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P48529 (PPX1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 101. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Serine/threonine-protein phosphatase PP-X isozyme 1
EC=3.1.3.16
Gene names
Name:PPX1
Synonyms:EP124, EP129
Ordered Locus Names:At4g26720
ORF Names:F10M23.60
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length305 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Catalytic activity

A phosphoprotein + H2O = a protein + phosphate.

Cofactor

Binds 1 iron ion per subunit By similarity.

Binds 1 manganese ion per subunit By similarity.

Subcellular location

Plastid stroma Ref.2.

Tissue specificity

Ubiquitous, mostly expressed in root mersitems, flowers, and vascular tissues. Ref.2

Sequence similarities

Belongs to the PPP phosphatase family. PP-4 (PP-X) subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 305305Serine/threonine-protein phosphatase PP-X isozyme 1
PRO_0000058886

Sites

Active site1121Proton donor By similarity
Metal binding511Iron By similarity
Metal binding531Iron By similarity
Metal binding791Iron By similarity
Metal binding791Manganese By similarity
Metal binding1111Manganese By similarity
Metal binding1611Manganese By similarity
Metal binding2361Manganese By similarity

Sequences

Sequence LengthMass (Da)Tools
P48529 [UniParc].

Last modified February 1, 1996. Version 1.
Checksum: 3FBBEADB2DA5B650

FASTA30534,738
        10         20         30         40         50         60 
MSDLDRQIGQ LKRCEPLSES EVKALCLKAM EILVEESNVQ RVDAPVTLCG DIHGQFYDMM 

        70         80         90        100        110        120 
ELFKVGGDCP KTNYLFMGDF VDRGYYSVET FLLLLALKVR YPDRITLIRG NHESRQITQV 

       130        140        150        160        170        180 
YGFYDECLRK YGSSNVWRYC TDIFDYMSLS AVVENKIFCV HGGLSPAIMT LDQIRTIDRK 

       190        200        210        220        230        240 
QEVPHDGAMC DLLWSDPEDI VDGWGLSPRG AGFLFGGSVV TSFNHSNNID YIARAHQLVM 

       250        260        270        280        290        300 
EGYKWMFDSQ IVTVWSAPNY CYRCGNVASI LELDENLNKE FRVFDAAQQD SRGPPAKKPA 


PDYFL

« Hide

References

« Hide 'large scale' references
[1]"Identification and molecular cloning of two homologues of protein phosphatase X from Arabidopsis thaliana."
Perez-Callejon E., Casamayor A., Pujol G., Clua E., Ferrer A., Arino J.
Plant Mol. Biol. 23:1177-1185(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Leaf.
[2]"The Arabidopsis thaliana PPX/PP4 phosphatases: molecular cloning and structural organization of the genes and immunolocalization of the proteins to plastids."
Pujol G., Baskin T.I., Casamayor A., Cortadellas N., Ferrer A., Arino J.
Plant Mol. Biol. 44:499-511(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
Strain: cv. Columbia.
[3]"Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."
Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B. expand/collapse author list , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R.
Nature 402:769-777(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[4]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[5]"Arabidopsis PPP family of serine/threonine phosphatases."
Farkas I., Dombradi V., Miskei M., Szabados L., Koncz C.
Trends Plant Sci. 12:169-176(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: GENE FAMILY, NOMENCLATURE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		Z22587 mRNA. Translation: CAA80302.1.
AF030289 Genomic DNA. Translation: AAB86418.1.
AL035440 Genomic DNA. Translation: CAB36518.1.
AL161565 Genomic DNA. Translation: CAB79527.1.
CP002687 Genomic DNA. Translation: AEE85245.1.
IPIIPI00534006.
PIRS42558.
RefSeqNP_194402.1. NM_118806.5.
UniGeneAt.106.

3D structure databases

ProteinModelPortalP48529.
SMRP48529. Positions 3-287.
ModBaseSearch...

Protein-protein interaction databases

STRING3702.AT4G26720.1-P.

Proteomic databases

PaxDbP48529.
PRIDEP48529.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT4G26720.1; AT4G26720.1; AT4G26720.
GeneID828779.
KEGGath:AT4G26720.

Organism-specific databases

TAIRAt4g26720.

Phylogenomic databases

eggNOGCOG0639.
HOGENOMHOG000172696.
InParanoidP48529.
KOK01090.
OMATIVTVWS.
PhylomeDBP48529.
ProtClustDBCLSN2686048.

Gene expression databases

ArrayExpressP48529.
GenevestigatorP48529.
GermOnlineAT4G26720. Arabidopsis thaliana.

Family and domain databases

InterProIPR004843. Metallo_PEstase_dom.
IPR006186. Ser/Thr-sp_prot-phosphatase.
[Graphical view]
PfamPF00149. Metallophos. 1 hit.
[Graphical view]
PRINTSPR00114. STPHPHTASE.
SMARTSM00156. PP2Ac. 1 hit.
[Graphical view]
PROSITEPS00125. SER_THR_PHOSPHATASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePPX1_ARATH
AccessionPrimary (citable) accession number: P48529
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: May 1, 2013
This is version 101 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents