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C724B_ORYSJ
ID   C724B_ORYSJ             Reviewed;         480 AA.
AC   Q6F4F5; Q01JN4; Q0JCH6; Q7XJU4;
DT   05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=Cytochrome P450 724B1 {ECO:0000303|PubMed:15705958};
DE            Short=OsCYP724B1 {ECO:0000303|PubMed:15705958};
DE   AltName: Full=(22S)-22-hydroxycampesterol synthase {ECO:0000303|PubMed:16369540};
DE            EC=1.14.14.- {ECO:0000269|PubMed:16369540};
DE   AltName: Full=Dwarf protein 11 {ECO:0000303|PubMed:15705958};
DE            Short=OsDWARF11 {ECO:0000303|PubMed:15705958};
GN   Name=CYP724B1 {ECO:0000303|PubMed:15705958};
GN   Synonyms=D11 {ECO:0000303|PubMed:15705958};
GN   OrderedLocusNames=Os04g0469800 {ECO:0000305}, LOC_Os04g39430 {ECO:0000305};
GN   ORFNames=OSIGBa0124N08.3 {ECO:0000312|EMBL:CAH67041.1},
GN   OsJ_15129 {ECO:0000312|EMBL:EEE61161.1},
GN   OSJNBa0016O02.25 {ECO:0000312|EMBL:CAE06016.1};
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 [MRNA], FUNCTION, TISSUE SPECIFICITY, INDUCTION,
RP   MUTAGENESIS OF THR-292, AND DISRUPTION PHENOTYPE.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=15705958; DOI=10.1105/tpc.104.024950;
RA   Tanabe S., Ashikari M., Fujioka S., Takatsuto S., Yoshida S., Yano M.,
RA   Yoshimura A., Kitano H., Matsuoka M., Fujisawa Y., Kato H., Iwasaki Y.;
RT   "A novel cytochrome p450 is implicated in brassinosteroid biosynthesis via
RT   the characterization of a rice dwarf mutant, dwarf11, with reduced seed
RT   length.";
RL   Plant Cell 17:776-790(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=12447439; DOI=10.1038/nature01183;
RA   Feng Q., Zhang Y., Hao P., Wang S., Fu G., Huang Y., Li Y., Zhu J., Liu Y.,
RA   Hu X., Jia P., Zhang Y., Zhao Q., Ying K., Yu S., Tang Y., Weng Q.,
RA   Zhang L., Lu Y., Mu J., Lu Y., Zhang L.S., Yu Z., Fan D., Liu X., Lu T.,
RA   Li C., Wu Y., Sun T., Lei H., Li T., Hu H., Guan J., Wu M., Zhang R.,
RA   Zhou B., Chen Z., Chen L., Jin Z., Wang R., Yin H., Cai Z., Ren S., Lv G.,
RA   Gu W., Zhu G., Tu Y., Jia J., Zhang Y., Chen J., Kang H., Chen X., Shao C.,
RA   Sun Y., Hu Q., Zhang X., Zhang W., Wang L., Ding C., Sheng H., Gu J.,
RA   Chen S., Ni L., Zhu F., Chen W., Lan L., Lai Y., Cheng Z., Gu M., Jiang J.,
RA   Li J., Hong G., Xue Y., Han B.;
RT   "Sequence and analysis of rice chromosome 4.";
RL   Nature 420:316-320(2002).
RN   [3]
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   [4]
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   [5]
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   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA   Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA   Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA   Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA   Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA   Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA   Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA   Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA   Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA   Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA   Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA   Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA   Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA   Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA   McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT   "The genomes of Oryza sativa: a history of duplications.";
RL   PLoS Biol. 3:266-281(2005).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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   [8]
RP   FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16369540; DOI=10.1038/nbt1173;
RA   Sakamoto T., Morinaka Y., Ohnishi T., Sunohara H., Fujioka S.,
RA   Ueguchi-Tanaka M., Mizutani M., Sakata K., Takatsuto S., Yoshida S.,
RA   Tanaka H., Kitano H., Matsuoka M.;
RT   "Erect leaves caused by brassinosteroid deficiency increase biomass
RT   production and grain yield in rice.";
RL   Nat. Biotechnol. 24:105-109(2006).
CC   -!- FUNCTION: Involved in brassinosteroid biosynthesis (PubMed:15705958,
CC       PubMed:16369540). May catalyze a C6-oxidation step and may be involved
CC       to supply 6-deoxotyphasterol and typhasterol (PubMed:15705958).
CC       Involved in internode elongation and seed development
CC       (PubMed:15705958). Catalyzes the conversion of campesterol (CR) to
CC       (22S)-22-hydroxycampesterol (22-OHCR, 22-hydroxyCR) (PubMed:16369540).
CC       {ECO:0000269|PubMed:15705958, ECO:0000269|PubMed:16369540}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=campesterol + O2 + reduced [NADPH--hemoprotein reductase] =
CC         (22S)-22-hydroxycampesterol + H(+) + H2O + oxidized [NADPH--
CC         hemoprotein reductase]; Xref=Rhea:RHEA:69835, Rhea:RHEA-COMP:11964,
CC         Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:28623, ChEBI:CHEBI:57618,
CC         ChEBI:CHEBI:58210, ChEBI:CHEBI:72331;
CC         Evidence={ECO:0000269|PubMed:16369540};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69836;
CC         Evidence={ECO:0000269|PubMed:16369540};
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000250|UniProtKB:P04798};
CC   -!- PATHWAY: Plant hormone biosynthesis; brassinosteroid biosynthesis.
CC       {ECO:0000269|PubMed:16369540}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC       protein {ECO:0000255}.
CC   -!- TISSUE SPECIFICITY: Ubiquitously expressed at low levels, but
CC       preferentially in the internodes and the florets before flowering.
CC       {ECO:0000269|PubMed:15705958}.
CC   -!- INDUCTION: Down-regulated by brassinolide in wild-type and the dwarf11
CC       mutant. {ECO:0000269|PubMed:15705958}.
CC   -!- DISRUPTION PHENOTYPE: The dwarf11 (d11) mutant shows the erection of
CC       leaves in mature stages, the shortening of the grain length and of the
CC       second internode in culm, and aberrant skotomorphogenesis. Treatment
CC       with exogenous brassinolide rescues the abnormal phenotype.
CC       {ECO:0000269|PubMed:15705958}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAE06016.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AB158759; BAD27424.1; -; mRNA.
DR   EMBL; AL606588; CAE06016.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CR855166; CAH67041.1; -; Genomic_DNA.
DR   EMBL; AP008210; BAF14961.1; -; Genomic_DNA.
DR   EMBL; AP014960; BAS89632.1; -; Genomic_DNA.
DR   EMBL; CM000141; EEE61161.1; -; Genomic_DNA.
DR   EMBL; AK106528; BAG97751.1; -; mRNA.
DR   EMBL; AK119772; BAG99780.1; -; mRNA.
DR   RefSeq; XP_015635418.1; XM_015779932.1.
DR   AlphaFoldDB; Q6F4F5; -.
DR   SMR; Q6F4F5; -.
DR   STRING; 4530.OS04T0469800-01; -.
DR   PaxDb; Q6F4F5; -.
DR   PRIDE; Q6F4F5; -.
DR   EnsemblPlants; Os04t0469800-01; Os04t0469800-01; Os04g0469800.
DR   GeneID; 4336116; -.
DR   Gramene; Os04t0469800-01; Os04t0469800-01; Os04g0469800.
DR   KEGG; osa:4336116; -.
DR   eggNOG; KOG0157; Eukaryota.
DR   HOGENOM; CLU_001570_15_5_1; -.
DR   InParanoid; Q6F4F5; -.
DR   OMA; PWRWETQ; -.
DR   OrthoDB; 871849at2759; -.
DR   UniPathway; UPA00381; -.
DR   Proteomes; UP000000763; Chromosome 4.
DR   Proteomes; UP000007752; Chromosome 4.
DR   Proteomes; UP000059680; Chromosome 4.
DR   ExpressionAtlas; Q6F4F5; baseline and differential.
DR   Genevisible; Q6F4F5; OS.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008199; F:ferric iron binding; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0004497; F:monooxygenase activity; IBA:GO_Central.
DR   GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR   GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR   GO; GO:0016132; P:brassinosteroid biosynthetic process; IMP:Gramene.
DR   GO; GO:0010268; P:brassinosteroid homeostasis; IBA:GO_Central.
DR   GO; GO:0006879; P:cellular iron ion homeostasis; IEA:InterPro.
DR   GO; GO:0006826; P:iron ion transport; IEA:InterPro.
DR   GO; GO:0009647; P:skotomorphogenesis; IMP:Gramene.
DR   GO; GO:0016125; P:sterol metabolic process; IBA:GO_Central.
DR   Gene3D; 1.10.630.10; -; 1.
DR   InterPro; IPR002024; Bacterioferritin.
DR   InterPro; IPR001128; Cyt_P450.
DR   InterPro; IPR017972; Cyt_P450_CS.
DR   InterPro; IPR002401; Cyt_P450_E_grp-I.
DR   InterPro; IPR036396; Cyt_P450_sf.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00463; EP450I.
DR   PRINTS; PR00385; P450.
DR   SUPFAM; SSF48264; SSF48264; 1.
DR   PROSITE; PS00086; CYTOCHROME_P450; 1.
PE   1: Evidence at protein level;
KW   Brassinosteroid biosynthesis; Heme; Iron; Lipid biosynthesis;
KW   Lipid metabolism; Membrane; Metal-binding; Monooxygenase; Oxidoreductase;
KW   Reference proteome; Steroid biosynthesis; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..480
FT                   /note="Cytochrome P450 724B1"
FT                   /id="PRO_0000052201"
FT   TRANSMEM        6..26
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         426
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250|UniProtKB:P04798"
FT   MUTAGEN         292
FT                   /note="T->I: In d11-3; dwarf and reduced seed length."
FT                   /evidence="ECO:0000269|PubMed:15705958"
SQ   SEQUENCE   480 AA;  53704 MW;  AD7FA92538822CC3 CRC64;
     MVGGELVLAA LVILLALLLT LVLSHFLPLL LNPKAPKGSF GWPLLGETLR FLSPHASNTL
     GSFLEDHCSR YGRVFKSHLF CTPTIVSCDQ ELNHFILQNE ERLFQCSYPR PIHGILGKSS
     MLVVLGEDHK RLRNLALALV TSTKLKPSYL GDIEKIALHI VGSWHGKSKD KGMVNVIAFC
     EEARKFAFSV IVKQVLGLSP EEPVTAMILE DFLAFMKGLI SFPLYIPGTP YAKAVQARAR
     ISSTVKGIIE ERRNAGSSNK GDFLDVLLSS NELSDEEKVS FVLDSLLGGY ETTSLLISMV
     VYFLGQSAQD LELVKREHEG IRSKKEKDEF LSSEDYKKME YTQHVINEAL RCGNIVKFVH
     RKALKDVRYK EYLIPSGWKV LPVFSAVHLN PLLHGNAQQF QPCRWEGASQ GTSKKFTPFG
     GGPRLCPGSE LAKVEAAFFL HHLVLNYRWR IDGDDIPMAY PYVEFQRGLP IEIEPLCSES
 
 
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