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   27-MAR-2024, entry version 139.
DE   RecName: Full=Purple acid phosphatase 11;
DE            EC=3.1.3.2;
DE   Flags: Precursor;
GN   Name=PAP11; Synonyms=AT8; OrderedLocusNames=At2g18130;
GN   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}.
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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.Q9SI18; -.
DR   GlyCosmos; Q9SI18; 5 sites, No reported glycans.
DR   iPTMnet; Q9SI18; -.
DR   PaxDb; 3702-AT2G18130-1; -.
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; AT2G18130; PAP11.
DR   eggNOG; KOG1378; Eukaryota.
DR   HOGENOM; CLU_013387_0_1_1; -.
DR   InParanoid; Q9SI18; -.
DR   OMA; YGNHDME; -.
DR   OrthoDB; 203742at2759; -.
DR   PhylomeDB; Q9SI18; -.
DR   BioCyc; ARA:AT2G18130-MONOMER; -.
DR   PRO; PR:Q9SI18; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; Q9SI18; 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   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:SF120; PURPLE ACID PHOSPHATASE 11-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; Q9SI18; AT.
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
//