P18898 (PGTB1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Geranylgeranyl transferase type-1 subunit beta
EC=2.5.1.59

Alternative name(s):
Cell division cycle protein 43
Geranylgeranyl transferase type I subunit beta
Short name=GGTase-I-beta
RAS proteins geranylgeranyltransferase subunit beta
Type I protein geranyl-geranyltransferase subunit beta
Short name=PGGT

Gene names

Name:	CDC43
Synonyms:	CAL1
Ordered Locus Names:	YGL155W
ORF Names:	G1864

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	376 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the transfer of a geranyl-geranyl moiety from geranyl-geranyl pyrophosphate to proteins having the C-terminal sequence Cys-Ile-Ile-Leu or Cys-Val-Leu-Leu. Acts, among other substrates, on Rho1 and Rho2 and CDC42 proteins. Participates in a RAS-like C-terminal modification of proteins involved in nuclear division and bud growth. It is involved in bud positioning and cell polarity. Ref.7
Catalytic activity	Geranylgeranyl diphosphate + protein-cysteine = S-geranylgeranyl-protein + diphosphate.
Cofactor	Binds 1 zinc ion per subunit By similarity.
Subunit structure	Heterodimer of an alpha and a beta subunit.
Miscellaneous	Present with 3940 molecules/cell in log phase SD medium. Ref.8
Sequence similarities	Belongs to the protein prenyltransferase subunit beta family. Contains 4 PFTB repeats.

Ontologies

Keywords
Domain	Repeat
Ligand	Metal-binding Zinc
Molecular function	Prenyltransferase Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	cellular calcium ion homeostasis Traceable author statement. Source: SGD establishment of cell polarity Traceable author statement. Source: SGD protein geranylgeranylation Inferred from direct assay Ref.7. Source: SGD small GTPase mediated signal transduction Traceable author statement. Source: SGD
Cellular component	CAAX-protein geranylgeranyltransferase complex Inferred from direct assay. Source: SGD
Molecular function	CAAX-protein geranylgeranyltransferase activity Inferred from direct assay. Source: SGD metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
RAM2	P29703	3	EBI-3961,EBI-14814

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 376	376	Geranylgeranyl transferase type-1 subunit beta		PRO_0000119775
Regions
	Repeat	128 – 179	52	PFTB 1
	Repeat	192 – 231	40	PFTB 2
	Repeat	259 – 301	43	PFTB 3
	Repeat	310 – 353	44	PFTB 4
	Compositional bias	138 – 180	43	Cys-rich
Sites
	Metal binding	286	1	Zinc By similarity
	Metal binding	288	1	Zinc By similarity
	Metal binding	341	1	Zinc By similarity
Experimental info
	Mutagenesis	328	1	G → S: Defect in nuclear division and bud formation.

Sequences

	Sequence		Length	Mass (Da)
	P18898 [UniParc]. Last modified April 1, 1993. Version 2. Checksum: B52E56F353B3914E	FASTA	376	42,690
	10 20 30 40 50 60 MCQATNGPSR VVTKKHRKFF ERHLQLLPSS HQGHDVNRMA IIFYSISGLS IFDVNVSAKY 70 80 90 100 110 120 GDHLGWMRKH YIKTVLDDTE NTVISGFVGS LVMNIPHATT INLPNTLFAL LSMIMLRDYE 130 140 150 160 170 180 YFETILDKRS LARFVSKCQR PDRGSFVSCL DYKTNCGSSV DSDDLRFCYI AVAILYICGC 190 200 210 220 230 240 RSKEDFDEYI DTEKLLGYIM SQQCYNGAFG AHNEPHSGYT SCALSTLALL SSLEKLSDKF 250 260 270 280 290 300 KEDTITWLLH RQVSSHGCMK FESELNASYD QSDDGGFQGR ENKFADTCYA FWCLNSLHLL 310 320 330 340 350 360 TKDWKMLCQT ELVTNYLLDR TQKTLTGGFS KNDEEDADLY HSCLGSAALA LIEGKFNGEL 370 CIPQEIFNDF SKRCCF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Isolation and sequence analysis of CDC43, a gene involved in the control of cell polarity in Saccharomyces cerevisiae." Johnson D.I., O'Brien J.M., Jacobs C.W. Gene 90:93-98(1990) [PubMed: 2199333] [Abstract] Cited for: PRELIMINARY NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Isolation and sequence analysis of CDC43, a gene involved in the control of cell polarity in Saccharomyces cerevisiae." Johnson D.I., O'Brien J.M., Jacobs C.W. Gene 98:149-150(1991) [PubMed: 2013407] [Abstract] Cited for: SEQUENCE REVISION.
[3]	"Yeast CAL1 is a structural and functional homologue to the DPR1 (RAM) gene involved in ras processing." Ohya Y., Goebl M., Goodman L.E., Petersen-Bjoern S., Friesen J.D., Tamanoi F., Anraku Y. J. Biol. Chem. 266:12356-12360(1991) [PubMed: 2061313] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: A5-8-1A.
[4]	"DNA sequence analysis of a 35 kb segment from Saccharomyces cerevisiae chromosome VII reveals 19 open reading frames including RAD54, ACE1/CUP2, PMR1, RCK1, AMS1 and CAL1/CDC43." James C.M., Indge K.J., Oliver S.G. Yeast 11:1413-1419(1995) [PubMed: 8585324] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome VII." Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E. , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K. Nature 387:81-84(1997) [PubMed: 9169869] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[6]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[7]	"Protein geranylgeranyltransferase of Saccharomyces cerevisiae is specific for Cys-Xaa-Xaa-Leu motif proteins and requires the CDC43 gene product but not the DPR1 gene product." Finegold A.A., Johnson D.I., Farnsworth C.C., Gelb M.H., Judd S.R., Glomset J.A., Tamanoi F. Proc. Natl. Acad. Sci. U.S.A. 88:4448-4452(1991) [PubMed: 2034682] [Abstract] Cited for: FUNCTION.
[8]	"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	M31114 Genomic DNA. Translation: AAA34481.1. M74109 Genomic DNA. Translation: AAA34464.1. Z48618 Genomic DNA. No translation available. Z72677 Genomic DNA. Translation: CAA96867.1. BK006941 Genomic DNA. Translation: DAA07957.1.
PIR	RGBY43. A40875.
RefSeq	NP_011360.1. NM_001181020.1.
3D structure databases
ProteinModelPortal	P18898.
SMR	P18898. Positions 9-374.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-1232N.
IntAct	P18898. 1 interaction.
MINT	MINT-396220.
STRING	P18898.
Proteomic databases
PeptideAtlas	P18898.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YGL155W; YGL155W; YGL155W.
GeneID	852722.
KEGG	sce:YGL155W.
NMPDR	fig|4932.3.peg.2464.
Organism-specific databases
CYGD	YGL155w.
SGD	S000003123. CDC43.
Phylogenomic databases
eggNOG	fuNOG10660.
GeneTree	EFGT00050000004981.
HOGENOM	HBG204267.
OMA	TCYSWWC.
OrthoDB	EOG4WQ4BS.
Gene expression databases
ArrayExpress	P18898.
Genevestigator	P18898.
GermOnline	YGL155W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR001330. Prenyltrans. IPR008930. Terpenoid_cyclase/PrenylTrfase. [Graphical view]
KO	K11713.
Pfam	PF00432. Prenyltrans. 4 hits. [Graphical view]
SUPFAM	SSF48239. Terp_cyc_toroid. 1 hit.
ProtoNet	Search...
Other
NextBio	972105.

Entry information

Entry name

PGTB1_YEAST

Accession

Primary (citable) accession number: P18898
Secondary accession number(s): D6VTZ6

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1990
Last sequence update:	April 1, 1993
Last modified:	December 14, 2011
This is version 108 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program