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YUC2_ARATH
ID   YUC2_ARATH              Reviewed;         415 AA.
AC   Q9SVQ1;
DT   02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 150.
DE   RecName: Full=Indole-3-pyruvate monooxygenase YUCCA2;
DE            EC=1.14.13.168;
DE   AltName: Full=Flavin-containing monooxygenase YUCCA2;
GN   Name=YUC2; Synonyms=YUCCA2; OrderedLocusNames=At4g13260;
GN   ORFNames=F17N18.150;
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 [GENOMIC DNA].
RX   PubMed=11209081; DOI=10.1126/science.291.5502.306;
RA   Zhao Y., Christensen S.K., Fankhauser C., Cashman J.R., Cohen J.D.,
RA   Weigel D., Chory J.;
RT   "A role for flavin monooxygenase-like enzymes in auxin biosynthesis.";
RL   Science 291:306-309(2001).
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.
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   FUNCTION, TISSUE SPECIFICITY, GENE FAMILY, NOMENCLATURE, AND DISRUPTION
RP   PHENOTYPE.
RX   PubMed=16818609; DOI=10.1101/gad.1415106;
RA   Cheng Y., Dai X., Zhao Y.;
RT   "Auxin biosynthesis by the YUCCA flavin monooxygenases controls the
RT   formation of floral organs and vascular tissues in Arabidopsis.";
RL   Genes Dev. 20:1790-1799(2006).
RN   [6]
RP   GENE FAMILY.
RC   STRAIN=cv. Columbia;
RX   PubMed=17461789; DOI=10.1111/j.1365-313x.2007.03101.x;
RA   Hansen B.G., Kliebenstein D.J., Halkier B.A.;
RT   "Identification of a flavin-monooxygenase as the S-oxygenating enzyme in
RT   aliphatic glucosinolate biosynthesis in Arabidopsis.";
RL   Plant J. 50:902-910(2007).
RN   [7]
RP   INDUCTION BY SPL.
RX   PubMed=18557819; DOI=10.1111/j.1469-8137.2008.02514.x;
RA   Li L.C., Qin G.J., Tsuge T., Hou X.H., Ding M.Y., Aoyama T., Oka A.,
RA   Chen Z., Gu H., Zhao Y., Qu L.J.;
RT   "SPOROCYTELESS modulates YUCCA expression to regulate the development of
RT   lateral organs in Arabidopsis.";
RL   New Phytol. 179:751-764(2008).
RN   [8]
RP   TISSUE SPECIFICITY.
RX   PubMed=18628351; DOI=10.1105/tpc.107.057570;
RA   Cecchetti V., Altamura M.M., Falasca G., Costantino P., Cardarelli M.;
RT   "Auxin regulates Arabidopsis anther dehiscence, pollen maturation, and
RT   filament elongation.";
RL   Plant Cell 20:1760-1774(2008).
RN   [9]
RP   INDUCTION BY LEC2.
RX   PubMed=18287041; DOI=10.1073/pnas.0712364105;
RA   Stone S.L., Braybrook S.A., Paula S.L., Kwong L.W., Meuser J.,
RA   Pelletier J., Hsieh T.-F., Fischer R.L., Goldberg R.B., Harada J.J.;
RT   "Arabidopsis LEAFY COTYLEDON2 induces maturation traits and auxin activity:
RT   implications for somatic embryogenesis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:3151-3156(2008).
RN   [10]
RP   INDUCTION BY NGA3.
RX   PubMed=19435937; DOI=10.1105/tpc.109.065508;
RA   Trigueros M., Navarrete-Gomez M., Sato S., Christensen S.K., Pelaz S.,
RA   Weigel D., Yanofsky M.F., Ferrandiz C.;
RT   "The NGATHA genes direct style development in the Arabidopsis gynoecium.";
RL   Plant Cell 21:1394-1409(2009).
RN   [11]
RP   INDUCTION BY GLUCOSE.
RX   PubMed=19223973; DOI=10.1371/journal.pone.0004502;
RA   Mishra B.S., Singh M., Aggrawal P., Laxmi A.;
RT   "Glucose and auxin signaling interaction in controlling Arabidopsis
RT   thaliana seedlings root growth and development.";
RL   PLoS ONE 4:E4502-E4502(2009).
RN   [12]
RP   INDUCTION BY HEAT.
RX   PubMed=20421476; DOI=10.1073/pnas.1000869107;
RA   Sakata T., Oshino T., Miura S., Tomabechi M., Tsunaga Y., Higashitani N.,
RA   Miyazawa Y., Takahashi H., Watanabe M., Higashitani A.;
RT   "Auxins reverse plant male sterility caused by high temperatures.";
RL   Proc. Natl. Acad. Sci. U.S.A. 107:8569-8574(2010).
RN   [13]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=22025724; DOI=10.1073/pnas.1108434108;
RA   Mashiguchi K., Tanaka K., Sakai T., Sugawara S., Kawaide H., Natsume M.,
RA   Hanada A., Yaeno T., Shirasu K., Yao H., McSteen P., Zhao Y., Hayashi K.,
RA   Kamiya Y., Kasahara H.;
RT   "The main auxin biosynthesis pathway in Arabidopsis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:18512-18517(2011).
RN   [14]
RP   FUNCTION.
RX   PubMed=22025721; DOI=10.1073/pnas.1108436108;
RA   Won C., Shen X., Mashiguchi K., Zheng Z., Dai X., Cheng Y., Kasahara H.,
RA   Kamiya Y., Chory J., Zhao Y.;
RT   "Conversion of tryptophan to indole-3-acetic acid by TRYPTOPHAN
RT   AMINOTRANSFERASES OF ARABIDOPSIS and YUCCAs in Arabidopsis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:18518-18523(2011).
CC   -!- FUNCTION: Involved in auxin biosynthesis. Converts the indole-3-pyruvic
CC       acid (IPA) produced by the TAA family to indole-3-acetic acid (IAA).
CC       Unable to use tryptamine (TAM) as substrate. Required for the formation
CC       of floral organs and vascular tissues. Belongs to the set of redundant
CC       YUCCA genes probably responsible for auxin biosynthesis in shoots.
CC       {ECO:0000269|PubMed:16818609, ECO:0000269|PubMed:22025721,
CC       ECO:0000269|PubMed:22025724}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + indole-3-pyruvate + NADPH + O2 = (indol-3-yl)acetate +
CC         CO2 + H2O + NADP(+); Xref=Rhea:RHEA:34331, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:17640, ChEBI:CHEBI:30854, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349; EC=1.14.13.168;
CC         Evidence={ECO:0000269|PubMed:22025724};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC   -!- PATHWAY: Plant hormone metabolism; auxin biosynthesis.
CC   -!- INTERACTION:
CC       Q9SVQ1; Q9SK32: MAIL1; NbExp=4; IntAct=EBI-25510831, EBI-25510817;
CC   -!- TISSUE SPECIFICITY: Expressed in anthers and in the apical gynoecium.
CC       {ECO:0000269|PubMed:16818609, ECO:0000269|PubMed:18628351}.
CC   -!- INDUCTION: Up-regulated by glucose. Down-regulated by heat stress.
CC       Positively regulated by LEC2 and by NGA3. Negatively regulated by SPL.
CC       {ECO:0000269|PubMed:18287041, ECO:0000269|PubMed:18557819,
CC       ECO:0000269|PubMed:19223973, ECO:0000269|PubMed:19435937,
CC       ECO:0000269|PubMed:20421476}.
CC   -!- DISRUPTION PHENOTYPE: No visible phenotype, due to the redundancy with
CC       the other members of the YUCCA family. {ECO:0000269|PubMed:16818609}.
CC   -!- SIMILARITY: Belongs to the FMO family. {ECO:0000305}.
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DR   EMBL; AY057103; AAL23751.1; -; Genomic_DNA.
DR   EMBL; AL049751; CAB41936.1; -; Genomic_DNA.
DR   EMBL; AL161536; CAB78368.1; -; Genomic_DNA.
DR   EMBL; CP002687; AEE83256.1; -; Genomic_DNA.
DR   EMBL; AY133691; AAM91625.1; -; mRNA.
DR   PIR; T07706; T07706.
DR   RefSeq; NP_193062.1; NM_117399.4.
DR   AlphaFoldDB; Q9SVQ1; -.
DR   SMR; Q9SVQ1; -.
DR   BioGRID; 12253; 1.
DR   IntAct; Q9SVQ1; 1.
DR   STRING; 3702.AT4G13260.1; -.
DR   PaxDb; Q9SVQ1; -.
DR   PRIDE; Q9SVQ1; -.
DR   EnsemblPlants; AT4G13260.1; AT4G13260.1; AT4G13260.
DR   GeneID; 826956; -.
DR   Gramene; AT4G13260.1; AT4G13260.1; AT4G13260.
DR   KEGG; ath:AT4G13260; -.
DR   Araport; AT4G13260; -.
DR   TAIR; locus:2119340; AT4G13260.
DR   eggNOG; KOG1399; Eukaryota.
DR   HOGENOM; CLU_006909_2_0_1; -.
DR   InParanoid; Q9SVQ1; -.
DR   OMA; CELILMP; -.
DR   OrthoDB; 630383at2759; -.
DR   PhylomeDB; Q9SVQ1; -.
DR   BioCyc; ARA:AT4G13260-MON; -.
DR   BioCyc; MetaCyc:AT4G13260-MON; -.
DR   BRENDA; 1.14.13.168; 399.
DR   UniPathway; UPA00151; -.
DR   PRO; PR:Q9SVQ1; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; Q9SVQ1; baseline and differential.
DR   Genevisible; Q9SVQ1; AT.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IBA:GO_Central.
DR   GO; GO:0103075; F:indole-3-pyruvate monooxygenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004497; F:monooxygenase activity; IBA:GO_Central.
DR   GO; GO:0004499; F:N,N-dimethylaniline monooxygenase activity; IEA:InterPro.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   GO; GO:0009851; P:auxin biosynthetic process; IMP:TAIR.
DR   GO; GO:0009723; P:response to ethylene; IEP:TAIR.
DR   Gene3D; 3.50.50.60; -; 1.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR020946; Flavin_mOase-like.
DR   Pfam; PF00743; FMO-like; 1.
DR   SUPFAM; SSF51905; SSF51905; 2.
PE   1: Evidence at protein level;
KW   Auxin biosynthesis; FAD; Flavoprotein; Monooxygenase; NADP; Oxidoreductase;
KW   Reference proteome.
FT   CHAIN           1..415
FT                   /note="Indole-3-pyruvate monooxygenase YUCCA2"
FT                   /id="PRO_0000400069"
FT   BINDING         32..37
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255"
FT   BINDING         200..205
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   415 AA;  46543 MW;  1C9D5F6FF8FECCAC CRC64;
     MEFVTETLGK RIHDPYVEET RCLMIPGPII VGSGPSGLAT AACLKSRDIP SLILERSTCI
     ASLWQHKTYD RLRLHLPKDF CELPLMPFPS SYPTYPTKQQ FVQYLESYAE HFDLKPVFNQ
     TVEEAKFDRR CGLWRVRTTG GKKDETMEYV SRWLVVATGE NAEEVMPEID GIPDFGGPIL
     HTSSYKSGEI FSEKKILVVG CGNSGMEVCL DLCNFNALPS LVVRDSVHVL PQEMLGISTF
     GISTSLLKWF PVHVVDRFLL RMSRLVLGDT DRLGLVRPKL GPLERKIKCG KTPVLDVGTL
     AKIRSGHIKV YPELKRVMHY SAEFVDGRVD NFDAIILATG YKSNVPMWLK GVNMFSEKDG
     FPHKPFPNGW KGESGLYAVG FTKLGLLGAA IDAKKIAEDI EVQRHFLPLA RPQHC
 
 
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