ID   PPA17_ARATH             Reviewed;         338 AA.
AC   Q9SCX8; Q8LFV2;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   04-NOV-2026, entry version 161.
DE   RecName: Full=Purple acid phosphatase 17;
DE            EC=3.1.3.2;
DE   AltName: Full=Acid phosphatase type 5;
DE   AltName: Full=Peroxidase;
DE            EC=1.11.1.7;
DE   Flags: Precursor;
GN   Name=PAP17; Synonyms=ACP5; OrderedLocusNames=At3g17790;
GN   ORFNames=MEB5.10;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, ACTIVITY REGULATION,
RP   AND INDUCTION.
RC   STRAIN=cv. Landsberg erecta;
RX   PubMed=10504579; DOI=10.1046/j.1365-313x.1999.00562.x;
RA   del Pozo J.C., Allona I., Rubio V., Leyva A., de la Pena A.,
RA   Aragoncillo C., Paz-Ares J.;
RT   "A type 5 acid phosphatase gene from Arabidopsis thaliana is induced by
RT   phosphate starvation and by some other types of phosphate
RT   mobilising/oxidative stress conditions.";
RL   Plant J. 19:579-589(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   STRAIN=cv. Columbia;
RX   PubMed=16244908; DOI=10.1007/s11103-005-0183-0;
RA   Zhu H., Qian W., Lu X., Li D., Liu X., Liu K., Wang D.;
RT   "Expression patterns of purple acid phosphatase genes in Arabidopsis organs
RT   and functional analysis of AtPAP23 predominantly transcribed in flower.";
RL   Plant Mol. Biol. 59:581-594(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10819329; DOI=10.1093/dnares/7.2.131;
RA   Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT   features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT   clones.";
RL   DNA Res. 7:131-135(2000).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [5]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RG   The Arabidopsis Information Resource (TAIR);
RT   "Community-consensus reference genome of Arabidopsis thaliana Col-0.";
RL   Submitted (FEB-2026) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RA   Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA   Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA   Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA   Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA   Shinozaki K.;
RT   "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL   Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA   Feldmann K.A.;
RT   "Full-length cDNA from Arabidopsis thaliana.";
RL   Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [9]
RP   GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=12021284; DOI=10.1074/jbc.m204183200;
RA   Li D., Zhu H., Liu K., Liu X., Leggewie G., Udvardi M., Wang D.;
RT   "Purple acid phosphatases of Arabidopsis thaliana. Comparative analysis and
RT   differential regulation by phosphate deprivation.";
RL   J. Biol. Chem. 277:27772-27781(2002).
CC   -!- FUNCTION: Metallo-phosphoesterase involved in phosphate metabolism. Has
CC       a peroxidase activity. {ECO:0000269|PubMed:10504579}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a phosphate monoester + H2O = an alcohol + phosphate;
CC         Xref=Rhea:RHEA:15017, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:67140; EC=3.1.3.2;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 a phenolic donor + H2O2 = 2 a phenolic radical donor + 2
CC         H2O; Xref=Rhea:RHEA:56136, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240,
CC         ChEBI:CHEBI:139520, ChEBI:CHEBI:139521; EC=1.11.1.7;
CC   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250};
CC       Note=Binds 1 Fe cation per subunit. {ECO:0000250};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC   -!- ACTIVITY REGULATION: Inhibited by phosphate and molybdate.
CC       {ECO:0000269|PubMed:10504579}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed in roots, stems, leaves, flowers and
CC       siliques. {ECO:0000269|PubMed:16244908}.
CC   -!- INDUCTION: By phosphate starvation, during senescence, by ABA, by
CC       H(2)O(2), and by salt stress. {ECO:0000269|PubMed:10504579}.
CC   -!- SIMILARITY: Belongs to the metallophosphoesterase superfamily. Purple
CC       acid phosphatase family. {ECO:0000305}.
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DR   EMBL; AJ133747; CAC09923.1; -; mRNA.
DR   EMBL; AJ243527; CAB63938.1; -; Genomic_DNA.
DR   EMBL; AY818189; AAV69751.1; -; mRNA.
DR   EMBL; AB019230; BAB02702.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE76007.1; -; Genomic_DNA.
DR   EMBL; OZ408685; CAO7041326.1; -; Genomic_DNA.
DR   EMBL; BT003135; AAO24567.1; -; mRNA.
DR   EMBL; AK228106; BAF00065.1; -; mRNA.
DR   EMBL; AY084629; AAM61192.1; -; mRNA.
DR   RefSeq; NP_566587.1; NM_112660.6.
DR   AlphaFoldDB; Q9SCX8; -.
DR   SMR; Q9SCX8; -.
DR   FunCoup; Q9SCX8; 362.
DR   STRING; 3702.Q9SCX8; -.
DR   GlyCosmos; Q9SCX8; 1 site, No reported glycans.
DR   GlyGen; Q9SCX8; 1 site.
DR   PaxDb; 3702-Q9SCX8; -.
DR   ProteomicsDB; 249017; -.
DR   GeneID; 821047; -.
DR   KEGG; ath:AT3G17790; -.
DR   Araport; AT3G17790; -.
DR   TAIR; AT3G17790; PAP17.
DR   eggNOG; KOG2679; Eukaryota.
DR   HOGENOM; CLU_043332_3_0_1; -.
DR   InParanoid; Q9SCX8; -.
DR   OMA; AADQWAW; -.
DR   PhylomeDB; Q9SCX8; -.
DR   BioCyc; ARA:AT3G17790-MONOMER; -.
DR   PRO; PR:Q9SCX8; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   Proteomes; UP001984100; Chromosome 3.
DR   ExpressionAtlas; Q9SCX8; baseline and differential.
DR   GO; GO:0009986; C:cell surface; ISS:TAIR.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0003993; F:acid phosphatase activity; ISS:TAIR.
DR   GO; GO:0008199; F:ferric iron binding; IBA:GO_Central.
DR   GO; GO:0008198; F:ferrous iron binding; IBA:GO_Central.
DR   GO; GO:0140825; F:lactoperoxidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016791; F:phosphatase activity; IDA:TAIR.
DR   GO; GO:0030643; P:intracellular phosphate ion homeostasis; IEP:TAIR.
DR   GO; GO:0042542; P:response to hydrogen peroxide; IEP:TAIR.
DR   CDD; cd07378; MPP_ACP5; 1.
DR   FunFam; 3.60.21.10:FF:000027; Purple acid phosphatase; 1.
DR   Gene3D; 3.60.21.10; -; 1.
DR   InterPro; IPR024927; Acid_PPase.
DR   InterPro; IPR004843; Calcineurin-like_PHP.
DR   InterPro; IPR029052; Metallo-depent_PP-like.
DR   InterPro; IPR051558; Metallophosphoesterase_PAP.
DR   PANTHER; PTHR10161; TARTRATE-RESISTANT ACID PHOSPHATASE TYPE 5; 1.
DR   PANTHER; PTHR10161:SF14; TARTRATE-RESISTANT ACID PHOSPHATASE TYPE 5; 1.
DR   Pfam; PF00149; Metallophos; 1.
DR   PIRSF; PIRSF000898; Acid_Ptase_5; 1.
DR   SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
PE   2: Evidence at transcript level;
KW   Glycoprotein; Hydrolase; Iron; Metal-binding; Oxidoreductase;
KW   Reference proteome; Secreted; Signal; Zinc.
FT   SIGNAL          1..31
FT                   /evidence="ECO:0000255"
FT   CHAIN           32..338
FT                   /note="Purple acid phosphatase 17"
FT                   /id="PRO_5000065319"
FT   ACT_SITE        227
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         53
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   BINDING         86
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   BINDING         86
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         89
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   BINDING         124
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         218
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         253..255
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         253
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         255
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        61
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        9
FT                   /note="M -> I (in Ref. 8; AAM61192)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        115
FT                   /note="Q -> R (in Ref. 8; AAM61192)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        245
FT                   /note="G -> S (in Ref. 8; AAM61192)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   338 AA;  38297 MW;  5183AE005E859740 CRC64;
     MNSGRRSLMS ATASLSLLLC IFTTFVVVSN GELQRFIEPA KSDGSVSFIV IGDWGRRGSF
     NQSLVAYQMG KIGEKIDLDF VVSTGDNFYD NGLFSEHDPN FEQSFSNIYT APSLQKQWYS
     VLGNHDYRGD AEAQLSSVLR EIDSRWICLR SFVVDAELVE MFFVDTTPFV KEYYTEADGH
     SYDWRAVPSR NSYVKALLRD LEVSLKSSKA RWKIVVGHHA MRSIGHHGDT KELNEELLPI
     LKENGVDLYM NGHDHCLQHM SDEDSPIQFL TSGAGSKAWR GDINPVTINP KLLKFYYDGQ
     GFMSARFTHS DAEIVFYDVF GEILHKWVTS KQLLHSSV
//