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Q9SFU3 (PPA15_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 75. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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 15
EC=3.1.3.-
EC=3.1.3.2
Alternative name(s):
Phytase
Gene names
Name:PAP15
Synonyms:AT1
Ordered Locus Names:At3g07130
ORF Names:T1B9.21
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 length532 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Acid phosphatase activity with p-nitrophenyl phosphate (pNPP), D-myoinositol 1-phosphate (Ins1P1), phytic acid and Myo-inositol hexakisphosphate. Low or no activity with Glc-6-P and ATP. Confers shoot growth stimulation, enhanced salt and osmotic stress tolerance, and ABA insensitivity. May modulate ascorbic acid (AsA) levels by controlling the input of myoinositol into this branch of AsA biosynthesis. Ref.5

Catalytic activity

Myo-inositol hexakisphosphate + H2O = myo-inositol pentakisphosphate + phosphate.

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, cotyledons, leaves, flowers and siliques. Ref.1 Ref.5

Sequence similarities

Belongs to the metallophosphoesterase superfamily. Purple acid phosphatase family.

Biophysicochemical properties

pH dependence:

Optimum pH is 4.5. Ref.5

Ontologies

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

Inferred from mutant phenotype PubMed 19633233. Source: TAIR

seed germination

Inferred from mutant phenotype PubMed 19633233. Source: TAIR

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionacid phosphatase activity

Inferred from direct assay PubMed 19587103PubMed 19633233. 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 – 1919 Potential
Chain20 – 532513Purple acid phosphatase 15
PRO_0000372819

Regions

Region396 – 3983Substrate binding By similarity

Sites

Active site3691Proton donor By similarity
Metal binding1941Iron By similarity
Metal binding2211Iron By similarity
Metal binding2211Zinc By similarity
Metal binding2241Iron By similarity
Metal binding2771Zinc By similarity
Metal binding3591Zinc By similarity
Metal binding3961Zinc By similarity
Metal binding3981Iron By similarity
Binding site2771Substrate By similarity

Amino acid modifications

Glycosylation1361N-linked (GlcNAc...) Potential
Glycosylation2001N-linked (GlcNAc...) Potential
Glycosylation2311N-linked (GlcNAc...) Potential
Glycosylation2641N-linked (GlcNAc...) Potential
Glycosylation2861N-linked (GlcNAc...) Potential
Glycosylation3011N-linked (GlcNAc...) Potential
Glycosylation4911N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
Q9SFU3 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 658F6C88779444CD

FASTA53260,435
        10         20         30         40         50         60 
MTFLLLLLFC FLSPAISSAH SIPSTLDGPF VPVTVPLDTS LRGQAIDLPD TDPRVRRRVI 

        70         80         90        100        110        120 
GFEPEQISLS LSSDHDSIWV SWITGEFQIG KKVKPLDPTS INSVVQFGTL RHSLSHEAKG 

       130        140        150        160        170        180 
HSLVYSQLYP FDGLLNYTSG IIHHVRITGL KPSTIYYYRC GDPSRRAMSK IHHFRTMPVS 

       190        200        210        220        230        240 
SPSSYPGRIA VVGDLGLTYN TTDTISHLIH NSPDLILLIG DVSYANLYLT NGTSSDCYSC 

       250        260        270        280        290        300 
SFPETPIHET YQPRWDYWGR FMENLTSKVP LMVIEGNHEI ELQAENKTFE AYSSRFAFPF 

       310        320        330        340        350        360 
NESGSSSTLY YSFNAGGIHF VMLGAYIAYD KSAEQYEWLK KDLAKVDRSV TPWLVASWHP 

       370        380        390        400        410        420 
PWYSSYTAHY REAECMKEAM EELLYSYGTD IVFNGHVHAY ERSNRVYNYE LDPCGPVYIV 

       430        440        450        460        470        480 
IGDGGNREKM AIEHADDPGK CPEPLTTPDP VMGGFCAWNF TPSDKFCWDR QPDYSALRES 

       490        500        510        520        530 
SFGHGILEMK NETWALWTWY RNQDSSSEVG DQIYIVRQPD RCPLHHRLVN HC

« 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]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[3]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[4]"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.
[5]"An Arabidopsis purple acid phosphatase with phytase activity increases foliar ascorbate."
Zhang W., Gruszewski H.A., Chevone B.I., Nessler C.L.
Plant Physiol. 146:431-440(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF448726 mRNA. Translation: AAN74650.1.
AC012395 Genomic DNA. Translation: AAF20233.1.
CP002686 Genomic DNA. Translation: AEE74502.1.
IPIIPI00537478.
RefSeqNP_187369.1. NM_111593.2.
UniGeneAt.40395.
At.71829.

3D structure databases

HSSPHSSP built from PDB template 4KBP based on UniProtKB P80366.
ProteinModelPortalQ9SFU3.
SMRQ9SFU3. Positions 102-518.
ModBaseSearch...

Protein-protein interaction databases

STRING3702.AT3G07130.1-P.

Proteomic databases

PaxDbQ9SFU3.
PRIDEQ9SFU3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT3G07130.1; AT3G07130.1; AT3G07130.
GeneID819899.
KEGGath:AT3G07130.

Organism-specific databases

TAIRAt3g07130.

Phylogenomic databases

eggNOGCOG1409.
HOGENOMHOG000238330.
InParanoidQ9SFU3.
OMAHPLPGYW.
PhylomeDBQ9SFU3.
ProtClustDBCLSN2683408.

Gene expression databases

GenevestigatorQ9SFU3.

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 namePPA15_ARATH
AccessionPrimary (citable) accession number: Q9SFU3
Entry history
Integrated into UniProtKB/Swiss-Prot: May 5, 2009
Last sequence update: May 1, 2000
Last modified: May 1, 2013
This is version 75 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