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C82C3_ARATH
ID   C82C3_ARATH             Reviewed;         512 AA.
AC   O49396;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 3.
DT   03-AUG-2022, entry version 139.
DE   RecName: Full=Cytochrome P450 82C3;
DE            EC=1.14.-.-;
GN   Name=CYP82C3; OrderedLocusNames=At4g31950; ORFNames=F10N7.240;
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=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   [2]
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   [3]
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   [4]
RP   INDUCTION.
RX   PubMed=21315474; DOI=10.1016/j.jplph.2010.11.020;
RA   Murgia I., Tarantino D., Soave C., Morandini P.;
RT   "Arabidopsis CYP82C4 expression is dependent on Fe availability and
RT   circadian rhythm, and correlates with genes involved in the early Fe
RT   deficiency response.";
RL   J. Plant Physiol. 168:894-902(2011).
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   -!- INDUCTION: By iron deficiency. {ECO:0000269|PubMed:21315474}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; AL021636; CAA16594.2; -; Genomic_DNA.
DR   EMBL; AL161580; CAB79913.1; -; Genomic_DNA.
DR   EMBL; CP002687; AEE85982.1; -; Genomic_DNA.
DR   EMBL; AY142533; AAN13076.1; -; mRNA.
DR   PIR; H85374; H85374.
DR   PIR; T04650; T04650.
DR   RefSeq; NP_194923.1; NM_119346.3.
DR   AlphaFoldDB; O49396; -.
DR   SMR; O49396; -.
DR   BioGRID; 14611; 1.
DR   IntAct; O49396; 1.
DR   STRING; 3702.AT4G31950.1; -.
DR   PaxDb; O49396; -.
DR   PRIDE; O49396; -.
DR   ProteomicsDB; 240306; -.
DR   EnsemblPlants; AT4G31950.1; AT4G31950.1; AT4G31950.
DR   GeneID; 829325; -.
DR   Gramene; AT4G31950.1; AT4G31950.1; AT4G31950.
DR   KEGG; ath:AT4G31950; -.
DR   Araport; AT4G31950; -.
DR   TAIR; locus:2116622; AT4G31950.
DR   eggNOG; KOG0156; Eukaryota.
DR   HOGENOM; CLU_001570_4_0_1; -.
DR   InParanoid; O49396; -.
DR   OMA; KCASEID; -.
DR   OrthoDB; 702827at2759; -.
DR   PhylomeDB; O49396; -.
DR   PRO; PR:O49396; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; O49396; baseline and differential.
DR   Genevisible; O49396; AT.
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:0098542; P:defense response to other organism; IBA:GO_Central.
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..512
FT                   /note="Cytochrome P450 82C3"
FT                   /id="PRO_0000411198"
FT   TRANSMEM        1..21
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         451
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   512 AA;  57886 MW;  72D377876AA4097E CRC64;
     MDTSLFSLFV SILVFVFIAL FKKSKKPKYV KAPAPSGAWP IIGHLHLLGG KEQLLYRTLG
     KMADHYGPAM SLRLGSSETF VGSSFEVAKD CFTVNDKALA SLMTAAAKHM GYVFWLEMRK
     IAMIELLSNR RLQMLNNVRV SEISMGVKDL YSLWVKKGGS EPVMVDLKSW LEDMIANMIM
     RMVAGKRYFG GGGAESSEHT EEARQWRKGI AKFFHLVGIF TVSDAFPKLG WLDLQGHEKE
     MKQTRRELDV ILERWIENHR QQRKVSGTKH NDSDFVDVML SLAEQGKLSH LQYDANTCIK
     TTCLALILGG SETSPSTLTW AISLLLNNKD MLKKVQDEID IHVGRDRNVE DSDIKNLVYL
     QAIIKETLRL YPAAPLLGHR EAMEDCTVAG YNVPCGTRLI VNVWKIQRDP KVYMEPNEFR
     PERFITGEAK DFDVRGQNFE LMPFGSGRRS CPGPSLAMQM LHLGLARFLH SFEVKTVLDR
     PVDMSESPGL TITKATPLEV LINPRLKREL FV
 
 
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