Protein-S-isoprenylcysteine O-methyltransferase

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Q9EQK7 (ICMT_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 86. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	283 AA.
Sequence status	Complete.
Protein existence	Evidence 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 isoprenylcysteine O-methyltransferase family.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum Membrane
Domain	Transmembrane Transmembrane helix
Ligand	S-adenosyl-L-methionine
Molecular function	Methyltransferase Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	in utero embryonic development Inferred from mutant phenotype PubMed 11121396 PubMed 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 regulation of Ras protein signal transduction Inferred from genetic interaction PubMed 14966563. Source: MGI
Cellular_component	endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	cAMP 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 10747846 PubMed 11121396. Source: MGI
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 283

283

Protein-S-isoprenylcysteine O-methyltransferase

PRO_0000209895

Regions

Topological domain

1 – 15

Cytoplasmic Potential

Transmembrane

16 – 32

Helical; Potential

Topological domain

33 – 40

Lumenal Potential

Transmembrane

41 – 58

Helical; Potential

Topological domain

59 – 68

Cytoplasmic Potential

Transmembrane

69 – 86

Helical; Potential

Topological domain

87 – 91

Lumenal Potential

Transmembrane

92 – 111

Helical; Potential

Topological domain

112 – 130

Cytoplasmic Potential

Transmembrane

131 – 148

Helical; Potential

Topological domain

149 – 153

Lumenal Potential

Transmembrane

154 – 173

Helical; Potential

Topological domain

174 – 211

Cytoplasmic Potential

Transmembrane

212 – 227

Helical; Potential

Topological domain

228

Lumenal Potential

Transmembrane

229 – 243

Helical; Potential

Topological domain

244 – 283

Cytoplasmic Potential

Experimental info

Sequence conflict

A → D in AA022288. Ref.2

Sequence conflict

G → A Ref.2

Sequences

Sequence

Length

Mass (Da)

Tools

Q9EQK7 [UniParc].

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

FASTA

283

31,790

        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. 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.
IPI	IPI00457544.
RefSeq	NP_598549.1. NM_133788.2.
UniGene	Mm.277464.
3D structure databases
ProteinModelPortal	Q9EQK7.
SMR	Q9EQK7. Positions 181-274.
ModBase	Search...
PTM databases
PhosphoSite	Q9EQK7.
Proteomic databases
PaxDb	Q9EQK7.
PRIDE	Q9EQK7.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	57295.
KEGG	mmu:57295.
Organism-specific databases
CTD	23463.
MGI	MGI:1888594. Icmt.
Phylogenomic databases
eggNOG	COG2020.
HOVERGEN	HBG019034.
InParanoid	Q9EQK7.
KO	K00587.
OrthoDB	EOG4NZTTX.
Enzyme and pathway databases
SABIO-RK	Q9EQK7.
Gene expression databases
CleanEx	MM_ICMT.
Genevestigator	Q9EQK7.
GermOnline	ENSMUSG00000039662. Mus musculus.
Family and domain databases
InterPro	IPR007269. ICMT_MeTrfase. IPR025770. PPMT_MeTrfase. [Graphical view]
Pfam	PF04140. ICMT. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	313651.
SOURCE	Search...

Entry information

Entry name

ICMT_MOUSE

Accession

Primary (citable) accession number: Q9EQK7

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 20, 2001
Last sequence update:	June 20, 2001
Last modified:	May 1, 2013
This is version 86 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

MGD cross-references

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

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents