P29702 (FNTA_BOVIN) 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

Bos taurus (Bovine)

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length	375 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript 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.
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.
Sequence caution	The sequence AAA30529.1 differs from that shown. Reason: Erroneous initiation. The sequence AAI12663.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.

Ontologies

Keywords
Domain	Repeat
Molecular function	Prenyltransferase Transferase
PTM	Acetylation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	protein prenylation Inferred from electronic annotation. Source: InterPro
Molecular function	CAAX-protein geranylgeranyltransferase activity Inferred from electronic annotation. Source: EC protein farnesyltransferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 375	374	Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha		PRO_0000119745
Regions
	Repeat	108 – 142	35	PFTA 1
	Repeat	143 – 176	34	PFTA 2
	Repeat	177 – 211	35	PFTA 3
	Repeat	212 – 245	34	PFTA 4
	Repeat	251 – 285	35	PFTA 5
	Compositional bias	16 – 37	22	Pro-rich
Amino acid modifications
	Modified residue	2	1	N-acetylalanine By similarity
Experimental info
	Sequence conflict	47	1	I → M in AAA30529. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P29702 [UniParc]. Last modified June 13, 2006. Version 2. Checksum: 7253AD4CED67296C	FASTA	375	43,845
	10 20 30 40 50 60 MAAADGVGEA AQGGDPGQPE PPPPPQPHPP PPPPQPPQEE AAAASPIDDG FLSLDSPTYV 70 80 90 100 110 120 LYRDRPEWAD IDPVPQNDGP NPVVQIIYSE KFQDVYDYFR AVLQRDERSE RAFKLTRDAI 130 140 150 160 170 180 ELNAANYTVW HFRRVLLKSL QKDLHEEMNY ISAIIEEQPK NYQVWHHRRV LVEWLRDPSQ 190 200 210 220 230 240 ELEFIADILT QDAKNYHAWQ HRQWVIQEFK LWDNELQYVD QLLKEDVRNN SVWNQRYFVI 250 260 270 280 290 300 SNTTGYNDRA ILEREVQYTL EMIKLVPHNE SAWNYLKGIL QDRGLSKYPN LLNQLLDLQP 310 320 330 340 350 360 SHSSPYLIAF LVDIYEDMLE NQCDNKEDIL NKALELCEIL AKEKDTIRKE YWRYIGRSLQ 370 SKHSTESDPP TNVQQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	NIH - Mammalian Gene Collection (MGC) project Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-249. Strain: Hereford. Tissue: Testis.
[2]	"Structural homology among mammalian and Saccharomyces cerevisiae isoprenyl-protein transferases." Kohl N.E., Diehl R.E., Schaber M.D., Rands E., Soderman D.D., He B., Moores S.L., Pompliano D.L., Ferro-Novick S., Powers S., Thomas K.A., Gibbs J.B. J. Biol. Chem. 266:18884-18888(1991) [PubMed: 1918005] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 36-375.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BC112662 mRNA. Translation: AAI12663.1. Sequence problems. M74083 mRNA. Translation: AAA30529.1. Different initiation.
IPI	IPI00706713.
PIR	A41013.
RefSeq	NP_803464.2. NM_177498.3.
UniGene	Bt.407.
3D structure databases
ProteinModelPortal	P29702.
SMR	P29702. Positions 51-365.
ModBase	Search...
Protein-protein interaction databases
STRING	P29702.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	281169.
KEGG	bta:281169.
Organism-specific databases
CTD	2339.
Phylogenomic databases
HOVERGEN	HBG004498.
InParanoid	P29702.
OrthoDB	EOG46DM39.
PhylomeDB	P29702.
Family and domain databases
InterPro	IPR002088. Prenyl_trans_a. IPR008940. Prenyltransferase. [Graphical view]
Gene3D	G3DSA:1.25.40.120. Prenyl_trans. 1 hit.
KO	K05955.
Pfam	PF01239. PPTA. 5 hits. [Graphical view]
PROSITE	PS51147. PFTA. 5 hits. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

FNTA_BOVIN

Accession

Primary (citable) accession number: P29702
Secondary accession number(s): Q2KIF0

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1993
Last sequence update:	June 13, 2006
Last modified:	January 25, 2012
This is version 78 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program