000269|PubMed:16567632, ECO:0000269|PubMed:16766666,
ECO:0000269|PubMed:22879969, ECO:0000269|PubMed:25464340}.
-!- CATALYTIC ACTIVITY: Protein tyrosine phosphate + H(2)O = protein
tyrosine + phosphate. {ECO:0000269|PubMed:15329414}.
-!- CATALYTIC ACTIVITY: Arsenate + glutaredoxin = arsenite +
glutaredoxin disulfide + H(2)O. {ECO:0000269|PubMed:16766666}.
-!- ENZYME REGULATION: Inhibited by NSC95397.
{ECO:0000269|PubMed:15329414}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=50 mM for para-nitrophenyl phosphate
{ECO:0000269|PubMed:15329414, ECO:0000269|PubMed:15336525};
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
-!- TISSUE SPECIFICITY: Expressed in roots and at lower levels in
shoots (at protein level). Expressed in leaves, stems and flowers.
{ECO:0000269|PubMed:15720653, ECO:0000269|PubMed:16567632,
ECO:0000269|PubMed:22879969}.
-!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
conditions, but plants show reduced root size when grown in
presence of hydroxyurea (PubMed:20647223). No visible phenotype,
but decreased accumulation of total arsenic in shoots
(PubMed:16507083). No effect on arsenate sensitivity
(PubMed:25099865). No effect on the accumulation of arsenate in
roots, efflux of arsenite or uptake of arsenate, or the total
arsenic accumulation in shoots (PubMed:22879969, PubMed:25464340).
{ECO:0000269|PubMed:16507083, ECO:0000269|PubMed:20647223,
ECO:0000269|PubMed:22879969, ECO:0000269|PubMed:25099865,
ECO:0000269|PubMed:25464340}.
-!- MISCELLANEOUS: Binds 1 zinc ion which is not required for enzyme
activity (PubMed:15329414). Plants silencing ACR2 show increased
sensitivity to arsenate but not arsenite (PubMed:16567632).
{ECO:0000305|PubMed:15329414, ECO:0000305|PubMed:16567632}.
-!- SIMILARITY: Belongs to the MPI phosphatase family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAM63780.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=CAB83305.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AL162751; CAB83305.1; ALT_SEQ; Genomic_DNA.
EMBL; CP002688; AED90607.1; -; Genomic_DNA.
EMBL; AK117898; BAC42537.1; -; mRNA.
EMBL; BT003658; AAO39886.1; -; mRNA.
EMBL; AY086729; AAM63780.1; ALT_INIT; mRNA.
PIR; T48370; T48370.
RefSeq; NP_568119.1; NM_120425.3.
UniGene; At.43043; -.
PDB; 1T3K; NMR; -; A=15-146.
PDBsum; 1T3K; -.
DisProt; DP00916; -.
ProteinModelPortal; Q8GY31; -.
SMR; Q8GY31; -.
BioGrid; 17108; 3.
IntAct; Q8GY31; 3.
STRING; 3702.AT5G03455.1; -.
PaxDb; Q8GY31; -.
EnsemblPlants; AT5G03455.1; AT5G03455.1; AT5G03455.
GeneID; 831832; -.
Gramene; AT5G03455.1; AT5G03455.1; AT5G03455.
KEGG; ath:AT5G03455; -.
Araport; AT5G03455; -.
TAIR; locus:505006579; AT5G03455.
eggNOG; ENOG410IQGW; Eukaryota.
eggNOG; ENOG4111VH0; LUCA.
HOGENOM; HOG000162894; -.
InParanoid; Q8GY31; -.
KO; K18065; -.
OMA; DYIGGHI; -.
OrthoDB; EOG09360QPX; -.
PhylomeDB; Q8GY31; -.
BioCyc; ARA:AT5G03455-MONOMER; -.
SABIO-RK; Q8GY31; -.
EvolutionaryTrace; Q8GY31; -.
PRO; PR:Q8GY31; -.
Proteomes; UP000006548; Chromosome 5.
ExpressionAtlas; Q8GY31; baseline and differential.
Genevisible; Q8GY31; AT.
GO; GO:0009507; C:chloroplast; IDA:TAIR.
GO; GO:0005739; C:mitochondrion; IDA:TAIR.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0008794; F:arsenate reductase (glutaredoxin) activity; IEA:UniProtKB-EC.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004725; F:protein tyrosine phosphatase activity; IDA:TAIR.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:0006468; P:protein phosphorylation; IDA:TAIR.
GO; GO:0046685; P:response to arsenic-containing substance; IMP:TAIR.
Gene3D; 3.40.250.10; -; 1.
InterPro; IPR001763; Rhodanese-like_dom.
InterPro; IPR036873; Rhodanese-like_dom_sf.
Pfam; PF00581; Rhodanese; 1.
SMART; SM00450; RHOD; 1.
SUPFAM; SSF52821; SSF52821; 1.
PROSITE; PS50206; RHODANESE_3; 1.
1: Evidence at protein level;
3D-structure; Cell cycle; Cell division; Complete proteome; Hydrolase;
Metal-binding; Mitosis; Nucleus; Oxidoreductase; Protein phosphatase;
Reference proteome; Zinc.
CHAIN 1 146 Dual specificity phosphatase Cdc25.
/FTId=PRO_0000198663.
DOMAIN 34 135 Rhodanese. {ECO:0000255|PROSITE-
ProRule:PRU00173}.
REGION 45 48 Substrate-binding.
REGION 68 71 Substrate-binding.
REGION 90 92 Substrate-binding.
COMPBIAS 11 14 Poly-Lys.
ACT_SITE 86 86 Cysteine persulfide intermediate.
{ECO:0000255|PROSITE-ProRule:PRU00173}.
METAL 53 53 Zinc. {ECO:0000269|PubMed:15329414,
ECO:0000269|PubMed:15336525}.
METAL 134 134 Zinc. {ECO:0000269|PubMed:15329414,
ECO:0000269|PubMed:15336525}.
METAL 136 136 Zinc. {ECO:0000269|PubMed:15329414,
ECO:0000269|PubMed:15336525}.
METAL 141 141 Zinc. {ECO:0000269|PubMed:15329414,
ECO:0000269|PubMed:15336525}.
MUTAGEN 86 86 C->S: Loss of phosphatase activity.
{ECO:0000269|PubMed:15329414}.
MUTAGEN 145 145 C->S: No major structural changes.
{ECO:0000269|PubMed:15336525}.
STRAND 19 24 {ECO:0000244|PDB:1T3K}.
TURN 26 31 {ECO:0000244|PDB:1T3K}.
STRAND 38 44 {ECO:0000244|PDB:1T3K}.
HELIX 47 50 {ECO:0000244|PDB:1T3K}.
STRAND 56 60 {ECO:0000244|PDB:1T3K}.
STRAND 63 66 {ECO:0000244|PDB:1T3K}.
HELIX 69 74 {ECO:0000244|PDB:1T3K}.
STRAND 81 87 {ECO:0000244|PDB:1T3K}.
STRAND 90 92 {ECO:0000244|PDB:1T3K}.
HELIX 93 106 {ECO:0000244|PDB:1T3K}.
STRAND 107 109 {ECO:0000244|PDB:1T3K}.
STRAND 113 121 {ECO:0000244|PDB:1T3K}.
HELIX 124 129 {ECO:0000244|PDB:1T3K}.
SEQUENCE 146 AA; 16450 MW; EA2DD0E79784D538 CRC64;
MGRSIFSFFT KKKKMAMARS ISYITSTQLL PLHRRPNIAI IDVRDEERNY DGHIAGSLHY
ASGSFDDKIS HLVQNVKDKD TLVFHCALSQ VRGPTCARRL VNYLDEKKED TGIKNIMILE
RGFNGWEASG KPVCRCAEVP CKGDCA


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Genprice Inc, Invoices and accounting
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