ID   CP511_ARATH             Reviewed;         488 AA.
AC   Q9SAA9;
DT   19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   27-MAR-2024, entry version 160.
DE   RecName: Full=Sterol 14-demethylase;
DE            EC=1.14.14.154 {ECO:0000269|PubMed:11437378, ECO:0000269|PubMed:16040657};
DE   AltName: Full=Cytochrome P450 51A2;
DE   AltName: Full=Cytochrome P450 51G1;
DE            Short=AtCYP51;
DE   AltName: Full=Obtusifoliol 14-demethylase;
DE   AltName: Full=Protein EMBRYO DEFECTIVE 1738;
GN   Name=CYP51G1; Synonyms=CYP51A2, EMB1738; OrderedLocusNames=At1g11680;
GN   ORFNames=F25C20.17;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC   STRAIN=cv. Columbia;
RX   PubMed=11437378; DOI=10.1006/bbrc.2001.5122;
RA   Kushiro M., Nakano T., Sato K., Yamagishi K., Asami T., Nakano A.,
RA   Takatsuto S., Fujioka S., Ebizuka Y., Yoshida S.;
RT   "Obtusifoliol 14alpha-demethylase (CYP51) antisense Arabidopsis shows slow
RT   growth and long life.";
RL   Biochem. Biophys. Res. Commun. 285:98-104(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA   Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA   Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA   Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA   Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA   Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA   Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA   Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA   Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA   Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA   Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA   Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA   Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA   Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL   Nature 408:816-820(2000).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA   Feldmann K.A.;
RT   "Full-length cDNA from Arabidopsis thaliana.";
RL   Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   IDENTIFICATION, AND DISRUPTION PHENOTYPE.
RX   PubMed=15266054; DOI=10.1104/pp.104.045179;
RA   Tzafrir I., Pena-Muralla R., Dickerman A., Berg M., Rogers R., Hutchens S.,
RA   Sweeney T.C., McElver J., Aux G., Patton D., Meinke D.;
RT   "Identification of genes required for embryo development in Arabidopsis.";
RL   Plant Physiol. 135:1206-1220(2004).
RN   [7]
RP   FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX   PubMed=16040657; DOI=10.1104/pp.105.061598;
RA   Kim H.B., Schaller H., Goh C.H., Kwon M., Choe S., An C.S., Durst F.,
RA   Feldmann K.A., Feyereisen R.;
RT   "Arabidopsis cyp51 mutant shows postembryonic seedling lethality associated
RT   with lack of membrane integrity.";
RL   Plant Physiol. 138:2033-2047(2005).
RN   [8]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=16169959; DOI=10.1104/pp.105.066639;
RA   O'Brien M., Chantha S.C., Rahier A., Matton D.P.;
RT   "Lipid signaling in plants. Cloning and expression analysis of the
RT   obtusifoliol 14alpha-demethylase from Solanum chacoense Bitt., a
RT   pollination- and fertilization-induced gene with both obtusifoliol and
RT   lanosterol demethylase activity.";
RL   Plant Physiol. 139:734-749(2005).
CC   -!- FUNCTION: Involved in sterol biosynthesis. Catalyzes the 14-alpha
CC       demethylation of obtusifoliol to 4 alpha-methyl-5 alpha-
CC       ergosta-8,14,24(28)-trien-3 beta-ol. {ECO:0000269|PubMed:11437378,
CC       ECO:0000269|PubMed:16040657, ECO:0000269|PubMed:16169959}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 14alpha-methyl steroid + 3 O2 + 3 reduced
CC         [NADPH--hemoprotein reductase] = a Delta(14) steroid + formate + 4
CC         H(+) + 4 H2O + 3 oxidized [NADPH--hemoprotein reductase];
CC         Xref=Rhea:RHEA:54028, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:15740, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC         ChEBI:CHEBI:138029, ChEBI:CHEBI:138031; EC=1.14.14.154;
CC         Evidence={ECO:0000269|PubMed:11437378, ECO:0000269|PubMed:16040657};
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC       protein {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed in leaves, roots, stems, siliques,
CC       flowers, flower buds and seedlings. {ECO:0000269|PubMed:16040657}.
CC   -!- DISRUPTION PHENOTYPE: Lack of membrane integrity. Seedling lethality.
CC       {ECO:0000269|PubMed:15266054, ECO:0000269|PubMed:16040657,
CC       ECO:0000269|PubMed:16169959}.
CC   -!- MISCELLANEOUS: Decreased expression of CYP51G1 by antisense leads to a
CC       semidwarf phenotype in the early growth stage and a longer life span.
CC       Disruption mutants accumulate obtusifoliol and 14-alpha-methyl-sterols
CC       and cannot be rescued by exogenous application of brassinosteroids.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; AB014459; BAB61873.1; -; mRNA.
DR   EMBL; AC007296; AAD30254.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE28769.1; -; Genomic_DNA.
DR   EMBL; AY050860; AAK92797.1; -; mRNA.
DR   EMBL; AF410338; AAK95324.1; -; mRNA.
DR   EMBL; AY091203; AAM14142.1; -; mRNA.
DR   EMBL; AY084517; AAM61085.1; -; mRNA.
DR   PIR; D86250; D86250.
DR   RefSeq; NP_172633.1; NM_101040.4.
DR   AlphaFoldDB; Q9SAA9; -.
DR   SMR; Q9SAA9; -.
DR   BioGRID; 22952; 1.
DR   IntAct; Q9SAA9; 1.
DR   STRING; 3702.Q9SAA9; -.
DR   PaxDb; 3702-AT1G11680-1; -.
DR   ProteomicsDB; 222700; -.
DR   EnsemblPlants; AT1G11680.1; AT1G11680.1; AT1G11680.
DR   GeneID; 837712; -.
DR   Gramene; AT1G11680.1; AT1G11680.1; AT1G11680.
DR   KEGG; ath:AT1G11680; -.
DR   Araport; AT1G11680; -.
DR   TAIR; AT1G11680; CYP51G1.
DR   eggNOG; KOG0684; Eukaryota.
DR   HOGENOM; CLU_001570_15_0_1; -.
DR   InParanoid; Q9SAA9; -.
DR   OMA; NFLMPWA; -.
DR   OrthoDB; 5474434at2759; -.
DR   PhylomeDB; Q9SAA9; -.
DR   BioCyc; MetaCyc:AT1G11680-MONOMER; -.
DR   PRO; PR:Q9SAA9; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9SAA9; baseline and differential.
DR   GO; GO:0005783; C:endoplasmic reticulum; HDA:TAIR.
DR   GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008398; F:sterol 14-demethylase activity; TAS:TAIR.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0016126; P:sterol biosynthetic process; IMP:TAIR.
DR   CDD; cd11042; CYP51-like; 1.
DR   Gene3D; 1.10.630.10; Cytochrome P450; 1.
DR   InterPro; IPR001128; Cyt_P450.
DR   InterPro; IPR017972; Cyt_P450_CS.
DR   InterPro; IPR002403; Cyt_P450_E_grp-IV.
DR   InterPro; IPR036396; Cyt_P450_sf.
DR   PANTHER; PTHR24304:SF2; 24-HYDROXYCHOLESTEROL 7-ALPHA-HYDROXYLASE; 1.
DR   PANTHER; PTHR24304; CYTOCHROME P450 FAMILY 7; 1.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00465; EP450IV.
DR   PRINTS; PR00385; P450.
DR   SUPFAM; SSF48264; Cytochrome P450; 1.
DR   PROSITE; PS00086; CYTOCHROME_P450; 1.
DR   Genevisible; Q9SAA9; AT.
PE   1: Evidence at protein level;
KW   Heme; Iron; Lipid biosynthesis; Lipid metabolism; Membrane; Metal-binding;
KW   Methyltransferase; Monooxygenase; Oxidoreductase; Reference proteome;
KW   Steroid biosynthesis; Steroid metabolism; Sterol biosynthesis;
KW   Sterol metabolism; Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..488
FT                   /note="Sterol 14-demethylase"
FT                   /id="PRO_0000413010"
FT   TRANSMEM        12..32
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         433
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   488 AA;  55495 MW;  6B68225BC13A4419 CRC64;
     MELDSENKLL KTGLVIVATL VIAKLIFSFF TSDSKKKRLP PTLKAWPPLV GSLIKFLKGP
     IIMLREEYPK LGSVFTVNLV HKKITFLIGP EVSAHFFKAS ESDLSQQEVY QFNVPTFGPG
     VVFDVDYSVR QEQFRFFTEA LRVNKLKGYV DMMVTEAEDY FSKWGESGEV DIKVELERLI
     ILTASRCLLG REVRDQLFDD VSALFHDLDN GMLPISVLFP YLPIPAHRRR DRAREKLSEI
     FAKIIGSRKR SGKTENDMLQ CFIESKYKDG RQTTESEVTG LLIAALFAGQ HTSSITSTWT
     GAYLMRYKEY FSAALDEQKN LIAKHGDKID HDILSEMDVL YRCIKEALRL HPPLIMLMRA
     SHSDFSVTAR DGKTYDIPKG HIVATSPAFA NRLPHIFKDP DTYDPERFSP GREEDKAAGA
     FSYIAFGGGR HGCLGEPFAY LQIKAIWSHL LRNFELELVS PFPEIDWNAM VVGVKGNVMV
     RYKRRQLS
//