C14C2_ORYSJ
ID C14C2_ORYSJ Reviewed; 522 AA.
AC Q2QYH7; A0A0P0Y6E1;
DT 29-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Cytochrome P450 714C2;
DE EC=1.14.-.-;
GN Name=CYP714C2; OrderedLocusNames=Os12g0119000, LOC_Os12g02640;
GN ORFNames=OsJ_35025;
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=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 [2]
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 [3]
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 [4]
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 [5]
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 [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 IDENTIFICATION.
RX PubMed=19951895; DOI=10.1186/1479-7364-4-1-59;
RA Nelson D.R.;
RT "The cytochrome p450 homepage.";
RL Hum. Genomics 4:59-65(2009).
RN [8]
RP FUNCTION.
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: Probably not involved in gibberellin metabolism since over-
CC expression of CYP714C2 in a heterologous system does not induce semi-
CC dwarfism. {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 -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; DP000011; ABA95660.1; -; Genomic_DNA.
DR EMBL; AP008218; BAF29030.1; -; Genomic_DNA.
DR EMBL; AP014968; BAT15635.1; -; Genomic_DNA.
DR EMBL; CM000149; EEE52657.1; -; Genomic_DNA.
DR EMBL; AK066943; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; XP_015619747.1; XM_015764261.1.
DR AlphaFoldDB; Q2QYH7; -.
DR SMR; Q2QYH7; -.
DR STRING; 4530.OS12T0119000-01; -.
DR PaxDb; Q2QYH7; -.
DR PRIDE; Q2QYH7; -.
DR EnsemblPlants; Os12t0119000-01; Os12t0119000-01; Os12g0119000.
DR GeneID; 4351346; -.
DR Gramene; Os12t0119000-01; Os12t0119000-01; Os12g0119000.
DR KEGG; osa:4351346; -.
DR eggNOG; KOG0157; Eukaryota.
DR HOGENOM; CLU_001570_5_0_1; -.
DR InParanoid; Q2QYH7; -.
DR OMA; WYHYTIV; -.
DR OrthoDB; 825914at2759; -.
DR Proteomes; UP000000763; Chromosome 12.
DR Proteomes; UP000007752; Chromosome 12.
DR Proteomes; UP000059680; Chromosome 12.
DR Genevisible; Q2QYH7; 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 2: Evidence at transcript level;
KW Heme; Iron; Membrane; Metal-binding; Monooxygenase; Oxidoreductase;
KW Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..522
FT /note="Cytochrome P450 714C2"
FT /id="PRO_0000422416"
FT TOPO_DOM 1..11
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 12..32
FT /note="Helical; Signal-anchor for type III membrane
FT protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 33..522
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT BINDING 470
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 59
FT /note="P -> A (in Ref. 6; AK066943)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 522 AA; 58815 MW; FEC2B6C16B4EC448 CRC64;
MELFSSQQWL ALLPPIILCI LLFSYVYIIL WLRPERLRQK LRSQGVRGPK PSFLFGNIPE
MRRIQQLAKS AHEQEAGSTD MFSSNYVATL FPYFLHWSRV YGSIYLYSTG SIQVLNVTDP
NMVKELANCK SLDLGKPCYL QKERGALLGM GILTSNGDLW VHQRKVIAPE LFMERVKGMV
NLMMEAAMSM LNSWKNEVED RGGSAEIVVD EFLRTFSADV ISRACFGSSF SEGKEIFIKI
RQLQKAMAKQ SMLIGVPGSR YLPTRSNRGI WNLDSSIRTL ILNISKKYEH DSSTSVNKDL
LHSIIQGSKD GPFASCTPED FIVDNCKNIY FAGHETTSTT AAWCLMLLAS HHEWQSRARV
ESLDICQGRP LDFDILRKLK KLTMVIQETL RLYPPASFVA REALNDMKLG GIDIPKGTNI
WIPIAMAHRD PSVWGPSADK FDPDRFANGI AGACKPPHMY MPFGVGVRTC AGQNLAMVEL
KVVLSLLLSK FEFKLSPNYV HCPAFRLTIE PGKGVPLIFR EL