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U87A2_ARATH
ID   U87A2_ARATH             Reviewed;         455 AA.
AC   O64733; A8MS44;
DT   31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 134.
DE   RecName: Full=UDP-glycosyltransferase 87A2;
DE            EC=2.4.1.-;
GN   Name=UGT87A2; OrderedLocusNames=At2g30140; ORFNames=T27E13.12;
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 [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   [2]
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   [3]
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   [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   GENE FAMILY.
RX   PubMed=11042215; DOI=10.1074/jbc.m007447200;
RA   Li Y., Baldauf S., Lim E.K., Bowles D.J.;
RT   "Phylogenetic analysis of the UDP-glycosyltransferase multigene family of
RT   Arabidopsis thaliana.";
RL   J. Biol. Chem. 276:4338-4343(2001).
RN   [6]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA   Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA   Giglione C.;
RT   "Comparative large-scale characterisation of plant vs. mammal proteins
RT   reveals similar and idiosyncratic N-alpha acetylation features.";
RL   Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=O64733-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=O64733-2; Sequence=VSP_041232;
CC   -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; AC004165; AAC16958.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC08350.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC08351.1; -; Genomic_DNA.
DR   EMBL; AY093176; AAM13175.1; -; mRNA.
DR   EMBL; BT006597; AAP31941.1; -; mRNA.
DR   EMBL; AK226350; BAE98498.1; -; mRNA.
DR   PIR; T00584; T00584.
DR   RefSeq; NP_001077979.1; NM_001084510.1. [O64733-2]
DR   RefSeq; NP_180575.1; NM_128569.4. [O64733-1]
DR   AlphaFoldDB; O64733; -.
DR   SMR; O64733; -.
DR   BioGRID; 2915; 1.
DR   STRING; 3702.AT2G30140.1; -.
DR   CAZy; GT1; Glycosyltransferase Family 1.
DR   iPTMnet; O64733; -.
DR   PaxDb; O64733; -.
DR   PRIDE; O64733; -.
DR   ProteomicsDB; 228651; -. [O64733-1]
DR   EnsemblPlants; AT2G30140.1; AT2G30140.1; AT2G30140. [O64733-1]
DR   EnsemblPlants; AT2G30140.2; AT2G30140.2; AT2G30140. [O64733-2]
DR   GeneID; 817566; -.
DR   Gramene; AT2G30140.1; AT2G30140.1; AT2G30140. [O64733-1]
DR   Gramene; AT2G30140.2; AT2G30140.2; AT2G30140. [O64733-2]
DR   KEGG; ath:AT2G30140; -.
DR   Araport; AT2G30140; -.
DR   TAIR; locus:2060832; AT2G30140.
DR   eggNOG; KOG1192; Eukaryota.
DR   InParanoid; O64733; -.
DR   OMA; FEGLERC; -.
DR   PhylomeDB; O64733; -.
DR   PRO; PR:O64733; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; O64733; baseline and differential.
DR   Genevisible; O64733; AT.
DR   GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR   GO; GO:0005829; C:cytosol; HDA:TAIR.
DR   GO; GO:0005634; C:nucleus; IDA:TAIR.
DR   GO; GO:0008194; F:UDP-glycosyltransferase activity; IEA:InterPro.
DR   GO; GO:0009909; P:regulation of flower development; IMP:TAIR.
DR   CDD; cd03784; GT1_Gtf-like; 1.
DR   InterPro; IPR002213; UDP_glucos_trans.
DR   Pfam; PF00201; UDPGT; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Glycosyltransferase; Reference proteome;
KW   Transferase.
FT   CHAIN           1..455
FT                   /note="UDP-glycosyltransferase 87A2"
FT                   /id="PRO_0000409134"
FT   BINDING         278
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250"
FT   BINDING         327..329
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250"
FT   BINDING         344..352
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250"
FT   BINDING         366..369
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0007744|PubMed:22223895"
FT   VAR_SEQ         166
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_041232"
SQ   SEQUENCE   455 AA;  51728 MW;  286B1D2B279A320D CRC64;
     MDPNESPPNQ FRHVVAMPYP GRGHINPMMN LCKRLVRRYP NLHVTFVVTE EWLGFIGPDP
     KPDRIHFSTL PNLIPSELVR AKDFIGFIDA VYTRLEEPFE KLLDSLNSPP PSVIFADTYV
     IWAVRVGRKR NIPVVSLWTM SATILSFFLH SDLLISHGHA LFEPSEEEVV DYVPGLSPTK
     LRDLPPIFDG YSDRVFKTAK LCFDELPGAR SLLFTTAYEL EHKAIDAFTS KLDIPVYAIG
     PLIPFEELSV QNDNKEPNYI QWLEEQPEGS VLYISQGSFL SVSEAQMEEI VKGLRESGVR
     FLWVARGGEL KLKEALEGSL GVVVSWCDQL RVLCHKAVGG FWTHCGFNST LEGIYSGVPM
     LAFPLFWDQI LNAKMIVEDW RVGMRIERTK KNELLIGREE IKEVVKRFMD RESEEGKEMR
     RRACDLSEIS RGAVAKSGSS NVNIDEFVRH ITNTN
 
 
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