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 03-AUG-2022, entry version 138.
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.AT1G63710.1; -.
DR PaxDb; Q9CAD6; -.
DR PRIDE; Q9CAD6; -.
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; locus:2026659; AT1G63710.
DR eggNOG; KOG0157; Eukaryota.
DR HOGENOM; CLU_001570_27_2_1; -.
DR InParanoid; Q9CAD6; -.
DR OMA; LTWVLNE; -.
DR OrthoDB; 1247045at2759; -.
DR PhylomeDB; Q9CAD6; -.
DR BioCyc; ARA:AT1G63710-MON; -.
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:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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 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; 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
