PPA10_ARATH
ID PPA10_ARATH Reviewed; 468 AA.
AC Q9SIV9; Q8RX39;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Purple acid phosphatase 10;
DE EC=3.1.3.2;
DE Flags: Precursor;
GN Name=PAP10; Synonyms=AT11; OrderedLocusNames=At2g16430; ORFNames=F16F14.7;
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 2), SUBCELLULAR LOCATION,
RP 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 [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 1).
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 [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; disulfide-linked. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Secreted {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9SIV9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9SIV9-2; Sequence=VSP_037192;
CC -!- TISSUE SPECIFICITY: Expressed in roots, stems, leaves, flowers and
CC siliques. {ECO:0000269|PubMed:16244908}.
CC -!- INDUCTION: By phosphate deprivation, mostly isoform 2.
CC {ECO:0000269|PubMed:12021284}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to intron retention.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the metallophosphoesterase superfamily. Purple
CC acid phosphatase family. {ECO:0000305}.
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DR EMBL; AF492662; AAM15911.1; -; mRNA.
DR EMBL; AY090893; AAM16283.1; -; mRNA.
DR EMBL; AC007047; AAD22297.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC06495.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC06496.1; -; Genomic_DNA.
DR EMBL; AY093236; AAM13235.1; -; mRNA.
DR EMBL; BT008761; AAP49523.1; -; mRNA.
DR PIR; B84540; B84540.
DR RefSeq; NP_179235.1; NM_127196.4. [Q9SIV9-1]
DR RefSeq; NP_849960.1; NM_179629.2. [Q9SIV9-2]
DR AlphaFoldDB; Q9SIV9; -.
DR SMR; Q9SIV9; -.
DR STRING; 3702.AT2G16430.2; -.
DR PaxDb; Q9SIV9; -.
DR PRIDE; Q9SIV9; -.
DR ProteomicsDB; 249010; -. [Q9SIV9-1]
DR EnsemblPlants; AT2G16430.1; AT2G16430.1; AT2G16430. [Q9SIV9-2]
DR EnsemblPlants; AT2G16430.2; AT2G16430.2; AT2G16430. [Q9SIV9-1]
DR GeneID; 816141; -.
DR Gramene; AT2G16430.1; AT2G16430.1; AT2G16430. [Q9SIV9-2]
DR Gramene; AT2G16430.2; AT2G16430.2; AT2G16430. [Q9SIV9-1]
DR KEGG; ath:AT2G16430; -.
DR Araport; AT2G16430; -.
DR TAIR; locus:2042689; AT2G16430.
DR eggNOG; KOG1378; Eukaryota.
DR InParanoid; Q9SIV9; -.
DR OMA; EEPCEQY; -.
DR PhylomeDB; Q9SIV9; -.
DR BioCyc; ARA:AT2G16430-MON; -.
DR PRO; PR:Q9SIV9; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9SIV9; baseline and differential.
DR Genevisible; Q9SIV9; AT.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0009505; C:plant-type cell wall; HDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0003993; F:acid phosphatase activity; IDA:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016036; P:cellular response to phosphate starvation; IMP:TAIR.
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; Cytoplasm; Disulfide bond; Glycoprotein; Hydrolase;
KW Iron; Metal-binding; Reference proteome; Secreted; Signal; Zinc.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..468
FT /note="Purple acid phosphatase 10"
FT /id="PRO_0000372815"
FT ACT_SITE 328
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 167
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 196
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 196
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 199
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 233
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 233
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 318
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 355..357
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 355
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 357
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT CARBOHYD 95
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 113
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 175
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 428
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 377
FT /note="Interchain"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..128
FT /note="MGRVRKSDFGSIVLVLCCVLNSLLCNGGITSRYVRKLEATVDMPLDSDVFRV
FT PCGYNAPQQVHITQGDVEGKAVIVSWVTQEAKGSNKVIYWKENSTKKHKAHGKTNTYKF
FT YNYTSGFIHHCPIRNLE -> MLWFFLLQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12021284"
FT /id="VSP_037192"
FT CONFLICT 167
FT /note="D -> N (in Ref. 1; AAM16283)"
FT /evidence="ECO:0000305"
FT CONFLICT 280
FT /note="I -> V (in Ref. 1; AAM16283)"
FT /evidence="ECO:0000305"
FT CONFLICT 441
FT /note="D -> G (in Ref. 1; AAM16283)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 468 AA; 54219 MW; ED1EB9821C5C118B CRC64;
MGRVRKSDFG SIVLVLCCVL NSLLCNGGIT SRYVRKLEAT VDMPLDSDVF RVPCGYNAPQ
QVHITQGDVE GKAVIVSWVT QEAKGSNKVI YWKENSTKKH KAHGKTNTYK FYNYTSGFIH
HCPIRNLEYD TKYYYVLGVG QTERKFWFFT PPEIGPDVPY TFGLIGDLGQ SYDSNITLTH
YENNPTKGQA VLFVGDISYA DTYPDHDNRR WDSWGRFAER STAYQPWIWT TGNHELDFAP
EIGENRPFKP FTHRYRTPYR SSGSTEPFWY SIKRGPAYII VLASYSAYGK YTPQYQWLEE
EFPKVNRTET PWLIVLMHSP WYNSYDYHYM EGETMRVMYE AWFVKYKVDV VFAGHVHAYE
RSERVSNIAY NVVNGICTPV KDQSAPVYIT IGDGGNIEGL ATKMTEPQPK YSAFREASFG
HAIFSIKNRT HAHYGWHRNH DGYAVEGDRM WFYNRFWHPV DDSPSCNS
