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Q9FMW9 (ICMTA_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 76. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein-S-isoprenylcysteine O-methyltransferase A

Short name=AtICMTA
EC=2.1.1.100
Alternative name(s):
Isoprenylcysteine carboxylmethyltransferase A
Prenylated protein carboxyl methyltransferase A
Prenylcysteine carboxyl methyltransferase A
Short name=AtPCM
Gene names
Name:ICMTA
Synonyms:PCM, STE14, STE14A
Ordered Locus Names:At5g23320
ORF Names:MKD15.18
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length197 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the post-translational methylation of isoprenylated C-terminal cysteine residues, resulting in the modulation of the function of prenylated proteins. Involved in negative regulation of abscisic acid signaling. Carboxyl methylation is a reversible and potentially regulated step in the post-translational modification of prenylated proteins. Ref.1 Ref.2 Ref.6 Ref.8

Catalytic activity

S-adenosyl-L-methionine + protein C-terminal S-farnesyl-L-cysteine = S-adenosyl-L-homocysteine + protein C-terminal S-farnesyl-L-cysteine methyl ester.

Cofactor

Divalent cations. Probably zinc By similarity.

Enzyme regulation

Inhibited by farnesylthioacetic acid (FTAA) and N-acetyl-S-trans, trans-farnesyl-l-cysteine (AFC).

Subcellular location

Endoplasmic reticulum membrane; Multi-pass membrane protein Ref.1 Ref.7.

Tissue specificity

Expressed primarily in flowers, stems, leaves and roots. Almost not expressed in siliques. Detected in root tips and vascular tissues of roots, cotyledons, petiols, hypocotyls, filaments, pollen grains and the distal and proximal portions of the gynoecium. Ref.2 Ref.6

Induction

Not induced by abscisic acid or auxin. Ref.8

Disruption phenotype

No visible phenotype; due to redundancy with ICMTB. Icmta and icmtb double mutants have altered phyllotaxis, fasciated stems and development of axillary flowers. Ref.7

Miscellaneous

ICMTA is less widely expressed and has a lower catalytic activity than ICMTB.

Sequence similarities

Belongs to the class VI-like SAM-binding methyltransferase superfamily. Isoprenylcysteine carboxyl methyltransferase family.

Biophysicochemical properties

Kinetic parameters:

KM=22.7 µM for AFC as methyl acceptor Ref.6

KM=13.7 µM for AGGC as methyl acceptor

Vmax=5.0 pmol/min/mg enzyme toward AFC as methyl acceptor

Vmax=3.7 pmol/min/mg enzyme toward AGGC as methyl acceptor

Sequence caution

The sequence ABK28709.1 differs from that shown. Reason: Erroneous termination at position 198. Translated as stop.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 197197Protein-S-isoprenylcysteine O-methyltransferase A
PRO_0000356249

Regions

Transmembrane16 – 3621Helical; Potential
Transmembrane52 – 7221Helical; Potential
Transmembrane81 – 10121Helical; Potential
Transmembrane140 – 16021Helical; Potential

Experimental info

Mutagenesis1111N → R: No effect; when associated with R-112 and E-165. Activity increased to the level of that of ICMTB; when associated with R-112; E-165; Q-187 and R-188. Ref.7
Mutagenesis1121Y → R: No effect; when associated with R-111 and E-165. Activity increased to the level of that of ICMTB; when associated with R-111; E-165; Q-187 and R-188. Ref.7
Mutagenesis1651Q → E: No effect. No effect; when associated with R-111 and R-112. Activity increased to the level of that of ICMTB; when associated with R-111; R-112; Q-187 and R-188. Ref.7
Mutagenesis1871E → Q: Activity increased to the level of that of ICMTB; when associated with R-111; R-112; E-165 and R-188. Ref.7
Mutagenesis1881S → R: Activity increased to the level of that of ICMTB; when associated with R-111; R-112; E-165 and Q-187. Ref.7

Sequences

Sequence LengthMass (Da)Tools
Q9FMW9 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: 11ED13E628D3A47B

FASTA19722,525
        10         20         30         40         50         60 
MTEIFSDTSI RQLSQMLLSL IFFHISEYIL AITIHGASNV TLSSLLITKH YALAMLLSLL 

        70         80         90        100        110        120 
EYLTEIILFP GLKQHWWVSN FGLIMIIVGE IIRKAAIITA GRSFTHLIKI NYEEHHGLVT 

       130        140        150        160        170        180 
HGVYRLMRHP SYCGFLIWSV GTQVMLCNPV SAVAFAVVVW RFFAQRIPYE EYFLNQFFGV 

       190 
QYLEYAESVA SGVPFVN 

« Hide

References

« Hide 'large scale' references
[1]"Carboxyl-methylation of prenylated calmodulin CaM53 is required for efficient plasma membrane targeting of the protein."
Rodriguez-Concepcion M., Toledo-Ortiz G., Yalovsky S., Caldelari D., Gruissem W.
Plant J. 24:775-784(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION.
[2]"Identification and functional expression in yeast of a prenylcysteine alpha-carboxyl methyltransferase gene from Arabidopsis thaliana."
Crowell D.N., Kennedy M.
Plant Mol. Biol. 45:469-476(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.
[3]"Structural analysis of Arabidopsis thaliana chromosome 5. III. Sequence features of the regions of 1,191,918 bp covered by seventeen physically assigned P1 clones."
Nakamura Y., Sato S., Kaneko T., Kotani H., Asamizu E., Miyajima N., Tabata S.
DNA Res. 4:401-414(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[4]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[5]"Simultaneous high-throughput recombinational cloning of open reading frames in closed and open configurations."
Underwood B.A., Vanderhaeghen R., Whitford R., Town C.D., Hilson P.
Plant Biotechnol. J. 4:317-324(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
[6]"Prenylcysteine alpha-carboxyl methyltransferase expression and function in Arabidopsis thaliana."
Narasimha Chary S., Bultema R.L., Packard C.E., Crowell D.N.
Plant J. 32:735-747(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY.
[7]"Functional analysis of Arabidopsis postprenylation CaaX processing enzymes and their function in subcellular protein targeting."
Bracha-Drori K., Shichrur K., Lubetzky T.C., Yalovsky S.
Plant Physiol. 148:119-131(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, MUTAGENESIS OF ASN-111; TYR-112; GLN-165; GLU-187 AND SER-188, DISRUPTION PHENOTYPE.
[8]"Isoprenylcysteine methylation and demethylation regulate abscisic acid signaling in Arabidopsis."
Huizinga D.H., Omosegbon O., Omery B., Crowell D.N.
Plant Cell 20:2714-2728(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INDUCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB007648 Genomic DNA. Translation: BAB11187.1.
CP002688 Genomic DNA. Translation: AED93151.1.
DQ446977 mRNA. Translation: ABE66176.1.
DQ653301 mRNA. Translation: ABK28709.1. Sequence problems.
RefSeqNP_197723.1. NM_122238.1.
UniGeneAt.54958.

3D structure databases

ProteinModelPortalQ9FMW9.
SMRQ9FMW9. Positions 101-185.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT5G23320.1; AT5G23320.1; AT5G23320.
GeneID832396.
KEGGath:AT5G23320.

Organism-specific databases

TAIRAT5G23320.

Phylogenomic databases

eggNOGCOG2020.
HOGENOMHOG000213961.
InParanoidQ9FMW9.
KOK00587.
OMAYCGFLIW.
PhylomeDBQ9FMW9.
ProtClustDBCLSN2686135.

Enzyme and pathway databases

BioCycARA:AT5G23320-MONOMER.
MetaCyc:AT5G23320-MONOMER.
SABIO-RKQ9FMW9.

Gene expression databases

GenevestigatorQ9FMW9.

Family and domain databases

InterProIPR007269. ICMT_MeTrfase.
IPR025770. PPMT_MeTrfase.
[Graphical view]
PfamPF04140. ICMT. 1 hit.
[Graphical view]
PROSITEPS51564. SAM_ICMT. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameICMTA_ARATH
AccessionPrimary (citable) accession number: Q9FMW9
Secondary accession number(s): A0MFH5
Entry history
Integrated into UniProtKB/Swiss-Prot: December 16, 2008
Last sequence update: March 1, 2001
Last modified: April 16, 2014
This is version 76 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names