Reviewed, UniProtKB/Swiss-Prot Q04631 (FNTA_RAT)

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:

Fnta

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	377 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
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. Ref.5
Sequence similarities	Belongs to the protein prenyltransferase subunit alpha family. Contains 5 PFTA repeats.

Ontologies

Keywords
Domain	Repeat
Molecular function	Prenyltransferase Transferase
PTM	Acetylation
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	negative regulation of apoptosis Inferred from mutant phenotype. Source: RGD negative regulation of nitric-oxide synthase 2 biosynthetic process Inferred from mutant phenotype. Source: RGD positive regulation of cell cycle Inferred from mutant phenotype. Source: RGD positive regulation of cell proliferation Inferred from mutant phenotype. Source: RGD positive regulation of nitric-oxide synthase 2 biosynthetic process Inferred from mutant phenotype. Source: RGD protein amino acid prenylation Inferred from electronic annotation. Source: InterPro response to cytokine stimulus Inferred from mutant phenotype. Source: RGD response to inorganic substance Inferred from mutant phenotype. Source: RGD response to organic cyclic substance Inferred from mutant phenotype. Source: RGD response to protein stimulus Inferred from direct assay. Source: RGD
Cellular component	CAAX-protein geranylgeranyltransferase complex Inferred from direct assay. Source: RGD cytoplasm Inferred from direct assay. Source: RGD
Molecular function	CAAX-protein geranylgeranyltransferase activity Inferred from electronic annotation. Source: EC protein binding Inferred from physical interaction. Source: IntAct protein farnesyltransferase activity Ref.1 Inferred from direct assay. Source: RGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Fntb	Q02293	7	EBI-602447,EBI-602454

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed By similarity

Chain

2 – 377

376

Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha

PRO_0000119748

Regions

Repeat

112 – 146

35

PFTA 1

Repeat

147 – 181

35

PFTA 2

Repeat

182 – 214

33

PFTA 3

Repeat

215 – 249

35

PFTA 4

Repeat

255 – 289

35

PFTA 5

Compositional bias

22 – 30

9

Pro-rich

Amino acid modifications

Modified residue

2

1

N-acetylalanine By similarity

Secondary structure

1

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377

Helix Strand Turn

Details...

Helix

66 – 68

3

Helix

70 – 72

3

Beta strand

87 – 90

4

Helix

94 – 109

16

Helix

114 – 126

13

Helix

131 – 143

13

Helix

148 – 161

14

Helix

166 – 179

14

Helix

185 – 195

11

Helix

200 – 213

14

Helix

219 – 229

11

Helix

234 – 246

13

Helix

253 – 269

17

Helix

274 – 284

11

Turn

285 – 287

3

Helix

289 – 291

3

Helix

293 – 300

8

Helix

303 – 306

4

Helix

309 – 324

16

Helix

330 – 346

17

Helix

350 – 352

3

Helix

353 – 367

15

Turn

369 – 372

4

Sequences

	Sequence		Length	Mass (Da)
	Q04631-1 [UniParc]. Last modified October 1, 1993. Version 1. Checksum: DFFFECC1B88BC080	FASTA	377	44,049
	10 20 30 40 50 60 MAATEGVGES APGGEPGQPE QPPPPPPPPP AQQPQEEEMA AEAGEAAASP MDDGFLSLDS 70 80 90 100 110 120 PTYVLYRDRA EWADIDPVPQ NDGPSPVVQI IYSEKFRDVY DYFRAVLQRD ERSERAFKLT 130 140 150 160 170 180 RDAIELNAAN YTVWHFRRVL LRSLQKDLQE EMNYIIAIIE EQPKNYQVWH HRRVLVEWLK 190 200 210 220 230 240 DPSQELEFIA DILNQDAKNY HAWQHRQWVI QEFRLWDNEL QYVDQLLKED VRNNSVWNQR 250 260 270 280 290 300 HFVISNTTGY SDRAVLEREV QYTLEMIKLV PHNESAWNYL KGILQDRGLS RYPNLLNQLL 310 320 330 340 350 360 DLQPSHSSPY LIAFLVDIYE DMLENQCDNK EDILNKALEL CEILAKEKDT IRKEYWRYIG 370 RSLQSKHSRE SDIPASV

References

[1]	"Cloning and expression of a cDNA encoding the alpha subunit of rat p21ras protein farnesyltransferase." Chen W.-J., Andres D.A., Goldstein J.L., Brown M.S. Proc. Natl. Acad. Sci. U.S.A. 88:11368-11372(1991) [PubMed: 1763049] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE. Tissue: Brain.
[2]	"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: 9065406] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS).
[3]	Erratum Park H.-W., Boduluri S.R., Mooomaw J.F., Casey P.J., Beese L.S. Science 276:21-21(1997)
[4]	"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: 9657673] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.4 ANGSTROMS).
[5]	"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: 11687658] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH BETA SUBUNIT AND GERANYLGERANYL DIPHOSPHATE.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M81225 mRNA. Translation: AAA41833.1.

IPI

IPI00188070.

PIR

A41625.

RefSeq

NP_036979.1.

UniGene

Rn.5990

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1D8D	X-ray	2.00	A	1-377	[»]
1D8E	X-ray	3.00	A	1-377	[»]
1FPP	X-ray	2.75	A	1-377	[»]
1FT1	X-ray	2.25	A	1-377	[»]
1FT2	X-ray	3.40	A	55-369	[»]
1FTI	model	-	A	55-369	[»]
1HZ7	model	-	A	116-247	[»]
1JCR	X-ray	2.00	A	1-377	[»]
1JCS	X-ray	2.20	A	1-377	[»]
1KZO	X-ray	2.20	A	1-377	[»]
1KZP	X-ray	2.10	A	1-377	[»]
1KZR	model	-	A	55-377	[»]
1N4P	X-ray	2.65	A/C/E/G/I/K	1-377	[»]
1N4Q	X-ray	2.40	A/C/E/G/I/K	1-377	[»]
1N4R	X-ray	2.80	A/C/E/G/I/K	1-377	[»]
1N4S	X-ray	2.60	A/C/E/G/I/K	1-377	[»]
1N94	X-ray	3.50	A	55-369	[»]
1N95	X-ray	2.30	A	55-369	[»]
1N9A	X-ray	3.20	A	55-369	[»]
1NI1	X-ray	2.30	A	55-369	[»]
1NL4	X-ray	2.70	A	55-366	[»]
1O1R	X-ray	2.30	A	1-377	[»]
1O1S	X-ray	2.30	A	1-377	[»]
1O1T	X-ray	2.10	A	1-377	[»]
1O5M	X-ray	2.30	A	1-377	[»]
1QBQ	X-ray	2.40	A	45-377	[»]
1QE2	model	-	A	116-247	[»]
1S64	X-ray	2.55	A/C/E/G/I/K	1-377	[»]
1SA5	X-ray	2.60	A	1-377	[»]
1TN7	X-ray	2.30	A	1-377	[»]
1TN8	X-ray	2.25	A	1-377	[»]
1TNB	X-ray	2.85	A/C/E/G/I/K	1-377	[»]
1TNO	X-ray	2.70	A/C/E/G/I/K	1-377	[»]
1TNU	X-ray	2.70	A/C/E/G/I/K	1-377	[»]
1TNY	X-ray	2.70	A/C/E/G/I/K	1-377	[»]
1TNZ	X-ray	2.90	A/C/E/G/I/K	1-377	[»]
1X81	X-ray	3.50	A	55-369	[»]
2BED	X-ray	2.70	A	54-366	[»]
2FTI	model	-	A	55-369	[»]
2R2L	X-ray	2.23	A	54-368	[»]
2ZIR	X-ray	2.40	A	1-377	[»]
2ZIS	X-ray	2.60	A	1-377	[»]
3DPY	X-ray	2.70	A	1-377	[»]
3E30	X-ray	2.45	A	1-377	[»]
3E32	X-ray	2.45	A	1-377	[»]
3E33	X-ray	1.90	A	1-377	[»]
3E34	X-ray	2.05	A	1-377	[»]
3EU5	X-ray	2.80	A	1-377	[»]
3EUV	X-ray	2.75	A	1-377	[»]
3FTI	model	-	A	55-369	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-6131N.

IntAct

Q04631. 9 interactions.

STRING

Q04631.

Genome annotation databases

Ensembl

ENSRNOT00000019594; ENSRNOP00000019594; ENSRNOG00000014462; Rattus norvegicus. [Genome view]

GeneID

25318.

KEGG

rno:25318.

UCSC

NM_012847. rat.

Organism-specific databases

CTD

25318.

RGD

2625. Fnta.

Phylogenomic databases

HOVERGEN

Q04631.

InParanoid

Q04631.

PhylomeDB

Q04631.

Enzyme and pathway databases

BRENDA

2.5.1.58. 248.
2.5.1.59. 248.

Gene expression databases

ArrayExpress

Q04631.

Genevestigator

Q04631.

GermOnline

ENSRNOG00000014462. Rattus norvegicus.

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

606153.

Entry information

Entry name

FNTA_RAT

Accession

Primary (citable) accession number: Q04631

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1993
Last sequence update:	October 1, 1993
Last modified:	January 19, 2010
This is version 84 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)