Reviewed, UniProtKB/Swiss-Prot P29703 (FNTA_YEAST)

Names and origin

Protein names

Recommended name:
    Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha
    EC=2.5.1.58
    EC=2.5.1.59
Alternative name(s):
    CAAX farnesyltransferase subunit alpha
    Ras proteins prenyltransferase subunit alpha
    FTase-alpha
    Type I protein geranyl-geranyltransferase subunit alpha
      Short name=GGTase-I-alpha

Gene names

Name:	RAM2
Ordered Locus Names:	YKL019W

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	316 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Catalyzes the transfer of a farnesyl or geranyl-geranyl moiety from farnesyl or geranyl-geranyl pyrophosphate to a cysteine at the fourth position from the C-terminus of several proteins having the C-terminal sequence Cys-aliphatic-aliphatic-X. The alpha subunit is thought to participate in a stable complex with the substrate. The beta subunit binds the peptide substrate.
Catalytic activity	Farnesyl diphosphate + protein-cysteine = S-farnesyl protein + diphosphate. Geranylgeranyl diphosphate + protein-cysteine = S-geranylgeranyl-protein + diphosphate.
Subunit structure	Heterodimer of an alpha and a beta subunit.
Miscellaneous	Present with 396 molecules/cell in log phase SD medium. Ref.4
Sequence similarities	Belongs to the protein prenyltransferase subunit alpha family. Contains 5 PFTA repeats.

Ontologies

Keywords
Domain	Repeat
Molecular function	Prenyltransferase Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	peptide pheromone maturation Ref.1 Inferred from direct assay. Source: SGD protein amino acid farnesylation Inferred from direct assay. Source: SGD protein amino acid geranylgeranylation Inferred from direct assay. Source: SGD
Cellular component	CAAX-protein geranylgeranyltransferase complex Inferred from direct assay. Source: SGD protein farnesyltransferase complex Ref.1 Inferred from direct assay. Source: SGD
Molecular function	CAAX-protein geranylgeranyltransferase activity Inferred from direct assay. Source: SGD identical protein binding Inferred from physical interaction. Source: IntAct protein farnesyltransferase activity Ref.1 Inferred from direct assay. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		1	EBI-14814,EBI-14814
CAL1	P18898	3	EBI-14814,EBI-3961
RAM1	P22007	2	EBI-14814,EBI-14806

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 316	316	Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha		PRO_0000119754
Regions
	Repeat	47 – 81	35	PFTA 1
	Repeat	89 – 123	35	PFTA 2
	Repeat	125 – 159	35	PFTA 3
	Repeat	160 – 193	34	PFTA 4
	Repeat	199 – 233	35	PFTA 5

Sequences

	Sequence		Length	Mass (Da)
	P29703-1 [UniParc]. Last modified April 1, 1993. Version 1. Checksum: D828519BB9914608	FASTA	316	37,508
	10 20 30 40 50 60 MEEYDYSDVK PLPIETDLQD ELCRIMYTED YKRLMGLARA LISLNELSPR ALQLTAEIID 70 80 90 100 110 120 VAPAFYTIWN YRFNIVRHMM SESEDTVLYL NKELDWLDEV TLNNPKNYQI WSYRQSLLKL 130 140 150 160 170 180 HPSPSFKREL PILKLMIDDD SKNYHVWSYR KWCCLFFSDF QHELAYASDL IETDIYNNSA 190 200 210 220 230 240 WTHRMFYWVN AKDVISKVEL ADELQFIMDK IQLVPQNISP WTYLRGFQEL FHDRLQWDSK 250 260 270 280 290 300 VVDFATTFIG DVLSLPIGSP EDLPEIESSY ALEFLAYHWG ADPCTRDNAV KAYSLLAIKY 310 DPIRKNLWHH KINNLN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"RAM2, an essential gene of yeast, and RAM1 encode the two polypeptide components of the farnesyltransferase that prenylates a-factor and Ras proteins." He B., Chen P., Chen S.-Y., Vancura K.L., Michaelis S., Powers S. Proc. Natl. Acad. Sci. U.S.A. 88:11373-11377(1991) [PubMed: 1763050] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Complete DNA sequence of yeast chromosome XI." Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V., Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P., Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L., Daignan-Fornier B., del Rey F., Dion C. , Domdey H., Duesterhoeft A., Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H., Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L., Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M., Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H., Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J., Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H., Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J., Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S., Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F., Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R., Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W., Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M., Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C., Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H., Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L., van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S., von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M., Becker I., Mewes H.-W. Nature 369:371-378(1994) [PubMed: 8196765] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[3]	"Molecular characterization of the SPT23 gene: a dosage-dependent suppressor of Ty-induced promoter mutations from Saccharomyces cerevisiae." Burkett T.J., Garfinkel D.J. Yeast 10:81-92(1994) [PubMed: 8203154] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-110.
[4]	"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: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M88584 Genomic DNA. Translation: AAA34957.1. Z28019 Genomic DNA. Translation: CAA81854.1. L24760 Genomic DNA. Translation: AAA20574.1.
PIR	A41626.
RefSeq	NP_012906.1.
3D structure databases
SMR	P29703. Positions 4-315.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-1233N.
IntAct	P29703. 10 interactions.
STRING	P29703.
Proteomic databases
PRIDE	P29703.
Genome annotation databases
Ensembl	YKL019W; YKL019W; YKL019W; Saccharomyces cerevisiae. [Genome view]
GeneID	853849.
KEGG	sce:YKL019W.
NMPDR	fig|4932.3.peg.3891.
Organism-specific databases
CYGD	YKL019w.
SGD	S000001502. RAM2.
Phylogenomic databases
eggNOG	fuNOG08714.
HOGENOM	HBG623262.
OMA	FNNSAWN.
OrthoDB	EOG9G7DG7.
PhylomeDB	P29703.
Enzyme and pathway databases
BRENDA	2.5.1.58. 250. 2.5.1.59. 250.
Gene expression databases
ArrayExpress	P29703.
Genevestigator	P29703.
GermOnline	YKL019W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR002088. Prenyl_trans_a. IPR008940. Prenyltransferase. [Graphical view]
Gene3D	G3DSA:1.25.40.120. Prenyl_trans. 1 hit.
Pfam	PF01239. PPTA. 5 hits. [Graphical view]
PROSITE	PS51147. PFTA. 5 hits. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	975076.

Entry information

Entry name

FNTA_YEAST

Accession

Primary (citable) accession number: P29703

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1993
Last sequence update:	April 1, 1993
Last modified:	January 19, 2010
This is version 83 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)