Q04631 (FNTA_RAT) Reviewed, UniProtKB/Swiss-Prot

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
FTase-alpha
Ras proteins prenyltransferase subunit alpha
Type I protein geranyl-geranyltransferase subunit alpha
Short name=GGTase-I-alpha

Gene names

Name:

Fnta

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	377 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. Through RAC1 prenylation and activation may positively regulate neuromuscular junction development downstream of MUSK By similarity.
Catalytic activity	Farnesyl diphosphate + protein-cysteine = S-farnesyl protein + diphosphate. Geranylgeranyl diphosphate + protein-cysteine = S-geranylgeranyl-protein + diphosphate.
Enzyme regulation	Activated by the AGRIN-induced phosphorylation which is mediated by MUSK By similarity.
Subunit structure	Heterodimer of an alpha and a beta subunit. Interacts with MUSK; the interaction is direct and mediates AGRIN-induced phosphorylation of FNTA By similarity. Ref.5
Post-translational modification	Phosphorylated. Phosphorylation is mediated by MUSK upon AGRIN stimulation and results in the activation of FNTA By similarity.
Sequence similarities	Belongs to the protein prenyltransferase subunit alpha family. Contains 5 PFTA repeats.

Ontologies

Keywords
Domain	Repeat
Molecular function	Prenyltransferase Transferase
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	negative regulation of apoptotic process Inferred from mutant phenotype PubMed 11313965. Source: RGD negative regulation of nitric-oxide synthase biosynthetic process Inferred from mutant phenotype PubMed 9153192. Source: RGD 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 nitric-oxide synthase biosynthetic process Inferred from mutant phenotype PubMed 9153192. Source: RGD protein prenylation 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
Cellular_component	CAAX-protein geranylgeranyltransferase complex Inferred from direct assay PubMed 15248757. Source: RGD cytoplasm Inferred from direct assay PubMed 17192483. Source: RGD
Molecular_function	CAAX-protein geranylgeranyltransferase activity Inferred from electronic annotation. Source: EC protein farnesyltransferase activity Inferred from direct assay Ref.1. Source: RGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Fntb	Q02293	14	EBI-602447,EBI-602454
KRAS	P01116-2	2	EBI-602447,EBI-367427	From a different organism.
Pggt1b	P53610	5	EBI-602447,EBI-602610

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 377

377

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

Secondary structure

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377

Helix Strand Turn

Details...

Beta strand

58 – 60

3

Helix

66 – 68

3

Helix

70 – 72

3

Beta strand

73 – 75

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

Turn

182 – 184

3

Helix

185 – 195

11

Helix

200 – 213

14

Helix

216 – 218

3

Helix

219 – 229

11

Turn

230 – 232

3

Helix

234 – 246

13

Beta strand

250 – 252

3

Helix

253 – 269

17

Beta strand

270 – 272

3

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

Turn

347 – 349

3

Helix

350 – 352

3

Helix

353 – 367

15

Turn

369 – 372

4

Sequences

	Sequence		Length	Mass (Da)
	Q04631 [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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. NM_012847.1.

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	[»]
3KSL	X-ray	2.05	A	1-377	[»]
3KSQ	X-ray	2.10	A	1-377	[»]
4GTM	X-ray	2.20	A	1-377	[»]
4GTO	X-ray	2.15	A	1-377	[»]
4GTP	X-ray	2.75	A	1-377	[»]
4GTQ	X-ray	2.60	A	1-377	[»]
4GTR	X-ray	2.20	A	1-377	[»]

ProteinModelPortal

Q04631.

SMR

Q04631. Positions 55-377.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-6131N.

IntAct

Q04631. 8 interactions.

MINT

MINT-121907.

STRING

10116.ENSRNOP00000019594.

PTM databases

PhosphoSite

Q04631.

Proteomic databases

PaxDb

Q04631.

PRIDE

Q04631.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

25318.

KEGG

rno:25318.

UCSC

RGD:2625. rat.

Organism-specific databases

CTD

2339.

RGD

2625. Fnta.

Phylogenomic databases

eggNOG

COG5536.

HOGENOM

HOG000188957.

HOVERGEN

HBG004498.

InParanoid

Q04631.

KO

K05955.

OrthoDB

EOG46DM39.

Enzyme and pathway databases

SABIO-RK

Q04631.

Gene expression databases

ArrayExpress

Q04631.

Genevestigator

Q04631.

GermOnline

ENSRNOG00000014462. Rattus norvegicus.

Family and domain databases

InterPro

IPR002088. Prenyl_trans_a.
[Graphical view]

Pfam

PF01239. PPTA. 5 hits.
[Graphical view]

PROSITE

PS51147. PFTA. 5 hits.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

Q04631.

ChEMBL

CHEMBL4432.

EvolutionaryTrace

Q04631.

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:	April 3, 2013
This is version 111 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program