PPA9_ARATH
ID PPA9_ARATH Reviewed; 651 AA.
AC Q9ZQ81; Q7XY12; Q84QH4;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Probable inactive purple acid phosphatase 9;
DE Flags: Precursor;
GN Name=PAP9; OrderedLocusNames=At2g03450; ORFNames=T4M8.12;
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] (ISOFORMS 1 AND 2), 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 1).
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 482-641 (ISOFORMS 1/2).
RC TISSUE=Seedling;
RA Lohrasebi T., Malboobi M.A.;
RT "Identification of differentially displayed Arabidopsis thaliana acid
RT phosphatase-encoding genes.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
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 -!- 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=2;
CC Name=1;
CC IsoId=Q9ZQ81-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9ZQ81-2; Sequence=VSP_037191;
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; AF492661; AAM15910.1; -; mRNA.
DR EMBL; AY090895; AAM16285.1; -; mRNA.
DR EMBL; AC006284; AAD17431.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC05701.1; -; Genomic_DNA.
DR EMBL; AK228718; BAF00620.1; -; mRNA.
DR EMBL; AY297743; AAP81216.1; -; mRNA.
DR PIR; F84448; F84448.
DR RefSeq; NP_178444.1; NM_126396.2. [Q9ZQ81-1]
DR AlphaFoldDB; Q9ZQ81; -.
DR SMR; Q9ZQ81; -.
DR STRING; 3702.AT2G03450.1; -.
DR PaxDb; Q9ZQ81; -.
DR PRIDE; Q9ZQ81; -.
DR ProteomicsDB; 249035; -. [Q9ZQ81-1]
DR EnsemblPlants; AT2G03450.1; AT2G03450.1; AT2G03450. [Q9ZQ81-1]
DR GeneID; 814874; -.
DR Gramene; AT2G03450.1; AT2G03450.1; AT2G03450. [Q9ZQ81-1]
DR KEGG; ath:AT2G03450; -.
DR Araport; AT2G03450; -.
DR TAIR; locus:2063777; AT2G03450.
DR eggNOG; KOG1378; Eukaryota.
DR HOGENOM; CLU_013387_4_1_1; -.
DR InParanoid; Q9ZQ81; -.
DR OMA; RIFHWTQ; -.
DR PhylomeDB; Q9ZQ81; -.
DR PRO; PR:Q9ZQ81; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9ZQ81; baseline and differential.
DR Genevisible; Q9ZQ81; 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; IPR008963; Purple_acid_Pase-like_N.
DR InterPro; IPR015914; Purple_acid_Pase_N.
DR InterPro; IPR025733; Purple_acid_PPase_C_dom.
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; Iron; Metal-binding;
KW Reference proteome; Secreted; Signal; Zinc.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..651
FT /note="Probable inactive purple acid phosphatase 9"
FT /id="PRO_0000372814"
FT BINDING 305
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 305
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 308
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 338
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 338
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 444
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 483..485
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 483
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 485
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT CARBOHYD 32
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 96
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 202
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 378
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 432
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 495
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 640
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..257
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12021284"
FT /id="VSP_037191"
SQ SEQUENCE 651 AA; 73813 MW; 2FDBB3831C74A927 CRC64;
MIAAVYTLFF FFLLISSVYS KATISISPQT LNRSGDIVVI KWSGVESPSD LDWLGIYSPP
DSPHDHFIGY KFLSDSPTWQ SGSGSISLPL TNLRSNYTFR IFHWTQSEIN PKHQDHDHNP
LPGTRHLLTE SNQLNFRFAV NRPEQIHLSY TDNINEMRVV FVTGDGEERE ARYGEVKDKL
DNIAVARGVR YEIEHMCHAP ANSTVGWRDP GWTFDAVMKN LKQGIRYYYQ VGSDLKGWSE
IHSFVSRNEG SEETLAFMFG DMGCYTPYTT FIRGEEESLS TVKWILRDIE ALGDDKPVIV
SHIGDISYAR GYSWIWDEFF TQIEPIASKV PYHVCIGNHE YDWPNQPWKP DWAAYVYGKD
SGGECGVPYS VKFNMPGNST EATGMVKGPQ SRNLYYSYDM GSVHFVYIST ETDFLKGGKQ
YSFLKSDLES VNRSKTPFVV VQGHRPMYTT SRKIRDAAIR EKMIEHLEPL LVKNNVTVAL
WGHVHRYERF CAISNNTCGE RWQGNPVHLV IGMAGKDSQP MWEPRANHED VPIFPQPANS
MYRGGEFGYI RLVANKERLT LSYVGNHDGE VHDVVEILAS GEVISGSDDG TKDSNFGSES
DFAVLWYIEG ASVMVVGVIF GYFVGFLSRK KKESGVGSSN RSWIQVKNEE T
