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Protein-S-isoprenylcysteine O-methyltransferase (EC 2.1.1.100) (Farnesyl cysteine carboxyl methyltransferase) (FCMT) (Isoprenylcysteine carboxylmethyltransferase) (Prenylated protein carboxyl methyltransferase) (PPMT) (Prenylcysteine carboxyl methyltransferase) (pcCMT) (Fragment)

 ICMT_RAT                Reviewed;         232 AA.
Q9WVM4;
20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
01-NOV-1999, sequence version 1.
23-MAY-2018, entry version 99.
RecName: Full=Protein-S-isoprenylcysteine O-methyltransferase;
EC=2.1.1.100;
AltName: Full=Farnesyl cysteine carboxyl methyltransferase;
Short=FCMT;
AltName: Full=Isoprenylcysteine carboxylmethyltransferase;
AltName: Full=Prenylated protein carboxyl methyltransferase;
Short=PPMT;
AltName: Full=Prenylcysteine carboxyl methyltransferase;
Short=pcCMT;
Flags: Fragment;
Name=Icmt;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Sprague-Dawley; TISSUE=Olfactory bulb;
Otaki J.M., Firestein S.;
"Molecular cloning of farnesyl cysteine carboxyl methyltransferase
gene from rat olfactory bulb.";
Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
[2]
CHARACTERIZATION.
STRAIN=Sprague-Dawley;
PubMed=10441503; DOI=10.1006/bbrc.1999.0936;
Desrosiers R.R., Nguyen Q.T., Beliveau R.;
"The carboxyl methyltransferase modifying G proteins is a
metalloenzyme.";
Biochem. Biophys. Res. Commun. 261:790-797(1999).
-!- FUNCTION: Catalyzes the post-translational methylation of
isoprenylated C-terminal cysteine residues.
-!- 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;
Note=Divalent metal cations. Probably Zn(2+).;
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
{ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
-!- SIMILARITY: Belongs to the class VI-like SAM-binding
methyltransferase superfamily. Isoprenylcysteine carboxyl
methyltransferase family. {ECO:0000305}.
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EMBL; AF075595; AAD42926.1; -; mRNA.
UniGene; Rn.48709; -.
SMR; Q9WVM4; -.
STRING; 10116.ENSRNOP00000014625; -.
BindingDB; Q9WVM4; -.
ChEMBL; CHEMBL2298; -.
PhosphoSitePlus; Q9WVM4; -.
PaxDb; Q9WVM4; -.
PRIDE; Q9WVM4; -.
UCSC; RGD:621618; rat.
RGD; 621618; Icmt.
eggNOG; KOG2628; Eukaryota.
eggNOG; COG2020; LUCA.
HOGENOM; HOG000213961; -.
HOVERGEN; HBG019034; -.
InParanoid; Q9WVM4; -.
PhylomeDB; Q9WVM4; -.
SABIO-RK; Q9WVM4; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0016020; C:membrane; IDA:RGD.
GO; GO:0004671; F:protein C-terminal S-isoprenylcysteine carboxyl O-methyltransferase activity; IMP:RGD.
GO; GO:0006481; P:C-terminal protein methylation; IMP:RGD.
GO; GO:0046498; P:S-adenosylhomocysteine metabolic process; IMP:RGD.
GO; GO:0046499; P:S-adenosylmethioninamine metabolic process; IMP:RGD.
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 <1 232 Protein-S-isoprenylcysteine O-
methyltransferase.
/FTId=PRO_0000209896.
TRANSMEM <1 7 Helical. {ECO:0000255}.
TOPO_DOM 8 17 Cytoplasmic. {ECO:0000255}.
TRANSMEM 18 35 Helical. {ECO:0000255}.
TOPO_DOM 36 40 Lumenal. {ECO:0000255}.
TRANSMEM 41 60 Helical. {ECO:0000255}.
TOPO_DOM 61 79 Cytoplasmic. {ECO:0000255}.
TRANSMEM 80 97 Helical. {ECO:0000255}.
TOPO_DOM 98 102 Lumenal. {ECO:0000255}.
TRANSMEM 103 122 Helical. {ECO:0000255}.
TOPO_DOM 123 160 Cytoplasmic. {ECO:0000255}.
TRANSMEM 161 176 Helical. {ECO:0000255}.
TOPO_DOM 177 177 Lumenal. {ECO:0000255}.
TRANSMEM 178 192 Helical. {ECO:0000255}.
TOPO_DOM 193 232 Cytoplasmic. {ECO:0000255}.
NON_TER 1 1
SEQUENCE 232 AA; 26661 MW; BBB6D1CC14A8704E CRC64;
ALLLLLYRPP HYQIAIRACF LGFVFGCGVL LSFSQSSWNH FGWYVCSLSL FHYSEYLVTT
VNNPKSLSLD SFLLNHSLEY TVAALSSWIE FTLENIFWPE LKQITWLSAA GLLMVIFGEC
LRKVAMFTAG SNFNHVVQSE KSDTHTLVTS GVYAWCRHPS YVGWFYWSIG TQVMLCNPIC
GVVYALTVWR FFRDRTEEEE ISLIHFFGEE YLDYKKRVPT GLPFIKGVKV GL


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