PPA17_ARATH
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 03-AUG-2022, entry version 143.
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; 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 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 [6]
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 [7]
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 [8]
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; 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 STRING; 3702.AT3G17790.1; -.
DR PaxDb; Q9SCX8; -.
DR PRIDE; Q9SCX8; -.
DR ProteomicsDB; 249017; -.
DR EnsemblPlants; AT3G17790.1; AT3G17790.1; AT3G17790.
DR GeneID; 821047; -.
DR Gramene; AT3G17790.1; AT3G17790.1; AT3G17790.
DR KEGG; ath:AT3G17790; -.
DR Araport; AT3G17790; -.
DR TAIR; locus:2088590; AT3G17790.
DR eggNOG; KOG2679; Eukaryota.
DR HOGENOM; CLU_043332_3_0_1; -.
DR InParanoid; Q9SCX8; -.
DR OMA; VTVAIFM; -.
DR OrthoDB; 711825at2759; -.
DR PhylomeDB; Q9SCX8; -.
DR BioCyc; ARA:AT3G17790-MON; -.
DR PRO; PR:Q9SCX8; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9SCX8; baseline and differential.
DR Genevisible; Q9SCX8; AT.
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:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0016791; F:phosphatase activity; IDA:TAIR.
DR GO; GO:0030643; P:cellular phosphate ion homeostasis; IEP:TAIR.
DR GO; GO:0042542; P:response to hydrogen peroxide; IEP:TAIR.
DR CDD; cd07378; MPP_ACP5; 1.
DR Gene3D; 3.60.21.10; -; 1.
DR InterPro; IPR024927; Acid_PPase.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR Pfam; PF00149; Metallophos; 1.
DR PIRSF; PIRSF000898; Acid_Ptase_5; 1.
DR SUPFAM; SSF56300; SSF56300; 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. 7; AAM61192)"
FT /evidence="ECO:0000305"
FT CONFLICT 115
FT /note="Q -> R (in Ref. 7; AAM61192)"
FT /evidence="ECO:0000305"
FT CONFLICT 245
FT /note="G -> S (in Ref. 7; 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
