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C7A15_ARATH
ID   C7A15_ARATH             Reviewed;         512 AA.
AC   Q9LUC5;
DT   19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 144.
DE   RecName: Full=Cytochrome P450 72A15;
DE            EC=1.14.-.-;
GN   Name=CYP72A15; OrderedLocusNames=At3g14690; ORFNames=MIE1.20;
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 [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10819329; DOI=10.1093/dnares/7.2.131;
RA   Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT   features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT   clones.";
RL   DNA Res. 7:131-135(2000).
RN   [2]
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   [3]
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).
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC       protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; AB023038; BAB02401.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE75556.1; -; Genomic_DNA.
DR   EMBL; AY050827; AAK92762.1; -; mRNA.
DR   EMBL; AY096748; AAM20382.1; -; mRNA.
DR   RefSeq; NP_188087.1; NM_112330.4.
DR   AlphaFoldDB; Q9LUC5; -.
DR   SMR; Q9LUC5; -.
DR   STRING; 3702.AT3G14690.1; -.
DR   MetOSite; Q9LUC5; -.
DR   PaxDb; Q9LUC5; -.
DR   ProteomicsDB; 240270; -.
DR   EnsemblPlants; AT3G14690.1; AT3G14690.1; AT3G14690.
DR   GeneID; 820697; -.
DR   Gramene; AT3G14690.1; AT3G14690.1; AT3G14690.
DR   KEGG; ath:AT3G14690; -.
DR   Araport; AT3G14690; -.
DR   TAIR; locus:2089521; AT3G14690.
DR   eggNOG; KOG0157; Eukaryota.
DR   HOGENOM; CLU_001570_5_0_1; -.
DR   InParanoid; Q9LUC5; -.
DR   PhylomeDB; Q9LUC5; -.
DR   PRO; PR:Q9LUC5; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q9LUC5; baseline and differential.
DR   Genevisible; Q9LUC5; AT.
DR   GO; GO:0005829; C:cytosol; HDA:TAIR.
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; 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.
PE   2: Evidence at transcript level;
KW   Heme; Iron; Membrane; Metal-binding; Monooxygenase; Oxidoreductase;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..512
FT                   /note="Cytochrome P450 72A15"
FT                   /id="PRO_0000425858"
FT   TRANSMEM        2..22
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         460
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   512 AA;  58442 MW;  19DDEEAD9C9BAF0B CRC64;
     MEISVASVTI SVVLAVVSWW IWRTLQWVWF KPKMLEHYLR RQGLAGTPYT PLVGDLKKNF
     TMLSEARSKP LKLTDDISPR VVPYPLQMFK TYGRTYFTWF GPIPTITIMD PEQIKEVFNK
     VYDFQKPHTF PLATIIAKGL ANYDGDKWAK HRRIINPAFH IEKIKNMVPA FHQSCREVVG
     EWDQLVSDKG SSCEVDVWPG LVSMTADVIS RTAFGSSYKE GQRIFELQAE LAQLIIQAFR
     KAFIPGYSYL PTKSNRRMKA AAREIQVILR GIVNKRLRAR EAGEAPSDDL LGILLESNLR
     QTEGNGMSTE DLMEECKLFY FAGQETTSVL LVWTMVLLSQ HQDWQARARE EVKQVFGDKE
     PDAEGLNQLK VMTMILYEVL RLYPPVTQLT RAIHKELKLG DLTLPGGVQI SLPILLVQHD
     IELWGNDAAE FNPDRFKDGL SKATKSQVSF FPFAWGPRIC IGQNFALLEA KMAMALILRR
     FSFEISPSYV HAPYTVITIH PQFGAQLIMH KL
 
 
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