PPA11_ARATH
ID PPA11_ARATH Reviewed; 441 AA.
AC Q9SI18; Q7XY10;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Purple acid phosphatase 11;
DE EC=3.1.3.2;
DE Flags: Precursor;
GN Name=PAP11; Synonyms=AT8; OrderedLocusNames=At2g18130; ORFNames=F8D23.9;
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], INDUCTION, 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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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].
RC STRAIN=cv. Columbia;
RA Kim C.J., Chen H., Quinitio C., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 241-400.
RC TISSUE=Seedling;
RA Lohrasebi T., Malboobi M.A.;
RT "Identification of differentially displayed Arabidopsis thaliana acid
RT phosphatase-encoding genes.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
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 -!- TISSUE SPECIFICITY: Specifically expressed in flowers.
CC {ECO:0000269|PubMed:16244908}.
CC -!- INDUCTION: By phosphate deprivation. {ECO:0000269|PubMed:12021284}.
CC -!- SIMILARITY: Belongs to the metallophosphoesterase superfamily. Purple
CC acid phosphatase family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF492663; AAM15912.1; -; mRNA.
DR EMBL; AC007212; AAD31353.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC06729.1; -; Genomic_DNA.
DR EMBL; BT026132; ABG48488.1; -; mRNA.
DR EMBL; AY297745; AAP81218.1; -; mRNA.
DR PIR; F84560; F84560.
DR RefSeq; NP_179405.1; NM_127370.1.
DR AlphaFoldDB; Q9SI18; -.
DR SMR; Q9SI18; -.
DR STRING; 3702.AT2G18130.1; -.
DR iPTMnet; Q9SI18; -.
DR PaxDb; Q9SI18; -.
DR PRIDE; Q9SI18; -.
DR EnsemblPlants; AT2G18130.1; AT2G18130.1; AT2G18130.
DR GeneID; 816326; -.
DR Gramene; AT2G18130.1; AT2G18130.1; AT2G18130.
DR KEGG; ath:AT2G18130; -.
DR Araport; AT2G18130; -.
DR TAIR; locus:2053149; AT2G18130.
DR eggNOG; KOG1378; Eukaryota.
DR HOGENOM; CLU_013387_0_1_1; -.
DR InParanoid; Q9SI18; -.
DR OMA; DSLWIYN; -.
DR OrthoDB; 426430at2759; -.
DR PhylomeDB; Q9SI18; -.
DR BioCyc; ARA:AT2G18130-MON; -.
DR PRO; PR:Q9SI18; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9SI18; baseline and differential.
DR Genevisible; Q9SI18; 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; 2.
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 Glycoprotein; Hydrolase; Iron; Metal-binding; Reference proteome; Secreted;
KW Signal; Zinc.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..441
FT /note="Purple acid phosphatase 11"
FT /id="PRO_0000372816"
FT ACT_SITE 305
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 145
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 173
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 173
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 176
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 210
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 210
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 295
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 332..334
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 332
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 334
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT CARBOHYD 111
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 153
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 283
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 348
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 405
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 319
FT /note="W -> M (in Ref. 5; AAP81218)"
FT /evidence="ECO:0000305"
FT CONFLICT 324
FT /note="K -> I (in Ref. 5; AAP81218)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 441 AA; 50362 MW; 861E402A9A936424 CRC64;
MELSHLALVC AAIAFSSIFV VSQAGITSTH ARVSEPSEEM SLETFPPPAG YNAPEQVHIT
QGDNAGRAMI ISWVMPLNED GSNVVTYWIA SSDGSDNKNA IATTSSYRYF NYTSGYLHHA
TIKKLEYDPS KSRSRCSLHI RYYSDLGQTY ASNQTLYNYM SNPKGQAVLF VGDLSYADDH
PNHDQRKWDS YGRFVEPSAA YQPWSWAAGN YEIDYAQSIS ETQPFKPYKN RYHVPYKASQ
STSPLWYSIK RASTYIIVLS SYSAYDKYTP QNSWLQDELK KVNRSETSWL IVLVHAPWYN
SNNYHYMEGE SMRVTFEPWF VENKVDIVFA GHVHAYERSK RISNIHYNIT DGMSTPVKDQ
NAPIYITIGD GGNIEGIANS FTDPQPSYSA FREASFGHAL LEIKNRTHAH YTWHRNKEDE
AVIADSIWLK KRYYLPEEET A
