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Protein-S-isoprenylcysteine O-methyltransferase A (AtICMTA) (EC 2.1.1.100) (Isoprenylcysteine carboxylmethyltransferase A) (Prenylated protein carboxyl methyltransferase A) (Prenylcysteine carboxyl methyltransferase A) (AtPCM)

 ICMTA_ARATH             Reviewed;         197 AA.
Q9FMW9; A0MFH5;
16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
01-MAR-2001, sequence version 1.
23-MAY-2018, entry version 97.
RecName: Full=Protein-S-isoprenylcysteine O-methyltransferase A;
Short=AtICMTA;
EC=2.1.1.100;
AltName: Full=Isoprenylcysteine carboxylmethyltransferase A;
AltName: Full=Prenylated protein carboxyl methyltransferase A;
AltName: Full=Prenylcysteine carboxyl methyltransferase A;
Short=AtPCM;
Name=ICMTA; Synonyms=PCM, STE14, STE14A; OrderedLocusNames=At5g23320;
ORFNames=MKD15.18;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=11135111; DOI=10.1046/j.1365-313x.2000.00924.x;
Rodriguez-Concepcion M., Toledo-Ortiz G., Yalovsky S., Caldelari D.,
Gruissem W.;
"Carboxyl-methylation of prenylated calmodulin CaM53 is required for
efficient plasma membrane targeting of the protein.";
Plant J. 24:775-784(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
PubMed=11352465; DOI=10.1023/A:1010671202925;
Crowell D.N., Kennedy M.;
"Identification and functional expression in yeast of a prenylcysteine
alpha-carboxyl methyltransferase gene from Arabidopsis thaliana.";
Plant Mol. Biol. 45:469-476(2001).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=9501997; DOI=10.1093/dnares/4.6.401;
Nakamura Y., Sato S., Kaneko T., Kotani H., Asamizu E., Miyajima N.,
Tabata S.;
"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.";
DNA Res. 4:401-414(1997).
[4]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=17147637; DOI=10.1111/j.1467-7652.2006.00183.x;
Underwood B.A., Vanderhaeghen R., Whitford R., Town C.D., Hilson P.;
"Simultaneous high-throughput recombinational cloning of open reading
frames in closed and open configurations.";
Plant Biotechnol. J. 4:317-324(2006).
[6]
FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE SPECIFICITY.
PubMed=12472689; DOI=10.1046/j.1365-313X.2002.01463.x;
Narasimha Chary S., Bultema R.L., Packard C.E., Crowell D.N.;
"Prenylcysteine alpha-carboxyl methyltransferase expression and
function in Arabidopsis thaliana.";
Plant J. 32:735-747(2002).
[7]
SUBCELLULAR LOCATION, MUTAGENESIS OF ASN-111; TYR-112; GLN-165;
GLU-187 AND SER-188, AND DISRUPTION PHENOTYPE.
PubMed=18641086; DOI=10.1104/pp.108.120477;
Bracha-Drori K., Shichrur K., Lubetzky T.C., Yalovsky S.;
"Functional analysis of Arabidopsis postprenylation CaaX processing
enzymes and their function in subcellular protein targeting.";
Plant Physiol. 148:119-131(2008).
[8]
FUNCTION, AND INDUCTION.
PubMed=18957507; DOI=10.1105/tpc.107.053389;
Huizinga D.H., Omosegbon O., Omery B., Crowell D.N.;
"Isoprenylcysteine methylation and demethylation regulate abscisic
acid signaling in Arabidopsis.";
Plant Cell 20:2714-2728(2008).
-!- 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.
{ECO:0000269|PubMed:11135111, ECO:0000269|PubMed:11352465,
ECO:0000269|PubMed:12472689, ECO:0000269|PubMed:18957507}.
-!- 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:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
Note=Divalent metal cations. Probably Zn(2+). {ECO:0000250};
-!- ENZYME REGULATION: Inhibited by farnesylthioacetic acid (FTAA) and
N-acetyl-S-trans, trans-farnesyl-l-cysteine (AFC).
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=22.7 uM for AFC as methyl acceptor
{ECO:0000269|PubMed:12472689};
KM=13.7 uM for AGGC as methyl acceptor
{ECO:0000269|PubMed:12472689};
Vmax=5.0 pmol/min/mg enzyme toward AFC as methyl acceptor
{ECO:0000269|PubMed:12472689};
Vmax=3.7 pmol/min/mg enzyme toward AGGC as methyl acceptor
{ECO:0000269|PubMed:12472689};
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
{ECO:0000269|PubMed:11135111, ECO:0000269|PubMed:18641086}; Multi-
pass membrane protein {ECO:0000269|PubMed:11135111,
ECO:0000269|PubMed:18641086}.
-!- 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. {ECO:0000269|PubMed:11352465,
ECO:0000269|PubMed:12472689}.
-!- INDUCTION: Not induced by abscisic acid or auxin.
{ECO:0000269|PubMed:18957507}.
-!- 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.
{ECO:0000269|PubMed:18641086}.
-!- MISCELLANEOUS: ICMTA is less widely expressed and has a lower
catalytic activity than ICMTB.
-!- SIMILARITY: Belongs to the class VI-like SAM-binding
methyltransferase superfamily. Isoprenylcysteine carboxyl
methyltransferase family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=ABK28709.1; Type=Erroneous termination; Positions=198; Note=Translated as stop.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AB007648; BAB11187.1; -; Genomic_DNA.
EMBL; CP002688; AED93151.1; -; Genomic_DNA.
EMBL; DQ446977; ABE66176.1; -; mRNA.
EMBL; DQ653301; ABK28709.1; ALT_SEQ; mRNA.
RefSeq; NP_197723.1; NM_122238.2.
UniGene; At.54958; -.
ProteinModelPortal; Q9FMW9; -.
SMR; Q9FMW9; -.
BioGrid; 17671; 2.
STRING; 3702.AT5G23320.1; -.
PaxDb; Q9FMW9; -.
PRIDE; Q9FMW9; -.
EnsemblPlants; AT5G23320.1; AT5G23320.1; AT5G23320.
GeneID; 832396; -.
Gramene; AT5G23320.1; AT5G23320.1; AT5G23320.
KEGG; ath:AT5G23320; -.
Araport; AT5G23320; -.
TAIR; locus:2166963; AT5G23320.
eggNOG; KOG2628; Eukaryota.
eggNOG; COG2020; LUCA.
HOGENOM; HOG000213961; -.
InParanoid; Q9FMW9; -.
KO; K00587; -.
OMA; FRTIAMY; -.
OrthoDB; EOG09360MH5; -.
PhylomeDB; Q9FMW9; -.
BioCyc; MetaCyc:AT5G23320-MONOMER; -.
Reactome; R-ATH-163841; Gamma carboxylation, hypusine formation and arylsulfatase activation.
SABIO-RK; Q9FMW9; -.
PRO; PR:Q9FMW9; -.
Proteomes; UP000006548; Chromosome 5.
ExpressionAtlas; Q9FMW9; baseline and differential.
Genevisible; Q9FMW9; AT.
GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0010340; F:carboxyl-O-methyltransferase activity; IMP:TAIR.
GO; GO:0004671; F:protein C-terminal S-isoprenylcysteine carboxyl O-methyltransferase activity; IDA:TAIR.
GO; GO:0006481; P:C-terminal protein methylation; IDA:TAIR.
GO; GO:0009908; P:flower development; IMP:TAIR.
GO; GO:0009788; P:negative regulation of abscisic acid-activated signaling pathway; NAS:TAIR.
GO; GO:0048367; P:shoot system development; IMP:TAIR.
InterPro; IPR007269; ICMT_MeTrfase.
InterPro; IPR025770; PPMT_MeTrfase.
Pfam; PF04140; ICMT; 1.
PROSITE; PS51564; SAM_ICMT; 1.
1: Evidence at protein level;
Complete proteome; Endoplasmic reticulum; Membrane; Methyltransferase;
Reference proteome; S-adenosyl-L-methionine; Transferase;
Transmembrane; Transmembrane helix.
CHAIN 1 197 Protein-S-isoprenylcysteine O-
methyltransferase A.
/FTId=PRO_0000356249.
TRANSMEM 16 36 Helical. {ECO:0000255}.
TRANSMEM 52 72 Helical. {ECO:0000255}.
TRANSMEM 81 101 Helical. {ECO:0000255}.
TRANSMEM 140 160 Helical. {ECO:0000255}.
MUTAGEN 111 111 N->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.
{ECO:0000269|PubMed:18641086}.
MUTAGEN 112 112 Y->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.
{ECO:0000269|PubMed:18641086}.
MUTAGEN 165 165 Q->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. {ECO:0000269|PubMed:18641086}.
MUTAGEN 187 187 E->Q: Activity increased to the level of
that of ICMTB; when associated with R-
111; R-112; E-165 and R-188.
{ECO:0000269|PubMed:18641086}.
MUTAGEN 188 188 S->R: Activity increased to the level of
that of ICMTB; when associated with R-
111; R-112; E-165 and Q-187.
{ECO:0000269|PubMed:18641086}.
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


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