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Q6TPH1 (PPA23_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 63. 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

Names and origin

Protein namesRecommended name:
Purple acid phosphatase 23

EC=3.1.3.2
Gene names
Name:PAP23
Synonyms:AT3
Ordered Locus Names:At4g13700
ORF Names:F18A5.90
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length458 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 ATP, ADP, dATP, pyrophosphate, polyphosphate, phosphoserine and phosphothreonine. Low or no activity with phosphotyrosine, AMP and phytate. Ref.1

Catalytic activity

A phosphate monoester + H2O = an alcohol + phosphate.

Cofactor

Binds 1 iron ion per subunit. Ref.1

Binds 1 manganese ion per subunit. Ref.1

Subunit structure

Homodimer By similarity.

Subcellular location

Secreted By similarity.

Tissue specificity

Specifically expressed in flowers. Ref.1

Developmental stage

First observed in the floral apical meristem (FAP). In flowers, observed in petals and anthers, particularly in anther filaments. Ref.1

Sequence similarities

Belongs to the metallophosphoesterase superfamily. Purple acid phosphatase family.

Biophysicochemical properties

pH dependence:

Optimum pH is 5-6. Ref.1

Sequence caution

The sequence CAB36834.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence CAB78412.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

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

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionacid phosphatase activity

Inferred from electronic annotation. Source: UniProtKB-EC

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 – 458439Purple acid phosphatase 23
PRO_0000372826

Regions

Region397 – 3993Substrate binding By similarity

Sites

Active site3701Proton donor By similarity
Metal binding1941Iron Probable
Metal binding2211Iron Probable
Metal binding2211Manganese Probable
Metal binding2241Iron Probable
Metal binding2781Manganese Probable
Metal binding3601Manganese Probable
Metal binding3971Manganese Probable
Metal binding3991Iron Probable
Binding site2781Substrate By similarity

Amino acid modifications

Glycosylation591N-linked (GlcNAc...) Potential
Glycosylation1211N-linked (GlcNAc...) Potential
Glycosylation1361N-linked (GlcNAc...) Potential
Glycosylation2001N-linked (GlcNAc...) Potential
Glycosylation3311N-linked (GlcNAc...) Potential
Glycosylation4091N-linked (GlcNAc...) Potential
Glycosylation4551N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict3101L → F in AAQ93685. Ref.1
Sequence conflict3101L → F in AEE83314. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q6TPH1 [UniParc].

Last modified May 5, 2009. Version 2.
Checksum: 3FE6A789CBDF7A72

FASTA45851,551
        10         20         30         40         50         60 
MTLLIMITLT SISLLLAAAE TIPTTLDGPF KPLTRRFEPS LRRGSDDLPM DHPRLRKRNV 

        70         80         90        100        110        120 
SSDFPEQIAL ALSTPTSMWV SWVTGDAIVG KDVKPLDPSS IASEVWYGKE KGNYMLKKKG 

       130        140        150        160        170        180 
NATVYSQLYP SDGLLNYTSG IIHHVLIDGL EPETRYYYRC GDSSVPAMSE EISFETLPLP 

       190        200        210        220        230        240 
SKDAYPHRIA FVGDLGLTSN TTTTIDHLME NDPSLVIIVG DLTYANQYRT IGGKGVPCFS 

       250        260        270        280        290        300 
CSFPDAPIRE TYQPRWDAWG RFMEPLTSKV PTMVIEGNHE IEPQASGITF KSYSERFAVP 

       310        320        330        340        350        360 
ASESGSNSNL YYSFDAGGVH FVMLGAYVDY NNTGLQYAWL KEDLSKVDRA VTPWLVATMH 

       370        380        390        400        410        420 
PPWYNSYSSH YQEFECMRQE MEELLYQYRV DIVFAGHVHA YERMNRIYNY TLDPCGPVYI 

       430        440        450 
TIGDGGNIEK VDVDFADDPG KCHSSYDLFF FNSLNLSN 

« 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], FUNCTION, DEVELOPMENTAL STAGE, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, TISSUE SPECIFICITY.
Strain: cv. Columbia.
[2]"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.
[3]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION, SEQUENCE REVISION.
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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY390530 mRNA. Translation: AAQ93685.1.
AL035528 Genomic DNA. Translation: CAB36834.1. Sequence problems.
AL161537 Genomic DNA. Translation: CAB78412.1. Sequence problems.
CP002687 Genomic DNA. Translation: AEE83314.1.
PIRT05239.
RefSeqNP_193106.3. NM_117444.3.
UniGeneAt.33346.

3D structure databases

ProteinModelPortalQ6TPH1.
SMRQ6TPH1. Positions 47-432.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING3702.AT4G13700.1-P.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID827004.
KEGGath:AT4G13700.

Organism-specific databases

TAIRAT4G13700.

Phylogenomic databases

eggNOGCOG1409.
HOGENOMHOG000238330.
InParanoidQ6TPH1.
PhylomeDBQ6TPH1.
ProtClustDBCLSN2925562.

Enzyme and pathway databases

BioCycARA:AT4G13700-MONOMER.

Gene expression databases

GenevestigatorQ6TPH1.

Family and domain databases

Gene3D2.60.40.380. 1 hit.
InterProIPR004843. Calcineurin-like_PHP_apaH.
IPR008963. Purple_acid_Pase-like_N.
IPR015914. Purple_acid_Pase_N.
[Graphical view]
PfamPF00149. Metallophos. 1 hit.
[Graphical view]
SUPFAMSSF49363. SSF49363. 1 hit.
ProtoNetSearch...

Other

PROQ6TPH1.

Entry information

Entry namePPA23_ARATH
AccessionPrimary (citable) accession number: Q6TPH1
Secondary accession number(s): Q9SVP2
Entry history
Integrated into UniProtKB/Swiss-Prot: May 5, 2009
Last sequence update: May 5, 2009
Last modified: April 16, 2014
This is version 63 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names