PPA13_ARATH
ID PPA13_ARATH Reviewed; 545 AA.
AC O48840; Q3EBP9; Q8RX38;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 22-SEP-2009, sequence version 2.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Purple acid phosphatase 13;
DE EC=3.1.3.2;
DE Flags: Precursor;
GN Name=PAP13; Synonyms=AT2; OrderedLocusNames=At2g32770; ORFNames=F24L7.9;
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] (ISOFORMS 1 AND 3), GENE FAMILY, AND
RP 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 [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] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RX PubMed=14993207; DOI=10.1101/gr.1515604;
RA Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M.,
RA Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M.,
RA Weissenbach J., Salanoubat M.;
RT "Whole genome sequence comparisons and 'full-length' cDNA sequences: a
RT combined approach to evaluate and improve Arabidopsis genome annotation.";
RL Genome Res. 14:406-413(2004).
RN [5]
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. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=2;
CC IsoId=O48840-2; Sequence=Displayed;
CC Name=1;
CC IsoId=O48840-1; Sequence=VSP_038047;
CC Name=3;
CC IsoId=O48840-3; Sequence=VSP_037193, VSP_037196, VSP_037197;
CC -!- TISSUE SPECIFICITY: Expressed in stems, leaves, flowers and siliques.
CC {ECO:0000269|PubMed:16244908}.
CC -!- MISCELLANEOUS: [Isoform 1]: May be due to a competing donor splice
CC site. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 3]: May be due to introns retention.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the metallophosphoesterase superfamily. Purple
CC acid phosphatase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BX818780; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF492665; AAM15914.1; -; mRNA.
DR EMBL; AC003974; AAC04486.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC08736.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC08737.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC08738.1; -; Genomic_DNA.
DR EMBL; AY090894; AAM16284.1; -; mRNA.
DR EMBL; BX818780; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; T00791; T00791.
DR RefSeq; NP_180836.1; NM_128837.1. [O48840-1]
DR RefSeq; NP_850198.1; NM_179867.1. [O48840-3]
DR RefSeq; NP_973585.1; NM_201856.4. [O48840-2]
DR AlphaFoldDB; O48840; -.
DR SMR; O48840; -.
DR STRING; 3702.AT2G32770.3; -.
DR PaxDb; O48840; -.
DR PRIDE; O48840; -.
DR ProteomicsDB; 249013; -. [O48840-2]
DR EnsemblPlants; AT2G32770.1; AT2G32770.1; AT2G32770. [O48840-1]
DR EnsemblPlants; AT2G32770.2; AT2G32770.2; AT2G32770. [O48840-3]
DR EnsemblPlants; AT2G32770.3; AT2G32770.3; AT2G32770. [O48840-2]
DR GeneID; 817838; -.
DR Gramene; AT2G32770.1; AT2G32770.1; AT2G32770. [O48840-1]
DR Gramene; AT2G32770.2; AT2G32770.2; AT2G32770. [O48840-3]
DR Gramene; AT2G32770.3; AT2G32770.3; AT2G32770. [O48840-2]
DR KEGG; ath:AT2G32770; -.
DR Araport; AT2G32770; -.
DR TAIR; locus:2046407; AT2G32770.
DR eggNOG; KOG1378; Eukaryota.
DR HOGENOM; CLU_013387_1_0_1; -.
DR InParanoid; O48840; -.
DR OMA; CCEEDSL; -.
DR OrthoDB; 426430at2759; -.
DR PhylomeDB; O48840; -.
DR BioCyc; ARA:AT2G32770-MON; -.
DR BRENDA; 3.1.3.2; 399.
DR PRO; PR:O48840; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O48840; baseline and differential.
DR Genevisible; O48840; 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; 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 Alternative splicing; Glycoprotein; Hydrolase; Iron; Metal-binding;
KW Reference proteome; Secreted; Signal; Zinc.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..545
FT /note="Purple acid phosphatase 13"
FT /id="PRO_0000372817"
FT ACT_SITE 389
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 203
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 233
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 416..418
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 416
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT CARBOHYD 125
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 145
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 209
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 240
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 254
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 306
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 321
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 351
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 367
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 428
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 466
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 475
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 510
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..88
FT /note="MVVKYTMSMSFFVIFASTVTIIVHGFPSTLDGPLNPVTAPLDPNLNPIAFDL
FT PESDPSFVKPISEFLLPEQISVSLSYSFDSVWISWV -> MVVVLYT (in isoform
FT 3)"
FT /evidence="ECO:0000303|PubMed:12021284"
FT /id="VSP_037193"
FT VAR_SEQ 324..353
FT /note="GSFSPLYYSFNAGGAHFIVLNSYTLYDNSS -> A (in isoform 1)"
FT /evidence="ECO:0000303|PubMed:12021284"
FT /id="VSP_038047"
FT VAR_SEQ 509
FT /note="K -> S (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:12021284"
FT /id="VSP_037196"
FT VAR_SEQ 510..545
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:12021284"
FT /id="VSP_037197"
FT CONFLICT 384
FT /note="S -> R (in Ref. 4; BX818780)"
FT /evidence="ECO:0000305"
FT CONFLICT 387..388
FT /note="KG -> TR (in Ref. 4; BX818780)"
FT /evidence="ECO:0000305"
FT CONFLICT 392
FT /note="E -> D (in Ref. 4; BX818780)"
FT /evidence="ECO:0000305"
FT CONFLICT 402
FT /note="D -> N (in Ref. 4; BX818780)"
FT /evidence="ECO:0000305"
FT CONFLICT O48840-3:47
FT /note="G -> D (in Ref. 4; AAM16284)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 545 AA; 61543 MW; 4E35C8DCDD2B293C CRC64;
MVVKYTMSMS FFVIFASTVT IIVHGFPSTL DGPLNPVTAP LDPNLNPIAF DLPESDPSFV
KPISEFLLPE QISVSLSYSF DSVWISWVTG EYQIGEKDSA PLDPNCVQSI VQYREFDVRR
TRKQNATGHS IVYNQQYSSE NGFMNYTSGI IHHVQLTGLK PNTLYRYQCG DPSLSAMSKE
YYFRTMPKST SENYPHRIVV AGDLGLTYNT STVLGHILSN HPDLVVLLGG FSYADTYLAN
KTKLDCSSCH CDQNGTSSDC GSCYSSGETY QPRWDYWGRF MEPLTANVPT MMVAGEHEIE
PQTENNLTFA AYSSRFAFPS NESGSFSPLY YSFNAGGAHF IVLNSYTLYD NSSDQYIWLE
SDLIKINRSE TPWVVATWSL PWYSTFKGHY REAESMRIHL EDLLYNYRVD IVFNSHVDAY
ERSNRVYNYT LDQCGPVYIT TGAGGAGKLE TQHVDDPGNI PDPSQNYSCR SSGLNSTLEP
VKDETCPVKQ PEYSAYRESS FGFGILEVKN ETHALWSWNR NQDLYYLAAD VIHIVRQPEM
CSVCN
