Q8GY31 (CDC25_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Dual specificity phosphatase Cdc25
EC=3.1.3.48

Alternative name(s):
Arath;CDC25
Arsenate reductase 2
EC=1.20.4.-
Sulfurtransferase 5
Short name=AtStr5

Gene names

Name:	CDC25
Synonyms:	ACR2, STR5
Ordered Locus Names:	At5g03455
ORF Names:	F12E4_220

Organism

Arabidopsis thaliana (Mouse-ear cress) [Reference proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	146 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Tyrosine protein phosphatase that dephosphorylates CDK complex and activate its kinase activity in vitro. Ref.7 Ref.11 Arsenate reductase that plays a major role in the reduction of arsenate to arsenite and arsenic retention in roots. Ref.7 Ref.11
Catalytic activity	Protein tyrosine phosphate + H2O = protein tyrosine + phosphate. Ref.11
Enzyme regulation	Inhibited by NSC95397. Ref.11
Subcellular location	Nucleus Probable.
Tissue specificity	Expressed in roots and at lower levels in shoots (at protein level). Expressed in leaves, stems and flowers. Ref.6 Ref.7
Disruption phenotype	No visible phenotype under normal growth conditions, but plants show reduced root size when grown in presence of hydroxyurea. Ref.9
Miscellaneous	Binds 1 zinc ion which is not required for enzyme activity (Ref.11). Plants silencing ACR2 show increased sensitivity to arsenate but not arsenite (Ref.7).
Sequence similarities	Belongs to the MPI phosphatase family. Contains 1 rhodanese domain.
Biophysicochemical properties	Kinetic parameters: KM=50 mM for para-nitrophenyl phosphate Ref.10 Ref.11
Sequence caution	The sequence AAM63780.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. The sequence CAB83305.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Biological process	Cell cycle Cell division Mitosis
Cellular component	Nucleus
Ligand	Metal-binding Zinc
Molecular function	Hydrolase Oxidoreductase Protein phosphatase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell division Inferred from electronic annotation. Source: UniProtKB-KW mitosis Inferred from electronic annotation. Source: UniProtKB-KW protein phosphorylation Inferred from direct assay Ref.10. Source: TAIR response to arsenic-containing substance Inferred from mutant phenotype Ref.7. Source: TAIR
Cellular_component	chloroplast Inferred from direct assay PubMed 18431481. Source: TAIR mitochondrion Inferred from direct assay PubMed 21908688. Source: TAIR nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	arsenate reductase activity Inferred from genetic interaction Ref.7. Source: TAIR metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein tyrosine phosphatase activity Inferred from direct assay Ref.10. Source: TAIR
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 146

146

Dual specificity phosphatase Cdc25

PRO_0000198663

Regions

Domain

34 – 135

102

Rhodanese

Region

45 – 48

4

Substrate-binding

Region

68 – 71

4

Substrate-binding

Region

90 – 92

3

Substrate-binding

Compositional bias

11 – 14

4

Poly-Lys

Sites

Active site

86

1

Phosphocysteine intermediate Probable

Metal binding

53

1

Zinc

Metal binding

134

1

Zinc

Metal binding

136

1

Zinc

Metal binding

141

1

Zinc

Experimental info

Mutagenesis

86

1

C → S: Loss of phosphatase activity. Ref.11

Mutagenesis

145

1

C → S: No major structural changes. Ref.10

Secondary structure

1

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146

Helix Strand Turn

Details...

Beta strand

19 – 24

6

Turn

26 – 31

6

Beta strand

38 – 44

7

Helix

47 – 50

4

Beta strand

56 – 60

5

Beta strand

63 – 66

4

Helix

69 – 74

6

Beta strand

81 – 87

7

Beta strand

90 – 92

3

Helix

93 – 106

14

Beta strand

107 – 109

3

Beta strand

113 – 121

9

Helix

124 – 129

6

Sequences

	Sequence		Length	Mass (Da)
	Q8GY31 [UniParc]. Last modified March 1, 2003. Version 1. Checksum: EA2DD0E79784D538	FASTA	146	16,450
	10 20 30 40 50 60 MGRSIFSFFT KKKKMAMARS ISYITSTQLL PLHRRPNIAI IDVRDEERNY DGHIAGSLHY 70 80 90 100 110 120 ASGSFDDKIS HLVQNVKDKD TLVFHCALSQ VRGPTCARRL VNYLDEKKED TGIKNIMILE 130 140 RGFNGWEASG KPVCRCAEVP CKGDCA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana." 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. Nature 408:823-826(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[2]	The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: cv. Columbia.
[3]	"Functional annotation of a full-length Arabidopsis cDNA collection." 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. Science 296:141-145(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[4]	"Empirical analysis of transcriptional activity in the Arabidopsis genome." 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. Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[5]	"Full-length cDNA from Arabidopsis thaliana." Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A. Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[6]	"The Arabidopsis CDC25 induces a short cell length when overexpressed in fission yeast: evidence for cell cycle function." Sorrell D.A., Chrimes D., Dickinson J.R., Rogers H.J., Francis D. New Phytol. 165:425-428(2005) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY.
[7]	"Hyperaccumulation of arsenic in the shoots of Arabidopsis silenced for arsenate reductase (ACR2)." Dhankher O.P., Rosen B.P., McKinney E.C., Meagher R.B. Proc. Natl. Acad. Sci. U.S.A. 103:5413-5418(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, TISSUE SPECIFICITY.
[8]	"Differential expression of Arabidopsis sulfurtransferases under various growth conditions." Bartels A., Mock H.P., Papenbrock J. Plant Physiol. Biochem. 45:178-187(2007) [PubMed] [Europe PMC] [Abstract] Cited for: GENE FAMILY.
[9]	"Arabidopsis T-DNA insertional lines for CDC25 are hypersensitive to hydroxyurea but not to zeocin or salt stress." Spadafora N.D., Doonan J.H., Herbert R.J., Bitonti M.B., Wallace E., Rogers H.J., Francis D. Ann. Bot. 107:1183-1192(2011) [PubMed] [Europe PMC] [Abstract] Cited for: DISRUPTION PHENOTYPE.
[10]	"Characterization of the Arabidopsis thaliana Arath;CDC25 dual-specificity tyrosine phosphatase." Landrieu I., Hassan S., Sauty M., Dewitte F., Wieruszeski J.-M., Inze D., de Veylder L., Lippens G. Biochem. Biophys. Res. Commun. 322:734-739(2004) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 15-146 OF CYS-145 IN COMPLEX WITH ZINC, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF CYS-145.
[11]	"A small CDC25 dual-specificity tyrosine-phosphatase isoform in Arabidopsis thaliana." 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. 101:13380-13385(2004) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 15-146 OF CYS-86 MUTANT IN COMPLEX WITH ZINC, FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF CYS-86.
[12]	Erratum 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)
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AL162751 Genomic DNA. Translation: CAB83305.1. Sequence problems.
CP002688 Genomic DNA. Translation: AED90607.1.
AK117898 mRNA. Translation: BAC42537.1.
BT003658 mRNA. Translation: AAO39886.1.
AY086729 mRNA. Translation: AAM63780.1. Different initiation.

IPI

IPI00542538.

PIR

T48370.

RefSeq

NP_568119.1. NM_120425.2.

UniGene

At.43043.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1T3K	NMR	-	A	15-146	[»]

ProteinModelPortal

Q8GY31.

SMR

Q8GY31. Positions 15-146.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q8GY31. 3 interactions.

Proteomic databases

PaxDb

Q8GY31.

PRIDE

Q8GY31.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblPlants

AT5G03455.1; AT5G03455.1; AT5G03455.

GeneID

831832.

KEGG

ath:AT5G03455.

Organism-specific databases

TAIR

At5g03455.

Phylogenomic databases

eggNOG

NOG294009.

HOGENOM

HOG000162894.

InParanoid

Q8GY31.

OMA

RSISYIT.

PhylomeDB

Q8GY31.

ProtClustDB

CLSN2689432.

Gene expression databases

Genevestigator

Q8GY31.

GermOnline

AT5G03455. Arabidopsis thaliana.

Family and domain databases

Gene3D

3.40.250.10. 1 hit.

InterPro

IPR001763. Rhodanese-like_dom.
[Graphical view]

Pfam

PF00581. Rhodanese. 1 hit.
[Graphical view]

SMART

SM00450. RHOD. 1 hit.
[Graphical view]

SUPFAM

SSF52821. Rhodanese-like. 1 hit.

PROSITE

PS00380. RHODANESE_1. False negative.
PS00683. RHODANESE_2. False negative.
PS50206. RHODANESE_3. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q8GY31.

Entry information

Entry name

CDC25_ARATH

Accession

Primary (citable) accession number: Q8GY31
Secondary accession number(s): Q8LC90, Q9LZE1

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 29, 2005
Last sequence update:	March 1, 2003
Last modified:	May 1, 2013
This is version 80 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program