ID   PPA20_ARATH             Reviewed;         427 AA.
AC   Q9LXI7; Q3EAK8;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   27-MAR-2024, entry version 143.
DE   RecName: Full=Probable purple acid phosphatase 20;
DE            EC=3.1.3.2;
DE   Flags: Precursor;
GN   Name=PAP20; Synonyms=AT4; OrderedLocusNames=At3g52780;
GN   ORFNames=F3C22.180;
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 [MRNA] (ISOFORM 1), GENE FAMILY, AND NOMENCLATURE.
RC   STRAIN=cv. Col-1;
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).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130713; DOI=10.1038/35048706;
RA   Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA   Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA   Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA   Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA   Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA   Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA   Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA   Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA   Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA   Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA   Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA   de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA   Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA   Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA   Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA   Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA   Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA   Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA   Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA   Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA   Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA   Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA   Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL   Nature 408:820-822(2000).
RN   [3]
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=cv. Columbia;
RA   Bautista V.R., Kim C.J., Chen H., Wu S.Y., De Los Reyes C., Ecker J.R.;
RT   "Arabidopsis ORF clones.";
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   TISSUE SPECIFICITY.
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).
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   -!- 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   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9LXI7-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9LXI7-2; Sequence=VSP_037200, VSP_038048;
CC   -!- TISSUE SPECIFICITY: Expressed flowers and siliques.
CC       {ECO:0000269|PubMed:16244908}.
CC   -!- MISCELLANEOUS: [Isoform 2]: May be due to a competing donor splice
CC       site. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the metallophosphoesterase superfamily. Purple
CC       acid phosphatase family. {ECO:0000305}.
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DR   EMBL; AF492666; AAM15915.1; -; mRNA.
DR   EMBL; AL353912; CAB89239.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE78992.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE78993.1; -; Genomic_DNA.
DR   EMBL; BT029748; ABM06018.1; -; mRNA.
DR   PIR; T49031; T49031.
DR   RefSeq; NP_190846.1; NM_115138.3. [Q9LXI7-1]
DR   RefSeq; NP_850686.1; NM_180355.1. [Q9LXI7-2]
DR   AlphaFoldDB; Q9LXI7; -.
DR   SMR; Q9LXI7; -.
DR   STRING; 3702.Q9LXI7; -.
DR   GlyCosmos; Q9LXI7; 2 sites, No reported glycans.
DR   PaxDb; 3702-AT3G52780-1; -.
DR   ProteomicsDB; 249021; -. [Q9LXI7-1]
DR   EnsemblPlants; AT3G52780.1; AT3G52780.1; AT3G52780. [Q9LXI7-1]
DR   EnsemblPlants; AT3G52780.2; AT3G52780.2; AT3G52780. [Q9LXI7-2]
DR   GeneID; 824444; -.
DR   Gramene; AT3G52780.1; AT3G52780.1; AT3G52780. [Q9LXI7-1]
DR   Gramene; AT3G52780.2; AT3G52780.2; AT3G52780. [Q9LXI7-2]
DR   KEGG; ath:AT3G52780; -.
DR   Araport; AT3G52780; -.
DR   TAIR; AT3G52780; PAP20.
DR   eggNOG; KOG1378; Eukaryota.
DR   HOGENOM; CLU_013387_0_0_1; -.
DR   InParanoid; Q9LXI7; -.
DR   OMA; FGVHFIM; -.
DR   OrthoDB; 5485592at2759; -.
DR   PhylomeDB; Q9LXI7; -.
DR   BioCyc; ARA:AT3G52780-MONOMER; -.
DR   PRO; PR:Q9LXI7; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q9LXI7; baseline and differential.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0003993; F:acid phosphatase activity; ISS:TAIR.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd00839; MPP_PAPs; 1.
DR   Gene3D; 3.60.21.10; -; 1.
DR   Gene3D; 2.60.40.380; Purple acid phosphatase-like, N-terminal; 1.
DR   InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR   InterPro; IPR029052; Metallo-depent_PP-like.
DR   InterPro; IPR041792; MPP_PAP.
DR   InterPro; IPR039331; PPA-like.
DR   InterPro; IPR008963; Purple_acid_Pase-like_N.
DR   InterPro; IPR015914; Purple_acid_Pase_N.
DR   InterPro; IPR025733; Purple_acid_PPase_C_dom.
DR   PANTHER; PTHR22953; ACID PHOSPHATASE RELATED; 1.
DR   PANTHER; PTHR22953:SF127; PURPLE ACID PHOSPHATASE 20-RELATED; 1.
DR   Pfam; PF00149; Metallophos; 1.
DR   Pfam; PF14008; Metallophos_C; 1.
DR   Pfam; PF16656; Pur_ac_phosph_N; 1.
DR   SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
DR   SUPFAM; SSF49363; Purple acid phosphatase, N-terminal domain; 1.
DR   Genevisible; Q9LXI7; AT.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Glycoprotein; Hydrolase; Iron; Metal-binding;
KW   Reference proteome; Secreted; Signal; Zinc.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..427
FT                   /note="Probable purple acid phosphatase 20"
FT                   /id="PRO_0000372823"
FT   ACT_SITE        301
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         147
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   BINDING         174
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   BINDING         174
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         177
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   BINDING         207
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         207
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         291
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         330..332
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         330
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         332
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        85
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        392
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         338..385
FT                   /note="SRVYQDKFDKCGPVYINIGDGGNLEGLATKYRDPNPEISLFREASFGH ->
FT                   VIECTKISSTNVVRFILTSEMVGI (in isoform 2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_037200"
FT   VAR_SEQ         386..427
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_038048"
SQ   SEQUENCE   427 AA;  48462 MW;  E9CF7BE0E26BFCCD CRC64;
     MVKVLGLVAI LLIVLAGNVL SYDRQGTRKN LVIHPTNEDD PTFPDQVHIS LVGPDKMRIS
     WITQSSISPS VVYGTVSGKY EGSANGTSSS YHYLLIYRSG QINDVVIGPL KPNTVYYYKC
     GGPSSTQEFS FRTPPSKFPI KFAVSGDLGT SEWSKSTLEH VSKWDYDVFI LPGDLSYANM
     YQPLWDTFGR LVQPLASQRP WMVTHGNHEL EKIPILHSNP FTAYNKRWRM PFEESGSSSN
     LYYSFNVYGV HIIMLGSYTD FEPGSEQYQW LENNLKKIDR KTTPWVVAVV HAPWYNSNEA
     HQGEKESVEM KESMETLLYK ARVDLVFAGH VHAYERFSRV YQDKFDKCGP VYINIGDGGN
     LEGLATKYRD PNPEISLFRE ASFGHGQLVV ENATHARWEW HRNDDDVSVE KDSVWLTSLL
     ADSSCKI
//