Q02293 (FNTB_RAT) 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:

Fntb

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	437 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.
Catalytic activity	Farnesyl diphosphate + protein-cysteine = S-farnesyl protein + diphosphate.
Cofactor	Binds 1 zinc ion per subunit.
Subunit structure	Heterodimer of an alpha and a beta subunit. Ref.6
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	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	negative regulation of cell proliferation Inferred from electronic annotation. Source: Compara positive regulation of cell cycle Inferred from mutant phenotype PubMed 10544242. Source: RGD positive regulation of cell proliferation Inferred from mutant phenotype PubMed 10544242. Source: RGD positive regulation of fibroblast proliferation Inferred from electronic annotation. Source: Compara positive regulation of nitric-oxide synthase biosynthetic process Inferred from mutant phenotype PubMed 9153192. Source: RGD protein farnesylation Inferred from electronic annotation. Source: InterPro response to cytokine stimulus Inferred from mutant phenotype PubMed 9153192. Source: RGD response to inorganic substance Inferred from mutant phenotype PubMed 18957540. Source: RGD response to organic cyclic compound Inferred from mutant phenotype PubMed 16257390. Source: RGD wound healing Inferred from electronic annotation. Source: Compara
Cellular_component	protein complex Inferred from direct assay PubMed 15248757. Source: RGD protein farnesyltransferase complex Inferred from electronic annotation. Source: InterPro
Molecular_function	farnesyltranstransferase activity Inferred from electronic annotation. Source: Compara metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein farnesyltransferase activity Inferred from direct assay Ref.1. Source: RGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Fnta	Q04631	14	EBI-602454,EBI-602447

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 437

437

Protein farnesyltransferase subunit beta

PRO_0000119763

Regions

Repeat

123 – 164

42

PFTB 1

Repeat

174 – 215

42

PFTB 2

Repeat

222 – 263

42

PFTB 3

Repeat

270 – 312

43

PFTB 4

Repeat

332 – 374

43

PFTB 5

Sites

Metal binding

297

1

Zinc

Metal binding

299

1

Zinc

Metal binding

362

1

Zinc

Secondary structure

1

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437

Helix Strand Turn

Details...

Helix

24 – 26

3

Helix

28 – 33

6

Helix

43 – 65

23

Helix

75 – 85

11

Helix

91 – 96

6

Helix

100 – 113

14

Helix

120 – 133

14

Beta strand

138 – 143

6

Helix

150 – 163

14

Helix

166 – 171

6

Helix

174 – 184

11

Beta strand

191 – 194

4

Helix

201 – 213

13

Turn

219 – 224

6

Helix

225 – 232

8

Beta strand

237 – 239

3

Helix

249 – 261

13

Helix

265 – 267

3

Helix

270 – 278

9

Turn

283 – 285

3

Beta strand

287 – 291

5

Helix

300 – 303

4

Turn

304 – 306

3

Helix

307 – 317

11

Beta strand

321 – 323

3

Beta strand

325 – 327

3

Helix

332 – 342

11

Beta strand

348 – 350

3

Beta strand

352 – 355

4

Helix

360 – 374

15

Beta strand

375 – 378

4

Beta strand

381 – 384

4

Helix

390 – 392

3

Turn

399 – 401

3

Helix

405 – 415

11

Helix

424 – 426

3

Helix

434 – 436

3

Sequences

	Sequence		Length	Mass (Da)
	Q02293 [UniParc]. Last modified April 1, 1993. Version 1. Checksum: 41A9D6D79CD319A8	FASTA	437	48,673
	10 20 30 40 50 60 MASSSSFTYY CPPSSSPVWS EPLYSLRPEH ARERLQDDSV ETVTSIEQAK VEEKIQEVFS 70 80 90 100 110 120 SYKFNHLVPR LVLQREKHFH YLKRGLRQLT DAYECLDASR PWLCYWILHS LELLDEPIPQ 130 140 150 160 170 180 IVATDVCQFL ELCQSPDGGF GGGPGQYPHL APTYAAVNAL CIIGTEEAYN VINREKLLQY 190 200 210 220 230 240 LYSLKQPDGS FLMHVGGEVD VRSAYCAASV ASLTNIITPD LFEGTAEWIA RCQNWEGGIG 250 260 270 280 290 300 GVPGMEAHGG YTFCGLAALV ILKKERSLNL KSLLQWVTSR QMRFEGGFQG RCNKLVDGCY 310 320 330 340 350 360 SFWQAGLLPL LHRALHAQGD PALSMSHWMF HQQALQEYIL MCCQCPAGGL LDKPGKSRDF 370 380 390 400 410 420 YHTCYCLSGL SIAQHFGSGA MLHDVVMGVP ENVLQPTHPV YNIGPDKVIQ ATTHFLQKPV 430 PGFEECEDAV TSDPATD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"cDNA cloning and expression of the peptide-binding beta subunit of rat p21ras farnesyltransferase, the counterpart of yeast DPR1/RAM1." Chen W.-J., Andres D.A., Goldstein J.L., Russell D.W., Brown M.S. Cell 66:327-334(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE. Tissue: Brain.
[2]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
[3]	Erratum Park H.-W., Boduluri S.R., Mooomaw J.F., Casey P.J., Beese L.S. Science 276:21-21(1997)
[4]	"Crystal structure of protein farnesyltransferase at 2.25-A resolution." Park H.-W., Boduluri S.R., Mooomaw J.F., Casey P.J., Beese L.S. Science 275:1800-1804(1997) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS).
[5]	"Cocrystal structure of protein farnesyltransferase complexed with a farnesyl diphosphate substrate." Long S.B., Casey P.J., Beese L.S. Biochemistry 37:9612-9618(1998) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.4 ANGSTROMS).
[6]	"The crystal structure of human protein farnesyltransferase reveals the basis for inhibition by CaaX tetrapeptides and their mimetics." Long S.B., Hancock P.J., Kral A.M., Hellinga H.W., Beese L.S. Proc. Natl. Acad. Sci. U.S.A. 98:12948-12953(2001) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH ALPHA SUBUNIT AND GERANYLGERANYL DIPHOSPHATE.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M69056 mRNA. Translation: AAA41176.1.
BC087675 mRNA. Translation: AAH87675.1.

IPI

IPI00205139.

PIR

A40037.

RefSeq

NP_742031.1. NM_172034.2.

UniGene

Rn.8873.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1D8D	X-ray	2.00	B	1-437	[»]
1D8E	X-ray	3.00	B	1-437	[»]
1FPP	X-ray	2.75	B	1-437	[»]
1FT1	X-ray	2.25	B	1-437	[»]
1FT2	X-ray	3.40	B	22-422	[»]
1FTI	model	-	B	22-422	[»]
1HZ7	model	-	B	41-406	[»]
1JCR	X-ray	2.00	B	1-437	[»]
1JCS	X-ray	2.20	B	1-437	[»]
1KZO	X-ray	2.20	B	1-437	[»]
1KZP	X-ray	2.10	B	1-437	[»]
1KZR	model	-	B	17-423	[»]
1N94	X-ray	3.50	B	22-418	[»]
1N95	X-ray	2.30	B	22-423	[»]
1N9A	X-ray	3.20	B	22-423	[»]
1NI1	X-ray	2.30	B	22-423	[»]
1NL4	X-ray	2.70	B	23-423	[»]
1O1R	X-ray	2.30	B	1-427	[»]
1O1S	X-ray	2.30	B	1-427	[»]
1O1T	X-ray	2.10	B	1-427	[»]
1O5M	X-ray	2.30	B	1-437	[»]
1QBQ	X-ray	2.40	B	1-437	[»]
1QE2	model	-	B	41-406	[»]
1SA5	X-ray	2.60	B	1-437	[»]
1TN7	X-ray	2.30	B	1-437	[»]
1TN8	X-ray	2.25	B	1-437	[»]
1X81	X-ray	3.50	B	22-418	[»]
2BED	X-ray	2.70	B	23-423	[»]
2FTI	model	-	B	22-422	[»]
2R2L	X-ray	2.23	B	23-423	[»]
2ZIR	X-ray	2.40	B	1-437	[»]
2ZIS	X-ray	2.60	B	1-437	[»]
3DPY	X-ray	2.70	B	1-437	[»]
3E30	X-ray	2.45	B	1-437	[»]
3E32	X-ray	2.45	B	1-437	[»]
3E33	X-ray	1.90	B	1-437	[»]
3E34	X-ray	2.05	B	1-437	[»]
3EU5	X-ray	2.80	B	1-427	[»]
3EUV	X-ray	2.75	B	1-427	[»]
3FTI	model	-	B	22-422	[»]
3KSL	X-ray	2.05	B	1-437	[»]
3KSQ	X-ray	2.10	B	1-437	[»]
4GTM	X-ray	2.20	B	1-427	[»]
4GTO	X-ray	2.15	B	1-427	[»]
4GTP	X-ray	2.75	B	1-427	[»]
4GTQ	X-ray	2.60	B	1-427	[»]
4GTR	X-ray	2.20	B	1-427	[»]

ProteinModelPortal

Q02293.

SMR

Q02293. Positions 22-437.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-6132N.

IntAct

Q02293. 1 interaction.

MINT

MINT-121917.

STRING

10116.ENSRNOP00000010588.

PTM databases

PhosphoSite

Q02293.

Proteomic databases

PaxDb

Q02293.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSRNOT00000010588; ENSRNOP00000010588; ENSRNOG00000007660.

GeneID

64511.

KEGG

rno:64511.

UCSC

RGD:620119. rat.

Organism-specific databases

CTD

2342.

RGD

620119. Fntb.

Phylogenomic databases

eggNOG

COG5029.

GeneTree

ENSGT00550000075042.

HOGENOM

HOG000190594.

HOVERGEN

HBG008173.

InParanoid

Q02293.

KO

K05954.

OMA

HPVYNIC.

OrthoDB

EOG4KKZ33.

Enzyme and pathway databases

SABIO-RK

Q02293.

Gene expression databases

Genevestigator

Q02293.

GermOnline

ENSRNOG00000007660. Rattus norvegicus.

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. 2 hits.
[Graphical view]

SUPFAM

SSF48239. Terp_cyc_toroid. 1 hit.

ProtoNet

Search...

Other

BindingDB

Q02293.

ChEMBL

CHEMBL4890.

EvolutionaryTrace

Q02293.

NextBio

613294.

Entry information

Entry name

FNTB_RAT

Accession

Primary (citable) accession number: Q02293

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1993
Last sequence update:	April 1, 1993
Last modified:	April 3, 2013
This is version 121 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program