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Protein

Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha

Gene

Fnta

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Essential subunit of both the farnesyltransferase and the geranylgeranyltransferase complex. Contributes to the transfer of a farnesyl or geranylgeranyl moiety from farnesyl or geranylgeranyl diphosphate to a cysteine at the fourth position from the C-terminus of several proteins having the C-terminal sequence Cys-aliphatic-aliphatic-X. May positively regulate neuromuscular junction development downstream of MUSK via its function in RAC1 prenylation and activation.1 Publication

Catalytic activityi

Farnesyl diphosphate + protein-cysteine = S-farnesyl protein + diphosphate.
Geranylgeranyl diphosphate + protein-cysteine = S-geranylgeranyl-protein + diphosphate.

Enzyme regulationi

Activated by the AGRIN-induced phosphorylation which is mediated by MUSK.1 Publication

GO - Molecular functioni

  • acetylcholine receptor regulator activity Source: MGI
  • alpha-tubulin binding Source: MGI
  • CAAX-protein geranylgeranyltransferase activity Source: UniProtKB-EC
  • microtubule binding Source: MGI
  • protein farnesyltransferase activity Source: UniProtKB
  • protein geranylgeranyltransferase activity Source: UniProtKB
  • Rab geranylgeranyltransferase activity Source: UniProtKB
  • receptor tyrosine kinase binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Prenyltransferase, Transferase

Enzyme and pathway databases

ReactomeiR-MMU-111465. Apoptotic cleavage of cellular proteins.
R-MMU-2514859. Inactivation, recovery and regulation of the phototransduction cascade.

Names & Taxonomyi

Protein namesi
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 namesi
Name:Fnta
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 8

Organism-specific databases

MGIiMGI:104683. Fnta.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL3301421.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00001197472 – 377Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alphaAdd BLAST376

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineBy similarity1

Post-translational modificationi

Phosphorylated. Phosphorylation is mediated by MUSK upon AGRIN stimulation and results in the activation of FNTA.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ61239.
MaxQBiQ61239.
PaxDbiQ61239.
PRIDEiQ61239.

PTM databases

iPTMnetiQ61239.
PhosphoSitePlusiQ61239.
SwissPalmiQ61239.

Expressioni

Gene expression databases

BgeeiENSMUSG00000015994.
CleanExiMM_FNTA.
ExpressionAtlasiQ61239. baseline and differential.
GenevisibleiQ61239. MM.

Interactioni

Subunit structurei

Heterodimer of FNTA and FNTB (farnesyltransferase). Heterodimer of FNTA and PGGT1B (geranylgeranyltransferase). Interacts with MUSK; the interaction is direct and mediates AGRIN-induced phosphorylation of FNTA.1 Publication

GO - Molecular functioni

  • alpha-tubulin binding Source: MGI
  • microtubule binding Source: MGI
  • receptor tyrosine kinase binding Source: UniProtKB

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000016138.

Chemistry databases

BindingDBiQ61239.

Structurei

3D structure databases

ProteinModelPortaliQ61239.
SMRiQ61239.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati112 – 146PFTA 1Add BLAST35
Repeati147 – 181PFTA 2Add BLAST35
Repeati182 – 214PFTA 3Add BLAST33
Repeati215 – 249PFTA 4Add BLAST35
Repeati255 – 289PFTA 5Add BLAST35

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi22 – 30Poly-Pro9

Sequence similaritiesi

Contains 5 PFTA repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG0530. Eukaryota.
COG5536. LUCA.
GeneTreeiENSGT00550000074935.
HOGENOMiHOG000188957.
HOVERGENiHBG004498.
InParanoidiQ61239.
KOiK05955.
OMAiRQWAIRS.
OrthoDBiEOG091G0CNT.
PhylomeDBiQ61239.
TreeFamiTF313038.

Family and domain databases

InterProiIPR002088. Prenyl_trans_a.
[Graphical view]
PfamiPF01239. PPTA. 5 hits.
[Graphical view]
PROSITEiPS51147. PFTA. 5 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q61239-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAATEGVGES AAGGEPGQPE QPPPPPPPPP AQQPQEEEMA AEAGEAAASP
60 70 80 90 100
MDDGFLSLDS PTYVLYRDRA EWADIDPVPQ NDGPNPVVQI IYSEKFRDVY
110 120 130 140 150
DYFRAVLQRD ERSERAFKLT RDAIELNAAN YTVWHFRRVL LRSLQKDLQE
160 170 180 190 200
EMNYITAIIE EQPKNYQVWH HRRVLVEWLK DPSQELEFIA DILSQDAKNY
210 220 230 240 250
HAWQHRQWVI QEFRLWDNEL QYVDQLLKED VRNNSVWNQR HFVISNTTGY
260 270 280 290 300
SDRAVLEREV QYTLEMIKLV PHNESAWNYL KGILQDRGLS RYPNLLNQLL
310 320 330 340 350
DLQPSHSSPY LIAFLVDVYE DMLENQCDNK EDILNKALEL CEILAKEKDT
360 370
IRKEYWRYIG RSLQSKHCRE SDIPASV
Length:377
Mass (Da):44,013
Last modified:November 1, 1996 - v1
Checksum:iF3D60B9899F36D66
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti191D → N in AAH12711 (PubMed:15489334).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D49744 mRNA. Translation: BAA08578.1.
BC012711 mRNA. Translation: AAH12711.1.
CCDSiCCDS22205.1.
PIRiJC4368.
RefSeqiNP_032059.1. NM_008033.3.
UniGeneiMm.3496.

Genome annotation databases

EnsembliENSMUST00000016138; ENSMUSP00000016138; ENSMUSG00000015994.
GeneIDi14272.
KEGGimmu:14272.
UCSCiuc009lhi.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D49744 mRNA. Translation: BAA08578.1.
BC012711 mRNA. Translation: AAH12711.1.
CCDSiCCDS22205.1.
PIRiJC4368.
RefSeqiNP_032059.1. NM_008033.3.
UniGeneiMm.3496.

3D structure databases

ProteinModelPortaliQ61239.
SMRiQ61239.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000016138.

Chemistry databases

BindingDBiQ61239.
ChEMBLiCHEMBL3301421.

PTM databases

iPTMnetiQ61239.
PhosphoSitePlusiQ61239.
SwissPalmiQ61239.

Proteomic databases

EPDiQ61239.
MaxQBiQ61239.
PaxDbiQ61239.
PRIDEiQ61239.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000016138; ENSMUSP00000016138; ENSMUSG00000015994.
GeneIDi14272.
KEGGimmu:14272.
UCSCiuc009lhi.1. mouse.

Organism-specific databases

CTDi2339.
MGIiMGI:104683. Fnta.

Phylogenomic databases

eggNOGiKOG0530. Eukaryota.
COG5536. LUCA.
GeneTreeiENSGT00550000074935.
HOGENOMiHOG000188957.
HOVERGENiHBG004498.
InParanoidiQ61239.
KOiK05955.
OMAiRQWAIRS.
OrthoDBiEOG091G0CNT.
PhylomeDBiQ61239.
TreeFamiTF313038.

Enzyme and pathway databases

ReactomeiR-MMU-111465. Apoptotic cleavage of cellular proteins.
R-MMU-2514859. Inactivation, recovery and regulation of the phototransduction cascade.

Miscellaneous databases

PROiQ61239.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000015994.
CleanExiMM_FNTA.
ExpressionAtlasiQ61239. baseline and differential.
GenevisibleiQ61239. MM.

Family and domain databases

InterProiIPR002088. Prenyl_trans_a.
[Graphical view]
PfamiPF01239. PPTA. 5 hits.
[Graphical view]
PROSITEiPS51147. PFTA. 5 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiFNTA_MOUSE
AccessioniPrimary (citable) accession number: Q61239
Secondary accession number(s): Q921F7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: November 2, 2016
This is version 126 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.