C7051_ARATH
ID C7051_ARATH Reviewed; 513 AA.
AC Q0WQ07; O23387;
DT 20-JUN-2018, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Cytochrome P450 705A1 {ECO:0000303|PubMed:23570231};
DE EC=1.14.-.- {ECO:0000305};
GN Name=CYP705A1 {ECO:0000303|PubMed:23570231};
GN OrderedLocusNames=At4g15330 {ECO:0000312|Araport:AT4G15330};
GN ORFNames=dl3710c {ECO:0000312|EMBL:CAB10312.1},
GN FCAALL.270 {ECO:0000312|EMBL:CAB78575.1};
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9461215; DOI=10.1038/35140;
RA Bevan M., Bancroft I., Bent E., Love K., Goodman H.M., Dean C.,
RA Bergkamp R., Dirkse W., van Staveren M., Stiekema W., Drost L., Ridley P.,
RA Hudson S.-A., Patel K., Murphy G., Piffanelli P., Wedler H., Wedler E.,
RA Wambutt R., Weitzenegger T., Pohl T., Terryn N., Gielen J., Villarroel R.,
RA De Clercq R., van Montagu M., Lecharny A., Aubourg S., Gy I., Kreis M.,
RA Lao N., Kavanagh T., Hempel S., Kotter P., Entian K.-D., Rieger M.,
RA Schaefer M., Funk B., Mueller-Auer S., Silvey M., James R., Monfort A.,
RA Pons A., Puigdomenech P., Douka A., Voukelatou E., Milioni D.,
RA Hatzopoulos P., Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A.,
RA Moores T., Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S.,
RA Ansorge W., Cooke R., Berger C., Delseny M., Voet M., Volckaert G.,
RA Mewes H.-W., Klosterman S., Schueller C., Chalwatzis N.;
RT "Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of Arabidopsis
RT thaliana.";
RL Nature 391:485-488(1998).
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;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION.
RX PubMed=23570231; DOI=10.1021/ja401535g;
RA Castillo D.A., Kolesnikova M.D., Matsuda S.P.;
RT "An effective strategy for exploring unknown metabolic pathways by genome
RT mining.";
RL J. Am. Chem. Soc. 135:5885-5894(2013).
RN [6]
RP FUNCTION, TISSUE SPECIFICITY, AND INDUCTION BY JASMONATE.
RX PubMed=25724638; DOI=10.1105/tpc.114.132209;
RA Sohrabi R., Huh J.H., Badieyan S., Rakotondraibe L.H., Kliebenstein D.J.,
RA Sobrado P., Tholl D.;
RT "In planta variation of volatile biosynthesis: an alternative biosynthetic
RT route to the formation of the pathogen-induced volatile homoterpene DMNT
RT via triterpene degradation in Arabidopsis roots.";
RL Plant Cell 27:874-890(2015).
CC -!- FUNCTION: Cleaves the arabidiol side chain at C15 to form 14-apo-
CC arabidiol and a side-chain fragment (PubMed:23570231, PubMed:25724638).
CC Involved in the biosynthesis of the volatile homoterpene (E)-4,8-
CC dimethyl-1,3,7-nonatriene (DMNT) in roots. Involved in the production
CC of DMNT by degrading the triterpene arabidiol. May be involved in the
CC defense again the fungal root pathogen Pythium irregulare by producing
CC DMNT (PubMed:25724638). {ECO:0000269|PubMed:23570231,
CC ECO:0000269|PubMed:25724638}.
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:P04798};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in root stele, root cortex, root
CC epidermis, root pericycle of the root hair zone, and quiescent center
CC at the root meristematic zone. {ECO:0000269|PubMed:25724638}.
CC -!- INDUCTION: Induced by jasmonate. {ECO:0000269|PubMed:25724638}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB10312.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB78575.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; Z97338; CAB10312.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161541; CAB78575.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE83585.1; -; Genomic_DNA.
DR EMBL; AK228903; BAF00792.1; -; mRNA.
DR PIR; F71417; F71417.
DR RefSeq; NP_193268.3; NM_117621.5.
DR AlphaFoldDB; Q0WQ07; -.
DR SMR; Q0WQ07; -.
DR STRING; 3702.AT4G15330.1; -.
DR iPTMnet; Q0WQ07; -.
DR PaxDb; Q0WQ07; -.
DR PRIDE; Q0WQ07; -.
DR ProteomicsDB; 239203; -.
DR EnsemblPlants; AT4G15330.1; AT4G15330.1; AT4G15330.
DR GeneID; 827199; -.
DR Gramene; AT4G15330.1; AT4G15330.1; AT4G15330.
DR KEGG; ath:AT4G15330; -.
DR Araport; AT4G15330; -.
DR TAIR; locus:2129980; AT4G15330.
DR eggNOG; KOG0156; Eukaryota.
DR HOGENOM; CLU_001570_4_0_1; -.
DR InParanoid; Q0WQ07; -.
DR OMA; CTIRGFY; -.
DR OrthoDB; 702827at2759; -.
DR PhylomeDB; Q0WQ07; -.
DR BioCyc; ARA:AT4G15330-MON; -.
DR BioCyc; MetaCyc:AT4G15330-MON; -.
DR PRO; PR:Q0WQ07; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q0WQ07; baseline and differential.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IDA:UniProtKB.
DR GO; GO:0016709; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen; IBA:GO_Central.
DR GO; GO:0050832; P:defense response to fungus; IDA:UniProtKB.
DR GO; GO:0046246; P:terpene biosynthetic process; IDA:UniProtKB.
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 Plant defense; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..513
FT /note="Cytochrome P450 705A1"
FT /id="PRO_0000444434"
FT TRANSMEM 9..29
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 448
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|UniProtKB:P04798"
FT CONFLICT 117
FT /note="F -> Y (in Ref. 1; CAB10312/CAB78575)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 513 AA; 58495 MW; C655CDC10E686729 CRC64;
MDAIVVDSQN CFIIILLCSF SLISYFVFFK KPKVNFDLLP SPPSLPIIGH LHLLLSTLIH
KSLQKLSSKY GPLLHLRIFN IPFILVSSDS LAYEIFRDHD VNVSSRGVGA IDESLAFGSS
GFIQAPYGDY WKFMKKLIAT KLLGPQPLVR SQDFRSEELE RFYKRLFDKA MKKESVMIHK
EASRFVNNSL YKMCTGRSFS VENNEVERIM ELTADLGALS QKFFVSKMFR KLLEKLGISL
FKTEIMVVSR RFSELVERIL IEYEEKMDGH QGTQFMDALL AAYRDENTEY KITRSHIKSL
LTEFFIGAAD ASSIAIQWAM ADIINNREIL EKLREEIDSV VGKTRLVQET DLPNLPYLQA
VVKEGLRLHP PTPLVVREFQ EGCEIGGFFV PKNTTLIVNS YAMMRDPDSW QDPDEFKPER
FLASLSREED KKEKILNFLP FGSGRRMCPG SNLGYIFVGT AIGMMVQCFD WEINGDKINM
EEATGGFLIT MAHPLTCTPI PLPRTQNSLI SHL
