ID   PPA12_ARATH             Reviewed;         469 AA.
AC   Q38924; Q42349; Q540Q7; Q8VZC6; Q9SHS9;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   03-MAY-2011, sequence version 3.
DT   24-JAN-2024, entry version 172.
DE   RecName: Full=Fe(3+)-Zn(2+) purple acid phosphatase 12;
DE            Short=PAP;
DE            EC=3.1.3.2;
DE   AltName: Full=Iron(III)-zinc(II) purple acid phosphatase 12;
DE   Flags: Precursor;
GN   Name=PAP12; Synonyms=At10, Ath1, PAP1; OrderedLocusNames=At2g27190;
GN   ORFNames=T22O13.4;
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 [GENOMIC DNA].
RC   STRAIN=cv. Landsberg erecta;
RA   Patel K.S., Lockless S.W., McKnight T.D.;
RL   Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases.
RN   [3]
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   [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] OF 138-268.
RC   STRAIN=cv. Columbia;
RX   PubMed=8580968; DOI=10.1046/j.1365-313x.1996.09010101.x;
RA   Cooke R., Raynal M., Laudie M., Grellet F., Delseny M., Morris P.-C.,
RA   Guerrier D., Giraudat J., Quigley F., Clabault G., Li Y.-F., Mache R.,
RA   Krivitzky M., Gy I.J.-J., Kreis M., Lecharny A., Parmentier Y., Marbach J.,
RA   Fleck J., Clement B., Philipps G., Herve C., Bardet C., Tremousaygue D.,
RA   Lescure B., Lacomme C., Roby D., Jourjon M.-F., Chabrier P.,
RA   Charpenteau J.-L., Desprez T., Amselem J., Chiapello H., Hoefte H.;
RT   "Further progress towards a catalogue of all Arabidopsis genes: analysis of
RT   a set of 5000 non-redundant ESTs.";
RL   Plant J. 9:101-124(1996).
RN   [7]
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; disulfide-linked. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed in roots, stems, leaves, flowers and
CC       siliques. {ECO:0000269|PubMed:16244908}.
CC   -!- INDUCTION: Slightly by phosphate deprivation.
CC       {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; AF492664; AAM15913.1; -; mRNA.
DR   EMBL; U48448; AAA91803.1; -; Genomic_DNA.
DR   EMBL; AC007290; AAD26885.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC07951.1; -; Genomic_DNA.
DR   EMBL; AY065067; AAL57700.1; -; mRNA.
DR   EMBL; AY133599; AAM91429.1; -; mRNA.
DR   EMBL; F20043; CAA23388.1; -; mRNA.
DR   PIR; H84669; H84669.
DR   RefSeq; NP_180287.2; NM_128277.5.
DR   AlphaFoldDB; Q38924; -.
DR   SMR; Q38924; -.
DR   STRING; 3702.Q38924; -.
DR   GlyCosmos; Q38924; 4 sites, No reported glycans.
DR   PaxDb; 3702-AT2G27190-1; -.
DR   ProteomicsDB; 249012; -.
DR   EnsemblPlants; AT2G27190.1; AT2G27190.1; AT2G27190.
DR   GeneID; 817261; -.
DR   Gramene; AT2G27190.1; AT2G27190.1; AT2G27190.
DR   KEGG; ath:AT2G27190; -.
DR   Araport; AT2G27190; -.
DR   TAIR; AT2G27190; PAP12.
DR   eggNOG; KOG1378; Eukaryota.
DR   HOGENOM; CLU_013387_0_1_1; -.
DR   InParanoid; Q38924; -.
DR   OMA; NSSRQFW; -.
DR   OrthoDB; 203742at2759; -.
DR   PRO; PR:Q38924; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; Q38924; baseline and differential.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0003993; F:acid phosphatase activity; IMP:TAIR.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016036; P:cellular response to phosphate starvation; IEP:TAIR.
DR   CDD; cd00063; FN3; 1.
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; IPR003961; FN3_dom.
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:SF35; FE(3+)-ZN(2+) PURPLE ACID PHOSPHATASE 12; 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; Q38924; AT.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Glycoprotein; Hydrolase; Iron; Metal-binding;
KW   Reference proteome; Secreted; Signal; Zinc.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000255"
FT   CHAIN           29..469
FT                   /note="Fe(3+)-Zn(2+) purple acid phosphatase 12"
FT                   /id="PRO_0000023993"
FT   ACT_SITE        329
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         168
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   BINDING         197
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   BINDING         197
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         200
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   BINDING         234
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         234
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         319
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         356..358
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         356
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         358
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        114
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        176
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        307
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        429
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        378
FT                   /note="Interchain"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        57
FT                   /note="P -> H (in Ref. 1; AAM15913 and 3; AAD26885)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        91
FT                   /note="Q -> R (in Ref. 2; AAA91803)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        97
FT                   /note="E -> K (in Ref. 2; AAA91803)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        151
FT                   /note="I -> T (in Ref. 2; AAA91803)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        216
FT                   /note="G -> R (in Ref. 6; CAA23388)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        264
FT                   /note="G -> R (in Ref. 6; CAA23388)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   469 AA;  54123 MW;  7B75A7A097DAEFAF CRC64;
     MSSRSDLKIK RVSLIIFLLS VLVEFCYGGF TSEYVRGSDL PDDMPLDSDV FEVPPGPNSP
     QQVHVTQGNH EGNGVIISWV TPVKPGSKTV QYWCENEKSR KQAEATVNTY RFFNYTSGYI
     HHCLIDDLEF DTKYYYEIGS GKWSRRFWFF IPPKSGPDVP YTFGLIGDLG QTYDSNSTLS
     HYEMNPGKGQ AVLFVGDLSY ADRYPNHDNN RWDTWGRFVE RSVAYQPWIW TAGNHEIDFV
     PDIGEIEPFK PFMNRYHTPH KASGSISPLW YSIKRASAYI IVMSCYSSYG IYTPQYKWLE
     KELQGVNRTE TPWLIVLVHS PFYSSYVHHY MEGETLRVMY EQWFVKYKVD VVFAGHVHAY
     ERSERVSNIA YNIVNGLCEP ISDESAPIYI TIGDGGNSEG LLTDMMQPQP KYSAFREASF
     GHGLLEIKNR THAYFSWNRN QDGNAVAADS VWLLNRFWRA QKKTWLDAF
//