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 27-MAR-2024, entry version 124. 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}, STE14 GN {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 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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.Q9FMW9; -. DR PaxDb; 3702-AT5G23320-1; -. 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; AT5G23320; STE14A. DR eggNOG; KOG2628; Eukaryota. DR HOGENOM; CLU_065200_0_2_1; -. DR InParanoid; Q9FMW9; -. DR OMA; FSHHIVD; -. DR PhylomeDB; Q9FMW9; -. DR BioCyc; MetaCyc:AT5G23320-MONOMER; -. DR SABIO-RK; Q9FMW9; -. DR PRO; PR:Q9FMW9; -. DR Proteomes; UP000006548; Chromosome 5. DR ExpressionAtlas; Q9FMW9; baseline and differential. DR GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. 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 Gene3D; 1.20.120.1630; -; 1. DR InterPro; IPR007269; ICMT_MeTrfase. DR InterPro; IPR025770; PPMT_MeTrfase. DR PANTHER; PTHR12714; PROTEIN-S ISOPRENYLCYSTEINE O-METHYLTRANSFERASE; 1. DR PANTHER; PTHR12714:SF9; PROTEIN-S-ISOPRENYLCYSTEINE O-METHYLTRANSFERASE; 1. DR Pfam; PF04140; ICMT; 1. DR PROSITE; PS51564; SAM_ICMT; 1. DR Genevisible; Q9FMW9; AT. 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 FT E-165. Activity increased to the level of that of ICMTB; FT when 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 FT E-165. Activity increased to the level of that of ICMTB; FT when 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 FT R-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 //