ID   C90A3_ORYSJ             Reviewed;         501 AA.
AC   Q2RAP4; Q5CCK2;
DT   15-FEB-2017, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   03-AUG-2022, entry version 132.
DE   RecName: Full=Cytochrome P450 90A3 {ECO:0000305};
DE            Short=OsCYP90A3 {ECO:0000305};
DE            EC=1.14.99.- {ECO:0000305|Ref.7};
DE   AltName: Full=Protein CONSTITUTIVE PHOTOMORPHOGENESIS AND DWARFISM 1 {ECO:0000303|Ref.7};
DE            Short=OsCPD1 {ECO:0000303|Ref.7};
DE   AltName: Full=Steroid 23-alpha-hydroxylase {ECO:0000305};
GN   Name=CYP90A3 {ECO:0000303|Ref.7}; Synonyms=CPD1 {ECO:0000303|Ref.7};
GN   OrderedLocusNames=Os11g0143200 {ECO:0000312|EMBL:BAF27566.1},
GN   LOC_Os11g04710 {ECO:0000312|EMBL:ABA91412.1};
GN   ORFNames=OsJ_32928 {ECO:0000312|EMBL:EAZ17406.1};
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. 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=16188032; DOI=10.1186/1741-7007-3-20;
RG   The rice chromosomes 11 and 12 sequencing consortia;
RT   "The sequence of rice chromosomes 11 and 12, rich in disease resistance
RT   genes and recent gene duplications.";
RL   BMC Biol. 3:20-20(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 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   FUNCTION, TISSUE SPECIFICITY, INDUCTION, AND DISRUPTION PHENOTYPE.
RX   DOI=10.1007/s00344-006-0041-6;
RA   Sakamoto T., Matsuoka M.;
RT   "Characterization of CONSTITUTIVE PHOTOMORPHOGENESIS AND DWARFISM homologs
RT   in rice (Oryza sativa L.).";
RL   J. Plant Growth Regul. 25:245-251(2006).
CC   -!- FUNCTION: Catalyzes the C23-alpha-hydroxylation step in brassinosteroid
CC       biosynthesis (Probable). Converts 6-deoxocathasterone (6-deoxoCT) to 6-
CC       deoxoteasterone (6-deoxoTE) in the late C6-oxidation pathway and
CC       cathasterone (CT) to teasterone (TE) in the early C6-oxidation pathway
CC       of brassinolide (BL) biosynthesis (Probable). {ECO:0000305|Ref.7}.
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000250|UniProtKB:P04798};
CC   -!- PATHWAY: Plant hormone biosynthesis; brassinosteroid biosynthesis.
CC       {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC       protein {ECO:0000255}.
CC   -!- TISSUE SPECIFICITY: Highly expressed in shoot apex and inflorenscence.
CC       Expressed in roots, stems, leaf blades and leaf sheaths.
CC       {ECO:0000269|Ref.7}.
CC   -!- INDUCTION: Down-regulated by brassinolide (BL). {ECO:0000269|Ref.7}.
CC   -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC       conditions. {ECO:0000269|Ref.7}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; AB206580; BAD90973.1; -; mRNA.
DR   EMBL; DP000010; ABA91412.1; -; Genomic_DNA.
DR   EMBL; AP008217; BAF27566.1; -; Genomic_DNA.
DR   EMBL; AP014967; BAT12633.1; -; Genomic_DNA.
DR   EMBL; CM000148; EAZ17406.1; -; Genomic_DNA.
DR   RefSeq; XP_015616657.1; XM_015761171.1.
DR   AlphaFoldDB; Q2RAP4; -.
DR   SMR; Q2RAP4; -.
DR   STRING; 4530.OS11T0143200-01; -.
DR   PaxDb; Q2RAP4; -.
DR   PRIDE; Q2RAP4; -.
DR   EnsemblPlants; Os11t0143200-01; Os11t0143200-01; Os11g0143200.
DR   GeneID; 4349746; -.
DR   Gramene; Os11t0143200-01; Os11t0143200-01; Os11g0143200.
DR   KEGG; osa:4349746; -.
DR   eggNOG; KOG0157; Eukaryota.
DR   HOGENOM; CLU_001570_15_5_1; -.
DR   InParanoid; Q2RAP4; -.
DR   OMA; KLWEVYM; -.
DR   OrthoDB; 1247045at2759; -.
DR   PlantReactome; R-OSA-1119456; Brassinosteroid biosynthesis II.
DR   UniPathway; UPA00381; -.
DR   Proteomes; UP000000763; Chromosome 11.
DR   Proteomes; UP000007752; Chromosome 11.
DR   Proteomes; UP000059680; Chromosome 11.
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; 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; IDA:UniProtKB.
DR   GO; GO:0010268; P:brassinosteroid homeostasis; IBA:GO_Central.
DR   GO; GO:0016125; P:sterol metabolic 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   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   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..501
FT                   /note="Cytochrome P450 90A3"
FT                   /id="PRO_0000439012"
FT   TRANSMEM        2..22
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         446
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        144
FT                   /note="L -> F (in Ref. 1; BAD90973)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   501 AA;  55711 MW;  2D8FEED4D34E7CD3 CRC64;
     MAAAALLLLA AAAAIVVVAM VLRWLLLLGG PAAGRLGKRA LMPPGSTGLP LIGETLRLIS
     AYKTPNPEPF IDERVARHGG VFTTHVFGER TVFSADPAFN RLLLAAEGRA VHSSYPSSIA
     TLLGARSLLL TRGAAHKRLH SLTLTRLGRP ASPPLLAHID RLVLATMRQW EPAATVRLMD
     EAKKITFNLT VKQLVSIEPG PWTESLRREY VKLIDGFFSI PFPLANLLPF TTYGQALKAR
     KKVAGALREV IKKRMEEKAE NGGSIGDDEG KKEKKDMVEE LLEAEGGSFS EEEMVDFCLS
     LLVAGYETTS MLMTLAVKFL TETPAALAEL KEEHANIRDM KGKKQPLEWS DYKSMPFTQC
     VINETLRVGN IISGVFRRAN TDIHYKDYTI PKGCKIFASF RAVHLNNEHY ENARTFNPWR
     WQINNKLQNA VGANIFTPFG GGPRLCPGYE LARVVVSIFL HHLVTRFSWE ETEEDRLVFF
     PTTRTLKGYP INLRLLSESI C