C14B1_ORYSJ
ID C14B1_ORYSJ Reviewed; 534 AA.
AC Q7XHW5; A0A0P0XA58; A3BNH2;
DT 29-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2013, sequence version 2.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Cytochrome P450 714B1;
DE EC=1.14.-.-;
DE AltName: Full=GA 13-oxidase 1;
DE AltName: Full=Gibberellin 13 oxidase 1;
GN Name=CYP714B1; OrderedLocusNames=Os07g0681300, LOC_Os07g48330;
GN ORFNames=OsJ_25604, OSJNBa0008J01.23;
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 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 [5]
RP FUNCTION, TISSUE SPECIFICITY, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE, AND
RP INDUCTION BY GIBBERELLIN.
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 13-hydroxylation of gibberellins (GAs).
CC Determines the ratio of GA4 and GA1. Converts GA12 into GA53.
CC {ECO:0000269|PubMed:23319637}.
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type III
CC membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Highly expressed in spikelet and uppermost
CC internode. Detected in shoots, roots, leaves and anthers.
CC {ECO:0000269|PubMed:23319637}.
CC -!- INDUCTION: Up-regulated by bioactive gibberellins.
CC {ECO:0000269|PubMed:23319637}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype and no change in the levels
CC of 13-OH GAs; due to the redundancy with CYP714B2. Cyp714b1 and
CC cyp714b2 double mutants have decreased levels of 13-OH GAs, increased
CC levels of 13-H GAs, including GA4, and longer uppermost internode.
CC {ECO:0000269|PubMed:23319637}.
CC -!- MISCELLANEOUS: Overexpression of CYP714B1 in a heterologous system
CC causes semi-dwarfism and increased 13-OH GAs content.
CC {ECO:0000305|PubMed:23319637}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC80012.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAF22566.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=EAZ41111.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AP005099; BAC80012.1; ALT_INIT; Genomic_DNA.
DR EMBL; AP008213; BAF22566.1; ALT_INIT; Genomic_DNA.
DR EMBL; AP014963; BAT03245.1; -; Genomic_DNA.
DR EMBL; CM000144; EAZ41111.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_015645488.1; XM_015790002.1.
DR AlphaFoldDB; Q7XHW5; -.
DR SMR; Q7XHW5; -.
DR STRING; 4530.OS07T0681300-00; -.
DR PaxDb; Q7XHW5; -.
DR PRIDE; Q7XHW5; -.
DR EnsemblPlants; Os07t0681300-00; Os07t0681300-00; Os07g0681300.
DR GeneID; 4344303; -.
DR Gramene; Os07t0681300-00; Os07t0681300-00; Os07g0681300.
DR KEGG; osa:4344303; -.
DR eggNOG; KOG0157; Eukaryota.
DR HOGENOM; CLU_001570_5_0_1; -.
DR InParanoid; Q7XHW5; -.
DR OMA; NMVFLHV; -.
DR OrthoDB; 825914at2759; -.
DR BioCyc; MetaCyc:MON-17926; -.
DR Proteomes; UP000000763; Chromosome 7.
DR Proteomes; UP000007752; Chromosome 7.
DR Proteomes; UP000059680; Chromosome 7.
DR Genevisible; Q7XHW5; OS.
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 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; Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..534
FT /note="Cytochrome P450 714B1"
FT /id="PRO_0000422412"
FT TOPO_DOM 1
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 2..22
FT /note="Helical; Signal-anchor for type III membrane
FT protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 23..534
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT BINDING 472
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 35
FT /note="A -> G (in Ref. 4; EAZ41111)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 534 AA; 58036 MW; 9D7488C2505F15E5 CRC64;
MVVVVAAAMA AASLCCGVAA YLYYVLWLAP ERLRAHLRRQ GIGGPTPSFP YGNLADMRSH
AAAAAGGKAT GEGRQEGDIV HDYRQAVFPF YENWRKQYGP VFTYSVGNMV FLHVSRPDIV
RELSLCVSLD LGKSSYMKAT HQPLFGEGIL KSNGNAWAHQ RKLIAPEFFP DKVKGMVDLM
VDSAQVLVSS WEDRIDRSGG NALDLMIDDD IRAYSADVIS RTCFGSSYVK GKQIFDMIRE
LQKTVSTKKQ NLLAEMTGLS FLFPKASGRA AWRLNGRVRA LILDLVGENG EEDGGNLLSA
MLRSARGGGG GGGEVAAAAE DFVVDNCKNI YFAGYESTAV TAAWCLMLLA LHPEWQDRVR
DEVQAACCGG GGRSPDFPAL QKMKNLTMVI QETLRLYPAG AVVSRQALRE LSLGGVRVPR
GVNIYVPVST LHLDAELWGG GAGAAEFDPA RFADARPPLH AYLPFGAGAR TCLGQTFAMA
ELKVLLSLVL CRFEVALSPE YVHSPAHKLI VEAEHGVRLV LKKVRSKCDW AGFD
