O13782 (FNTB_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Protein farnesyltransferase subunit beta
Short name=FTase-beta
EC=2.5.1.58

Alternative name(s):
CAAX farnesyltransferase subunit beta
Ras proteins prenyltransferase subunit beta

Gene names

Name:	cpp1
ORF Names:	SPAC17G6.04c

Organism

Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]

Taxonomic identifier

284812 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces › Schizosaccharomyces pombe

Protein attributes

Sequence length	382 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the transfer of a farnesyl moiety from farnesyl pyrophosphate to a cysteine at the fourth position from the C-terminus of several proteins. The beta subunit is responsible for peptide-binding. Ref.1
Catalytic activity	Farnesyl diphosphate + protein-cysteine = S-farnesyl protein + diphosphate.
Cofactor	Binds 1 zinc ion per subunit By similarity.
Subunit structure	Heterodimer of an alpha and a beta subunit. Ref.1
Sequence similarities	Belongs to the protein prenyltransferase subunit beta family. Contains 5 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 response to nitrogen starvation Inferred from genetic interaction PubMed 16624901. Source: PomBase protein farnesylation Inferred from direct assay Ref.1. Source: PomBase protein targeting to membrane Inferred by curator. Source: PomBase regulation of amino acid import Inferred from genetic interaction PubMed 16624901. Source: PomBase regulation of cell proliferation Inferred from electronic annotation. Source: InterPro
Cellular_component	cytosol Inferred from direct assay PubMed 16823372. Source: PomBase nucleus Inferred from direct assay PubMed 16823372. Source: PomBase protein farnesyltransferase complex Inferred from electronic annotation. Source: InterPro
Molecular_function	protein farnesyltransferase activity Inferred from mutant phenotype PubMed 16624901. Source: PomBase zinc ion binding Non-traceable author statement. Source: PomBase
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 382	382	Protein farnesyltransferase subunit beta		PRO_0000119767
Regions
	Repeat	78 – 119	42	PFTB 1
	Repeat	129 – 170	42	PFTB 2
	Repeat	178 – 219	42	PFTB 3
	Repeat	226 – 268	43	PFTB 4
	Repeat	286 – 328	43	PFTB 5
Sites
	Metal binding	253	1	Zinc By similarity
	Metal binding	255	1	Zinc By similarity
	Metal binding	316	1	Zinc By similarity

Sequences

	Sequence		Length	Mass (Da)
	O13782 [UniParc]. Last modified January 1, 1998. Version 1. Checksum: C3F2705D93F84203	FASTA	382	42,189
	10 20 30 40 50 60 MDELSETQVM QNETATAVLP LLNGESQSFN LQKHLKYLTK MLDPLPSPFT VLDASRAWMV 70 80 90 100 110 120 YWELSSLAIL GKLDSSVCER AISSVRQLKG PSGGFCGGNG QDEHLLSTYA SILSICLCDS 130 140 150 160 170 180 TDAYSLIERD RLYDWLFSLK NPDGSFRVNN EGESDARSVY AAVCVSSLVG ISMDDPLFEG 190 200 210 220 230 240 TLQWLCKCQT YEGGLSGVPY AEAHGGYTFC ALAAIALLGG LDNLNEIKLS TWLVQRQDPA 250 260 270 280 290 300 LYGFSGRSNK LVDGCYSWWV GASHVIVASG YGSASHKSLP NLFYNPEKLL GYILQCCQST 310 320 330 340 350 360 SGGLRDKPPK RPDQYHTCYC LLGLSSIAYD YRYHTSDGWS YKPSILHSSL SSLLPAHPIY 370 380 CVPFGFEERI KSYFLSQESS KF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Protein farnesylation is critical for maintaining normal cell morphology and canavanine resistance in Schizosaccharomyces pombe." Yang W., Urano J., Tamanoi F. J. Biol. Chem. 275:429-438(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBUNIT.
[2]	"The genome sequence of Schizosaccharomyces pombe." Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P. Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 972 / ATCC 24843.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CU329670 Genomic DNA. Translation: CAB16215.1.
PIR	T37836.
RefSeq	NP_594251.1. NM_001019674.2.
3D structure databases
ProteinModelPortal	O13782.
ModBase	Search...
Protein-protein interaction databases
STRING	4896.SPAC17G6.04c-1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	SPAC17G6.04c.1; SPAC17G6.04c.1:pep; SPAC17G6.04c.
GeneID	2542380.
KEGG	spo:SPAC17G6.04c.
Organism-specific databases
PomBase	SPAC17G6.04c.
Phylogenomic databases
eggNOG	COG5029.
HOGENOM	HOG000190594.
KO	K05954.
OMA	HPVYNIC.
OrthoDB	EOG4ZPJ4B.
Family and domain databases
InterPro	IPR026872. FTB. IPR001330. Prenyltrans. IPR008930. Terpenoid_cyclase/PrenylTrfase. [Graphical view]
PANTHER	PTHR11774:SF6. PTHR11774:SF6. 1 hit.
Pfam	PF00432. Prenyltrans. 1 hit. [Graphical view]
SUPFAM	SSF48239. Terp_cyc_toroid. 1 hit.
ProtoNet	Search...
Other
NextBio	20803439.

Entry information

Entry name

FNTB_SCHPO

Accession

Primary (citable) accession number: O13782

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 6, 2002
Last sequence update:	January 1, 1998
Last modified:	May 1, 2013
This is version 95 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program