Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha

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Q04631 (FNTA_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 101. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

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)

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. 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
PTM	Acetylation
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. Source: RGD negative regulation of nitric-oxide synthase 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 biosynthetic process Inferred from mutant phenotype. Source: RGD protein 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 compound Inferred from mutant phenotype. 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 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

Initiator methionine

Removed By similarity

Chain

2 – 377

376

Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha

PRO_0000119748

Regions

Repeat

112 – 146

PFTA 1

Repeat

147 – 181

PFTA 2

Repeat

182 – 214

PFTA 3

Repeat

215 – 249

PFTA 4

Repeat

255 – 289

PFTA 5

Compositional bias

22 – 30

Pro-rich

Amino acid modifications

Modified residue

N-acetylalanine By similarity

Secondary structure

377

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

Q04631 [UniParc].

Last modified October 1, 1993. Version 1.
Checksum: DFFFECC1B88BC080
Show »

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

« Hide

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. 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	[»]

ProteinModelPortal

Q04631.

SMR

Q04631. Positions 55-377.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-6131N.

IntAct

Q04631. 8 interactions.

MINT

MINT-121907.

STRING

Q04631.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

25318.

KEGG

rno:25318.

UCSC

NM_012847. rat.

Organism-specific databases

CTD

2339.

RGD

2625. Fnta.

Phylogenomic databases

HOVERGEN

HBG004498.

InParanoid

Q04631.

OrthoDB

EOG46DM39.

PhylomeDB

Q04631.

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.

K05955.

Pfam

PF01239. PPTA. 5 hits.
[Graphical view]

PROSITE

PS51147. PFTA. 5 hits.
[Graphical view]

ProtoNet

Search...

Other

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 25, 2012
This is version 101 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents