PPA2_ARATH
ID PPA2_ARATH Reviewed; 656 AA.
AC Q9LMG7; Q5MAU7;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Probable inactive purple acid phosphatase 2;
DE Flags: Precursor;
GN Name=PAP2; OrderedLocusNames=At1g13900; ORFNames=F16A14.11;
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
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 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; AY842028; AAW29952.1; -; mRNA.
DR EMBL; AC068197; AAF79414.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE29081.1; -; Genomic_DNA.
DR RefSeq; NP_172843.1; NM_101256.3.
DR AlphaFoldDB; Q9LMG7; -.
DR SMR; Q9LMG7; -.
DR BioGRID; 23189; 1.
DR STRING; 3702.AT1G13900.1; -.
DR PaxDb; Q9LMG7; -.
DR PRIDE; Q9LMG7; -.
DR ProteomicsDB; 249031; -.
DR EnsemblPlants; AT1G13900.1; AT1G13900.1; AT1G13900.
DR GeneID; 837949; -.
DR Gramene; AT1G13900.1; AT1G13900.1; AT1G13900.
DR KEGG; ath:AT1G13900; -.
DR Araport; AT1G13900; -.
DR TAIR; locus:2014839; AT1G13900.
DR eggNOG; KOG1378; Eukaryota.
DR HOGENOM; CLU_013387_4_1_1; -.
DR InParanoid; Q9LMG7; -.
DR OMA; HFFNQIE; -.
DR OrthoDB; 426430at2759; -.
DR PhylomeDB; Q9LMG7; -.
DR PRO; PR:Q9LMG7; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9LMG7; baseline and differential.
DR Genevisible; Q9LMG7; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; IDA:TAIR.
DR GO; GO:0005768; C:endosome; HDA:TAIR.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
DR GO; GO:0005740; C:mitochondrial envelope; IDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR GO; GO:0005802; C:trans-Golgi network; HDA:TAIR.
DR GO; GO:0003993; F:acid phosphatase activity; IMP:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030943; F:mitochondrion targeting sequence binding; IPI:TAIR.
DR GO; GO:0045040; P:protein insertion into mitochondrial outer membrane; IDA:TAIR.
DR GO; GO:0006626; P:protein targeting to mitochondrion; IDA:TAIR.
DR GO; GO:0006109; P:regulation of carbohydrate metabolic process; 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; 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 Glycoprotein; Iron; Metal-binding; Reference proteome; Secreted; Signal;
KW Zinc.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..656
FT /note="Probable inactive purple acid phosphatase 2"
FT /id="PRO_0000372807"
FT BINDING 306
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 306
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 309
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 339
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 339
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 34
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 76
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 98
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 204
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 379
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 CONFLICT 161
FT /note="V -> G (in Ref. 1; AAW29952)"
FT /evidence="ECO:0000305"
FT CONFLICT 370
FT /note="Y -> H (in Ref. 1; AAW29952)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 656 AA; 73717 MW; 50A538F2111FDF21 CRC64;
MIVNFSFFLL LFVSVFVSSA DSKATISISP NALNRSGDSV VIQWSGVDSP SDLDWLGLYS
PPESPNDHFI GYKFLNESST WKDGFGSISL PLTNLRSNYT FRIFRWSESE IDPKHKDHDQ
NPLPGTKHLL AESEQLTFGS GVGMPEQIHL SFTNMVNTMR VMFVAGDGEE RFVRYGESKD
LLGNSAAARG MRYEREHMCD SPANSTIGWR DPGWIFDTVM KNLNDGVRYY YQVGSDSKGW
SEIHSYIARD VTAEETVAFM FGDMGCATPY TTFIRTQDES ISTVKWILRD IEALGDKPAM
ISHIGDISYA RGYSWVWDEF FAQVEPIAST VPYHVCIGNH EYDFSTQPWK PDWAASIYGN
DGGGECGVPY SLKFNMPGNS SESTGMKAPP TRNLYYSYDM GTVHFVYIST ETNFLKGGSQ
YEFIKRDLES VDRKKTPFVV VQGHRPMYTT SNEVRDTMIR QKMVEHLEPL FVKNNVTLAL
WGHVHRYERF CPISNNTCGT QWQGNPVHLV IGMAGQDWQP IWQPRPNHPD LPIFPQPEQS
MYRTGEFGYT RLVANKEKLT VSFVGNHDGE VHDTVEMLAS GVVISGSKES TKIPNLKTVP
ASATLMGKSE SNALWYAKGA GLMVVGVLLG FIIGFFTRGK KSSSGNRWIP VKNEET
