PPA29_ARATH
ID PPA29_ARATH Reviewed; 389 AA.
AC Q9FMK9;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Probable inactive purple acid phosphatase 29;
DE Flags: Precursor;
GN Name=PAP29; OrderedLocusNames=At5g63140; ORFNames=MDC12.10;
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=9501997; DOI=10.1093/dnares/4.6.401;
RA Nakamura Y., Sato S., Kaneko T., Kotani H., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. III. Sequence
RT features of the regions of 1,191,918 bp covered by seventeen physically
RT assigned P1 clones.";
RL DNA Res. 4:401-414(1997).
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 Shinn P., Chen H., Cheuk R.F., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
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}.
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DR EMBL; AY882861; AAW80661.1; -; mRNA.
DR EMBL; AB008265; BAB10556.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97710.1; -; Genomic_DNA.
DR EMBL; BT014894; AAT44970.1; -; mRNA.
DR EMBL; BT015022; AAT70473.1; -; mRNA.
DR RefSeq; NP_201119.1; NM_125709.5.
DR AlphaFoldDB; Q9FMK9; -.
DR STRING; 3702.AT5G63140.1; -.
DR PaxDb; Q9FMK9; -.
DR PRIDE; Q9FMK9; -.
DR ProteomicsDB; 249030; -.
DR EnsemblPlants; AT5G63140.1; AT5G63140.1; AT5G63140.
DR GeneID; 836435; -.
DR Gramene; AT5G63140.1; AT5G63140.1; AT5G63140.
DR KEGG; ath:AT5G63140; -.
DR Araport; AT5G63140; -.
DR TAIR; locus:2161937; AT5G63140.
DR eggNOG; KOG1432; Eukaryota.
DR HOGENOM; CLU_019692_0_0_1; -.
DR InParanoid; Q9FMK9; -.
DR OMA; TCGFGSY; -.
DR OrthoDB; 908967at2759; -.
DR PhylomeDB; Q9FMK9; -.
DR PRO; PR:Q9FMK9; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FMK9; baseline and differential.
DR Genevisible; Q9FMK9; AT.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0003993; F:acid phosphatase activity; ISS:TAIR.
DR GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 3.60.21.10; -; 1.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR InterPro; IPR011230; Pesterase_At2g46.
DR Pfam; PF00149; Metallophos; 1.
DR PIRSF; PIRSF030250; Ptase_At2g46880; 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..34
FT /evidence="ECO:0000255"
FT CHAIN 35..389
FT /note="Probable inactive purple acid phosphatase 29"
FT /id="PRO_0000372831"
FT BINDING 136
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 136
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 303..305
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 303
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 305
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT CARBOHYD 80
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 191
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 267
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 380
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 389 AA; 43548 MW; 0E483ABCB10AF18A CRC64;
MADNRRRRSL FDFLLFSVFL GLACLCLSPI PATAQRRKLR FSVNGEFKIL QVADMHFANG
AKTQCQNVLP SQRAHCSDLN TTIFMSRVIA AEKPDLIVFT GDNIFGFDVK DALKSINAAF
APAIASKIPW VAILGNHDQE STFTRQQVMN HIVKLPNTLS QVNPPEAAHY IDGFGNYNLQ
IHGAADSKLQ NKSVLNLYFL DSGDYSSVPY MEGYDWIKTS QQFWFDRTSK RLKREYNAKP
NPQEGIAPGL AYFHIPLPEF LSFDSKNATK GVRQEGTSAA STNSGFFTTL IARGDVKSVF
VGHDHVNDFC GELKGLNLCY GGGFGYHAYG KAGWERRARV VVVDLNKKRK GKWGAVKSIK
TWKRLDDKHL SVIDSQVLWN NSANKLVVR
