C86A8_ARATH
ID C86A8_ARATH Reviewed; 537 AA.
AC O80823;
DT 11-DEC-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Cytochrome P450 86A8;
DE EC=1.14.14.1;
DE AltName: Full=Protein LACERATA;
GN Name=CYP86A8; Synonyms=LCR; OrderedLocusNames=At2g45970; ORFNames=F4I18.5;
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], FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=11493698; DOI=10.1073/pnas.171285998;
RA Wellesen K., Durst F., Pinot F., Benveniste I., Nettesheim K., Wisman E.,
RA Steiner-Lange S., Saedler H., Yephremov A.;
RT "Functional analysis of the LACERATA gene of Arabidopsis provides evidence
RT for different roles of fatty acid omega -hydroxylation in development.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:9694-9699(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(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, 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 [6]
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. May be involved in the biosynthesis of cutin in the
CC epidermis which prevents post-genital organ fusions. Hydroxylated FAs
CC may be important for trichome differentiation, establishment of apical
CC dominance and senescence. {ECO:0000269|PubMed:11493698,
CC ECO:0000269|PubMed:15709153, 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. {ECO:0000269|PubMed:15709153}.
CC -!- INDUCTION: Induced by abscisic acid (ABA) and auxin. Down-regulated by
CC wounding. {ECO:0000269|PubMed:15709153}.
CC -!- DISRUPTION PHENOTYPE: Organ fusion between rosette leaves and in
CC inflorescences. {ECO:0000269|PubMed:11493698}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; AJ301678; CAC67445.1; -; Genomic_DNA.
DR EMBL; AC004665; AAM14972.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC10625.1; -; Genomic_DNA.
DR EMBL; AY064966; AAL38383.1; -; mRNA.
DR EMBL; BT002239; AAN72250.1; -; mRNA.
DR PIR; T02450; T02450.
DR RefSeq; NP_182121.1; NM_130160.3.
DR AlphaFoldDB; O80823; -.
DR SMR; O80823; -.
DR STRING; 3702.AT2G45970.1; -.
DR PaxDb; O80823; -.
DR PRIDE; O80823; -.
DR ProteomicsDB; 223855; -.
DR EnsemblPlants; AT2G45970.1; AT2G45970.1; AT2G45970.
DR GeneID; 819205; -.
DR Gramene; AT2G45970.1; AT2G45970.1; AT2G45970.
DR KEGG; ath:AT2G45970; -.
DR Araport; AT2G45970; -.
DR TAIR; locus:2050787; AT2G45970.
DR eggNOG; KOG0157; Eukaryota.
DR HOGENOM; CLU_001570_27_2_1; -.
DR InParanoid; O80823; -.
DR OMA; FWLITQH; -.
DR OrthoDB; 1247045at2759; -.
DR PhylomeDB; O80823; -.
DR BioCyc; ARA:AT2G45970-MON; -.
DR BioCyc; MetaCyc:AT2G45970-MON; -.
DR BRENDA; 1.14.14.80; 399.
DR PRO; PR:O80823; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O80823; baseline and differential.
DR Genevisible; O80823; 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 GO; GO:0008610; P:lipid biosynthetic process; IMP:TAIR.
DR GO; GO:0010214; P:seed coat development; 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 2: Evidence at transcript level;
KW Heme; Iron; Membrane; Metal-binding; Monooxygenase; Oxidoreductase;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..537
FT /note="Cytochrome P450 86A8"
FT /id="PRO_0000424614"
FT TRANSMEM 3..23
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 458
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"
SQ SEQUENCE 537 AA; 60916 MW; 95B1A1F0F055E5D4 CRC64;
MEISTALMIL SAITAYFLWL TFISRCLKGP RVWPILGSLP GLIENCERMH DWISDNLRAC
SGTYQTCICA IPFLAKKQGL VTVTCDPRNL EHILKNRFDN YPKGPTWQAV FHDLLGQGIF
NSDGDTWLFQ RKTAALEFTT RTLRQAMARW VNRAIKLRFL PILENARLGS EPIDLQDLLL
RLTFDNICGL TFGKDPRTCA PGLPVNTFAV AFDRATEASL QRFILPEILW KFKRWLRLGL
EVSLTRSLVQ VDNYLSEIIT TRKEEMMTQH NNGKHHDDLL SRFIKKKESY SDETLQRVAL
NFILAGRDTS SVALSWFFWL ITQHPAIEDK ILREICTVLV ETRGDDVALW TDEPLSCEEL
DRLVFLKAAL SETLRLYPSV PEDSKRAVKD DVLPDGTFVP AGSSITYSIY SAGRMKSTWG
EDCLEFKPER WISQSDGGRF INHDPFKFVA FNAGPRICLG KDLAYLQMKS IASAVLLRHR
LTVVTGHKVE QKMSLTLFMK YGLLVNVHER DLTAIAADLR ECKSNVVNDG VGNGVSS
