PPA14_ARATH
ID PPA14_ARATH Reviewed; 401 AA.
AC Q84LR6; Q5MAV1; Q84LR5; Q9SLM3;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Probable inactive purple acid phosphatase 14;
DE Flags: Precursor;
GN Name=PAP14; OrderedLocusNames=At2g46880; ORFNames=F14M4.29;
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] (ISOFORM 2), 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=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] (ISOFORMS 1 AND 3).
RC STRAIN=cv. Columbia;
RX PubMed=12481096; DOI=10.1104/pp.010207;
RA Xiao Y.-L., Malik M., Whitelaw C.A., Town C.D.;
RT "Cloning and sequencing of cDNAs for hypothetical genes from chromosome 2
RT of Arabidopsis.";
RL Plant Physiol. 130:2118-2128(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RA Underwood B.A., Xiao Y.-L., Moskal W.A. Jr., Monaghan E.L., Wang W.,
RA Redman J.C., Wu H.C., Utterback T., Town C.D.;
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q84LR6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q84LR6-2; Sequence=VSP_037199;
CC Name=3;
CC IsoId=Q84LR6-3; Sequence=VSP_037198;
CC -!- TISSUE SPECIFICITY: Specifically expressed in flowers.
CC {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=AAC34232.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAM15023.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AY842023; AAW29948.1; -; mRNA.
DR EMBL; AC004411; AAC34232.2; ALT_SEQ; Genomic_DNA.
DR EMBL; AC005310; AAM15023.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; AEC10766.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC10767.1; -; Genomic_DNA.
DR EMBL; AY261790; AAP21684.1; -; mRNA.
DR EMBL; AY261791; AAP21685.1; -; mRNA.
DR EMBL; AY649304; AAT69221.1; -; mRNA.
DR PIR; D84908; D84908.
DR PIR; T02689; T02689.
DR RefSeq; NP_182211.2; NM_130255.2. [Q84LR6-1]
DR RefSeq; NP_973704.1; NM_201975.3. [Q84LR6-3]
DR AlphaFoldDB; Q84LR6; -.
DR STRING; 3702.AT2G46880.1; -.
DR PaxDb; Q84LR6; -.
DR PRIDE; Q84LR6; -.
DR ProteomicsDB; 249014; -. [Q84LR6-1]
DR EnsemblPlants; AT2G46880.1; AT2G46880.1; AT2G46880. [Q84LR6-1]
DR EnsemblPlants; AT2G46880.2; AT2G46880.2; AT2G46880. [Q84LR6-3]
DR GeneID; 819301; -.
DR Gramene; AT2G46880.1; AT2G46880.1; AT2G46880. [Q84LR6-1]
DR Gramene; AT2G46880.2; AT2G46880.2; AT2G46880. [Q84LR6-3]
DR KEGG; ath:AT2G46880; -.
DR Araport; AT2G46880; -.
DR TAIR; locus:2041379; AT2G46880.
DR eggNOG; KOG1432; Eukaryota.
DR InParanoid; Q84LR6; -.
DR OMA; WGAVDTI; -.
DR OrthoDB; 908967at2759; -.
DR PhylomeDB; Q84LR6; -.
DR PRO; PR:Q84LR6; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q84LR6; baseline and differential.
DR Genevisible; Q84LR6; AT.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
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 Alternative splicing; Glycoprotein; Iron; Metal-binding;
KW Reference proteome; Secreted; Signal; Zinc.
FT SIGNAL 1..30
FT /evidence="ECO:0000255"
FT CHAIN 31..401
FT /note="Probable inactive purple acid phosphatase 14"
FT /id="PRO_0000372818"
FT BINDING 197
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 197
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 256
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 305..307
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 305
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 307
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT CARBOHYD 79
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 246
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 266
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 371
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 384
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 328..401
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:12481096"
FT /id="VSP_037198"
FT VAR_SEQ 386..401
FT /note="TLEPNFGFSCSTIPQH -> SK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16244908"
FT /id="VSP_037199"
FT CONFLICT 92
FT /note="K -> E (in Ref. 1; AAW29948)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 401 AA; 45576 MW; 5A163B18B23FAE1E CRC64;
MEETRRRFVI SSVLSVSLIY LCLSTCHVSA FDFGRRQLRF NTDGRFKILQ VSDMHYGFGK
ETQCSDVSPA EFPYCSDLNT TSFLQRTIAS EKPDLIVFSG DNVYGLCETS DVAKSMDMAF
APAIESGIPW VAILGNHDQE SDMTRETMMK YIMKLPNSLS QVNPPDAWLY QIDGFGNYNL
QIEGPFGSPL FFKSILNLYL LDGGSYTKLD GFGYKYDWVK TSQQNWYEHT SKWLEMEHKR
WPFPQNSTAP GLVYLHIPMP EFALFNKSTE MTGVRQESTC SPPINSGFFT KLVERGEVKG
VFSGHDHVND FCAELHGINL CYAGGAGYHG YGQVGWARRV RVVEAQLEKT MYGRWGAVDT
IKTWKRLDDK NHSLIDTQLL WTKNTTLEPN FGFSCSTIPQ H
