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Q9EQK7 (ICMT_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 95. 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

EC=2.1.1.100
Alternative name(s):
Isoprenylcysteine carboxylmethyltransferase
Prenylated protein carboxyl methyltransferase
Short name=PPMT
Prenylcysteine carboxyl methyltransferase
Short name=pcCMT
Gene names
Name:Icmt
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length283 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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

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.

Subcellular location

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

Tissue specificity

Highly enriched in adult cerebellum, with a low level expression in other brain regions.

Developmental stage

During cerebellar development expression was low before postnatal day P6 and dramatically increased after P12.

Sequence similarities

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

Ontologies

Keywords
   Cellular componentEndoplasmic reticulum
Membrane
   DomainTransmembrane
Transmembrane helix
   LigandS-adenosyl-L-methionine
   Molecular functionMethyltransferase
Transferase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processC-terminal protein methylation

Inferred from mutant phenotype PubMed 10747846. Source: MGI

in utero embryonic development

Inferred from mutant phenotype PubMed 11121396PubMed 12105862. Source: MGI

liver development

Inferred from mutant phenotype PubMed 12105862. Source: MGI

multicellular organism growth

Inferred from mutant phenotype PubMed 11121396. Source: MGI

positive regulation of cell proliferation

Inferred from mutant phenotype PubMed 14966563. Source: MGI

protein localization

Inferred from mutant phenotype PubMed 10747846. Source: MGI

protein methylation

Inferred from mutant phenotype PubMed 11121396. Source: MGI

regulation of RNA biosynthetic process

Inferred from mutant phenotype PubMed 14966563. Source: GOC

regulation of Ras protein signal transduction

Inferred from genetic interaction PubMed 14966563. Source: MGI

   Cellular_componentendoplasmic reticulum membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functioncAMP response element binding protein binding

Inferred from mutant phenotype PubMed 14966563. Source: MGI

protein C-terminal S-isoprenylcysteine carboxyl O-methyltransferase activity

Inferred from mutant phenotype PubMed 10747846PubMed 11121396. Source: MGI

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 283283Protein-S-isoprenylcysteine O-methyltransferase
PRO_0000209895

Regions

Topological domain1 – 1515Cytoplasmic Potential
Transmembrane16 – 3217Helical; Potential
Topological domain33 – 408Lumenal Potential
Transmembrane41 – 5818Helical; Potential
Topological domain59 – 6810Cytoplasmic Potential
Transmembrane69 – 8618Helical; Potential
Topological domain87 – 915Lumenal Potential
Transmembrane92 – 11120Helical; Potential
Topological domain112 – 13019Cytoplasmic Potential
Transmembrane131 – 14818Helical; Potential
Topological domain149 – 1535Lumenal Potential
Transmembrane154 – 17320Helical; Potential
Topological domain174 – 21138Cytoplasmic Potential
Transmembrane212 – 22716Helical; Potential
Topological domain2281Lumenal Potential
Transmembrane229 – 24315Helical; Potential
Topological domain244 – 28340Cytoplasmic Potential

Experimental info

Sequence conflict241A → D in AA022288. Ref.2
Sequence conflict421G → A Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q9EQK7 [UniParc].

Last modified June 20, 2001. Version 2.
Checksum: A6C17436EDC27F40

FASTA28331,790
        10         20         30         40         50         60 
MAAARRGSAG SEARLSLATF LLGASVLALP LLTRAGLQGR TGLALYVAGL NALLLLLYRP 

        70         80         90        100        110        120 
PRYQIAIRAC FLGFVFGCGV LLSFSQSSWN HFGWYVCSLS LFHYSEYLVT AVNNPKSLSL 

       130        140        150        160        170        180 
DSFLLNHSLE YTVAALSSWI EFTLENIFWP ELKQITWLSA TGLLMVVFGE CLRKAAMFTA 

       190        200        210        220        230        240 
GSNFNHVVQS EKSDTHTLVT SGVYAWCRHP SYVGWFYWSI GTQVMLCNPI CGVVYALTVW 

       250        260        270        280 
RFFRDRTEEE EISLIHFFGE EYLDYKKRVP TGLPFIKGVK VEL 

« Hide

References

[1]"Polyglutamine expansion down-regulates specific neuronal genes before pathologic changes in SCA1."
Lin X., Antalffy B., Kang D., Orr H.T., Zoghbi H.Y.
Nat. Neurosci. 3:157-163(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 20-283.
[2]Marra M., Hillier L., Allen M., Bowles M., Dietrich N., Dubuque T., Geisel S., Kucaba T., Lacy M., Le M., Martin J., Morris M., Schellenberg K., Steptoe M., Tan F., Underwood K., Moore B., Theising B. expand/collapse author list , Wylie T., Lennon G., Soares B., Wilson R., Waterston R.
Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-153.
Strain: C57BL/6J.
Tissue: Placenta.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF209926 mRNA. Translation: AAG48552.1.
AA022288 mRNA. No translation available.
RefSeqNP_598549.1. NM_133788.2.
UniGeneMm.277464.

3D structure databases

ProteinModelPortalQ9EQK7.
SMRQ9EQK7. Positions 153-275.
ModBaseSearch...
MobiDBSearch...

PTM databases

PhosphoSiteQ9EQK7.

Proteomic databases

PaxDbQ9EQK7.
PRIDEQ9EQK7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID57295.
KEGGmmu:57295.

Organism-specific databases

CTD23463.
MGIMGI:1888594. Icmt.

Phylogenomic databases

eggNOGCOG2020.
HOVERGENHBG019034.
InParanoidQ9EQK7.
KOK00587.
PhylomeDBQ9EQK7.

Enzyme and pathway databases

SABIO-RKQ9EQK7.

Gene expression databases

CleanExMM_ICMT.
GenevestigatorQ9EQK7.

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

NextBio313651.
PROQ9EQK7.
SOURCESearch...

Entry information

Entry nameICMT_MOUSE
AccessionPrimary (citable) accession number: Q9EQK7
Entry history
Integrated into UniProtKB/Swiss-Prot: June 20, 2001
Last sequence update: June 20, 2001
Last modified: April 16, 2014
This is version 95 of the entry and version 2 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

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot