C86A1_ARATH
ID C86A1_ARATH Reviewed; 513 AA.
AC P48422; Q8RXG6; Q9FIM3;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 27-APR-2001, sequence version 2.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Cytochrome P450 86A1;
DE EC=1.14.14.80 {ECO:0000269|PubMed:9500987};
DE AltName: Full=CYPLXXXVI;
DE AltName: Full=P450-dependent fatty acid omega-hydroxylase;
DE AltName: Full=Protein HYDROXYLASE OF ROOT SUBERIZED TISSUE;
GN Name=CYP86A1; Synonyms=CYP86, HORST; OrderedLocusNames=At5g58860;
GN ORFNames=K19M22.6;
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 [MRNA].
RC STRAIN=cv. Columbia;
RA Benveniste I., Durst F.;
RT "Cloning, sequencing and expression of CYP86, a new cytochrome P450 from
RT Arabidopsis thaliana.";
RL (er) Plant Gene Register PGR95-074(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP CHARACTERIZATION.
RX PubMed=9500987; DOI=10.1006/bbrc.1998.8156;
RA Benveniste I., Tijet N., Adas F., Philipps G., Salaun J.P., Durst F.;
RT "CYP86A1 from Arabidopsis thaliana encodes a cytochrome P450-dependent
RT fatty acid omega-hydroxylase.";
RL Biochem. Biophys. Res. Commun. 243:688-693(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10048488; DOI=10.1093/dnares/5.6.379;
RA Asamizu E., Sato S., Kaneko T., Nakamura Y., Kotani H., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VIII. Sequence
RT features of the regions of 1,081,958 bp covered by seventeen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:379-391(1998).
RN [4]
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 [5]
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 [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).
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 but not on hexadecane. {ECO:0000269|PubMed:15709153,
CC ECO:0000269|PubMed:17427946, ECO:0000269|PubMed:9500987}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an omega-methyl-long-chain fatty acid + O2 + reduced [NADPH--
CC hemoprotein reductase] = an omega-hydroxy-long-chain fatty acid +
CC H(+) + H2O + oxidized [NADPH--hemoprotein reductase];
CC Xref=Rhea:RHEA:56748, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:140991,
CC ChEBI:CHEBI:140992; EC=1.14.14.80;
CC Evidence={ECO:0000269|PubMed:9500987};
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 roots. {ECO:0000269|PubMed:15709153}.
CC -!- INDUCTION: By abscisic acid (ABA), the ethylene precursor ACC, mannitol
CC or cold treatment. Down-regulated by auxin and salicylic acid (SA).
CC {ECO:0000269|PubMed:15709153}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; X90458; CAA62082.1; -; mRNA.
DR EMBL; AB016885; BAB09631.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97111.1; -; Genomic_DNA.
DR EMBL; AY081266; AAL91155.1; -; mRNA.
DR EMBL; BT003345; AAO29963.1; -; mRNA.
DR PIR; JC5965; JC5965.
DR RefSeq; NP_200694.1; NM_125276.3.
DR AlphaFoldDB; P48422; -.
DR SMR; P48422; -.
DR STRING; 3702.AT5G58860.1; -.
DR PaxDb; P48422; -.
DR PRIDE; P48422; -.
DR ProteomicsDB; 240455; -.
DR EnsemblPlants; AT5G58860.1; AT5G58860.1; AT5G58860.
DR GeneID; 836003; -.
DR Gramene; AT5G58860.1; AT5G58860.1; AT5G58860.
DR KEGG; ath:AT5G58860; -.
DR Araport; AT5G58860; -.
DR TAIR; locus:2154558; AT5G58860.
DR eggNOG; KOG0157; Eukaryota.
DR HOGENOM; CLU_001570_27_2_1; -.
DR InParanoid; P48422; -.
DR OMA; WTPKSWT; -.
DR OrthoDB; 1247045at2759; -.
DR PhylomeDB; P48422; -.
DR BioCyc; ARA:AT5G58860-MON; -.
DR BioCyc; MetaCyc:AT5G58860-MON; -.
DR BRENDA; 1.14.14.80; 399.
DR BRENDA; 1.14.15.3; 399.
DR PRO; PR:P48422; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; P48422; baseline and differential.
DR Genevisible; P48422; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0018685; F:alkane 1-monooxygenase activity; IDA:TAIR.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0102033; F:long-chain fatty acid omega-hydroxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0006631; P:fatty acid metabolic process; IDA:TAIR.
DR GO; GO:0010345; P:suberin biosynthetic process; IMP: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; NADP; Oxidoreductase;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..513
FT /note="Cytochrome P450 86A1"
FT /id="PRO_0000052175"
FT TRANSMEM 7..27
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 456
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 335
FT /note="M -> K (in Ref. 5; AAL91155/AAO29963)"
FT /evidence="ECO:0000305"
FT CONFLICT 387..388
FT /note="DD -> EH (in Ref. 1; CAA62082 and 2; no nucleotide
FT entry)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 513 AA; 58553 MW; 441A0CB1CEDB2DB5 CRC64;
MEALNSILTG YAVAALSVYA LWFYFLSRRL TGPKVLPFVG SLPYLIANRS RIHDWIADNL
RATGGTYQTC TMVIPFVAKA QGFYTVTCHP KNVEHILKTR FDNYPKGPMW RAAFHDLLGQ
GIFNSDGDTW LMQRKTAALE FTTRTLRQAM ARWVNGTIKN RLWLILDRAV QNNKPVDLQD
LFLRLTFDNI CGLTFGKDPE TLSLDLPDNP FSVAFDTATE ATLKRLLYTG FLWRIQKAMG
IGSEDKLKKS LEVVETYMND AIDARKNSPS DDLLSRFLKK RDVNGNVLPT DVLQRIALNF
VLAGRDTSSV ALSWFFWLVM NNREVETKIV NELSMVLKET RGNDQEKWTE EPLEFDEADR
LVYLKAALAE TLRLYPSVPQ DFKYVVDDDV LPDGTFVPRG STVTYSIYSI GRMKTIWGED
CLEFRPERWL TADGERFETP KDGYKFVAFN AGPRTCLGKD LAYNQMKSVA SAVLLRYRVF
PVPGHRVEQK MSLTLFMKNG LRVYLQPRGE VLA
