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Reviewed, UniProtKB/Swiss-Prot Q38924 (PPA12_ARATH)

Last modified February 9, 2010. Version 88. 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:
    Fe(3+)-Zn(2+) purple acid phosphatase 12
      Short name=PAP
    EC=3.1.3.2
Alternative name(s):
    Iron(III)-zinc(II) purple acid phosphatase 12
Gene names
Name: PAP12
Synonyms: At10, Ath1, PAP1
Ordered Locus Names: At2g27190
ORF Names: T22O13.4
OrganismArabidopsis thaliana (Mouse-ear cress) [Complete proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsrosidsmalvidsBrassicalesBrassicaceaeArabidopsis

Protein attributes

Sequence length469 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; disulfide-linked By similarity.

Subcellular location

Secreted.

Tissue specificity

Expressed in roots, stems, leaves, flowers and siliques. Ref.6

Induction

Sligthly by phosphate deprivation. Ref.1

Sequence similarities

Belongs to the metallophosphoesterase superfamily. Purple acid phosphatase family.

Ontologies

Keywords
   Cellular componentSecreted
   DomainSignal
   LigandIron
Metal-binding
Zinc
   Molecular functionHydrolase
   PTMDisulfide bond
Glycoprotein
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processcellular response to phosphate starvation

Inferred from expression pattern. Source: TAIR

   Cellular componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

plant-type cell wall

Inferred from direct assay. Source: TAIR

   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 – 2828 Potential
Chain29 – 469441Fe(3+)-Zn(2+) purple acid phosphatase 12
PRO_0000023993

Regions

Region356 – 3583Substrate binding By similarity

Sites

Active site3291Proton donor By similarity
Metal binding1681Iron By similarity
Metal binding1971Iron By similarity
Metal binding1971Zinc By similarity
Metal binding2001Iron By similarity
Metal binding2341Zinc By similarity
Metal binding3191Zinc By similarity
Metal binding3561Zinc By similarity
Metal binding3581Iron By similarity
Binding site2341Substrate By similarity

Amino acid modifications

Glycosylation1141N-linked (GlcNAc...) Potential
Glycosylation1761N-linked (GlcNAc...) Potential
Glycosylation3071N-linked (GlcNAc...) Potential
Glycosylation4291N-linked (GlcNAc...) Potential
Disulfide bond378Interchain By similarity

Experimental info

Sequence conflict571H → P in AAA91803. Ref.2
Sequence conflict571H → P in AAL57700. Ref.4
Sequence conflict571H → P in AAM91429. Ref.4
Sequence conflict911Q → R in AAA91803. Ref.2
Sequence conflict971E → K in AAA91803. Ref.2
Sequence conflict1511I → T in AAA91803. Ref.2
Sequence conflict2161G → R in CAA23388. Ref.5
Sequence conflict2641G → R in CAA23388. Ref.5

Sequences

Sequence LengthMass (Da)Tools
Q38924-1 [UniParc].

Last modified June 6, 2002. Version 2.
Checksum: 21BFB941002B931B

FASTA46954,163
        10         20         30         40         50         60 
MSSRSDLKIK RVSLIIFLLS VLVEFCYGGF TSEYVRGSDL PDDMPLDSDV FEVPPGHNSP 

        70         80         90        100        110        120 
QQVHVTQGNH EGNGVIISWV TPVKPGSKTV QYWCENEKSR KQAEATVNTY RFFNYTSGYI 

       130        140        150        160        170        180 
HHCLIDDLEF DTKYYYEIGS GKWSRRFWFF IPPKSGPDVP YTFGLIGDLG QTYDSNSTLS 

       190        200        210        220        230        240 
HYEMNPGKGQ AVLFVGDLSY ADRYPNHDNN RWDTWGRFVE RSVAYQPWIW TAGNHEIDFV 

       250        260        270        280        290        300 
PDIGEIEPFK PFMNRYHTPH KASGSISPLW YSIKRASAYI IVMSCYSSYG IYTPQYKWLE 

       310        320        330        340        350        360 
KELQGVNRTE TPWLIVLVHS PFYSSYVHHY MEGETLRVMY EQWFVKYKVD VVFAGHVHAY 

       370        380        390        400        410        420 
ERSERVSNIA YNIVNGLCEP ISDESAPIYI TIGDGGNSEG LLTDMMQPQP KYSAFREASF 

       430        440        450        460 
GHGLLEIKNR THAYFSWNRN QDGNAVAADS VWLLNRFWRA QKKTWLDAF 

« 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], INDUCTION, GENE FAMILY, NOMENCLATURE.
Strain: cv. Col-1.
[2]Patel K.S., Lockless S.W., McKnight T.D.
Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: cv. Landsberg erecta.
[3]"Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana."
Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D., Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V., Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S., Cronin L.A. expand/collapse author list , Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.
Nature 402:761-768(1999) [PubMed: 10617197] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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].
Strain: cv. Columbia.
[5]"Further progress towards a catalogue of all Arabidopsis genes: analysis of a set of 5000 non-redundant ESTs."
Cooke R., Raynal M., Laudie M., Grellet F., Delseny M., Morris P.-C., Guerrier D., Giraudat J., Quigley F., Clabault G., Li Y.-F., Mache R., Krivitzky M., Gy I.J.-J., Kreis M., Lecharny A., Parmentier Y., Marbach J. expand/collapse author list , Fleck J., Clement B., Philipps G., Herve C., Bardet C., Tremousaygue D., Lescure B., Lacomme C., Roby D., Jourjon M.-F., Chabrier P., Charpenteau J.-L., Desprez T., Amselem J., Chiapello H., Hoefte H.
Plant J. 9:101-124(1996) [PubMed: 8580968] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 138-268.
Strain: cv. Columbia.
[6]"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
AF492664 mRNA. Translation: AAM15913.1.
U48448 Genomic DNA. Translation: AAA91803.1.
AC007290 Genomic DNA. Translation: AAD26885.1.
AY065067 mRNA. Translation: AAL57700.1.
AY133599 mRNA. Translation: AAM91429.1.
F20043 mRNA. Translation: CAA23388.1.
IPIIPI00540349.
PIRH84669.
RefSeqNP_180287.2.
UniGeneAt.28647
Rsa.6200

3D structure databases

SMRQ38924. Positions 43-458.
ModBaseSearch...

Proteomic databases

PRIDEQ38924.

Genome annotation databases

GeneID817261.
GenomeReviewsGene locus AT2G27190 in contig CT485783_GR.
KEGGath:AT2G27190.
NMPDRfig|3702.1.peg.9750.

Organism-specific databases

TAIRAt2g27190.

Phylogenomic databases

eggNOGKOG1378.
HOGENOMHBG316723.
InParanoidQ38924.
OMAISDESAP.
PhylomeDBQ38924.

Enzyme and pathway databases

BRENDA3.1.3.2. 302.

Gene expression databases

ArrayExpressQ38924.
GenevestigatorQ38924.
GermOnlineAT2G27190. Arabidopsis thaliana.

Family and domain databases

InterProIPR004843. M-pesterase.
IPR008963. Purple_acid_Pase-like_N.
IPR015914. Purple_acid_Pase_N.
[Graphical view]
Gene3DG3DSA:2.60.40.380. Purple_acid_Pase_N. 1 hit.
PfamPF00149. Metallophos. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePPA12_ARATH
AccessionPrimary (citable) accession number: Q38924
Secondary accession number(s): Q42349 expand/collapse secondary AC list , Q540Q7, Q8VZC6, Q9SHS9
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: June 6, 2002
Last modified: February 9, 2010
This is version 88 of the entry and version 2 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