C14D1_ORYSJ
ID C14D1_ORYSJ Reviewed; 577 AA.
AC Q5KQH7; A0A0P0WNQ4; B9FJW9;
DT 29-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Cytochrome P450 714D1;
DE EC=1.14.-.-;
DE AltName: Full=Protein ELONGATED UPPERMOST INTERNODE 1;
DE Short=EUI1;
GN Name=CYP714D1; Synonyms=EUI1;
GN OrderedLocusNames=Os05g0482400, LOC_Os05g40384;
GN ORFNames=OsJ_18961, OSJNBa0095J22.13;
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 [GENOMIC DNA / MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=16399803; DOI=10.1105/tpc.105.038455;
RA Zhu Y., Nomura T., Xu Y., Zhang Y., Peng Y., Mao B., Hanada A., Zhou H.,
RA Wang R., Li P., Zhu X., Mander L.N., Kamiya Y., Yamaguchi S., He Z.;
RT "ELONGATED UPPERMOST INTERNODE encodes a cytochrome P450 monooxygenase that
RT epoxidizes gibberellins in a novel deactivation reaction in rice.";
RL Plant Cell 18:442-456(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16261349; DOI=10.1007/s00438-005-0039-y;
RA Cheng C.-H., Chung M.C., Liu S.-M., Chen S.-K., Kao F.Y., Lin S.-J.,
RA Hsiao S.-H., Tseng I.C., Hsing Y.-I.C., Wu H.-P., Chen C.-S., Shaw J.-F.,
RA Wu J., Matsumoto T., Sasaki T., Chen H.-C., Chow T.-Y.;
RT "A fine physical map of the rice chromosome 5.";
RL Mol. Genet. Genomics 274:337-345(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 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, AND TISSUE SPECIFICITY.
RX PubMed=23319637; DOI=10.1073/pnas.1215788110;
RA Magome H., Nomura T., Hanada A., Takeda-Kamiya N., Ohnishi T., Shinma Y.,
RA Katsumata T., Kawaide H., Kamiya Y., Yamaguchi S.;
RT "CYP714B1 and CYP714B2 encode gibberellin 13-oxidases that reduce
RT gibberellin activity in rice.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:1947-1952(2013).
CC -!- FUNCTION: Catalyzes the 16alpha,17-epoxidation on non-13-hydroxylated
CC gibberellins (GAs), including GA4, GA9, and GA12. No activity with GA1,
CC GA20, GA53 or ent-kaurenoic acid. Reduces the biological activity of
CC GAs. {ECO:0000269|PubMed:16399803, ECO:0000269|PubMed:23319637}.
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:16399803}; Single-pass type III membrane protein
CC {ECO:0000269|PubMed:16399803}.
CC -!- TISSUE SPECIFICITY: Expressed in rapidly elongating or dividing
CC tissues, including the shoot apical meristem, the intercalary meristem
CC and elongating zones of internodes, and panicle but not in young
CC seedlings, roots and leaves. During the heading stage, the highest
CC expression is detected in the flowering spikelets, anthers, the
CC divisional zone and the node of the uppermost internode.
CC {ECO:0000269|PubMed:16399803, ECO:0000269|PubMed:23319637}.
CC -!- MISCELLANEOUS: Overexpression of CYP714D1 causes severe dwarfism and
CC sterility. {ECO:0000305|PubMed:16399803}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EEE64129.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AY987039; AAY42600.1; -; mRNA.
DR EMBL; AY987040; AAY42601.1; -; Genomic_DNA.
DR EMBL; AC137619; AAW56875.1; -; Genomic_DNA.
DR EMBL; AP008211; BAF17780.1; -; Genomic_DNA.
DR EMBL; AP014961; BAS94595.1; -; Genomic_DNA.
DR EMBL; CM000142; EEE64129.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AK109526; BAG98789.1; -; mRNA.
DR RefSeq; XP_015637923.1; XM_015782437.1.
DR AlphaFoldDB; Q5KQH7; -.
DR SMR; Q5KQH7; -.
DR STRING; 4530.OS05T0482400-01; -.
DR PaxDb; Q5KQH7; -.
DR PRIDE; Q5KQH7; -.
DR EnsemblPlants; Os05t0482400-01; Os05t0482400-01; Os05g0482400.
DR GeneID; 4339131; -.
DR Gramene; Os05t0482400-01; Os05t0482400-01; Os05g0482400.
DR KEGG; osa:4339131; -.
DR eggNOG; KOG0157; Eukaryota.
DR HOGENOM; CLU_001570_5_0_1; -.
DR InParanoid; Q5KQH7; -.
DR OMA; KAYGETY; -.
DR OrthoDB; 1247045at2759; -.
DR BioCyc; MetaCyc:LOC_OS05G0482400-MON; -.
DR BRENDA; 1.14.14.1; 4460.
DR Proteomes; UP000000763; Chromosome 5.
DR Proteomes; UP000007752; Chromosome 5.
DR Proteomes; UP000059680; Chromosome 5.
DR Genevisible; Q5KQH7; OS.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR GO; GO:0045487; P:gibberellin catabolic process; IDA:Gramene.
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 Endoplasmic reticulum; Heme; Iron; Membrane; Metal-binding; Monooxygenase;
KW Oxidoreductase; Reference proteome; Signal-anchor; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..577
FT /note="Cytochrome P450 714D1"
FT /id="PRO_0000422418"
FT TOPO_DOM 1..3
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 4..24
FT /note="Helical; Signal-anchor for type III membrane
FT protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 25..577
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 315..343
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 504
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"
FT CONFLICT 321..322
FT /note="AA -> PR (in Ref. 6; EEE64129)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 577 AA; 63189 MW; 22B6B4A358A1642E CRC64;
MESFFVFFTA AALPVVVAAA VIAGLCITAA WLARPRRVAE VFRRQGIDGP PPSSFLAGNL
PEMKARVAAA ASAAAPTADG EETASAGGGG GGRDFEKDGF DDYCTRIFPY FHKWRKAYGE
TYLYWLRRRP ALYVTDPELI GEIGRCVSLD MGKPKYLQKG QEPLFGGGVL KANGACWARQ
RKVIAPEFYM ARVRAMVQLM VDAAQPLIAS WESRIDAAGG AAAAEVVVDG DLRSFSFDVI
SRACFGSDYS RGREIFLRLR ELSGLMSETS VIFSIPSLRH LPTGKNRRIW RLTGEIRSLI
MELVRERRCA ARAAREHGGK AAPPSPPERD FLGSIIENSG GQPRPDDFVV DNCKNIYFAG
HETSAVTATW CLMLLAAHPE WQDRARAEVL EVCGGDGAAA PAAPDFDMVS RMRTVGMVVQ
ETLRLFPPSS FVVRETFRDM QLGRLLAPKG TYLFVPVSTM HHDVAAWGPT ARLFDPSRFR
DGVAAACKHP QASFMPFGLG ARTCLGQNLA LVEVKTLVAV VLARFEFTLS PEYRHSPAFR
LIIEPEFGLR LRIRRAGGQD ATSQVDTSTA PVHSSHN
