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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.2 Publications

Catalytic activityi

Farnesyl diphosphate + protein-cysteine = S-farnesyl protein + diphosphate.1 Publication
Geranylgeranyl diphosphate + protein-cysteine = S-geranylgeranyl-protein + diphosphate.1 Publication

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

  • neurotransmitter receptor metabolic process Source: MGI
  • positive regulation of deacetylase activity Source: MGI
  • positive regulation of tubulin deacetylation Source: MGI
  • protein farnesylation Source: UniProtKB
  • protein geranylgeranylation Source: UniProtKB
  • regulation of neurotransmitter receptor activity Source: GOC
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

ChEMBLiCHEMBL2096912.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 377376Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alphaPRO_0000119747Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity

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.
PhosphoSiteiQ61239.
SwissPalmiQ61239.

Expressioni

Gene expression databases

BgeeiQ61239.
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.2 Publications

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

BindingDBiQ61239.

Structurei

Secondary structure

1
377
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi66 – 683
Helixi70 – 723
Beta strandi87 – 904
Helixi94 – 10916
Helixi114 – 12613
Helixi131 – 14313
Helixi148 – 16114
Helixi166 – 17914
Helixi185 – 1939
Helixi200 – 21314
Helixi219 – 22911
Helixi234 – 24411
Beta strandi250 – 2556
Helixi256 – 26914
Helixi274 – 2829
Turni283 – 2875
Helixi289 – 2913
Helixi293 – 2997
Turni300 – 3056
Helixi309 – 32416
Helixi330 – 34617
Helixi350 – 3523
Helixi353 – 36715

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3PZ4X-ray2.10A1-377[»]
ProteinModelPortaliQ61239.
SMRiQ61239. Positions 54-367.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati112 – 14635PFTA 1Add
BLAST
Repeati147 – 18135PFTA 2Add
BLAST
Repeati182 – 21433PFTA 3Add
BLAST
Repeati215 – 24935PFTA 4Add
BLAST
Repeati255 – 28935PFTA 5Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi22 – 309Poly-Pro

Sequence similaritiesi

Contains 5 PFTA repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG0530. Eukaryota.
COG5536. LUCA.
GeneTreeiENSGT00550000074935.
HOGENOMiHOG000188957.
HOVERGENiHBG004498.
InParanoidiQ61239.
KOiK05955.
OMAiSDPPTNV.
OrthoDBiEOG77M8NV.
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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti191 – 1911D → N in AAH12711 (PubMed:15489334).Curated

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

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3PZ4X-ray2.10A1-377[»]
ProteinModelPortaliQ61239.
SMRiQ61239. Positions 54-367.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000016138.

Chemistry

BindingDBiQ61239.
ChEMBLiCHEMBL2096912.

PTM databases

iPTMnetiQ61239.
PhosphoSiteiQ61239.
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.
OMAiSDPPTNV.
OrthoDBiEOG77M8NV.
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

NextBioi285645.
PROiQ61239.
SOURCEiSearch...

Gene expression databases

BgeeiQ61239.
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...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and sequencing of the murine farnesyltransferase alpha-encoding cDNA from a cell line which expresses the human papillomavirus type-16 E6 gene."
    Shirasawa H., Kinoshita T., Shino Y., Mori K., Shimizu K., Simizu B.
    Gene 164:373-374(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  3. "Implication of geranylgeranyltransferase I in synapse formation."
    Luo Z.G., Je H.S., Wang Q., Yang F., Dobbins G.C., Yang Z.H., Xiong W.C., Lu B., Mei L.
    Neuron 40:703-717(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN NEUROMUSCULAR JUNCTION DEVELOPMENT, FUNCTION IN RAC1 ACTIVATION, PHOSPHORYLATION, INTERACTION WITH MUSK, ENZYME REGULATION.
  4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brown adipose tissue, Heart, Kidney, Lung, Pancreas, Spleen and Testis.
  5. Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 1-377, SUBUNIT, CATALYTIC ACTIVITY, FUNCTION.

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: May 11, 2016
This is version 121 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.