C84A1_ARATH
ID C84A1_ARATH Reviewed; 520 AA.
AC Q42600;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Cytochrome P450 84A1;
DE EC=1.14.-.-;
DE AltName: Full=Ferulate-5-hydroxylase;
DE Short=F5H;
GN Name=CYP84A1; Synonyms=FAH1; OrderedLocusNames=At4g36220;
GN ORFNames=F23E13.110;
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 / MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=8692910; DOI=10.1073/pnas.93.14.6869;
RA Meyer K., Cusumano J.C., Somerville C.R., Chapple C.C.S.;
RT "Ferulate-5-hydroxylase from Arabidopsis thaliana defines a new family of
RT cytochrome P450-dependent monooxygenases.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:6869-6874(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=9880351; DOI=10.1104/pp.119.1.101;
RA Ruegger M., Meyer K., Cusumano J.C., Chapple C.;
RT "The regulation of ferulate-5-hydroxylase expression in Arabidopsis in the
RT context of sinapate ester biosynthesis.";
RL Plant Physiol. 119:101-110(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Can-0, cv. Cha-0, cv. Col-2, cv. Gr-5, cv. La-0, cv. Me-0,
RC cv. Nc-1, cv. Per-1, cv. Rub-1, cv. Tul-0, and cv. Yo-0;
RX PubMed=11141187; DOI=10.1093/oxfordjournals.molbev.a003714;
RA Aguade M.;
RT "Nucleotide sequence variation at two genes of the phenylpropanoid pathway,
RT the FAH1 and F3H genes, in Arabidopsis thaliana.";
RL Mol. Biol. Evol. 18:1-9(2001).
RN [4]
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 [5]
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 [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC -!- PATHWAY: Aromatic compound metabolism; phenylpropanoid biosynthesis.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; U38416; AAC49389.1; -; mRNA.
DR EMBL; AF068574; AAD11580.1; -; Genomic_DNA.
DR EMBL; AJ295566; CAC26922.1; -; Genomic_DNA.
DR EMBL; AJ295567; CAC26923.1; -; Genomic_DNA.
DR EMBL; AJ295568; CAC26924.1; -; Genomic_DNA.
DR EMBL; AJ295569; CAC26925.1; -; Genomic_DNA.
DR EMBL; AJ295570; CAC26926.1; -; Genomic_DNA.
DR EMBL; AJ295571; CAC26927.1; -; Genomic_DNA.
DR EMBL; AJ295572; CAC26928.1; -; Genomic_DNA.
DR EMBL; AJ295573; CAC26929.1; -; Genomic_DNA.
DR EMBL; AJ295574; CAC26930.1; -; Genomic_DNA.
DR EMBL; AJ295575; CAC26931.1; -; Genomic_DNA.
DR EMBL; AJ295578; CAC26934.1; -; Genomic_DNA.
DR EMBL; AJ295579; CAC26935.1; -; Genomic_DNA.
DR EMBL; AL022141; CAA18128.1; -; Genomic_DNA.
DR EMBL; AL161589; CAB80293.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE86636.1; -; Genomic_DNA.
DR PIR; T04591; T04591.
DR RefSeq; NP_195345.1; NM_119790.3.
DR AlphaFoldDB; Q42600; -.
DR SMR; Q42600; -.
DR BioGRID; 15061; 2.
DR STRING; 3702.AT4G36220.1; -.
DR iPTMnet; Q42600; -.
DR PaxDb; Q42600; -.
DR PRIDE; Q42600; -.
DR ProteomicsDB; 240307; -.
DR EnsemblPlants; AT4G36220.1; AT4G36220.1; AT4G36220.
DR GeneID; 829779; -.
DR Gramene; AT4G36220.1; AT4G36220.1; AT4G36220.
DR KEGG; ath:AT4G36220; -.
DR Araport; AT4G36220; -.
DR TAIR; locus:2122194; AT4G36220.
DR eggNOG; KOG0156; Eukaryota.
DR HOGENOM; CLU_001570_4_0_1; -.
DR InParanoid; Q42600; -.
DR OMA; AEINQTG; -.
DR OrthoDB; 702827at2759; -.
DR PhylomeDB; Q42600; -.
DR BioCyc; MetaCyc:AT4G36220-MON; -.
DR BRENDA; 1.14.14.B13; 399.
DR UniPathway; UPA00711; -.
DR PRO; PR:Q42600; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q42600; baseline and differential.
DR Genevisible; Q42600; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
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; IDA:TAIR.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR GO; GO:0009809; P:lignin biosynthetic process; IMP:TAIR.
DR GO; GO:0009699; P:phenylpropanoid biosynthetic process; TAS:TAIR.
DR GO; GO:0010224; P:response to UV-B; 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 Acetylation; Heme; Iron; Membrane; Metal-binding; Monooxygenase;
KW Oxidoreductase; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..520
FT /note="Cytochrome P450 84A1"
FT /id="PRO_0000052168"
FT TRANSMEM 12..32
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"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22223895"
SQ SEQUENCE 520 AA; 58721 MW; E812779AF5BF01BC CRC64;
MESSISQTLS KLSDPTTSLV IVVSLFIFIS FITRRRRPPY PPGPRGWPII GNMLMMDQLT
HRGLANLAKK YGGLCHLRMG FLHMYAVSSP EVARQVLQVQ DSVFSNRPAT IAISYLTYDR
ADMAFAHYGP FWRQMRKVCV MKVFSRKRAE SWASVRDEVD KMVRSVSCNV GKPINVGEQI
FALTRNITYR AAFGSACEKG QDEFIRILQE FSKLFGAFNV ADFIPYFGWI DPQGINKRLV
KARNDLDGFI DDIIDEHMKK KENQNAVDDG DVVDTDMVDD LLAFYSEEAK LVSETADLQN
SIKLTRDNIK AIIMDVMFGG TETVASAIEW ALTELLRSPE DLKRVQQELA EVVGLDRRVE
ESDIEKLTYL KCTLKETLRM HPPIPLLLHE TAEDTSIDGF FIPKKSRVMI NAFAIGRDPT
SWTDPDTFRP SRFLEPGVPD FKGSNFEFIP FGSGRRSCPG MQLGLYALDL AVAHILHCFT
WKLPDGMKPS ELDMNDVFGL TAPKATRLFA VPTTRLICAL
