PPA23_ARATH
ID PPA23_ARATH Reviewed; 458 AA.
AC Q6TPH1; Q9SVP2;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 2.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Purple acid phosphatase 23;
DE EC=3.1.3.2;
DE Flags: Precursor;
GN Name=PAP23; Synonyms=AT3; OrderedLocusNames=At4g13700; ORFNames=F18A5.90;
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], FUNCTION, DEVELOPMENTAL STAGE,
RP BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, 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=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [3]
RP GENOME REANNOTATION, AND SEQUENCE REVISION.
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 -!- FUNCTION: Acid phosphatase activity with ATP, ADP, dATP, pyrophosphate,
CC polyphosphate, phosphoserine and phosphothreonine. Low or no activity
CC with phosphotyrosine, AMP and phytate. {ECO:0000269|PubMed:16244908}.
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;
CC Evidence={ECO:0000269|PubMed:16244908};
CC Note=Binds 1 Fe cation per subunit. {ECO:0000269|PubMed:16244908};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:16244908};
CC Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000269|PubMed:16244908};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 5-6. {ECO:0000269|PubMed:16244908};
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Specifically expressed in flowers.
CC {ECO:0000269|PubMed:16244908}.
CC -!- DEVELOPMENTAL STAGE: First observed in the floral apical meristem
CC (FAP). In flowers, observed in petals and anthers, particularly in
CC anther filaments. {ECO:0000269|PubMed:16244908}.
CC -!- SIMILARITY: Belongs to the metallophosphoesterase superfamily. Purple
CC acid phosphatase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB36834.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB78412.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AY390530; AAQ93685.1; -; mRNA.
DR EMBL; AL035528; CAB36834.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161537; CAB78412.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE83314.1; -; Genomic_DNA.
DR PIR; T05239; T05239.
DR RefSeq; NP_193106.3; NM_117444.3.
DR AlphaFoldDB; Q6TPH1; -.
DR SMR; Q6TPH1; -.
DR STRING; 3702.AT4G13700.1; -.
DR PaxDb; Q6TPH1; -.
DR PeptideAtlas; Q6TPH1; -.
DR PRIDE; Q6TPH1; -.
DR GeneID; 827004; -.
DR KEGG; ath:AT4G13700; -.
DR Araport; AT4G13700; -.
DR eggNOG; KOG1378; Eukaryota.
DR HOGENOM; CLU_013387_0_0_1; -.
DR InParanoid; Q6TPH1; -.
DR OrthoDB; 426430at2759; -.
DR PhylomeDB; Q6TPH1; -.
DR BioCyc; ARA:AT4G13700-MON; -.
DR BRENDA; 3.1.3.2; 399.
DR PRO; PR:Q6TPH1; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q6TPH1; baseline and differential.
DR Genevisible; Q6TPH1; AT.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0003993; F:acid phosphatase activity; IEA:UniProtKB-EC.
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 PANTHER; PTHR22953; PTHR22953; 1.
DR Pfam; PF00149; Metallophos; 1.
DR Pfam; PF16656; Pur_ac_phosph_N; 1.
DR SUPFAM; SSF49363; SSF49363; 1.
DR SUPFAM; SSF56300; SSF56300; 1.
PE 1: Evidence at protein level;
KW Glycoprotein; Hydrolase; Iron; Metal-binding; Reference proteome; Secreted;
KW Signal; Zinc.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..458
FT /note="Purple acid phosphatase 23"
FT /id="PRO_0000372826"
FT ACT_SITE 370
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 194
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000305"
FT BINDING 221
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000305"
FT BINDING 221
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000305"
FT BINDING 224
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000305"
FT BINDING 278
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000305"
FT BINDING 278
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 360
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000305"
FT BINDING 397..399
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 397
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000305"
FT BINDING 399
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000305"
FT CARBOHYD 59
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 121
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 136
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 200
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 331
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 409
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 455
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 310
FT /note="L -> F (in Ref. 1; AAQ93685 and 3; AEE83314)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 458 AA; 51551 MW; 3FE6A789CBDF7A72 CRC64;
MTLLIMITLT SISLLLAAAE TIPTTLDGPF KPLTRRFEPS LRRGSDDLPM DHPRLRKRNV
SSDFPEQIAL ALSTPTSMWV SWVTGDAIVG KDVKPLDPSS IASEVWYGKE KGNYMLKKKG
NATVYSQLYP SDGLLNYTSG IIHHVLIDGL EPETRYYYRC GDSSVPAMSE EISFETLPLP
SKDAYPHRIA FVGDLGLTSN TTTTIDHLME NDPSLVIIVG DLTYANQYRT IGGKGVPCFS
CSFPDAPIRE TYQPRWDAWG RFMEPLTSKV PTMVIEGNHE IEPQASGITF KSYSERFAVP
ASESGSNSNL YYSFDAGGVH FVMLGAYVDY NNTGLQYAWL KEDLSKVDRA VTPWLVATMH
PPWYNSYSSH YQEFECMRQE MEELLYQYRV DIVFAGHVHA YERMNRIYNY TLDPCGPVYI
TIGDGGNIEK VDVDFADDPG KCHSSYDLFF FNSLNLSN
