PPA20_ARATH
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 03-AUG-2022, entry version 135.
DE RecName: Full=Probable purple acid phosphatase 20;
DE EC=3.1.3.2;
DE Flags: Precursor;
GN Name=PAP20; Synonyms=AT4; OrderedLocusNames=At3g52780; 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.AT3G52780.1; -.
DR PaxDb; Q9LXI7; -.
DR PRIDE; Q9LXI7; -.
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; locus:2083288; AT3G52780.
DR eggNOG; KOG1378; Eukaryota.
DR HOGENOM; CLU_013387_0_0_1; -.
DR InParanoid; Q9LXI7; -.
DR OMA; YDMFMLP; -.
DR OrthoDB; 426430at2759; -.
DR PhylomeDB; Q9LXI7; -.
DR BioCyc; ARA:AT3G52780-MON; -.
DR PRO; PR:Q9LXI7; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LXI7; baseline and differential.
DR Genevisible; Q9LXI7; AT.
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 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; PTHR22953; 1.
DR Pfam; PF00149; Metallophos; 1.
DR Pfam; PF14008; Metallophos_C; 1.
DR Pfam; PF16656; Pur_ac_phosph_N; 1.
DR SUPFAM; SSF49363; SSF49363; 1.
DR SUPFAM; SSF56300; SSF56300; 1.
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
