C701S_ORYSJ
ID C701S_ORYSJ Reviewed; 504 AA.
AC Q5Z5R7; A0A0P0WY89; Q68YV7;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Ent-kaurene oxidase-like 3 {ECO:0000303|PubMed:15316288};
DE Short=OsKOL3 {ECO:0000303|PubMed:15316288};
DE EC=1.14.13.- {ECO:0000305};
DE AltName: Full=Cytochrome P450 701A19 {ECO:0000305};
DE AltName: Full=Ent-kaurene oxidase 1 {ECO:0000303|PubMed:15075394};
DE Short=OsKO1 {ECO:0000303|PubMed:15075394};
DE AltName: Full=OsKOS4 {ECO:0000303|PubMed:16299167};
GN Name=CYP701A19 {ECO:0000305};
GN OrderedLocusNames=Os06g0569900 {ECO:0000312|EMBL:BAF19821.1},
GN LOC_Os06g37330 {ECO:0000305};
GN ORFNames=OSJNBa0062E01.34 {ECO:0000312|EMBL:BAD54595.1};
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].
RC STRAIN=cv. Xiushui 11;
RX PubMed=16299167; DOI=10.1104/pp.105.072306;
RA Zhu S., Gao F., Cao X., Chen M., Ye G., Wei C., Li Y.;
RT "The rice dwarf virus P2 protein interacts with ent-kaurene oxidases in
RT vivo, leading to reduced biosynthesis of gibberellins and rice dwarf
RT symptoms.";
RL Plant Physiol. 139:1935-1945(2005).
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].
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 TISSUE SPECIFICITY.
RX PubMed=15316288; DOI=10.1023/b:plan.0000038261.21060.47;
RA Itoh H., Tatsumi T., Sakamoto T., Otomo K., Toyomasu T., Kitano H.,
RA Ashikari M., Ichihara S., Matsuoka M.;
RT "A rice semi-dwarf gene, Tan-Ginbozu (D35), encodes the gibberellin
RT biosynthesis enzyme, ent-kaurene oxidase.";
RL Plant Mol. Biol. 54:533-547(2004).
RN [7]
RP GENE FAMILY.
RX PubMed=15075394; DOI=10.1104/pp.103.033696;
RA Sakamoto T., Miura K., Itoh H., Tatsumi T., Ueguchi-Tanaka M., Ishiyama K.,
RA Kobayashi M., Agrawal G.K., Takeda S., Abe K., Miyao A., Hirochika H.,
RA Kitano H., Ashikari M., Matsuoka M.;
RT "An overview of gibberellin metabolism enzyme genes and their related
RT mutants in rice.";
RL Plant Physiol. 134:1642-1653(2004).
CC -!- FUNCTION: May hydroxylate diterpenes. {ECO:0000305}.
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:P04798};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in leaf blades.
CC {ECO:0000269|PubMed:15316288}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family.
CC {ECO:0000255|RuleBase:RU000461}.
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DR EMBL; AY660666; AAT91065.1; -; mRNA.
DR EMBL; AP005471; BAD54595.1; -; Genomic_DNA.
DR EMBL; AP008212; BAF19821.1; -; Genomic_DNA.
DR EMBL; AP014962; BAS98308.1; -; Genomic_DNA.
DR EMBL; AK100964; BAG94854.1; -; mRNA.
DR RefSeq; XP_015643249.1; XM_015787763.1.
DR AlphaFoldDB; Q5Z5R7; -.
DR SMR; Q5Z5R7; -.
DR STRING; 4530.OS06T0569900-01; -.
DR PaxDb; Q5Z5R7; -.
DR PRIDE; Q5Z5R7; -.
DR EnsemblPlants; Os06t0569900-01; Os06t0569900-01; Os06g0569900.
DR GeneID; 112936021; -.
DR Gramene; Os06t0569900-01; Os06t0569900-01; Os06g0569900.
DR eggNOG; KOG0156; Eukaryota.
DR HOGENOM; CLU_001570_4_0_1; -.
DR InParanoid; Q5Z5R7; -.
DR OMA; FAGGRFK; -.
DR OrthoDB; 702827at2759; -.
DR BRENDA; 1.14.14.86; 8948.
DR PlantReactome; R-OSA-1119557; GA12 biosynthesis.
DR Proteomes; UP000000763; Chromosome 6.
DR Proteomes; UP000059680; Chromosome 6.
DR Genevisible; Q5Z5R7; OS.
DR GO; GO:0009707; C:chloroplast outer membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0052615; F:ent-kaurene oxidase activity; IEA:InterPro.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0016709; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen; IBA:GO_Central.
DR GO; GO:0010241; P:ent-kaurene oxidation to kaurenoic acid; IBA:GO_Central.
DR GO; GO:0009686; P:gibberellin biosynthetic process; IBA:GO_Central.
DR Gene3D; 1.10.630.10; -; 1.
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 InterPro; IPR044225; KO_chloroplastic.
DR PANTHER; PTHR47283; PTHR47283; 1.
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 2: Evidence at transcript level;
KW Heme; Iron; Membrane; Metal-binding; Monooxygenase; Oxidoreductase;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..504
FT /note="Ent-kaurene oxidase-like 3"
FT /id="PRO_0000430734"
FT TRANSMEM 3..23
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 448
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 CONFLICT 35
FT /note="N -> Y (in Ref. 1; AAT91065)"
FT CONFLICT 66
FT /note="K -> R (in Ref. 1; AAT91065)"
FT CONFLICT 187
FT /note="D -> N (in Ref. 1; AAT91065)"
FT CONFLICT 467
FT /note="Q -> R (in Ref. 1; AAT91065)"
FT CONFLICT 500
FT /note="P -> R (in Ref. 1; AAT91065)"
SQ SEQUENCE 504 AA; 56831 MW; A0B787647B7ECC29 CRC64;
MESLLAAGAG GIGVAAAAVG GFIAAATLAV APPKNRRNPP PAVPGLPIIG NLHQLKEKKP
HQTFTKWAEI YGPIYTIRTG ASSVVVLNST EVAKEAMVAK FSSISTRKLS KALTVLSHDK
SMVATSDSGD FHKMGKRYIM LSMLGTSAQK QFRDTRDMII NNMLSTFHQL VKDDPHAPLI
FRDVFKDELF RLSMIQSLGE DVSSVYVDEF GRDISKEEIY NATVTDMMMC AIEVDWRDFF
PYLSWVPNKS FETRVFTTES RRTAVMRALI KQQKERIVRG EARTCYLDFL LAENTLTDEQ
LMMLVWEALI EAADTTLVTT EWAMYELAKN PDKQERLYQE IREVCGDEAV TEEHLPWLPY
LNAVFQETLR RHSPVPLIPP RFVNEDTMLA GYDVPAGTEM VINLYGCNMN KKEWESPEEW
APERFAGGRF KVADMYKTMA FGAGRRVCAG SLQATHIACA AIARFVQEFG WRLREGDEEK
VDTVQLTAYK LHPLHVHLTP RGRM
