C86A4_ARATH
ID C86A4_ARATH Reviewed; 554 AA.
AC Q9LMM1; Q8GYT6;
DT 11-DEC-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Cytochrome P450 86A4;
DE EC=1.14.14.1;
GN Name=CYP86A4; OrderedLocusNames=At1g01600; ORFNames=F22L4.14;
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].
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
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).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-549, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19959665; DOI=10.1073/pnas.0909090106;
RA Li-Beisson Y., Pollard M., Sauveplane V., Pinot F., Ohlrogge J.,
RA Beisson F.;
RT "Nanoridges that characterize the surface morphology of flowers require the
RT synthesis of cutin polyester.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:22008-22013(2009).
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. Involved in the biosynthesis of 16-hydroxypalmitate.
CC {ECO:0000269|PubMed:15709153, ECO:0000269|PubMed:17427946,
CC ECO:0000269|PubMed:19959665}.
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 abscisic acid (ABA), auxin, the etylene precursor ACC and
CC cold treatment. Down-regulated by wounding and in etiolated seedlings.
CC {ECO:0000269|PubMed:15709153}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but mutant plants have reduced content of the flower
CC polyesters 16-hydroxypalmitate, 10,16-dihydroxypalmitate and 1,16-
CC hexadecanedioate. {ECO:0000269|PubMed:19959665}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; AC061957; AAF81318.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE27310.1; -; Genomic_DNA.
DR EMBL; AK117400; BAC42067.1; -; mRNA.
DR PIR; G86146; G86146.
DR RefSeq; NP_171666.1; NM_100042.4.
DR AlphaFoldDB; Q9LMM1; -.
DR SMR; Q9LMM1; -.
DR STRING; 3702.AT1G01600.1; -.
DR iPTMnet; Q9LMM1; -.
DR PaxDb; Q9LMM1; -.
DR PRIDE; Q9LMM1; -.
DR ProteomicsDB; 240271; -.
DR EnsemblPlants; AT1G01600.1; AT1G01600.1; AT1G01600.
DR GeneID; 839347; -.
DR Gramene; AT1G01600.1; AT1G01600.1; AT1G01600.
DR KEGG; ath:AT1G01600; -.
DR Araport; AT1G01600; -.
DR TAIR; locus:2025371; AT1G01600.
DR eggNOG; KOG0157; Eukaryota.
DR HOGENOM; CLU_001570_27_2_1; -.
DR InParanoid; Q9LMM1; -.
DR OMA; THKKNAR; -.
DR OrthoDB; 1247045at2759; -.
DR PhylomeDB; Q9LMM1; -.
DR BRENDA; 1.14.14.80; 399.
DR PRO; PR:Q9LMM1; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9LMM1; baseline and differential.
DR Genevisible; Q9LMM1; 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 1: Evidence at protein level;
KW Heme; Iron; Membrane; Metal-binding; Monooxygenase; Oxidoreductase;
KW Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..554
FT /note="Cytochrome P450 86A4"
FT /id="PRO_0000424612"
FT TRANSMEM 6..23
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 461
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 MOD_RES 549
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19245862"
FT CONFLICT 515
FT /note="L -> P (in Ref. 3; BAC42067)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 554 AA; 62603 MW; DA12056093BFFDD2 CRC64;
MEISNAMLLV AIVTGYWLWF KRISRWLKGP RVWPLLGSLP GLIEQRDRMH EWITENLRAC
GGTYQTCIFA VPFLAKKQGL VTVTCDPKNL EHMLKTRFDN YPKGPTWQSV FHDLLGQGIF
NSDGDTWLFQ RKTAALEFTT RTLRQAMGRW VNRGIKLRFC PILATAQDNA EPVDLQDLIL
RLTFDNICGL AFGKDTRTCA PGLPENGFAS AFDRATEASL QRFIIPKFMW KLKKWLGLGL
EVSLSRSLGE IDEYLAAVIN TRKQELMSQQ ESGTHQRHDD LLSRFMMKKT ESYSDTFLQH
VALNFILAGR DTSSVALSWF FWLITMHPTV EDKIVREICS VLIETRGTDD VASWTEEPLG
FDEIDRLVYL KAAISETLRL YPSVPEDSKH VENDDVLPDG TFVPAGSSVT YSIYAAGRMK
STWGEDCLEF NPERWISPID GKFINHDQYR FVAFNAGPRI CLGKDLAYLQ MKTIAAAVLL
RHRLTVVPGH KVEQKMSLTL FMKNGLLVNL YKRDLQGIIK SLVVKKSDGV SNGQCNGVIG
EGVAVYLNTG VAVV
