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Reviewed, UniProtKB/Swiss-Prot Q8S340 (PPA22_ARATH)

Last modified February 9, 2010. Version 46. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Purple acid phosphatase 22
    EC=3.1.3.2
Gene names
Name: PAP22
Synonyms: AT6
Ordered Locus Names: At3g52820
ORF Names: F3C22.220
OrganismArabidopsis thaliana (Mouse-ear cress) [Complete proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsrosidsmalvidsBrassicalesBrassicaceaeArabidopsis

Protein attributes

Sequence length434 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

Expressed in roots, stems, leaves, flowers and siliques. Ref.5

Sequence similarities

Belongs to the metallophosphoesterase superfamily. Purple acid phosphatase family.

Sequence caution

The sequence CAB89243.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

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

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionacid phosphatase activity

Inferred from electronic annotation. Source: EC

iron ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

zinc 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 – 2222 Potential
Chain23 – 434412Purple acid phosphatase 22
PRO_0000372825

Regions

Region329 – 3313Substrate binding By similarity

Sites

Active site3021Proton donor By similarity
Metal binding1481Iron By similarity
Metal binding1751Iron By similarity
Metal binding1751Zinc By similarity
Metal binding1781Iron By similarity
Metal binding2081Zinc By similarity
Metal binding2921Zinc By similarity
Metal binding3291Zinc By similarity
Metal binding3311Iron By similarity
Binding site2081Substrate By similarity

Amino acid modifications

Glycosylation1161N-linked (GlcNAc...) Potential
Glycosylation4031N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
Q8S340-1 [UniParc].

Last modified June 1, 2002. Version 1.
Checksum: 103381F91CB4EB00

FASTA43449,357
        10         20         30         40         50         60 
MKLFGLFLSF TLLFLCPFIS QADVPELSRQ PPRPIVFVHN DRSKSDPQQV HISLAGKDHM 

        70         80         90        100        110        120 
RVTFITEDNK VESVVEYGKQ PGKYDGKATG ECTSYKYFFY KSGKIHHVKI GPLQANTTYY 

       130        140        150        160        170        180 
YRCGGNGPEF SFKTPPSTFP VEFAIVGDLG QTEWTAATLS HINSQDYDVF LLPGDLSYAD 

       190        200        210        220        230        240 
THQPLWDSFG RLVEPLASKR PWMVTEGNHE IEFFPIIEHT TFKSYNARWL MPHTESFSTS 

       250        260        270        280        290        300 
NLYYSFDVAG VHTVMLGSYT DFDCESDQYQ WLQADLAKVD RKTTPWVVVL LHAPWYNTNE 

       310        320        330        340        350        360 
AHEGEGESMR EAMESLLFNA RVDVVFSGHV HAYERFKRVY NNKADPCGPI HITIGDGGNR 

       370        380        390        400        410        420 
EGLALSFKKP PSPLSEFRES SFGHGRLKVM DGKRAHWSWH RNNDSNSLLA DEVWLDSLST 

       430 
SSSCWPSSRS NDEL 

« Hide

References

« Hide 'large scale' references
[1]"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: 12021284] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], GENE FAMILY, NOMENCLATURE.
Strain: cv. Col-1.
[2]"Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana."
Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., Choisne N., Artiguenave F. expand/collapse author list , Robert C., Brottier P., Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.
Nature 408:820-822(2000) [PubMed: 11130713] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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: 11910074] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 172-434.
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: 14593172] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 203-434.
Strain: cv. Columbia.
[5]"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: 16244908] [Abstract]
Cited for: TISSUE SPECIFICITY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF492668 mRNA. Translation: AAM15917.1.
AL353912 Genomic DNA. Translation: CAB89243.1. Sequence problems.
AK118546 mRNA. Translation: BAC43148.1.
BT006218 mRNA. Translation: AAP12867.1.
IPIIPI00541443.
PIRT49035.
RefSeqNP_190850.2.
UniGeneAt.35258

3D structure databases

HSSPHSSP built from PDB template 4KBP based on UniProtKB P80366.
SMRQ8S340. Positions 45-416.
ModBaseSearch...

Proteomic databases

PRIDEQ8S340.

Genome annotation databases

GeneID824448.
GenomeReviewsGene locus AT3G52820 in contig BA000014_GR.
KEGGath:AT3G52820.
NMPDRfig|3702.1.peg.16554.

Organism-specific databases

TAIRAt3g52820.

Phylogenomic databases

eggNOGKOG1378.
InParanoidQ8S340.
OMALTRSHDN.
PhylomeDBQ8S340.

Gene expression databases

GenevestigatorQ8S340.

Family and domain databases

InterProIPR004843. M-pesterase.
IPR008963. Purple_acid_Pase-like_N.
[Graphical view]
PfamPF00149. Metallophos. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePPA22_ARATH
AccessionPrimary (citable) accession number: Q8S340
Secondary accession number(s): Q8GWZ2, Q9LXI3
Entry history
Integrated into UniProtKB/Swiss-Prot: May 5, 2009
Last sequence update: June 1, 2002
Last modified: February 9, 2010
This is version 46 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents