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PPA8_ARATH
ID   PPA8_ARATH              Reviewed;         335 AA.
AC   Q8VYZ2; Q3EC86; Q9SDZ8; Q9SIS5;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 123.
DE   RecName: Full=Purple acid phosphatase 8;
DE            EC=3.1.3.2;
DE   Flags: Precursor;
GN   Name=PAP8; OrderedLocusNames=At2g01890; ORFNames=T23K3.8;
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] (ISOFORM 1), 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], AND ALTERNATIVE SPLICING
RP   (ISOFORM 2).
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   NUCLEOTIDE SEQUENCE [MRNA] OF 1-314 (ISOFORM 1).
RC   STRAIN=cv. Columbia;
RX   PubMed=10854785; DOI=10.1016/s0378-1119(00)00186-4;
RA   Schenk G., Guddat L.W., Ge Y., Carrington L.E., Hume D.A., Hamilton S.,
RA   de Jersey J.;
RT   "Identification of mammalian-like purple acid phosphatases in a wide range
RT   of plants.";
RL   Gene 250:117-125(2000).
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   -!- 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   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8VYZ2-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8VYZ2-2; Sequence=VSP_037190;
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   -!- SEQUENCE CAUTION:
CC       Sequence=AAD21785.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=AAF19823.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AF492660; AAM15909.1; -; mRNA.
DR   EMBL; AC007069; AAD21785.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002685; AEC05512.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC05513.1; -; Genomic_DNA.
DR   EMBL; AY065434; AAL38875.1; -; mRNA.
DR   EMBL; AY117232; AAM51307.1; -; mRNA.
DR   EMBL; AF200827; AAF19823.1; ALT_FRAME; mRNA.
DR   PIR; D84430; D84430.
DR   RefSeq; NP_178298.2; NM_126250.5. [Q8VYZ2-1]
DR   RefSeq; NP_973397.1; NM_201668.2. [Q8VYZ2-2]
DR   AlphaFoldDB; Q8VYZ2; -.
DR   SMR; Q8VYZ2; -.
DR   BioGRID; 123; 1.
DR   IntAct; Q8VYZ2; 1.
DR   STRING; 3702.AT2G01890.1; -.
DR   PaxDb; Q8VYZ2; -.
DR   PRIDE; Q8VYZ2; -.
DR   ProteomicsDB; 249117; -. [Q8VYZ2-1]
DR   EnsemblPlants; AT2G01890.1; AT2G01890.1; AT2G01890. [Q8VYZ2-1]
DR   EnsemblPlants; AT2G01890.2; AT2G01890.2; AT2G01890. [Q8VYZ2-2]
DR   GeneID; 814720; -.
DR   Gramene; AT2G01890.1; AT2G01890.1; AT2G01890. [Q8VYZ2-1]
DR   Gramene; AT2G01890.2; AT2G01890.2; AT2G01890. [Q8VYZ2-2]
DR   KEGG; ath:AT2G01890; -.
DR   Araport; AT2G01890; -.
DR   TAIR; locus:2059748; AT2G01890.
DR   eggNOG; KOG2679; Eukaryota.
DR   InParanoid; Q8VYZ2; -.
DR   OMA; CTHHPYL; -.
DR   OrthoDB; 711825at2759; -.
DR   PhylomeDB; Q8VYZ2; -.
DR   BioCyc; ARA:AT2G01890-MON; -.
DR   PRO; PR:Q8VYZ2; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; Q8VYZ2; baseline and differential.
DR   Genevisible; Q8VYZ2; AT.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0003993; F:acid phosphatase activity; ISS:TAIR.
DR   GO; GO:0008199; F:ferric iron binding; IBA:GO_Central.
DR   GO; GO:0008198; F:ferrous iron binding; IBA:GO_Central.
DR   GO; GO:0016311; P:dephosphorylation; ISS:TAIR.
DR   CDD; cd07378; MPP_ACP5; 1.
DR   Gene3D; 3.60.21.10; -; 1.
DR   InterPro; IPR024927; Acid_PPase.
DR   InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR   InterPro; IPR029052; Metallo-depent_PP-like.
DR   Pfam; PF00149; Metallophos; 1.
DR   PIRSF; PIRSF000898; Acid_Ptase_5; 1.
DR   SUPFAM; SSF56300; SSF56300; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Glycoprotein; Hydrolase; Iron; Metal-binding;
KW   Reference proteome; Secreted; Signal; Zinc.
FT   SIGNAL          1..30
FT                   /evidence="ECO:0000255"
FT   CHAIN           31..335
FT                   /note="Purple acid phosphatase 8"
FT                   /id="PRO_0000372813"
FT   ACT_SITE        226
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         52
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   BINDING         85
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   BINDING         85
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         88
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   BINDING         123
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         217
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         252..254
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         252
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         254
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        60
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         128..155
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_037190"
FT   CONFLICT        261
FT                   /note="S -> G (in Ref. 5; AAF19823)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        266
FT                   /note="I -> M (in Ref. 5; AAF19823)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        275
FT                   /note="S -> F (in Ref. 5; AAF19823)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        287
FT                   /note="P -> L (in Ref. 5; AAF19823)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   335 AA;  38173 MW;  4202286D73CBFF7C CRC64;
     MDSLRDVKPI KLIFSIFCLV IILSACNSTA ELPRFVQPPE PDGSLSFLVV GDWGRRGSYN
     QSQVALQMGK IGKDLNIDFL ISTGDNFYDD GIISPYDSQF QDSFTNIYTA TSLQKPWYNV
     LGNHDYRGNV YAQLSPILRD LDCRWICLRS YVVNAEIVDI FFVDTTPFVD RYFDEPKDHV
     YDWRGVLPRN KYLNSLLTDV DVALQESMAK WKIVVGHHTI KSAGHHGNTI ELEKQLLPIL
     EANEVDLYIN GHDHCLEHIS SINSGIQFMT SGGGSKAWKG DVNDWNPQEM RFYYDGQGFM
     SVYTSEAELR VVFYDGLGHV LHRWSTLKNG VYSDI
 
 
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