C70A3_ORYSJ
ID C70A3_ORYSJ Reviewed; 525 AA.
AC Q7EZR4;
DT 10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Cytochrome P450 703A2 {ECO:0000303|PubMed:24798002};
DE EC=1.14.14.130 {ECO:0000269|PubMed:24798002};
DE AltName: Full=Laurate 7-monooxygenase {ECO:0000305};
GN Name=CYP703A3 {ECO:0000303|PubMed:24798002};
GN OrderedLocusNames=Os08g0131100 {ECO:0000312|EMBL:BAF22841.1},
GN LOC_Os08g03682 {ECO:0000305};
GN ORFNames=OSJNBb0009H02.9 {ECO:0000312|EMBL:BAD33366.1},
GN P0582D05.139 {ECO:0000312|EMBL:BAD09645.1};
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=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 [2]
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 [3]
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 [4]
RP FUNCTION, CATALYTIC ACTIVITY, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=24798002; DOI=10.1111/jipb.12212;
RA Yang X., Wu D., Shi J., He Y., Pinot F., Grausem B., Yin C., Zhu L.,
RA Chen M., Luo Z., Liang W., Zhang D.;
RT "Rice CYP703A3, a cytochrome P450 hydroxylase, is essential for development
RT of anther cuticle and pollen exine.";
RL J. Integr. Plant Biol. 56:979-994(2014).
CC -!- FUNCTION: Involved in pollen exine and anther epicuticular layer
CC development. Catalyzes the in-chain hydroxylation of lauric acid
CC (C12:0) preferentially on position 7, generating 7-hydroxylated lauric
CC acid. Does not possess activity with other fatty acids (C14:0, C16:0,
CC C16:1, and C18:0). Participates in a conserved pathway of in-chain
CC hydroxylation of lauric acid required for anther cuticle and pollen
CC exine formation. Directly regulated by TDR, a known regulator of
CC tapetum programmed cell death (PCD) and pollen exine formation.
CC {ECO:0000269|PubMed:24798002}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dodecanoate + O2 + reduced [NADPH--hemoprotein reductase] = 7-
CC hydroxydodecanoate + H(+) + H2O + oxidized [NADPH--hemoprotein
CC reductase]; Xref=Rhea:RHEA:45084, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:18262, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC ChEBI:CHEBI:84921; EC=1.14.14.130;
CC Evidence={ECO:0000269|PubMed:24798002};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- DEVELOPMENTAL STAGE: Expressed in anthers of developing flowers during
CC meiosis, tapetal cell death stage and microspore stage.
CC -!- DISRUPTION PHENOTYPE: Male sterile. Defective in pollen exine and
CC anther epicuticular layer development. {ECO:0000269|PubMed:24798002}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; AP004591; BAD09645.1; -; Genomic_DNA.
DR EMBL; AP005250; BAD33366.1; -; Genomic_DNA.
DR EMBL; AP008214; BAF22841.1; -; Genomic_DNA.
DR EMBL; AP014964; BAT03702.1; -; Genomic_DNA.
DR RefSeq; XP_015648492.1; XM_015793006.1.
DR AlphaFoldDB; Q7EZR4; -.
DR SMR; Q7EZR4; -.
DR STRING; 4530.OS08T0131100-01; -.
DR PaxDb; Q7EZR4; -.
DR PRIDE; Q7EZR4; -.
DR EnsemblPlants; Os08t0131100-01; Os08t0131100-01; Os08g0131100.
DR GeneID; 4344594; -.
DR Gramene; Os08t0131100-01; Os08t0131100-01; Os08g0131100.
DR KEGG; osa:4344594; -.
DR eggNOG; KOG0156; Eukaryota.
DR HOGENOM; CLU_001570_4_0_1; -.
DR InParanoid; Q7EZR4; -.
DR OMA; GPQEAME; -.
DR OrthoDB; 702827at2759; -.
DR Proteomes; UP000000763; Chromosome 8.
DR Proteomes; UP000059680; Chromosome 8.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0052722; F:fatty acid in-chain 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: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; IEA:EnsemblPlants.
DR GO; GO:0048653; P:anther development; IMP:UniProtKB.
DR GO; GO:0002933; P:lipid hydroxylation; IDA:UniProtKB.
DR GO; GO:0051792; P:medium-chain fatty acid biosynthetic process; IEA:EnsemblPlants.
DR GO; GO:0010584; P:pollen exine formation; IMP:UniProtKB.
DR GO; GO:0080110; P:sporopollenin biosynthetic process; IEA:EnsemblPlants.
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 1: Evidence at protein level;
KW Heme; Iron; Membrane; Metal-binding; Monooxygenase; Oxidoreductase;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..525
FT /note="Cytochrome P450 703A2"
FT /id="PRO_0000439819"
FT TRANSMEM 3..23
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 455
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"
SQ SEQUENCE 525 AA; 59631 MW; B70050715078E158 CRC64;
MDPFLLSIIL CSWIFVVVSW KKLNCMRRRL PPGPPRWPIF GNLLQLSPLP HKDFARFCTK
YGPLVYLRLG TIDAITTDDP EVIREILIRQ DEVFASRPRT LAAVHLAYGC GDVALAPLGP
NWKRMRRVCM EHLLTTKRLE SFAAHRALEA EHLCQFVWAK AQSGKPVNLR EVLGAFSMNN
VTRMLLGKQY FGLQSAGPGE AMEFMHITHE LFWLLGLIYL GDYLPAWRWL DPYGCEKKMR
EVEKKVDDFH QKIIDEHRKA REAKKSASLD DDNKEDMDFV DVLLSLPGEN GKEHMDDVEI
KALMQDMIAA ATDTSSVTNE WVMAEVIKNP RVLRKIQEEL DGVVGRGRMV AESDLGQLTY
LRCVVRESFR MHPAGPFLIP HESLKPTTIM GYDIPARTRI FINTHALGRN TRIWDDVDAF
RPERHLPASA DGGRVEISHL PDFKILPFSA GKRKCPGAPL GVILVLMALA RLFHCFDWSP
PDGLRPDDID TQEVYGMTMP KAKPLVAVAT PRLPPQMYGR HGKQV
