Purple acid phosphatase 17 precursor - Arabidopsis thaliana (Mouse-ear cress)

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Q9SCX8 (PPA17_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 89. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Purple acid phosphatase 17
EC=3.1.3.2

Alternative name(s):
Acid phosphatase type 5
Peroxidase
EC=1.11.1.7

Gene names

Name:	PAP17
Synonyms:	ACP5
Ordered Locus Names:	At3g17790
ORF Names:	MEB5.10

Organism

Arabidopsis thaliana (Mouse-ear cress) [Reference proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	338 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Metallo-phosphoesterase involved in phosphate metabolism. Has a peroxidase activity. Ref.1
Catalytic activity	A phosphate monoester + H₂O = an alcohol + phosphate. 2 phenolic donor + H₂O₂ = 2 phenoxyl radical of the donor + 2 H₂O.
Cofactor	Binds 1 iron ion per subunit By similarity. Binds 1 zinc ion per subunit By similarity.
Enzyme regulation	Inhibited by phosphate and molybdate. Ref.1
Subunit structure	Homodimer By similarity.
Subcellular location	Secreted By similarity.
Tissue specificity	Expressed in roots, stems, leaves, flowers and siliques. Ref.2
Induction	By phosphate starvation, during senescence, by ABA, by H₂O₂, and by salt stress. Ref.1
Sequence similarities	Belongs to the metallophosphoesterase superfamily. Purple acid phosphatase family.

Ontologies

Keywords
Cellular component	Secreted
Domain	Signal
Ligand	Iron Metal-binding Zinc
Molecular function	Hydrolase Oxidoreductase
PTM	Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cellular phosphate ion homeostasis Inferred from expression pattern Ref.1. Source: TAIR response to hydrogen peroxide Inferred from expression pattern Ref.1. Source: TAIR
Cellular_component	cell surface Inferred from sequence or structural similarity Ref.1. Source: TAIR extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	acid phosphatase activity Inferred from sequence or structural similarity Ref.2. Source: TAIR metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW peroxidase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 31

Potential

Chain

32 – 338

307

Purple acid phosphatase 17

PRO_5000065319

Regions

Region

253 – 255

Substrate binding By similarity

Sites

Active site

227

Proton donor By similarity

Metal binding

Iron By similarity

Metal binding

Iron By similarity

Metal binding

Zinc By similarity

Metal binding

Iron By similarity

Metal binding

124

Zinc By similarity

Metal binding

218

Zinc By similarity

Metal binding

253

Zinc By similarity

Metal binding

255

Iron By similarity

Amino acid modifications

Glycosylation

N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict

M → I in AAM61192. Ref.7

Sequence conflict

115

Q → R in AAM61192. Ref.7

Sequence conflict

245

G → S in AAM61192. Ref.7

Sequences

Sequence

Length

Mass (Da)

Tools

Q9SCX8 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 5183AE005E859740
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FASTA

338

38,297

        10         20         30         40         50         60 
MNSGRRSLMS ATASLSLLLC IFTTFVVVSN GELQRFIEPA KSDGSVSFIV IGDWGRRGSF 

        70         80         90        100        110        120 
NQSLVAYQMG KIGEKIDLDF VVSTGDNFYD NGLFSEHDPN FEQSFSNIYT APSLQKQWYS 

       130        140        150        160        170        180 
VLGNHDYRGD AEAQLSSVLR EIDSRWICLR SFVVDAELVE MFFVDTTPFV KEYYTEADGH 

       190        200        210        220        230        240 
SYDWRAVPSR NSYVKALLRD LEVSLKSSKA RWKIVVGHHA MRSIGHHGDT KELNEELLPI 

       250        260        270        280        290        300 
LKENGVDLYM NGHDHCLQHM SDEDSPIQFL TSGAGSKAWR GDINPVTINP KLLKFYYDGQ 

       310        320        330 
GFMSARFTHS DAEIVFYDVF GEILHKWVTS KQLLHSSV

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A type 5 acid phosphatase gene from Arabidopsis thaliana is induced by phosphate starvation and by some other types of phosphate mobilising/oxidative stress conditions." del Pozo J.C., Allona I., Rubio V., Leyva A., de la Pena A., Aragoncillo C., Paz-Ares J. Plant J. 19:579-589(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, ENZYME REGULATION, INDUCTION. Strain: cv. Landsberg erecta.
[2]	"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.
[3]	"Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence features of the regions of 4,504,864 bp covered by sixty P1 and TAC clones." Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S. DNA Res. 7:131-135(2000) [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]	"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. Ecker J.R. Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[6]	"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs." Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K. Shinozaki K. Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[7]	"Full-length cDNA from Arabidopsis thaliana." Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A. Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[8]	"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	AJ133747 mRNA. Translation: CAC09923.1. AJ243527 Genomic DNA. Translation: CAB63938.1. AY818189 mRNA. Translation: AAV69751.1. AB019230 Genomic DNA. Translation: BAB02702.1. CP002686 Genomic DNA. Translation: AEE76007.1. BT003135 mRNA. Translation: AAO24567.1. AK228106 mRNA. Translation: BAF00065.1. AY084629 mRNA. Translation: AAM61192.1.
IPI	IPI00546945.
RefSeq	NP_566587.1. NM_112660.5.
UniGene	At.22111. At.71032. At.74878. At.74926.
3D structure databases
ProteinModelPortal	Q9SCX8.
SMR	Q9SCX8. Positions 46-326.
ModBase	Search...
Proteomic databases
PaxDb	Q9SCX8.
PRIDE	Q9SCX8.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT3G17790.1; AT3G17790.1; AT3G17790.
GeneID	821047.
KEGG	ath:AT3G17790.
Organism-specific databases
TAIR	At3g17790.
Phylogenomic databases
eggNOG	COG1409.
HOGENOM	HOG000239892.
InParanoid	Q9SCX8.
OMA	SARFTHS.
PhylomeDB	Q9SCX8.
ProtClustDB	CLSN2688499.
Gene expression databases
Genevestigator	Q9SCX8.
Family and domain databases
InterPro	IPR024927. Acid_Pase_5. IPR004843. Metallo_PEstase_dom. [Graphical view]
Pfam	PF00149. Metallophos. 1 hit. [Graphical view]
PIRSF	PIRSF000898. Acid_Ptase_5. 1 hit.
ProtoNet	Search...

Entry information

Entry name

PPA17_ARATH

Accession

Primary (citable) accession number: Q9SCX8
Secondary accession number(s): Q8LFV2

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 5, 2009
Last sequence update:	May 1, 2000
Last modified:	May 1, 2013
This is version 89 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program

Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents