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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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