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Database: UniProt
Entry: C86A7_ARATH
LinkDB: C86A7_ARATH
Original site: C86A7_ARATH 
ID   C86A7_ARATH             Reviewed;         523 AA.
AC   Q9CAD6; Q8LAQ9;
DT   11-DEC-2013, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   27-MAR-2024, entry version 146.
DE   RecName: Full=Cytochrome P450 86A7;
DE            EC=1.14.14.1;
GN   Name=CYP86A7; OrderedLocusNames=At1g63710; ORFNames=F24D7.10;
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=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   [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].
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   [4]
RP   FUNCTION, TISSUE SPECIFICITY, INDUCTION, AND GENE FAMILY.
RX   PubMed=15709153; DOI=10.1104/pp.104.055715;
RA   Duan H., Schuler M.A.;
RT   "Differential expression and evolution of the Arabidopsis CYP86A
RT   subfamily.";
RL   Plant Physiol. 137:1067-1081(2005).
RN   [5]
RP   FUNCTION.
RX   PubMed=17427946; DOI=10.1002/prot.21335;
RA   Rupasinghe S.G., Duan H., Schuler M.A.;
RT   "Molecular definitions of fatty acid hydroxylases in Arabidopsis
RT   thaliana.";
RL   Proteins 68:279-293(2007).
CC   -!- FUNCTION: Catalyzes the omega-hydroxylation of various fatty acids
CC       (FA). Acts on saturated and unsaturated fatty acids with chain lengths
CC       from C12 to C18. {ECO:0000269|PubMed:15709153,
CC       ECO:0000269|PubMed:17427946}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an organic molecule + O2 + reduced [NADPH--hemoprotein
CC         reductase] = an alcohol + H(+) + H2O + oxidized [NADPH--hemoprotein
CC         reductase]; Xref=Rhea:RHEA:17149, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC         COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:30879, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC         ChEBI:CHEBI:142491; EC=1.14.14.1;
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   -!- TISSUE SPECIFICITY: Expressed in stems, flowers and siliques.
CC       {ECO:0000269|PubMed:15709153}.
CC   -!- INDUCTION: By methyl jasmonate (MeJA) and abscisic acid (ABA). Down-
CC       regulated by salicylic acid (SA), the ethylene precursor ACC, drought,
CC       wounding and mannitol treatment, and in both etiolated and dark-adapted
CC       seedlings. {ECO:0000269|PubMed:15709153}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; AC011622; AAG52424.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE34136.1; -; Genomic_DNA.
DR   EMBL; AY087670; AAM65207.1; -; mRNA.
DR   PIR; B96662; B96662.
DR   RefSeq; NP_176558.1; NM_105048.3.
DR   AlphaFoldDB; Q9CAD6; -.
DR   SMR; Q9CAD6; -.
DR   STRING; 3702.Q9CAD6; -.
DR   PaxDb; 3702-AT1G63710-1; -.
DR   ProteomicsDB; 239172; -.
DR   EnsemblPlants; AT1G63710.1; AT1G63710.1; AT1G63710.
DR   GeneID; 842675; -.
DR   Gramene; AT1G63710.1; AT1G63710.1; AT1G63710.
DR   KEGG; ath:AT1G63710; -.
DR   Araport; AT1G63710; -.
DR   TAIR; AT1G63710; CYP86A7.
DR   eggNOG; KOG0157; Eukaryota.
DR   HOGENOM; CLU_001570_27_2_1; -.
DR   InParanoid; Q9CAD6; -.
DR   OMA; VLMTNEP; -.
DR   OrthoDB; 3217781at2759; -.
DR   PhylomeDB; Q9CAD6; -.
DR   BioCyc; ARA:AT1G63710-MONOMER; -.
DR   BRENDA; 1.14.14.80; 399.
DR   PRO; PR:Q9CAD6; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9CAD6; baseline and differential.
DR   Genevisible; Q9CAD6; AT.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0018685; F:alkane 1-monooxygenase activity; IDA:TAIR.
DR   GO; GO:0070330; F:aromatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0006631; P:fatty acid metabolic process; IDA:TAIR.
DR   CDD; cd11064; CYP86A; 1.
DR   Gene3D; 1.10.630.10; Cytochrome P450; 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   PANTHER; PTHR24296; CYTOCHROME P450; 1.
DR   PANTHER; PTHR24296:SF277; CYTOCHROME P450 86A7; 1.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00463; EP450I.
DR   PRINTS; PR00385; P450.
DR   SUPFAM; SSF48264; Cytochrome P450; 1.
DR   PROSITE; PS00086; CYTOCHROME_P450; 1.
PE   2: Evidence at transcript level;
KW   Heme; Iron; Membrane; Metal-binding; Monooxygenase; Oxidoreductase;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..523
FT                   /note="Cytochrome P450 86A7"
FT                   /id="PRO_0000424613"
FT   TRANSMEM        3..23
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         455
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        273
FT                   /note="E -> G (in Ref. 3; AAM65207)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        308
FT                   /note="D -> N (in Ref. 3; AAM65207)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   523 AA;  60352 MW;  D5BCE880388F6B22 CRC64;
     MDGSTAAIIL TLIVTYIIWF VSLRRSYKGP RVWPLVGSLP ALITNAHRMH DFIADNLRMC
     GGTYQTCIFP IPFLAKKQGH VTVTCDPKNL EHILKTRFDN YPKGPSWQSV FHDLLGDGIF
     NSDGDTWRFQ RKTAALEFTT RTLRQAMARW VDRAIKNRLV PILESARSRA EPIDLQDVLL
     RLTFDNICGL TFGKDPRTLS PEFPENGFAV AFDGATEATL QRFIMPEFIW KIRKWLRLGL
     EDDMSRSISH VDNYLSEIIN TRKLELLGQQ QDESRHDDLL SRFMKKKESY SDKYLKYVAL
     NFILAGRDTS SVAMSWFFWL VSLNPRVEEK IINEICTILI KTRDTNVSKW TDEPLTFDEI
     DQLVYLKAAL SETLRLYPSV PEDSKFVVAN DVLPDGTFVP SGSNVTYSIY SVGRMKFIWG
     EDCLEFKPER WLEESRDEKC NQYKFVAFNA GPRICLGKDL AYLQMKSITA SILLRHRLTV
     APGHRVEQKM SLTLFMKFGL KMDVHKRDLT LPVEKVVNEM RKK
//
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