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O23244 (PPA25_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 87. 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:
Purple acid phosphatase 25
EC=3.1.3.2
Gene names
Name:PAP25
Synonyms:AT7, ATH2
Ordered Locus Names:At4g36350
ORF Names:C7A10.1010, F23E13.190
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 length466 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Catalytic activity

A phosphate monoester + H2O = an alcohol + phosphate.

Cofactor

Binds 1 iron ion per subunit By similarity.

Binds 1 zinc ion per subunit By similarity.

Subunit structure

Homodimer By similarity.

Subcellular location

Secreted By similarity.

Tissue specificity

Specifically expressed in flowers. Ref.1

Sequence similarities

Belongs to the metallophosphoesterase superfamily. Purple acid phosphatase family.

Ontologies

Keywords
   Cellular componentSecreted
   DomainSignal
   LigandIron
Metal-binding
Zinc
   Molecular functionHydrolase
   PTMGlycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Cellular_componentcell wall

Inferred from direct assay PubMed 14595688. Source: TAIR

extracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionacid phosphatase activity

Inferred from sequence or structural similarity Ref.1. Source: TAIR

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2121 Potential
Chain22 – 466445Purple acid phosphatase 25
PRO_0000372828

Regions

Region351 – 3533Substrate binding By similarity

Sites

Active site3241Proton donor By similarity
Metal binding1641Iron By similarity
Metal binding1921Iron By similarity
Metal binding1921Zinc By similarity
Metal binding1951Iron By similarity
Metal binding2291Zinc By similarity
Metal binding3141Zinc By similarity
Metal binding3511Zinc By similarity
Metal binding3531Iron By similarity
Binding site2291Substrate By similarity

Amino acid modifications

Glycosylation1721N-linked (GlcNAc...) Potential
Glycosylation3671N-linked (GlcNAc...) Potential
Glycosylation4241N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
O23244 [UniParc].

Last modified November 1, 1998. Version 2.
Checksum: A2AF1C1687922817

FASTA46652,969
        10         20         30         40         50         60 
MRMNKILLVF VFLSIATVIN SGTTSNFVRT AQPSTEMSLE TFPSPAGHNA PEQVHIVQGD 

        70         80         90        100        110        120 
YNGRGIIISW VTPLNLAGSN VVTYWKAVDG DVKPKKKRGH ASTSSYRFYD YTSGFLHHAT 

       130        140        150        160        170        180 
IKGLEYDTKY IYEVGTDGSV RQFSFTSPPK VGPDVPYTFG IIGDLGQTLA SNETLYHYMS 

       190        200        210        220        230        240 
NPKGQAVLFP GDLSYADDHP NHDQRKWDSW GRFVEPCAAY QTFIYAAGNH EIDFVPNIGE 

       250        260        270        280        290        300 
PHAFKPYIHR YHNAYKASKS ISPLWYSIRR ASAHIIVLSS YSAYGKYTPQ YVWLEQELKK 

       310        320        330        340        350        360 
VNREETPWLI VMVHSPWYNS NNYHYMEGES MRAMFESWFV NSKVDLVLSG HVHSYERSER 

       370        380        390        400        410        420 
VSNIKYNITN GLSYPVKDPS APIYITIGDG GNIEGIANSF TDPQPSYSAY REASFGHAVL 

       430        440        450        460 
EIYNRTHAYY TWHRNQDNEP VAADSIMLHN RYFFPVEELE SGNTRA

« Hide

References

« Hide 'large scale' references
[1]"Expression patterns of purple acid phosphatase genes in Arabidopsis organs and functional analysis of AtPAP23 predominantly transcribed in flower."
Zhu H., Qian W., Lu X., Li D., Liu X., Liu K., Wang D.
Plant Mol. Biol. 59:581-594(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
Strain: cv. Columbia.
[2]"Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of Arabidopsis thaliana."
Bevan M., Bancroft I., Bent E., Love K., Goodman H.M., Dean C., Bergkamp R., Dirkse W., van Staveren M., Stiekema W., Drost L., Ridley P., Hudson S.-A., Patel K., Murphy G., Piffanelli P., Wedler H., Wedler E. expand/collapse author list , Wambutt R., Weitzenegger T., Pohl T., Terryn N., Gielen J., Villarroel R., De Clercq R., van Montagu M., Lecharny A., Aubourg S., Gy I., Kreis M., Lao N., Kavanagh T., Hempel S., Kotter P., Entian K.-D., Rieger M., Schaefer M., Funk B., Mueller-Auer S., Silvey M., James R., Monfort A., Pons A., Puigdomenech P., Douka A., Voukelatou E., Milioni D., Hatzopoulos P., Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A., Moores T., Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S., Ansorge W., Cooke R., Berger C., Delseny M., Voet M., Volckaert G., Mewes H.-W., Klosterman S., Schueller C., Chalwatzis N.
Nature 391:485-488(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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]"Purple acid phosphatases of Arabidopsis thaliana. Comparative analysis and differential regulation by phosphate deprivation."
Li D., Zhu H., Liu K., Liu X., Leggewie G., Udvardi M., Wang D.
J. Biol. Chem. 277:27772-27781(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: GENE FAMILY, NOMENCLATURE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AY390529 mRNA. Translation: AAQ93684.1.
Z99708 Genomic DNA. Translation: CAB16853.1.
AL022141 Genomic DNA. Translation: CAA18136.1.
AL161589 Genomic DNA. Translation: CAB80301.1.
CP002687 Genomic DNA. Translation: AEE86645.1.
IPIIPI00536177.
PIRT04599.
RefSeqNP_195353.1. NM_119798.1.
UniGeneAt.31333.

3D structure databases

HSSPHSSP built from PDB template 4KBP based on UniProtKB P80366.
ProteinModelPortalO23244.
SMRO23244. Positions 40-453.
ModBaseSearch...

Protein-protein interaction databases

STRING3702.AT4G36350.1-P.

Proteomic databases

PaxDbO23244.
PRIDEO23244.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT4G36350.1; AT4G36350.1; AT4G36350.
GeneID829787.
KEGGath:AT4G36350.

Organism-specific databases

TAIRAt4g36350.

Phylogenomic databases

eggNOGCOG1409.
HOGENOMHOG000238330.
InParanoidO23244.
OMAVEPCAAY.
PhylomeDBO23244.
ProtClustDBCLSN2682888.

Gene expression databases

GenevestigatorO23244.

Family and domain databases

Gene3D2.60.40.380. 1 hit.
InterProIPR004843. Metallo_PEstase_dom.
IPR008963. Purple_acid_Pase-like_N.
IPR015914. Purple_acid_Pase_N.
IPR025733. Purple_acid_PPase_C_dom.
[Graphical view]
PfamPF00149. Metallophos. 1 hit.
PF14008. Metallophos_C. 1 hit.
[Graphical view]
SUPFAMSSF49363. Purple_Pase_N. 1 hit.
ProtoNetSearch...

Entry information

Entry namePPA25_ARATH
AccessionPrimary (citable) accession number: O23244
Entry history
Integrated into UniProtKB/Swiss-Prot: May 5, 2009
Last sequence update: November 1, 1998
Last modified: May 1, 2013
This is version 87 of the entry and version 2 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