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YUC1_ORYSJ
ID   YUC1_ORYSJ              Reviewed;         406 AA.
AC   A0A0P0V5U9; C7IW71; Q5VRB9;
DT   10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT   20-JAN-2016, sequence version 1.
DT   03-AUG-2022, entry version 38.
DE   RecName: Full=Indole-3-pyruvate monooxygenase YUCCA1 {ECO:0000305};
DE            Short=OsYUCCA1 {ECO:0000303|PubMed:17220367, ECO:0000303|PubMed:29740464};
DE            EC=1.14.13.168 {ECO:0000305|PubMed:17220367};
DE   AltName: Full=Flavin-containing monooxygenase YUCCA1 {ECO:0000305};
GN   Name=YUCCA1 {ECO:0000303|PubMed:17220367, ECO:0000303|PubMed:29740464};
GN   OrderedLocusNames=Os01g0645400 {ECO:0000312|EMBL:BAS73400.1},
GN   LOC_Os01g45760 {ECO:0000305};
GN   ORFNames=P0707D10.26 {ECO:0000312|EMBL:BAD68007.1};
OS   Oryza sativa subsp. japonica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=12447438; DOI=10.1038/nature01184;
RA   Sasaki T., Matsumoto T., Yamamoto K., Sakata K., Baba T., Katayose Y.,
RA   Wu J., Niimura Y., Cheng Z., Nagamura Y., Antonio B.A., Kanamori H.,
RA   Hosokawa S., Masukawa M., Arikawa K., Chiden Y., Hayashi M., Okamoto M.,
RA   Ando T., Aoki H., Arita K., Hamada M., Harada C., Hijishita S., Honda M.,
RA   Ichikawa Y., Idonuma A., Iijima M., Ikeda M., Ikeno M., Ito S., Ito T.,
RA   Ito Y., Ito Y., Iwabuchi A., Kamiya K., Karasawa W., Katagiri S.,
RA   Kikuta A., Kobayashi N., Kono I., Machita K., Maehara T., Mizuno H.,
RA   Mizubayashi T., Mukai Y., Nagasaki H., Nakashima M., Nakama Y.,
RA   Nakamichi Y., Nakamura M., Namiki N., Negishi M., Ohta I., Ono N., Saji S.,
RA   Sakai K., Shibata M., Shimokawa T., Shomura A., Song J., Takazaki Y.,
RA   Terasawa K., Tsuji K., Waki K., Yamagata H., Yamane H., Yoshiki S.,
RA   Yoshihara R., Yukawa K., Zhong H., Iwama H., Endo T., Ito H., Hahn J.H.,
RA   Kim H.-I., Eun M.-Y., Yano M., Jiang J., Gojobori T.;
RT   "The genome sequence and structure of rice chromosome 1.";
RL   Nature 420:312-316(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16100779; DOI=10.1038/nature03895;
RG   International rice genome sequencing project (IRGSP);
RT   "The map-based sequence of the rice genome.";
RL   Nature 436:793-800(2005).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=18089549; DOI=10.1093/nar/gkm978;
RG   The rice annotation project (RAP);
RT   "The rice annotation project database (RAP-DB): 2008 update.";
RL   Nucleic Acids Res. 36:D1028-D1033(2008).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA   Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA   Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA   Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA   Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT   "Improvement of the Oryza sativa Nipponbare reference genome using next
RT   generation sequence and optical map data.";
RL   Rice 6:4-4(2013).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=cv. Nipponbare;
RX   PubMed=12869764; DOI=10.1126/science.1081288;
RG   The rice full-length cDNA consortium;
RT   "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT   japonica rice.";
RL   Science 301:376-379(2003).
RN   [6]
RP   FUNCTION, CATALYTIC ACTIVITY, AND TISSUE SPECIFICITY.
RX   PubMed=17220367; DOI=10.1104/pp.106.091561;
RA   Yamamoto Y., Kamiya N., Morinaka Y., Matsuoka M., Sazuka T.;
RT   "Auxin biosynthesis by the YUCCA genes in rice.";
RL   Plant Physiol. 143:1362-1371(2007).
RN   [7]
RP   FUNCTION.
RX   PubMed=29740464; DOI=10.3389/fpls.2018.00523;
RA   Zhang T., Li R., Xing J., Yan L., Wang R., Zhao Y.;
RT   "The YUCCA-auxin-WOX11 module controls crown root development in rice.";
RL   Front. Plant Sci. 9:523-523(2018).
CC   -!- FUNCTION: Involved in auxin biosynthesis (PubMed:17220367,
CC       PubMed:29740464). Converts the indole-3-pyruvic acid (IPA) produced by
CC       the TAA family to indole-3-acetic acid (IAA) (Probable). Functions
CC       downstream of TAR2 in auxin biosynthesis (PubMed:29740464). Functions
CC       upstream of WOX11, a transcription factor that promotes the development
CC       of crown roots (PubMed:29740464). {ECO:0000269|PubMed:17220367,
CC       ECO:0000269|PubMed:29740464, ECO:0000305|PubMed:17220367}.
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:0000305|PubMed:17220367};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000305};
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=A0A0P0V5U9-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=A0A0P0V5U9-2; Sequence=VSP_059850;
CC   -!- TISSUE SPECIFICITY: Expressed in coleoptile tips, root tips, leaf blade
CC       tips, shoot apical meristem, vasculature of stems and flowers.
CC       {ECO:0000269|PubMed:17220367}.
CC   -!- MISCELLANEOUS: Calli overexpressing YUCCA1 exhibit high levels of
CC       auxin, low regeneration frequency, overgrowing roots, and abnormal root
CC       morphology (PubMed:17220367, PubMed:29740464). Plants silencing YUCCA1
CC       exhibit severe dwarfism, inhibition of shoot elongation and root
CC       formation and elongation (PubMed:17220367).
CC       {ECO:0000269|PubMed:17220367, ECO:0000269|PubMed:29740464}.
CC   -!- SIMILARITY: Belongs to the FMO family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAH91211.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AP002910; BAD68007.1; -; Genomic_DNA.
DR   EMBL; AP008207; BAH91211.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AP014957; BAS73400.1; -; Genomic_DNA.
DR   EMBL; AP014957; BAS73401.1; -; Genomic_DNA.
DR   EMBL; AK105488; BAG97267.1; -; mRNA.
DR   RefSeq; XP_015643006.1; XM_015787520.1. [A0A0P0V5U9-1]
DR   AlphaFoldDB; A0A0P0V5U9; -.
DR   SMR; A0A0P0V5U9; -.
DR   STRING; 4530.OS01T0645400-02; -.
DR   PaxDb; A0A0P0V5U9; -.
DR   EnsemblPlants; Os01t0645400-01; Os01t0645400-01; Os01g0645400. [A0A0P0V5U9-2]
DR   EnsemblPlants; Os01t0645400-02; Os01t0645400-02; Os01g0645400. [A0A0P0V5U9-1]
DR   GeneID; 9269185; -.
DR   Gramene; Os01t0645400-01; Os01t0645400-01; Os01g0645400. [A0A0P0V5U9-2]
DR   Gramene; Os01t0645400-02; Os01t0645400-02; Os01g0645400. [A0A0P0V5U9-1]
DR   KEGG; osa:9269185; -.
DR   eggNOG; KOG1399; Eukaryota.
DR   HOGENOM; CLU_006909_2_0_1; -.
DR   OMA; TWRHRTY; -.
DR   OrthoDB; 405736at2759; -.
DR   PlantReactome; R-OSA-1119486; IAA biosynthesis I.
DR   Proteomes; UP000000763; Chromosome 1.
DR   Proteomes; UP000059680; Chromosome 1.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IBA:GO_Central.
DR   GO; GO:0103075; F:indole-3-pyruvate monooxygenase activity; IDA:UniProtKB.
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; IDA:UniProtKB.
DR   GO; GO:2000280; P:regulation of root development; IDA:UniProtKB.
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; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; FAD; Flavoprotein; Monooxygenase; NADP;
KW   Oxidoreductase; Reference proteome.
FT   CHAIN           1..406
FT                   /note="Indole-3-pyruvate monooxygenase YUCCA1"
FT                   /id="PRO_0000445279"
FT   BINDING         21..26
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255"
FT   BINDING         184..189
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         335..406
FT                   /note="DAGDLFTREGISKVPFPNSWRGRNGLYTVGFTQRGLLGTSSDALNVAKDIHC
FT                   QWRERDRSAINVLEISNSSF -> VKQSVTHSCSFYFSFCPHCTILLLVIYISR (in
FT                   isoform 2)"
FT                   /id="VSP_059850"
SQ   SEQUENCE   406 AA;  44388 MW;  432622B7DA6F4F1C CRC64;
     MDNKPAQERR ETWVPGAVIV GAGPSGLAAA ACLAARGVPA TVLERSDSLA STWRHRMYDR
     LALHLPKRFC ELPLLPFPEE YPTYPSKDQF VAYMEAYAAA AGVAPRFGAT VEEAAFDAAV
     GAWRVRLDGG EVLMARWLVV ATGENAEPRV PDFPGMQKFA GCAMHTSEYK SGEQFAGKKV
     LVVGCGNSGM EVSLDLCRHG AKPSMVVRNT VHVLPREMFG LSTFGIAMAL LRWLPVQLVD
     RFLLTAAHLI LGNTGQFGLR RPKTGPIELK NLTGRTPVLD VGTLDHIKSG KIKVVGAVKE
     MTRQGVRFTD GKEEQFDTII LATGYRSNVP SWLKDAGDLF TREGISKVPF PNSWRGRNGL
     YTVGFTQRGL LGTSSDALNV AKDIHCQWRE RDRSAINVLE ISNSSF
 
 
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