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Protein

Protein-S-isoprenylcysteine O-methyltransferase

Gene

Icmt

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the post-translational methylation of isoprenylated C-terminal cysteine residues.

Catalytic activityi

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

Cofactori

Zn2+Note: Divalent metal cations. Probably Zn2+.

GO - Molecular functioni

  1. protein C-terminal S-isoprenylcysteine carboxyl O-methyltransferase activity Source: RGD

GO - Biological processi

  1. C-terminal protein methylation Source: RGD
  2. S-adenosylhomocysteine metabolic process Source: RGD
  3. S-adenosylmethioninamine metabolic process Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Ligandi

S-adenosyl-L-methionine

Enzyme and pathway databases

SABIO-RKQ9WVM4.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein-S-isoprenylcysteine O-methyltransferase (EC:2.1.1.100)
Alternative name(s):
Farnesyl cysteine carboxyl methyltransferase
Short name:
FCMT
Isoprenylcysteine carboxylmethyltransferase
Prenylated protein carboxyl methyltransferase
Short name:
PPMT
Prenylcysteine carboxyl methyltransferase
Short name:
pcCMT
Gene namesi
Name:Icmt
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Unplaced

Organism-specific databases

RGDi621618. Icmt.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei‹1 – 7›7HelicalSequence Analysis
Topological domaini8 – 1710CytoplasmicSequence Analysis
Transmembranei18 – 3518HelicalSequence AnalysisAdd
BLAST
Topological domaini36 – 405LumenalSequence Analysis
Transmembranei41 – 6020HelicalSequence AnalysisAdd
BLAST
Topological domaini61 – 7919CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei80 – 9718HelicalSequence AnalysisAdd
BLAST
Topological domaini98 – 1025LumenalSequence Analysis
Transmembranei103 – 12220HelicalSequence AnalysisAdd
BLAST
Topological domaini123 – 16038CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei161 – 17616HelicalSequence AnalysisAdd
BLAST
Topological domaini177 – 1771LumenalSequence Analysis
Transmembranei178 – 19215HelicalSequence AnalysisAdd
BLAST
Topological domaini193 – 23240CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. endoplasmic reticulum membrane Source: UniProtKB-SubCell
  2. integral component of membrane Source: UniProtKB-KW
  3. membrane Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini‹1 – 232›232Protein-S-isoprenylcysteine O-methyltransferasePRO_0000209896Add
BLAST

Proteomic databases

PRIDEiQ9WVM4.

PTM databases

PhosphoSiteiQ9WVM4.

Expressioni

Gene expression databases

GenevestigatoriQ9WVM4.

Interactioni

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG2020.
HOGENOMiHOG000213961.
HOVERGENiHBG019034.
InParanoidiQ9WVM4.
PhylomeDBiQ9WVM4.

Family and domain databases

InterProiIPR007269. ICMT_MeTrfase.
IPR025770. PPMT_MeTrfase.
[Graphical view]
PfamiPF04140. ICMT. 1 hit.
[Graphical view]
PROSITEiPS51564. SAM_ICMT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Fragment.

Q9WVM4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
ALLLLLYRPP HYQIAIRACF LGFVFGCGVL LSFSQSSWNH FGWYVCSLSL
60 70 80 90 100
FHYSEYLVTT VNNPKSLSLD SFLLNHSLEY TVAALSSWIE FTLENIFWPE
110 120 130 140 150
LKQITWLSAA GLLMVIFGEC LRKVAMFTAG SNFNHVVQSE KSDTHTLVTS
160 170 180 190 200
GVYAWCRHPS YVGWFYWSIG TQVMLCNPIC GVVYALTVWR FFRDRTEEEE
210 220 230
ISLIHFFGEE YLDYKKRVPT GLPFIKGVKV GL
Length:232
Mass (Da):26,661
Last modified:November 1, 1999 - v1
Checksum:iBBB6D1CC14A8704E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei1 – 11

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF075595 mRNA. Translation: AAD42926.1.
UniGeneiRn.48709.

Genome annotation databases

UCSCiRGD:621618. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF075595 mRNA. Translation: AAD42926.1.
UniGeneiRn.48709.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Chemistry

BindingDBiQ9WVM4.
ChEMBLiCHEMBL2298.

PTM databases

PhosphoSiteiQ9WVM4.

Proteomic databases

PRIDEiQ9WVM4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

UCSCiRGD:621618. rat.

Organism-specific databases

RGDi621618. Icmt.

Phylogenomic databases

eggNOGiCOG2020.
HOGENOMiHOG000213961.
HOVERGENiHBG019034.
InParanoidiQ9WVM4.
PhylomeDBiQ9WVM4.

Enzyme and pathway databases

SABIO-RKQ9WVM4.

Miscellaneous databases

PROiQ9WVM4.

Gene expression databases

GenevestigatoriQ9WVM4.

Family and domain databases

InterProiIPR007269. ICMT_MeTrfase.
IPR025770. PPMT_MeTrfase.
[Graphical view]
PfamiPF04140. ICMT. 1 hit.
[Graphical view]
PROSITEiPS51564. SAM_ICMT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Molecular cloning of farnesyl cysteine carboxyl methyltransferase gene from rat olfactory bulb."
    Otaki J.M., Firestein S.
    Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Sprague-Dawley.
    Tissue: Olfactory bulb.
  2. "The carboxyl methyltransferase modifying G proteins is a metalloenzyme."
    Desrosiers R.R., Nguyen Q.T., Beliveau R.
    Biochem. Biophys. Res. Commun. 261:790-797(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
    Strain: Sprague-Dawley.

Entry informationi

Entry nameiICMT_RAT
AccessioniPrimary (citable) accession number: Q9WVM4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 20, 2001
Last sequence update: November 1, 1999
Last modified: March 4, 2015
This is version 91 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.