PPA18_ARATH
ID PPA18_ARATH Reviewed; 437 AA.
AC Q9LJU7; Q7XY13; Q8H6W7;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Purple acid phosphatase 18;
DE EC=3.1.3.2;
DE Flags: Precursor;
GN Name=PAP18; Synonyms=PAP30; OrderedLocusNames=At3g20500; ORFNames=K10D20.4;
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=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 NUCLEOTIDE SEQUENCE [MRNA] OF 212-332.
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 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 -!- 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 -!- 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}.
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DR EMBL; AF448725; AAN74649.1; -; mRNA.
DR EMBL; AP000410; BAB01159.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE76388.1; -; Genomic_DNA.
DR EMBL; AY062488; AAL32566.1; -; mRNA.
DR EMBL; AY093272; AAM13271.1; -; mRNA.
DR EMBL; AY297742; AAP81215.1; -; mRNA.
DR RefSeq; NP_188686.2; NM_112942.5.
DR AlphaFoldDB; Q9LJU7; -.
DR SMR; Q9LJU7; -.
DR STRING; 3702.AT3G20500.1; -.
DR iPTMnet; Q9LJU7; -.
DR PaxDb; Q9LJU7; -.
DR PRIDE; Q9LJU7; -.
DR ProteomicsDB; 249018; -.
DR EnsemblPlants; AT3G20500.1; AT3G20500.1; AT3G20500.
DR GeneID; 821596; -.
DR Gramene; AT3G20500.1; AT3G20500.1; AT3G20500.
DR KEGG; ath:AT3G20500; -.
DR Araport; AT3G20500; -.
DR TAIR; locus:2085770; AT3G20500.
DR eggNOG; KOG1378; Eukaryota.
DR HOGENOM; CLU_013387_0_0_1; -.
DR InParanoid; Q9LJU7; -.
DR OMA; YADDWYL; -.
DR OrthoDB; 426430at2759; -.
DR PhylomeDB; Q9LJU7; -.
DR BioCyc; ARA:AT3G20500-MON; -.
DR PRO; PR:Q9LJU7; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LJU7; baseline and differential.
DR Genevisible; Q9LJU7; 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 Glycoprotein; Hydrolase; Iron; Metal-binding; Reference proteome; Secreted;
KW Signal; Zinc.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..437
FT /note="Purple acid phosphatase 18"
FT /id="PRO_0000372821"
FT ACT_SITE 301
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 148
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 175
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 175
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 178
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 208
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 208
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 291
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 328..330
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 328
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 330
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT CARBOHYD 390
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 212
FT /note="E -> A (in Ref. 5; AAP81215)"
FT /evidence="ECO:0000305"
FT CONFLICT 242
FT /note="Y -> N (in Ref. 1; AAN74649)"
FT /evidence="ECO:0000305"
FT CONFLICT 395
FT /note="L -> I (in Ref. 1; AAN74649)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 437 AA; 49870 MW; 1CD48C6F4E8E3ABE CRC64;
MEKWGILLLV TLSVSIIFTS AAADDYVRPK PRETLQFPWK QKSSSVPEQV HISLAGDKHM
RVTWVTNDKS SPSFVEYGTS PGKYSYLGQG ESTSYSYIMY RSGKIHHTVI GPLEADTVYY
YRCGGEGPEF HLKTPPAQFP ITFAVAGDLG QTGWTKSTLD HIDQCKYAVH LLPGDLSYAD
YMQHKWDTFG ELVQPLASVR PWMVTQGNHE KESIPFIVDE FVSFNSRWKM PYEESGSNSN
LYYSFEVAGV HAIMLGSYTD YDRYSDQYSW LKADLSKVDR ERTPWLIVLF HVPWYNSNNA
HQHEGDEMMA EMEPLLYASG VDIVFTGHVH AYERTKRVNN GKSDPCGPVH ITIGDGGNRE
GLARKYKDPS PEWSVFREAS FGHGELQMVN STHALWTWHR NDDDEPTRSD EVWLNSLVNS
GCLKKRPQEL RKMLLEP
