C94C1_ARATH
ID C94C1_ARATH Reviewed; 495 AA.
AC Q9ZUX1;
DT 19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Cytochrome P450 94C1 {ECO:0000305};
DE EC=1.14.14.49 {ECO:0000269|PubMed:22215670, ECO:0000269|PubMed:26164240};
DE AltName: Full=12-hydroxyjasmonoyl-L-amino acid 12-hydroxylase {ECO:0000303|PubMed:22215670};
GN Name=CYP94C1 {ECO:0000303|PubMed:17868380};
GN OrderedLocusNames=At2g27690 {ECO:0000312|Araport:AT2G27690};
GN ORFNames=F15K20.21;
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].
RA Civjan N.R., Duan H., Schuler M.A.;
RT "Arabidopsis CYP94B1 and CYP94C1: fatty acid hydroxylases induced by stress
RT signaling molecules.";
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Quinitio C., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF Clones.";
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, AND INDUCTION.
RX PubMed=17868380; DOI=10.1111/j.1742-4658.2007.06032.x;
RA Kandel S., Sauveplane V., Compagnon V., Franke R., Millet Y., Schreiber L.,
RA Werck-Reichhart D., Pinot F.;
RT "Characterization of a methyl jasmonate and wounding-responsive cytochrome
RT P450 of Arabidopsis thaliana catalyzing dicarboxylic fatty acid formation
RT in vitro.";
RL FEBS J. 274:5116-5127(2007).
RN [7]
RP INDUCTION BY WOUNDING.
RX PubMed=21576464; DOI=10.1073/pnas.1103542108;
RA Koo A.J., Cooke T.F., Howe G.A.;
RT "Cytochrome P450 CYP94B3 mediates catabolism and inactivation of the plant
RT hormone jasmonoyl-L-isoleucine.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:9298-9303(2011).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, INDUCTION BY WOUNDING, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=22215670; DOI=10.1074/jbc.m111.316364;
RA Heitz T., Widemann E., Lugan R., Miesch L., Ullmann P., Desaubry L.,
RA Holder E., Grausem B., Kandel S., Miesch M., Werck-Reichhart D., Pinot F.;
RT "Cytochromes P450 CYP94C1 and CYP94B3 catalyze two successive oxidation
RT steps of plant hormone jasmonoyl-isoleucine for catabolic turnover.";
RL J. Biol. Chem. 287:6296-6306(2012).
RN [9]
RP SUBCELLULAR LOCATION.
RX PubMed=25210037; DOI=10.1074/jbc.m114.603084;
RA Koo A.J., Thireault C., Zemelis S., Poudel A.N., Zhang T., Kitaoka N.,
RA Brandizzi F., Matsuura H., Howe G.A.;
RT "Endoplasmic reticulum-associated inactivation of the hormone jasmonoyl-L-
RT isoleucine by multiple members of the cytochrome P450 94 family in
RT Arabidopsis.";
RL J. Biol. Chem. 289:29728-29738(2014).
RN [10]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=26164240; DOI=10.1016/j.phytochem.2015.06.027;
RA Widemann E., Grausem B., Renault H., Pineau E., Heinrich C., Lugan R.,
RA Ullmann P., Miesch L., Aubert Y., Miesch M., Heitz T., Pinot F.;
RT "Sequential oxidation of jasmonoyl-phenylalanine and jasmonoyl-isoleucine
RT by multiple cytochrome P450 of the CYP94 family through newly identified
RT aldehyde intermediates.";
RL Phytochemistry 117:388-399(2015).
CC -!- FUNCTION: Involved in the oxidation of the plant hormone jasmonoyl-L-
CC isoleucine (JA-Ile), a bioactive phytohormone of the jasmonate-mediated
CC signaling pathway. Converts 12-hydroxy-JA-Ile (12OH-JA-Ile) to the
CC carboxy-derivative 12COOH-JA-Ile (PubMed:17868380, PubMed:22215670,
CC PubMed:26164240). Exerts negative feedback control on JA-Ile levels and
CC plays a role in attenuation of jasmonate responses (PubMed:22215670).
CC Functions also as in-chain fatty acids hydroxylase in vitro
CC (PubMed:17868380). Catalyzes the hydroxylation of 12-hydroxy-jasmonoyl-
CC L-phenylalanine (12OH-JA-Phe) in vitro. Converts 12OH-JA-Phe to the
CC carboxy-derivative 12COOH-JA-Phe (PubMed:26164240).
CC {ECO:0000269|PubMed:17868380, ECO:0000269|PubMed:22215670,
CC ECO:0000269|PubMed:26164240}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 12-hydroxyjasmonyl-L-alpha-amino acid + 2 O2 + 2 reduced
CC [NADPH--hemoprotein reductase] = a 12-hydroxy-12-oxojasmonyl-L-alpha-
CC amino acid + 3 H(+) + 3 H2O + 2 oxidized [NADPH--hemoprotein
CC reductase]; Xref=Rhea:RHEA:55056, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:138374,
CC ChEBI:CHEBI:138464; EC=1.14.14.49;
CC Evidence={ECO:0000269|PubMed:22215670, ECO:0000269|PubMed:26164240};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:Q96242};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}. Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:25210037}; Single-pass membrane protein
CC {ECO:0000255}.
CC -!- INDUCTION: Induced by methyl jasmonate and wounding.
CC {ECO:0000269|PubMed:17868380, ECO:0000269|PubMed:21576464,
CC ECO:0000269|PubMed:22215670}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but mutant plants accumulate high amounts of 12COOH-JA-Ile
CC in response to wounding. {ECO:0000269|PubMed:22215670}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; DQ201797; ABA61324.1; -; mRNA.
DR EMBL; AC005824; AAC73031.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC08026.1; -; Genomic_DNA.
DR EMBL; AF370593; AAK43912.1; -; mRNA.
DR EMBL; AF462844; AAL58931.1; -; mRNA.
DR EMBL; BT026386; ABH04493.1; -; mRNA.
DR PIR; G84675; G84675.
DR RefSeq; NP_180337.1; NM_128328.3.
DR AlphaFoldDB; Q9ZUX1; -.
DR SMR; Q9ZUX1; -.
DR STRING; 3702.AT2G27690.1; -.
DR iPTMnet; Q9ZUX1; -.
DR PaxDb; Q9ZUX1; -.
DR PRIDE; Q9ZUX1; -.
DR ProteomicsDB; 240240; -.
DR EnsemblPlants; AT2G27690.1; AT2G27690.1; AT2G27690.
DR GeneID; 817315; -.
DR Gramene; AT2G27690.1; AT2G27690.1; AT2G27690.
DR KEGG; ath:AT2G27690; -.
DR Araport; AT2G27690; -.
DR TAIR; locus:2042108; AT2G27690.
DR eggNOG; KOG0157; Eukaryota.
DR HOGENOM; CLU_001570_27_2_1; -.
DR InParanoid; Q9ZUX1; -.
DR OMA; MQIIWRL; -.
DR OrthoDB; 1247045at2759; -.
DR PhylomeDB; Q9ZUX1; -.
DR BioCyc; ARA:AT2G27690-MON; -.
DR BioCyc; MetaCyc:AT2G27690-MON; -.
DR BRENDA; 1.14.14.49; 399.
DR BRENDA; 1.14.14.80; 399.
DR PRO; PR:Q9ZUX1; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9ZUX1; baseline and differential.
DR Genevisible; Q9ZUX1; AT.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:TAIR.
DR GO; GO:0018685; F:alkane 1-monooxygenase activity; IDA:TAIR.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0009611; P:response to wounding; IEP:TAIR.
DR Gene3D; 1.10.630.10; -; 1.
DR InterPro; IPR001128; Cyt_P450.
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.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Heme; Iron; Jasmonic acid signaling pathway;
KW Membrane; Metal-binding; Monooxygenase; Oxidoreductase; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..495
FT /note="Cytochrome P450 94C1"
FT /id="PRO_0000425854"
FT TRANSMEM 2..22
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 439
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 495 AA; 56569 MW; 4D916945C7F72337 CRC64;
MLLIISFTIV SFFFIIIFSL FHLLFLQKLR YCNCEICHAY LTSSWKKDFI NLSDWYTHLL
RRSPTSTIKV HVLNSVITAN PSNVEHILKT NFHNYPKGKQ FSVILGDLLG RGIFNSDGDT
WRFQRKLASL ELGSVSVRVF AHEIVKTEIE TRLLPILTSF SDNPGSVLDL QDVFRRFSFD
TISKLSFGFD PDCLRLPFPI SEFAVAFDTA SLLSAKRALA PFPLLWKTKR LLRIGSEKKL
QESINVINRL AGDLIKQRRL TGLMGKNDLI SRFMAVVAED DDEYLRDIVV SFLLAGRDTV
AAGLTGFFWL LTRHPEVENR IREELDRVMG TGFDSVTARC DEMREMDYLH ASLYESMRLF
PPVQFDSKFA LNDDVLSDGT FVNSGTRVTY HAYAMGRMDR IWGPDYEEFK PERWLDNEGK
FRPENPVKYP VFQAGARVCI GKEMAIMEMK SIAVAIIRRF ETRVASPETT ETLRFAPGLT
ATVNGGLPVM IQERS
