C90B2_ORYSJ
ID C90B2_ORYSJ Reviewed; 506 AA.
AC Q5CCK3; Q8H848;
DT 15-FEB-2017, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Cytochrome P450 90B2 {ECO:0000305};
DE Short=OsCYP90B2 {ECO:0000305};
DE EC=1.14.13.- {ECO:0000269|PubMed:16369540};
DE AltName: Full=(22S)-22-hydroxycampesterol synthase {ECO:0000303|PubMed:16369540};
DE EC=1.14.14.- {ECO:0000269|PubMed:16369540};
DE AltName: Full=6-deoxycathasterone synthase {ECO:0000303|PubMed:16369540};
DE EC=1.14.14.- {ECO:0000269|PubMed:16369540};
DE AltName: Full=Protein DWARF4 homolog {ECO:0000303|PubMed:16369540};
DE Short=OsDWARF4 {ECO:0000303|PubMed:16369540, ECO:0000303|PubMed:19605414};
DE AltName: Full=Steroid 22-alpha-hydroxylase {ECO:0000305};
GN Name=CYP90B2 {ECO:0000303|PubMed:16369540};
GN Synonyms=CYP90B1 {ECO:0000303|PubMed:19605414},
GN DWARF4 {ECO:0000303|PubMed:16369540, ECO:0000303|PubMed:19605414};
GN OrderedLocusNames=Os03g0227700 {ECO:0000312|EMBL:BAF11361.2},
GN LOC_Os03g12660 {ECO:0000312|EMBL:ABF94760.1};
GN ORFNames=OJ1626B05.9 {ECO:0000312|EMBL:AAN60994.1};
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, CATALYTIC ACTIVITY, PATHWAY, TISSUE
RP SPECIFICITY, INDUCTION, BIOTECHNOLOGY, AND DISRUPTION PHENOTYPE.
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16109971; DOI=10.1101/gr.3869505;
RG The rice chromosome 3 sequencing consortium;
RA Buell C.R., Yuan Q., Ouyang S., Liu J., Zhu W., Wang A., Maiti R., Haas B.,
RA Wortman J., Pertea M., Jones K.M., Kim M., Overton L., Tsitrin T.,
RA Fadrosh D., Bera J., Weaver B., Jin S., Johri S., Reardon M., Webb K.,
RA Hill J., Moffat K., Tallon L., Van Aken S., Lewis M., Utterback T.,
RA Feldblyum T., Zismann V., Iobst S., Hsiao J., de Vazeille A.R.,
RA Salzberg S.L., White O., Fraser C.M., Yu Y., Kim H., Rambo T., Currie J.,
RA Collura K., Kernodle-Thompson S., Wei F., Kudrna K., Ammiraju J.S.S.,
RA Luo M., Goicoechea J.L., Wing R.A., Henry D., Oates R., Palmer M.,
RA Pries G., Saski C., Simmons J., Soderlund C., Nelson W., de la Bastide M.,
RA Spiegel L., Nascimento L., Huang E., Preston R., Zutavern T., Palmer L.,
RA O'Shaughnessy A., Dike S., McCombie W.R., Minx P., Cordum H., Wilson R.,
RA Jin W., Lee H.R., Jiang J., Jackson S.;
RT "Sequence, annotation, and analysis of synteny between rice chromosome 3
RT and diverged grass species.";
RL Genome Res. 15:1284-1291(2005).
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 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 [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19605414; DOI=10.1093/pcp/pcp106;
RA Nakamura A., Fujioka S., Takatsuto S., Tsujimoto M., Kitano H., Yoshida S.,
RA Asami T., Nakano T.;
RT "Involvement of C-22-hydroxylated brassinosteroids in auxin-induced lamina
RT joint bending in rice.";
RL Plant Cell Physiol. 50:1627-1635(2009).
CC -!- FUNCTION: Catalyzes the C22-alpha-hydroxylation step in brassinosteroid
CC biosynthesis, which is the rate-limiting step in this biosynthetic
CC pathway (PubMed:16369540). Catalyzes the conversion of campesterol (CR)
CC to (22S)-22-hydroxycampesterol (22-OHCR, 22-hydroxyCR) and of
CC campestanol (CN) to 6-deoxycathasterone (6-deoxoCT) (PubMed:16369540).
CC Required for auxin responses involved in the regulation of epidermal
CC cells length of the lamina joint (PubMed:19605414).
CC {ECO:0000269|PubMed:16369540, ECO:0000269|PubMed:19605414}.
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 -!- CATALYTIC ACTIVITY:
CC Reaction=campestanol + O2 + reduced [NADPH--hemoprotein reductase] = 6-
CC deoxycathasterone + H(+) + H2O + oxidized [NADPH--hemoprotein
CC reductase]; Xref=Rhea:RHEA:69831, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:20714, ChEBI:CHEBI:36799, ChEBI:CHEBI:57618,
CC ChEBI:CHEBI:58210; Evidence={ECO:0000269|PubMed:16369540};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69832;
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: Highly expressed in roots and leaf blades.
CC Expressed in shoot apex, stems, leaf sheaths, inflorescences and
CC flowers. {ECO:0000269|PubMed:16369540}.
CC -!- INDUCTION: Down-regulated by brassinolide (BL).
CC {ECO:0000269|PubMed:16369540}.
CC -!- DISRUPTION PHENOTYPE: Slight dwarf phenotype and erect leaves
CC (PubMed:16369540). Impaired response to auxin leading to reduced
CC epidermal cells length of the lamina joint (PubMed:19605414).
CC {ECO:0000269|PubMed:16369540, ECO:0000269|PubMed:19605414}.
CC -!- BIOTECHNOLOGY: Null mutant plants for CYP90B1/DWARF4 produce increased
CC biomass and grain yield at high density planting.
CC {ECO:0000269|PubMed:16369540}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAN60994.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB206579; BAD90972.1; -; mRNA.
DR EMBL; AC104473; AAN60994.1; ALT_INIT; Genomic_DNA.
DR EMBL; DP000009; ABF94760.1; -; Genomic_DNA.
DR EMBL; AP008209; BAF11361.2; -; Genomic_DNA.
DR EMBL; AP014959; BAS83075.1; -; Genomic_DNA.
DR EMBL; AK243298; BAH01529.1; -; mRNA.
DR RefSeq; XP_015633105.1; XM_015777619.1.
DR AlphaFoldDB; Q5CCK3; -.
DR SMR; Q5CCK3; -.
DR STRING; 4530.OS03T0227700-01; -.
DR PaxDb; Q5CCK3; -.
DR PRIDE; Q5CCK3; -.
DR EnsemblPlants; Os03t0227700-01; Os03t0227700-01; Os03g0227700.
DR GeneID; 4332134; -.
DR Gramene; Os03t0227700-01; Os03t0227700-01; Os03g0227700.
DR KEGG; osa:4332134; -.
DR eggNOG; KOG0157; Eukaryota.
DR HOGENOM; CLU_001570_15_5_1; -.
DR InParanoid; Q5CCK3; -.
DR OMA; FHWKLAA; -.
DR OrthoDB; 574756at2759; -.
DR PlantReactome; R-OSA-1119456; Brassinosteroid biosynthesis II.
DR UniPathway; UPA00381; -.
DR Proteomes; UP000000763; Chromosome 3.
DR Proteomes; UP000059680; Chromosome 3.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:EnsemblPlants.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0080132; F:fatty acid alpha-hydroxylase activity; IDA:UniProtKB.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IDA:Gramene.
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:0010012; F:steroid 22-alpha hydroxylase activity; IEA:EnsemblPlants.
DR GO; GO:0016132; P:brassinosteroid biosynthetic process; IMP:Gramene.
DR GO; GO:0010268; P:brassinosteroid homeostasis; IBA:GO_Central.
DR GO; GO:0009867; P:jasmonic acid mediated signaling pathway; IEA:EnsemblPlants.
DR GO; GO:0048366; P:leaf development; IMP:Gramene.
DR GO; GO:0010358; P:leaf shaping; IEA:EnsemblPlants.
DR GO; GO:0009741; P:response to brassinosteroid; IEA:EnsemblPlants.
DR GO; GO:0016125; P:sterol metabolic process; IBA:GO_Central.
DR GO; GO:0009826; P:unidimensional cell growth; IEA:EnsemblPlants.
DR Gene3D; 1.10.630.10; -; 1.
DR InterPro; IPR001128; Cyt_P450.
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.
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..506
FT /note="Cytochrome P450 90B2"
FT /id="PRO_5008970268"
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 449
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"
SQ SEQUENCE 506 AA; 57329 MW; 68E733DA80556B9F CRC64;
MAAMMASITS ELLFFLPFIL LALLTFYTTT VAKCHGGHWW RGGTTPAKRK RMNLPPGAAG
WPLVGETFGY LRAHPATSVG RFMEQHIARY GKIYRSSLFG ERTVVSADAG LNRYILQNEG
RLFECSYPRS IGGILGKWSM LVLVGDPHRE MRAISLNFLS SVRLRAVLLP EVERHTLLVL
RAWPPSSTFS AQHQAKKFTF NLMAKNIMSM DPGEEETERL RREYITFMKG VVSAPLNLPG
TPYWKALKSR AAILGVIERK MEERVEKLSK EDASVEQDDL LGWALKQSNL SKEQILDLLL
SLLFAGHETS SMALALAIFF LEGCPKAVQE LREEHLGIAR RQRLRGECKL SWEDYKEMVF
TQCVINETLR LGNVVRFLHR KVIKDVHYKG YDIPSGWKIL PVLAAVHLDS SLYEDPQRFN
PWRWKSSGSS GGLAQSSSFM PYGGGTRLCA GSELAKLEMA VFLHHLVLNF RWELAEPDQA
FVFPFVDFPK GLPIRVHRIA QDDEQE
