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Q9WVM4 (ICMT_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 86. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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

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 names
Name:Icmt
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length232 AA.
Sequence statusFragment.
Protein existenceEvidence at protein level

General annotation (Comments)

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

Divalent cations. Probably zinc.

Subcellular location

Endoplasmic reticulum membrane; Multi-pass membrane protein By similarity.

Sequence similarities

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain‹1 – 232›232Protein-S-isoprenylcysteine O-methyltransferase
PRO_0000209896

Regions

Transmembrane‹1 – 7›7Helical; Potential
Topological domain8 – 1710Cytoplasmic Potential
Transmembrane18 – 3518Helical; Potential
Topological domain36 – 405Lumenal Potential
Transmembrane41 – 6020Helical; Potential
Topological domain61 – 7919Cytoplasmic Potential
Transmembrane80 – 9718Helical; Potential
Topological domain98 – 1025Lumenal Potential
Transmembrane103 – 12220Helical; Potential
Topological domain123 – 16038Cytoplasmic Potential
Transmembrane161 – 17616Helical; Potential
Topological domain1771Lumenal Potential
Transmembrane178 – 19215Helical; Potential
Topological domain193 – 23240Cytoplasmic Potential

Experimental info

Non-terminal residue11

Sequences

Sequence LengthMass (Da)Tools
Q9WVM4 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: BBB6D1CC14A8704E

FASTA23226,661
        10         20         30         40         50         60 
ALLLLLYRPP HYQIAIRACF LGFVFGCGVL LSFSQSSWNH FGWYVCSLSL FHYSEYLVTT 

        70         80         90        100        110        120 
VNNPKSLSLD SFLLNHSLEY TVAALSSWIE FTLENIFWPE LKQITWLSAA GLLMVIFGEC 

       130        140        150        160        170        180 
LRKVAMFTAG SNFNHVVQSE KSDTHTLVTS GVYAWCRHPS YVGWFYWSIG TQVMLCNPIC 

       190        200        210        220        230 
GVVYALTVWR FFRDRTEEEE ISLIHFFGEE YLDYKKRVPT GLPFIKGVKV GL 

« Hide

References

[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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF075595 mRNA. Translation: AAD42926.1.
UniGeneRn.48709.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Chemistry

ChEMBLCHEMBL2298.

PTM databases

PhosphoSiteQ9WVM4.

Proteomic databases

PRIDEQ9WVM4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

UCSCRGD:621618. rat.

Organism-specific databases

RGD621618. Icmt.

Phylogenomic databases

eggNOGCOG2020.
HOGENOMHOG000213961.
HOVERGENHBG019034.
InParanoidQ9WVM4.
PhylomeDBQ9WVM4.

Enzyme and pathway databases

SABIO-RKQ9WVM4.

Gene expression databases

GenevestigatorQ9WVM4.

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...

Other

PROQ9WVM4.

Entry information

Entry nameICMT_RAT
AccessionPrimary (citable) accession number: Q9WVM4
Entry history
Integrated into UniProtKB/Swiss-Prot: June 20, 2001
Last sequence update: November 1, 1999
Last modified: April 16, 2014
This is version 86 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families