Reviewed, UniProtKB/Swiss-Prot Q8GY31 (CDC25_ARATH)

Names and origin

Protein names

Recommended name:
    Dual specificity phosphatase Cdc25
    EC=3.1.3.48
Alternative name(s):
    Arath;CDC25

Gene names

Name:	CDC25
Ordered Locus Names:	At5g03455
ORF Names:	F12E4_220

Organism

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

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › 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. Ref.6
Catalytic activity	Protein tyrosine phosphate + H2O = protein tyrosine + phosphate. Ref.6
Enzyme regulation	Inhibited by NSC95397. Ref.6
Subcellular location	Nucleus Probable.
Miscellaneous	Binds 1 zinc ion which is not required for enzyme activity.
Sequence similarities	Belongs to the MPI phosphatase family. Contains 1 rhodanese domain.
Biophysicochemical properties	Kinetic parameters: KM=50 mM for para-nitrophenyl phosphate
Sequence caution	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 Protein phosphatase
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	cell division Inferred from electronic annotation. Source: UniProtKB-KW mitosis Inferred from electronic annotation. Source: UniProtKB-KW protein amino acid phosphorylation Ref.5 Inferred from direct assay. Source: TAIR response to arsenic Inferred from mutant phenotype. Source: TAIR
Cellular component	chloroplast Inferred from direct assay. Source: TAIR nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	arsenate reductase activity Inferred from genetic interaction. Source: TAIR protein tyrosine phosphatase activity Ref.5 Inferred from direct assay. Source: TAIR zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
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.6

Mutagenesis

145

1

C → S: No major structural changes. Ref.5

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

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)
	Q8GY31-1 [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: 11130714] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[2]	"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: 11910074] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[3]	"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: 14593172] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[4]	"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].
[5]	"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: 15336525] [Abstract] Cited for: STRUCTURE BY NMR OF 15-146 OF CYS-145 IN COMPLEX WITH ZINC, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF CYS-145.
[6]	"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: 15329414] [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.
[7]	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.
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.

UniGene

At.43043
Rra.26784
Rsa.15200

3D structure databases

PDBe
RCSB PDB
PDBj

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

ModBase

Search...

Protein-protein interaction databases

STRING

Q8GY31.

Proteomic databases

PRIDE

Q8GY31.

Genome annotation databases

GeneID

831832.

GenomeReviews

Gene locus AT5G03455 in contig BA000015_GR.

KEGG

ath:AT5G03455.

NMPDR

fig|3702.1.peg.22431.

Organism-specific databases

TAIR

At5g03455.

Phylogenomic databases

eggNOG

KOG3772.

HOGENOM

HBG587364.

InParanoid

Q8GY31.

OMA

RGPTCAR.

PhylomeDB

Q8GY31.

Enzyme and pathway databases

BRENDA

3.1.3.48. 302.

Gene expression databases

ArrayExpress

Q8GY31.

Genevestigator

Q8GY31.

GermOnline

AT5G03455. Arabidopsis thaliana.

Family and domain databases

InterPro

IPR001763. Rhodanese-like.
[Graphical view]

Gene3D

G3DSA:3.40.250.10. Rhodanese-like. 1 hit.

Pfam

PF00581. Rhodanese. 1 hit.
[Graphical view]

SMART

SM00450. RHOD. 1 hit.
[Graphical view]

PROSITE

PS50206. RHODANESE_3. 1 hit.
[Graphical view]

ProtoNet

Search...

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:	February 9, 2010
This is version 56 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)