PPA12_ARATH
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 03-AUG-2022, entry version 166.
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}.
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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.AT2G27190.1; -.
DR PaxDb; Q38924; -.
DR PRIDE; Q38924; -.
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; locus:2005533; AT2G27190.
DR eggNOG; KOG1378; Eukaryota.
DR HOGENOM; CLU_013387_0_1_1; -.
DR InParanoid; Q38924; -.
DR OMA; LHNRYWK; -.
DR OrthoDB; 426430at2759; -.
DR PRO; PR:Q38924; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q38924; baseline and differential.
DR Genevisible; Q38924; AT.
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 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; 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 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
