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P32584 (STE14_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 113. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:STE14
Ordered Locus Names:YDR410C
ORF Names:D9461.1
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length239 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Mediates C-terminal methylation of the isoprenylated C-terminal cysteine in A-factor mating pheromone and Ras proteins. Ref.3

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.

Subcellular location

Membrane; Multi-pass membrane protein Probable.

Miscellaneous

Present with 2690 molecules/cell in log phase SD medium.

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

Chain1 – 239239Protein-S-isoprenylcysteine O-methyltransferase
PRO_0000209899

Regions

Topological domain1 – 2323Extracellular Potential
Transmembrane24 – 4421Helical; Potential
Topological domain45 – 473Cytoplasmic Potential
Transmembrane48 – 6821Helical; Potential
Topological domain69 – 8820Extracellular Potential
Transmembrane89 – 10921Helical; Potential
Topological domain1101Cytoplasmic Potential
Transmembrane111 – 13121Helical; Potential
Topological domain132 – 18251Extracellular Potential
Transmembrane183 – 20321Helical; Potential
Topological domain204 – 23936Cytoplasmic Potential

Sequences

Sequence LengthMass (Da)Tools
P32584 [UniParc].

Last modified October 1, 1993. Version 1.
Checksum: 189829AFD0BD6BD5

FASTA23927,888
        10         20         30         40         50         60 
MHQDFQEDEH EYPDIRRNPL HEVTMTSYIL GILLGIFVGL FPQIRFKNFN LFIIALSLFH 

        70         80         90        100        110        120 
FLEYYITAKY NPLKVHSESF LLNNGKSYMA AHSFAILECL VESFLFPDLK IFSYSLATKL 

       130        140        150        160        170        180 
CTVLGCLLVI LGQYTRTIAM HTAGHSFSHI VKTKKESDHV LVKTGVYSWS RHPSYLGFFW 

       190        200        210        220        230 
WAIGTQLLLL NPLSLVIFIF VLWKFFSDRI RVEEKYLIEF FSAEYIEYKN KVGVGIPFI 

« Hide

References

« Hide 'large scale' references
[1]"The Saccharomyces cerevisiae STE14 gene encodes a methyltransferase that mediates C-terminal methylation of a-factor and RAS proteins."
Hrycyna C.A., Sapperstein S.K., Clarke S., Michaelis S.
EMBO J. 10:1699-1709(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
[2]"Isolation and DNA sequence of the STE14 gene encoding farnesyl cysteine: carboxyl methyltransferase."
Ashby M.N., Errada P.R., Boyartchuk V.L., Rine J.
Yeast 9:907-913(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
[3]"Nucleotide sequence of the yeast STE14 gene, which encodes farnesylcysteine carboxyl methyltransferase, and demonstration of its essential role in a-factor export."
Sapperstein S., Berkower C., Michaelis S.
Mol. Cell. Biol. 14:1438-1449(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE, FUNCTION.
[4]"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T. expand/collapse author list , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[5]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[6]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[7]"A global topology map of the Saccharomyces cerevisiae membrane proteome."
Kim H., Melen K., Oesterberg M., von Heijne G.
Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: TOPOLOGY [LARGE SCALE ANALYSIS].
Strain: ATCC 208353 / W303-1A.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L07952 Unassigned DNA. Translation: AAA16520.1.
L15442 Unassigned DNA. Translation: AAA16840.1.
U33007 Genomic DNA. Translation: AAB64880.1.
BK006938 Genomic DNA. Translation: DAA12252.1.
PIRS37604.
RefSeqNP_010698.1. NM_001180718.1.

3D structure databases

ProteinModelPortalP32584.
SMRP32584. Positions 144-237.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid32470. 15 interactions.
DIPDIP-2678N.
IntActP32584. 3 interactions.
MINTMINT-1651790.
STRING4932.YDR410C.

Chemistry

BindingDBP32584.
ChEMBLCHEMBL4385.

Proteomic databases

MaxQBP32584.
PaxDbP32584.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYDR410C; YDR410C; YDR410C.
GeneID852019.
KEGGsce:YDR410C.

Organism-specific databases

CYGDYDR410c.
SGDS000002818. STE14.

Phylogenomic databases

eggNOGCOG2020.
GeneTreeENSGT00390000017394.
HOGENOMHOG000213961.
KOK00587.
OMAGSAIVEC.
OrthoDBEOG7WHHPD.

Enzyme and pathway databases

BioCycYEAST:G3O-29953-MONOMER.

Gene expression databases

GenevestigatorP32584.

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

NextBio970234.
PROP32584.

Entry information

Entry nameSTE14_YEAST
AccessionPrimary (citable) accession number: P32584
Secondary accession number(s): D6VT42
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: June 11, 2014
This is version 113 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome IV

Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families