IGMT4_ARATH
ID IGMT4_ARATH Reviewed; 373 AA.
AC Q9LPU8; A2RVV0; Q0WUM9; Q8LGI0;
DT 17-FEB-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Indole glucosinolate O-methyltransferase 4 {ECO:0000305};
DE EC=2.1.1.- {ECO:0000305};
GN Name=IGMT4 {ECO:0000305};
GN OrderedLocusNames=At1g21130 {ECO:0000312|Araport:AT1G21130};
GN ORFNames=T22I11.4 {ECO:0000312|EMBL:AAF80648.1};
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
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] (ISOFORM 1).
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RA Kim C.J., Bautista V.R., Chen H., De Los Reyes C., Wu S.Y., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP INDUCTION BY APHID.
RX PubMed=16167763; DOI=10.1094/mpmi-18-0923;
RA De Vos M., Van Oosten V.R., Van Poecke R.M., Van Pelt J.A., Pozo M.J.,
RA Mueller M.J., Buchala A.J., Metraux J.P., Van Loon L.C., Dicke M.,
RA Pieterse C.M.;
RT "Signal signature and transcriptome changes of Arabidopsis during pathogen
RT and insect attack.";
RL Mol. Plant Microbe Interact. 18:923-937(2005).
RN [7]
RP INTERACTION WITH B'GAMMA.
RX PubMed=27598402; DOI=10.1111/tpj.13326;
RA Rahikainen M., Trotta A., Alegre S., Pascual J., Vuorinen K., Overmyer K.,
RA Moffatt B., Ravanel S., Glawischnig E., Kangasjaervi S.;
RT "PP2A-B'gamma modulates foliar trans-methylation capacity and the formation
RT of 4-methoxy-indol-3-yl-methyl glucosinolate in Arabidopsis leaves.";
RL Plant J. 89:112-127(2017).
CC -!- FUNCTION: Involved in indole glucosinolate biosynthesis. Catalyzes
CC methoxylation reactions of the glucosinolate indole ring. Converts the
CC hydroxy intermediates 4-hydroxy-indol-3-yl-methylglucosinolate (4OH-
CC I3M) and 1-hydroxy-indol-3-yl-methylglucosinolate (1OH-I3M) to 4-
CC methoxy-indol-3-yl-methylglucosinolate (4MO-I3M) and 1-methoxy-indol-3-
CC yl-methylglucosinolate(1MO-I3M), respectively.
CC {ECO:0000250|UniProtKB:Q9LPU5}.
CC -!- PATHWAY: Secondary metabolite biosynthesis. {ECO:0000305}.
CC -!- SUBUNIT: Interacts with B'GAMMA. {ECO:0000269|PubMed:27598402}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9LPU8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9LPU8-2; Sequence=VSP_058103, VSP_058104;
CC -!- INDUCTION: By the green peach aphid Myzus persicae.
CC {ECO:0000269|PubMed:16167763}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. Cation-independent O-methyltransferase family.
CC {ECO:0000255|PROSITE-ProRule:PRU01020}.
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DR EMBL; AC012190; AAF80648.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE30067.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE30068.1; -; Genomic_DNA.
DR EMBL; AK227119; BAE99169.1; -; mRNA.
DR EMBL; BT030091; ABN04829.1; -; mRNA.
DR EMBL; AY084260; AAM67269.1; -; mRNA.
DR PIR; E86344; E86344.
DR RefSeq; NP_173537.1; NM_101967.4. [Q9LPU8-1]
DR RefSeq; NP_849693.1; NM_179362.1. [Q9LPU8-2]
DR AlphaFoldDB; Q9LPU8; -.
DR SMR; Q9LPU8; -.
DR IntAct; Q9LPU8; 1.
DR STRING; 3702.AT1G21130.1; -.
DR PaxDb; Q9LPU8; -.
DR PRIDE; Q9LPU8; -.
DR ProteomicsDB; 232280; -. [Q9LPU8-1]
DR EnsemblPlants; AT1G21130.1; AT1G21130.1; AT1G21130. [Q9LPU8-1]
DR EnsemblPlants; AT1G21130.2; AT1G21130.2; AT1G21130. [Q9LPU8-2]
DR GeneID; 838709; -.
DR Gramene; AT1G21130.1; AT1G21130.1; AT1G21130. [Q9LPU8-1]
DR Gramene; AT1G21130.2; AT1G21130.2; AT1G21130. [Q9LPU8-2]
DR KEGG; ath:AT1G21130; -.
DR Araport; AT1G21130; -.
DR TAIR; locus:2199582; AT1G21130.
DR eggNOG; KOG3178; Eukaryota.
DR HOGENOM; CLU_005533_12_1_1; -.
DR InParanoid; Q9LPU8; -.
DR OMA; MVKCDKF; -.
DR OrthoDB; 817726at2759; -.
DR PhylomeDB; Q9LPU8; -.
DR BioCyc; ARA:AT1G21130-MON; -.
DR PRO; PR:Q9LPU8; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9LPU8; baseline and differential.
DR GO; GO:0008171; F:O-methyltransferase activity; IBA:GO_Central.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IBA:GO_Central.
DR GO; GO:0019438; P:aromatic compound biosynthetic process; IBA:GO_Central.
DR GO; GO:0032259; P:methylation; IBA:GO_Central.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR016461; COMT-like.
DR InterPro; IPR001077; O_MeTrfase_dom.
DR InterPro; IPR012967; Plant_MeTrfase_dimerisation.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR11746; PTHR11746; 1.
DR Pfam; PF08100; Dimerisation; 1.
DR Pfam; PF00891; Methyltransf_2; 1.
DR PIRSF; PIRSF005739; O-mtase; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS51683; SAM_OMT_II; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Methyltransferase; Reference proteome;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..373
FT /note="Indole glucosinolate O-methyltransferase 4"
FT /id="PRO_0000435498"
FT ACT_SITE 278
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P28002,
FT ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 217
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P28002"
FT BINDING 240
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P28002,
FT ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 260
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P28002"
FT BINDING 261
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P28002"
FT BINDING 274
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P28002"
FT VAR_SEQ 274..296
FT /note="KRILHDWTDEDCVKILKNCWKSL -> KVSSIELITYMFWKFIHGTRTLY
FT (in isoform 2)"
FT /id="VSP_058103"
FT VAR_SEQ 297..373
FT /note="Missing (in isoform 2)"
FT /id="VSP_058104"
FT CONFLICT 107
FT /note="E -> V (in Ref. 5; AAM67269)"
FT /evidence="ECO:0000305"
FT CONFLICT 117
FT /note="E -> D (in Ref. 5; AAM67269)"
FT /evidence="ECO:0000305"
FT CONFLICT 209
FT /note="G -> D (in Ref. 5; AAM67269)"
FT /evidence="ECO:0000305"
FT CONFLICT 228
FT /note="A -> T (in Ref. 5; AAM67269)"
FT /evidence="ECO:0000305"
FT CONFLICT 265
FT /note="V -> I (in Ref. 5; AAM67269)"
FT /evidence="ECO:0000305"
FT CONFLICT 290
FT /note="K -> N (in Ref. 5; AAM67269)"
FT /evidence="ECO:0000305"
FT CONFLICT 299
FT /note="S -> N (in Ref. 5; AAM67269)"
FT /evidence="ECO:0000305"
FT CONFLICT 327
FT /note="D -> V (in Ref. 3; BAE99169)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 373 AA; 40748 MW; E21AED76ECE070AD CRC64;
MGYLLEETLS SNSKTPIVID DDNELGLMAV RLANAAAFPM VLKAALELGV FDTLYAEASR
SDSFLSPSEI ASKLPTTPRN PEAPVLLDRM LRLLASYSVV KCGKVSEGKG ERVYRAEPIC
RFFLKDNIQD IGSLASQVIV NFDSVFLNTW AQLKDVVLEG GDAFGRAHGG MKLFDYMGTD
ERFSKLFNQT GFTIAVVKKA LEVYQGFKGV NVLVDVGGGV GNTLGVVASK YPNIKGINFD
LTCALAQAPS YPGVEHVAGD MFVDVPTGDA MILKRILHDW TDEDCVKILK NCWKSLPESG
KVVVIELVTP DEAENGDINA NIAFDMDMLM FTQCSGGKER SRAEFEALAA ASGFTHCKFV
CQAYHCWIIE FCK
