ICMTA_ARATH
ID ICMTA_ARATH Reviewed; 197 AA.
AC Q9FMW9; A0MFH5;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Protein-S-isoprenylcysteine O-methyltransferase A {ECO:0000303|PubMed:12472689};
DE Short=AtICMTA {ECO:0000303|PubMed:18641086};
DE EC=2.1.1.100 {ECO:0000269|PubMed:11135111, ECO:0000269|PubMed:11352465, ECO:0000269|PubMed:12472689};
DE AltName: Full=Isoprenylcysteine carboxylmethyltransferase A {ECO:0000303|PubMed:12472689};
DE AltName: Full=Prenylated protein carboxyl methyltransferase A {ECO:0000303|PubMed:12472689};
DE AltName: Full=Prenylcysteine carboxyl methyltransferase A {ECO:0000303|PubMed:11135111};
DE Short=AtPCM {ECO:0000303|PubMed:11135111};
GN Name=ICMTA {ECO:0000303|PubMed:18641086};
GN Synonyms=PCM {ECO:0000303|PubMed:11135111},
GN STE14 {ECO:0000303|PubMed:12472689}, STE14A {ECO:0000303|PubMed:12472689};
GN OrderedLocusNames=At5g23320 {ECO:0000312|Araport:AT5G23320};
GN ORFNames=MKD15.18 {ECO:0000312|EMBL:BAB11187.1};
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 [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR
RP LOCATION.
RX PubMed=11135111; DOI=10.1046/j.1365-313x.2000.00924.x;
RA Rodriguez-Concepcion M., Toledo-Ortiz G., Yalovsky S., Caldelari D.,
RA Gruissem W.;
RT "Carboxyl-methylation of prenylated calmodulin CaM53 is required for
RT efficient plasma membrane targeting of the protein.";
RL Plant J. 24:775-784(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND TISSUE
RP SPECIFICITY.
RX PubMed=11352465; DOI=10.1023/a:1010671202925;
RA Crowell D.N., Kennedy M.;
RT "Identification and functional expression in yeast of a prenylcysteine
RT alpha-carboxyl methyltransferase gene from Arabidopsis thaliana.";
RL Plant Mol. Biol. 45:469-476(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9501997; DOI=10.1093/dnares/4.6.401;
RA Nakamura Y., Sato S., Kaneko T., Kotani H., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. III. Sequence
RT features of the regions of 1,191,918 bp covered by seventeen physically
RT assigned P1 clones.";
RL DNA Res. 4:401-414(1997).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=17147637; DOI=10.1111/j.1467-7652.2006.00183.x;
RA Underwood B.A., Vanderhaeghen R., Whitford R., Town C.D., Hilson P.;
RT "Simultaneous high-throughput recombinational cloning of open reading
RT frames in closed and open configurations.";
RL Plant Biotechnol. J. 4:317-324(2006).
RN [6]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, CATALYTIC ACTIVITY, TISSUE
RP SPECIFICITY, AND ACTIVITY REGULATION.
RX PubMed=12472689; DOI=10.1046/j.1365-313x.2002.01463.x;
RA Narasimha Chary S., Bultema R.L., Packard C.E., Crowell D.N.;
RT "Prenylcysteine alpha-carboxyl methyltransferase expression and function in
RT Arabidopsis thaliana.";
RL Plant J. 32:735-747(2002).
RN [7]
RP SUBCELLULAR LOCATION, MUTAGENESIS OF ASN-111; TYR-112; GLN-165; GLU-187 AND
RP SER-188, AND DISRUPTION PHENOTYPE.
RX PubMed=18641086; DOI=10.1104/pp.108.120477;
RA Bracha-Drori K., Shichrur K., Lubetzky T.C., Yalovsky S.;
RT "Functional analysis of Arabidopsis postprenylation CaaX processing enzymes
RT and their function in subcellular protein targeting.";
RL Plant Physiol. 148:119-131(2008).
RN [8]
RP FUNCTION, AND INDUCTION.
RX PubMed=18957507; DOI=10.1105/tpc.107.053389;
RA Huizinga D.H., Omosegbon O., Omery B., Crowell D.N.;
RT "Isoprenylcysteine methylation and demethylation regulate abscisic acid
RT signaling in Arabidopsis.";
RL Plant Cell 20:2714-2728(2008).
CC -!- FUNCTION: Catalyzes the post-translational methylation of isoprenylated
CC C-terminal cysteine residues, resulting in the modulation of the
CC function of prenylated proteins. Involved in negative regulation of
CC abscisic acid signaling. Carboxyl methylation is a reversible and
CC potentially regulated step in the post-translational modification of
CC prenylated proteins. {ECO:0000269|PubMed:11135111,
CC ECO:0000269|PubMed:11352465, ECO:0000269|PubMed:12472689,
CC ECO:0000269|PubMed:18957507}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[protein]-C-terminal S-[(2E,6E)-farnesyl]-L-cysteine + S-
CC adenosyl-L-methionine = [protein]-C-terminal S-[(2E,6E)-farnesyl]-L-
CC cysteine methyl ester + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:21672, Rhea:RHEA-COMP:12125, Rhea:RHEA-COMP:12126,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:90510,
CC ChEBI:CHEBI:90511; EC=2.1.1.100;
CC Evidence={ECO:0000269|PubMed:11135111, ECO:0000269|PubMed:11352465,
CC ECO:0000269|PubMed:12472689};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Divalent metal cations. Probably Zn(2+). {ECO:0000250};
CC -!- ACTIVITY REGULATION: Inhibited by farnesylthioacetic acid (FTAA) and N-
CC acetyl-S-trans, trans-farnesyl-l-cysteine (AFC).
CC {ECO:0000269|PubMed:12472689}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=22.7 uM for AFC as methyl acceptor {ECO:0000269|PubMed:12472689};
CC KM=13.7 uM for AGGC as methyl acceptor {ECO:0000269|PubMed:12472689};
CC Vmax=5.0 pmol/min/mg enzyme toward AFC as methyl acceptor
CC {ECO:0000269|PubMed:12472689};
CC Vmax=3.7 pmol/min/mg enzyme toward AGGC as methyl acceptor
CC {ECO:0000269|PubMed:12472689};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:11135111, ECO:0000269|PubMed:18641086}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:11135111,
CC ECO:0000269|PubMed:18641086}.
CC -!- TISSUE SPECIFICITY: Expressed primarily in flowers, stems, leaves and
CC roots. Almost not expressed in siliques. Detected in root tips and
CC vascular tissues of roots, cotyledons, petiols, hypocotyls, filaments,
CC pollen grains and the distal and proximal portions of the gynoecium.
CC {ECO:0000269|PubMed:11352465, ECO:0000269|PubMed:12472689}.
CC -!- INDUCTION: Not induced by abscisic acid or auxin.
CC {ECO:0000269|PubMed:18957507}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype; due to redundancy with
CC ICMTB. Icmta and icmtb double mutants have altered phyllotaxis,
CC fasciated stems and development of axillary flowers.
CC {ECO:0000269|PubMed:18641086}.
CC -!- MISCELLANEOUS: ICMTA is less widely expressed and has a lower catalytic
CC activity than ICMTB.
CC -!- SIMILARITY: Belongs to the class VI-like SAM-binding methyltransferase
CC superfamily. Isoprenylcysteine carboxyl methyltransferase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABK28709.1; Type=Erroneous termination; Note=Extended C-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB007648; BAB11187.1; -; Genomic_DNA.
DR EMBL; CP002688; AED93151.1; -; Genomic_DNA.
DR EMBL; DQ446977; ABE66176.1; -; mRNA.
DR EMBL; DQ653301; ABK28709.1; ALT_SEQ; mRNA.
DR RefSeq; NP_197723.1; NM_122238.2.
DR AlphaFoldDB; Q9FMW9; -.
DR SMR; Q9FMW9; -.
DR BioGRID; 17671; 2.
DR IntAct; Q9FMW9; 1.
DR STRING; 3702.AT5G23320.1; -.
DR PaxDb; Q9FMW9; -.
DR PRIDE; Q9FMW9; -.
DR EnsemblPlants; AT5G23320.1; AT5G23320.1; AT5G23320.
DR GeneID; 832396; -.
DR Gramene; AT5G23320.1; AT5G23320.1; AT5G23320.
DR KEGG; ath:AT5G23320; -.
DR Araport; AT5G23320; -.
DR TAIR; locus:2166963; AT5G23320.
DR eggNOG; KOG2628; Eukaryota.
DR HOGENOM; CLU_065200_0_2_1; -.
DR InParanoid; Q9FMW9; -.
DR OMA; SAFHWGE; -.
DR PhylomeDB; Q9FMW9; -.
DR BioCyc; MetaCyc:AT5G23320-MON; -.
DR SABIO-RK; Q9FMW9; -.
DR PRO; PR:Q9FMW9; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FMW9; baseline and differential.
DR Genevisible; Q9FMW9; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0010340; F:carboxyl-O-methyltransferase activity; IMP:TAIR.
DR GO; GO:0004671; F:protein C-terminal S-isoprenylcysteine carboxyl O-methyltransferase activity; IDA:TAIR.
DR GO; GO:0006481; P:C-terminal protein methylation; IDA:TAIR.
DR GO; GO:0009908; P:flower development; IMP:TAIR.
DR GO; GO:0009788; P:negative regulation of abscisic acid-activated signaling pathway; NAS:TAIR.
DR GO; GO:0048367; P:shoot system development; IMP:TAIR.
DR InterPro; IPR007269; ICMT_MeTrfase.
DR InterPro; IPR025770; PPMT_MeTrfase.
DR Pfam; PF04140; ICMT; 1.
DR PROSITE; PS51564; SAM_ICMT; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Membrane; Methyltransferase; Reference proteome;
KW S-adenosyl-L-methionine; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..197
FT /note="Protein-S-isoprenylcysteine O-methyltransferase A"
FT /id="PRO_0000356249"
FT TRANSMEM 16..36
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 52..72
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 81..101
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 140..160
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 116..119
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q8TMG0"
FT BINDING 124
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q8TMG0"
FT BINDING 129..132
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q8TMG0"
FT BINDING 166
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:D6WJ77"
FT BINDING 170
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q8TMG0"
FT MUTAGEN 111
FT /note="N->R: No effect; when associated with R-112 and E-
FT 165. Activity increased to the level of that of ICMTB; when
FT associated with R-112; E-165; Q-187 and R-188."
FT /evidence="ECO:0000269|PubMed:18641086"
FT MUTAGEN 112
FT /note="Y->R: No effect; when associated with R-111 and E-
FT 165. Activity increased to the level of that of ICMTB; when
FT associated with R-111; E-165; Q-187 and R-188."
FT /evidence="ECO:0000269|PubMed:18641086"
FT MUTAGEN 165
FT /note="Q->E: No effect. No effect; when associated with R-
FT 111 and R-112. Activity increased to the level of that of
FT ICMTB; when associated with R-111; R-112; Q-187 and R-188."
FT /evidence="ECO:0000269|PubMed:18641086"
FT MUTAGEN 187
FT /note="E->Q: Activity increased to the level of that of
FT ICMTB; when associated with R-111; R-112; E-165 and R-188."
FT /evidence="ECO:0000269|PubMed:18641086"
FT MUTAGEN 188
FT /note="S->R: Activity increased to the level of that of
FT ICMTB; when associated with R-111; R-112; E-165 and Q-187."
FT /evidence="ECO:0000269|PubMed:18641086"
SQ SEQUENCE 197 AA; 22525 MW; 11ED13E628D3A47B CRC64;
MTEIFSDTSI RQLSQMLLSL IFFHISEYIL AITIHGASNV TLSSLLITKH YALAMLLSLL
EYLTEIILFP GLKQHWWVSN FGLIMIIVGE IIRKAAIITA GRSFTHLIKI NYEEHHGLVT
HGVYRLMRHP SYCGFLIWSV GTQVMLCNPV SAVAFAVVVW RFFAQRIPYE EYFLNQFFGV
QYLEYAESVA SGVPFVN
