ID   PPA27_ARATH             Reviewed;         611 AA.
AC   Q5MAU8; Q9FK32;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Probable inactive purple acid phosphatase 27;
DE   Flags: Precursor;
GN   Name=PAP27; OrderedLocusNames=At5g50400; ORFNames=MXI22.12;
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], AND TISSUE SPECIFICITY.
RC   STRAIN=cv. Columbia;
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).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=9734815; DOI=10.1093/dnares/5.3.203;
RA   Kotani H., Nakamura Y., Sato S., Asamizu E., Kaneko T., Miyajima N.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. VI. Sequence
RT   features of the regions of 1,367,185 bp covered by 19 physically assigned
RT   P1 and TAC clones.";
RL   DNA Res. 5:203-216(1998).
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   GENE FAMILY, AND NOMENCLATURE.
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).
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: Expressed in roots, stems, leaves, flowers and
CC       siliques. {ECO:0000269|PubMed:16244908}.
CC   -!- SIMILARITY: Belongs to the metallophosphoesterase superfamily. Purple
CC       acid phosphatase family. {ECO:0000305}.
CC   -!- CAUTION: Lacks the conserved His residue essential for phosphatase
CC       activity. Its enzyme activity is therefore unsure. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB09459.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AY842027; AAW29951.1; -; mRNA.
DR   EMBL; AB012248; BAB09459.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002688; AED95939.1; -; Genomic_DNA.
DR   RefSeq; NP_199851.2; NM_124422.4.
DR   AlphaFoldDB; Q5MAU8; -.
DR   SMR; Q5MAU8; -.
DR   STRING; 3702.AT5G50400.1; -.
DR   PaxDb; Q5MAU8; -.
DR   PRIDE; Q5MAU8; -.
DR   ProteomicsDB; 249028; -.
DR   EnsemblPlants; AT5G50400.1; AT5G50400.1; AT5G50400.
DR   GeneID; 835108; -.
DR   Gramene; AT5G50400.1; AT5G50400.1; AT5G50400.
DR   KEGG; ath:AT5G50400; -.
DR   Araport; AT5G50400; -.
DR   TAIR; locus:2177547; AT5G50400.
DR   eggNOG; KOG1378; Eukaryota.
DR   HOGENOM; CLU_013387_4_1_1; -.
DR   InParanoid; Q5MAU8; -.
DR   OrthoDB; 426430at2759; -.
DR   PhylomeDB; Q5MAU8; -.
DR   PRO; PR:Q5MAU8; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q5MAU8; baseline and differential.
DR   Genevisible; Q5MAU8; 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; IPR040974; Fn3_PAP.
DR   InterPro; IPR029052; Metallo-depent_PP-like.
DR   InterPro; IPR041792; MPP_PAP.
DR   InterPro; IPR008963; Purple_acid_Pase-like_N.
DR   InterPro; IPR015914; Purple_acid_Pase_N.
DR   InterPro; IPR025733; Purple_acid_PPase_C_dom.
DR   Pfam; PF17808; fn3_PAP; 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   Glycoprotein; Iron; Metal-binding; Reference proteome; Secreted; Signal;
KW   Zinc.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..611
FT                   /note="Probable inactive purple acid phosphatase 27"
FT                   /id="PRO_0000372829"
FT   BINDING         293
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   BINDING         334
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   BINDING         334
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         337
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   BINDING         367
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         367
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         456
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         498..500
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         498
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         500
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        263
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        271
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        314
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   611 AA;  68897 MW;  C433FE6A790FF0F2 CRC64;
     MARNFLLVLL WFIVQVSSSH ENGRGDQALS QIDIYAINLA QHHSAFIHVS PLVLGSQGQD
     TEWVNVVISN PEPSSDDWVG VFSPAKFDSS SCAPTDDKEI APFICSAPVK YMYAKSSPDY
     MKTGNAVLKF MLINQRADFS FALFTGGLSN PTLVSVSNHV SFINPKAPVY PRLALGKKWD
     EMTVTWTSGY NIGEAVPFVE WSRKGTRSRR SPAGTLTFTR NSMCGAPART VGWRDPGFIH
     TASLKDLWPN LKYTYRMGHE LMNGSIVWSK NFTFKSSPYP GQDSLQRVII FGDMGKGERD
     GSNEYNDYQP GSLNTTDQLI KDLKNIDIVF HIGDITYANG YISQWDQFTA QVEPIASTVP
     YMVASGNHER DWPDSGSFYG GKDSGGECGV PAETMFDFPA ENKAKFWYSA DYGMFRFCVA
     DTEHDWREGS EQYQFIERCL ASVDRRAQPW LIFIAHRVLG YSTNDWYGQE GSFEEPMGRE
     SLQKLWQKYK VDIAFYGHVH NYERTCPIYQ NQCMDNEKSH YSGAFKGTIH VVVGGAGSHL
     SSFSSLKPKW SIFRDYDYGF VKLTAFDHSS LLFEYKKSSN GAVHDSFTIF REYRDVLACV
     RDSCEPTTLA S