C86A2_ARATH
ID C86A2_ARATH Reviewed; 553 AA.
AC O23066; Q8S9L1;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Cytochrome P450 86A2;
DE EC=1.14.14.1;
DE AltName: Full=Protein ABERRANT INDUCTION OF TYPE THREE 1;
GN Name=CYP86A2; Synonyms=ATT1; OrderedLocusNames=At4g00360;
GN ORFNames=A_IG005I10.21, F5I10.21;
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 [GENOMIC DNA].
RC STRAIN=cv. Columbia;
RA Andrews S.;
RL Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [3]
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 [4]
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).
RN [5]
RP FUNCTION, MUTAGENESIS OF ARG-309, AND DISRUPTION PHENOTYPE.
RX PubMed=15241470; DOI=10.1038/sj.emboj.7600290;
RA Xiao F., Goodwin S.M., Xiao Y., Sun Z., Baker D., Tang X., Jenks M.A.,
RA Zhou J.M.;
RT "Arabidopsis CYP86A2 represses Pseudomonas syringae type III genes and is
RT required for cuticle development.";
RL EMBO J. 23:2903-2913(2004).
RN [6]
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 [7]
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 [8]
RP DEVELOPMENTAL STAGE.
RX PubMed=18179651; DOI=10.1111/j.1365-313x.2007.03348.x;
RA Molina I., Ohlrogge J.B., Pollard M.;
RT "Deposition and localization of lipid polyester in developing seeds of
RT Brassica napus and Arabidopsis thaliana.";
RL Plant J. 53:437-449(2008).
RN [9]
RP TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=19704826; DOI=10.4161/psb.3.9.5820;
RA Francia P., Simoni L., Cominelli E., Tonelli C., Galbiati M.;
RT "Gene trap-based identification of a guard cell promoter in Arabidopsis.";
RL Plant Signal. Behav. 3:684-686(2008).
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. Plays a major role in the biosynthesis of
CC extracellular lipids. Involved in the biosynthesis of hydroxylated
CC fatty acids required for cutin biosynthesis, cuticle development and
CC repression of bacterial type III gene expression.
CC {ECO:0000269|PubMed:15241470, 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 leaves, stems, flowers and siliques.
CC Expressed at low levels in roots. Expressed in guard cells of
CC cotyledons and leaves. {ECO:0000269|PubMed:15709153,
CC ECO:0000269|PubMed:19704826}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the seed coat inner integument layer
CC facing the endosperm in the stages from globular to torpedo embryo.
CC {ECO:0000269|PubMed:18179651}.
CC -!- INDUCTION: By abscisic acid (ABA), auxin, wounding and drought, and in
CC etiolated and dark-adapted seedlings. {ECO:0000269|PubMed:15709153,
CC ECO:0000269|PubMed:19704826}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but mutant plants have reduced content of cutin, loose
CC cuticle membrane ultrastructure, show increased permeability to water
CC vapor and display enhanced disease severity to a virulent strain of the
CC bacterial pathogen P.syringae. {ECO:0000269|PubMed:15241470}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; AF013293; AAB62843.1; -; Genomic_DNA.
DR EMBL; AF195115; AAF02801.1; -; Genomic_DNA.
DR EMBL; AL161471; CAB80794.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE81869.1; -; Genomic_DNA.
DR EMBL; AY074851; AAL75903.1; -; mRNA.
DR EMBL; AY133539; AAM91369.1; -; mRNA.
DR PIR; T01535; T01535.
DR RefSeq; NP_191946.1; NM_116260.4.
DR AlphaFoldDB; O23066; -.
DR SMR; O23066; -.
DR BioGRID; 13310; 1.
DR IntAct; O23066; 1.
DR STRING; 3702.AT4G00360.1; -.
DR PaxDb; O23066; -.
DR PRIDE; O23066; -.
DR ProteomicsDB; 240536; -.
DR EnsemblPlants; AT4G00360.1; AT4G00360.1; AT4G00360.
DR GeneID; 828019; -.
DR Gramene; AT4G00360.1; AT4G00360.1; AT4G00360.
DR KEGG; ath:AT4G00360; -.
DR Araport; AT4G00360; -.
DR TAIR; locus:2126051; AT4G00360.
DR eggNOG; KOG0157; Eukaryota.
DR HOGENOM; CLU_001570_27_2_1; -.
DR InParanoid; O23066; -.
DR OMA; NTRILWK; -.
DR OrthoDB; 1247045at2759; -.
DR PhylomeDB; O23066; -.
DR BRENDA; 1.14.14.80; 399.
DR PRO; PR:O23066; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; O23066; baseline and differential.
DR Genevisible; O23066; 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:0006952; P:defense response; IEA:UniProtKB-KW.
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 Plant defense; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..553
FT /note="Cytochrome P450 86A2"
FT /id="PRO_0000052176"
FT TRANSMEM 2..20
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 459
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 MUTAGEN 309
FT /note="R->C: In cyp86a2-1; reduction of fatty acids in the
FT cuticle membrane."
FT /evidence="ECO:0000269|PubMed:15241470"
FT CONFLICT 489
FT /note="K -> E (in Ref. 4; AAM91369/AAL75903)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 553 AA; 62530 MW; 11802EDC325DBCB6 CRC64;
MDVSNTMLLV AVVAAYWLWF QRISRWLKGP RVWPVLGSLP GLIEQRDRMH DWITENLRAC
GGTYQTCICA VPFLAKKQGL VTVTCDPKNI EHMLKTRFDN YPKGPTWQAV FHDFLGQGIF
NSDGDTWLFQ RKTAALEFTT RTLRQAMGRW VNRGIKLRFC PILETAQNNY EPVDLQDLIL
RLTFDNICGL AFGKDTRTCA PGLPENGFAS AFDRATEASL QRFILPEFLW RLKKWLGLGL
EVSLSRSLGE IDGYLDAVIN TRKQELLSQR ESGVQRHDDL LSRFMKKKDQ SYSETFLRHV
ALNFILAGRD TSSVALSWFF WLITTHPTVE DKIVREICSV LIETRGTDVS SWTAEPLEFD
EVDRLVYLKA ALSETLRLYP SVPEDSKHVV NDDILPDGTF VPAGSSVTYS IYAAGRMKST
WGEDCLEFKP ERWISPDDGK FVNHDQYRFV AFNAGPRICL GKDLAYLQMK TIAAAVLLRH
RLTVAPGHKV EQKMSLTLFM KNGLLVNVHK RDLEVMMKSL VPKERNDVVV LNGKCNGGIG
EGVAVNAAVA VAV
