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Q8GY31 (CDC25_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 89. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length146 AA.
Sequence statusComplete.
Protein existenceEvidence 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 146146Dual specificity phosphatase Cdc25
PRO_0000198663

Regions

Domain34 – 135102Rhodanese
Region45 – 484Substrate-binding
Region68 – 714Substrate-binding
Region90 – 923Substrate-binding
Compositional bias11 – 144Poly-Lys

Sites

Active site861Phosphocysteine intermediate Probable
Metal binding531Zinc
Metal binding1341Zinc
Metal binding1361Zinc
Metal binding1411Zinc

Experimental info

Mutagenesis861C → S: Loss of phosphatase activity. Ref.11
Mutagenesis1451C → S: No major structural changes. Ref.10

Secondary structure

......................... 146
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q8GY31 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: EA2DD0E79784D538

FASTA14616,450
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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.
PIRT48370.
RefSeqNP_568119.1. NM_120425.2.
UniGeneAt.43043.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1T3KNMR-A15-146[»]
ProteinModelPortalQ8GY31.
SMRQ8GY31. Positions 15-146.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid17108. 3 interactions.
IntActQ8GY31. 3 interactions.

Proteomic databases

PaxDbQ8GY31.
PRIDEQ8GY31.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT5G03455.1; AT5G03455.1; AT5G03455.
GeneID831832.
KEGGath:AT5G03455.

Organism-specific databases

TAIRAT5G03455.

Phylogenomic databases

eggNOGNOG294009.
HOGENOMHOG000162894.
InParanoidQ8GY31.
KOK18065.
OMARSISYIT.
PhylomeDBQ8GY31.

Enzyme and pathway databases

BioCycARA:AT5G03455-MONOMER.
SABIO-RKQ8GY31.

Gene expression databases

GenevestigatorQ8GY31.

Family and domain databases

Gene3D3.40.250.10. 1 hit.
InterProIPR001763. Rhodanese-like_dom.
[Graphical view]
PfamPF00581. Rhodanese. 1 hit.
[Graphical view]
SMARTSM00450. RHOD. 1 hit.
[Graphical view]
SUPFAMSSF52821. SSF52821. 1 hit.
PROSITEPS50206. RHODANESE_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ8GY31.

Entry information

Entry nameCDC25_ARATH
AccessionPrimary (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: June 11, 2014
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names