C86B1_ARATH
ID C86B1_ARATH Reviewed; 559 AA.
AC Q9FMY1;
DT 02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Cytochrome P450 86B1;
DE EC=1.14.-.-;
GN Name=CYP86B1; OrderedLocusNames=At5g23190; ORFNames=MKD15.5;
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 [MRNA], AND SUBCELLULAR LOCATION.
RC TISSUE=Silique;
RX PubMed=11522915; DOI=10.1093/pcp/pce110;
RA Watson C.J., Froehlich J.E., Josefsson C.A., Chapple C., Durst F.,
RA Benveniste I., Coolbaugh R.C.;
RT "Localization of CYP86B1 in the outer envelope of chloroplasts.";
RL Plant Cell Physiol. 42:873-878(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9501997; DOI=10.1093/dnares/4.6.401;
RA Nakamura Y., Sato S., Kaneko T., Kotani H., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. III. Sequence
RT features of the regions of 1,191,918 bp covered by seventeen physically
RT assigned P1 clones.";
RL DNA Res. 4:401-414(1997).
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, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=19525321; DOI=10.1104/pp.109.141408;
RA Compagnon V., Diehl P., Benveniste I., Meyer D., Schaller H., Schreiber L.,
RA Franke R., Pinot F.;
RT "CYP86B1 is required for very long chain omega-hydroxyacid and alpha, omega
RT -dicarboxylic acid synthesis in root and seed suberin polyester.";
RL Plant Physiol. 150:1831-1843(2009).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19759341; DOI=10.1104/pp.109.144907;
RA Molina I., Li-Beisson Y., Beisson F., Ohlrogge J.B., Pollard M.;
RT "Identification of an Arabidopsis feruloyl-coenzyme A transferase required
RT for suberin synthesis.";
RL Plant Physiol. 151:1317-1328(2009).
CC -!- FUNCTION: Involved in very long chain fatty acids (VLCFA) omega-
CC hydroxylation. Required for the synthesis of saturated VLCFA alpha,
CC omega-bifunctional suberin monomers. {ECO:0000269|PubMed:19525321,
CC ECO:0000269|PubMed:19759341}.
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:11522915, ECO:0000269|PubMed:19525321}; Single-pass
CC membrane protein {ECO:0000269|PubMed:11522915,
CC ECO:0000269|PubMed:19525321}. Note=In vitro import assays suggest an
CC association with the outer chloroplastic membrane; also detected in the
CC chloroplasts of guard cells when expressed in a heterologous system.
CC -!- TISSUE SPECIFICITY: Expressed in roots endodermis, anthers, stigmas,
CC stomata of young pedicels of inflorescences, the placenta region of
CC siliques, at the level of the hilum in matures seeds, at the junction
CC of siliques to pedicels where abscission of floral parts takes place
CC and in nectary glands. {ECO:0000269|PubMed:19525321}.
CC -!- DISRUPTION PHENOTYPE: No visible vegetative growth phenotype. Very
CC large reduction in alpha, omega-bifunctional C22 to C24 saturated
CC suberin components in seeds. No effect on seed coat permeability.
CC {ECO:0000269|PubMed:19525321, ECO:0000269|PubMed:19759341}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; AF345898; AAK29622.1; -; mRNA.
DR EMBL; BT002045; AAN72056.1; -; mRNA.
DR EMBL; AB007648; BAB11174.1; -; Genomic_DNA.
DR EMBL; CP002688; AED93131.1; -; Genomic_DNA.
DR RefSeq; NP_197710.1; NM_122225.3.
DR AlphaFoldDB; Q9FMY1; -.
DR SMR; Q9FMY1; -.
DR STRING; 3702.AT5G23190.1; -.
DR PaxDb; Q9FMY1; -.
DR PRIDE; Q9FMY1; -.
DR ProteomicsDB; 223856; -.
DR EnsemblPlants; AT5G23190.1; AT5G23190.1; AT5G23190.
DR GeneID; 832383; -.
DR Gramene; AT5G23190.1; AT5G23190.1; AT5G23190.
DR KEGG; ath:AT5G23190; -.
DR Araport; AT5G23190; -.
DR TAIR; locus:2166786; AT5G23190.
DR eggNOG; KOG0157; Eukaryota.
DR HOGENOM; CLU_001570_27_2_1; -.
DR InParanoid; Q9FMY1; -.
DR OMA; MEMIPGP; -.
DR OrthoDB; 1247045at2759; -.
DR PhylomeDB; Q9FMY1; -.
DR BioCyc; ARA:AT5G23190-MON; -.
DR BioCyc; MetaCyc:AT5G23190-MON; -.
DR BRENDA; 1.14.15.3; 399.
DR PRO; PR:Q9FMY1; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FMY1; baseline and differential.
DR Genevisible; Q9FMY1; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0010345; P:suberin biosynthetic process; IMP:TAIR.
DR GO; GO:0042761; P:very long-chain fatty acid 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 2: Evidence at transcript level;
KW Cell wall biogenesis/degradation; Endoplasmic reticulum; Heme; Iron;
KW Membrane; Metal-binding; Monooxygenase; Oxidoreductase; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..559
FT /note="Cytochrome P450 86B1"
FT /id="PRO_0000392058"
FT TRANSMEM 31..51
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 488
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 559 AA; 64325 MW; 3564B35FE42B5EBC CRC64;
MNFNSSYNLT FNDVFFSSSS SSDPLVSRRL FLLRDVQILE LLIAIFVFVA IHALRQKKYQ
GLPVWPFLGM LPSLAFGLRG NIYEWLSDVL CLQNGTFQFR GPWFSSLNST ITCDPRNVEH
LLKNRFSVFP KGSYFRDNLR DLLGDGIFNA DDETWQRQRK TASIEFHSAK FRQLTTQSLF
ELVHKRLLPV LETSVKSSSP IDLQDVLLRL TFDNVCMIAF GVDPGCLGPD QPVIPFAKAF
EDATEAAVVR FVMPTCVWKF MRYLDIGTEK KLKESIKGVD DFADEVIRTR KKELSLEGET
TKRSDLLTVF MGLRDEKGES FSDKFLRDIC VNFILAGRDT SSVALSWFFW LLEKNPEVEE
KIMVEMCKIL RQRDDHGNAE KSDYEPVFGP EEIKKMDYLQ AALSEALRLY PSVPVDHKEV
QEDDVFPDGT MLKKGDKVIY AIYAMGRMEA IWGKDCLEFR PERWLRDGRF MSESAYKFTA
FNGGPRLCLG KDFAYYQMKS TAAAIVYRYK VKVVNGHKVE PKLALTMYMK HGLMVNLINR
SVSEIDQYYA KSFDEGYIN
