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Q61239 (FNTA_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 84. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended 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
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length377 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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. Ref.3

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. Ref.3

Subunit structure

Heterodimer of an alpha and a beta subunit. Interacts with MUSK; the interaction is direct and mediates AGRIN-induced phosphorylation of FNTA. Ref.3

Post-translational modification

Phosphorylated. Phosphorylation is mediated by MUSK upon AGRIN stimulation and results in the activation of FNTA. Ref.3

Sequence similarities

Belongs to the protein prenyltransferase subunit alpha family.

Contains 5 PFTA repeats.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 377376Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha
PRO_0000119747

Regions

Repeat112 – 14635PFTA 1
Repeat147 – 18135PFTA 2
Repeat182 – 21433PFTA 3
Repeat215 – 24935PFTA 4
Repeat255 – 28935PFTA 5
Compositional bias22 – 309Poly-Pro

Amino acid modifications

Modified residue21N-acetylalanine By similarity

Experimental info

Sequence conflict1911D → N in AAH12711. Ref.2

Secondary structure

1 .......................................... 377
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q61239 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: F3D60B9899F36D66

FASTA37744,013
        10         20         30         40         50         60 
MAATEGVGES AAGGEPGQPE QPPPPPPPPP AQQPQEEEMA AEAGEAAASP MDDGFLSLDS 

        70         80         90        100        110        120 
PTYVLYRDRA EWADIDPVPQ NDGPNPVVQI IYSEKFRDVY DYFRAVLQRD ERSERAFKLT 

       130        140        150        160        170        180 
RDAIELNAAN YTVWHFRRVL LRSLQKDLQE EMNYITAIIE EQPKNYQVWH HRRVLVEWLK 

       190        200        210        220        230        240 
DPSQELEFIA DILSQDAKNY HAWQHRQWVI QEFRLWDNEL QYVDQLLKED VRNNSVWNQR 

       250        260        270        280        290        300 
HFVISNTTGY SDRAVLEREV QYTLEMIKLV PHNESAWNYL KGILQDRGLS RYPNLLNQLL 

       310        320        330        340        350        360 
DLQPSHSSPY LIAFLVDVYE DMLENQCDNK EDILNKALEL CEILAKEKDT IRKEYWRYIG 

       370 
RSLQSKHCRE SDIPASV

« Hide

References

« Hide 'large scale' references
[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: 7590362] [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: 15489334] [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: 14622576] [Abstract]
Cited for: FUNCTION IN NEUROMUSCULAR JUNCTION DEVELOPMENT, FUNCTION IN RAC1 ACTIVATION, PHOSPHORYLATION, INTERACTION WITH MUSK, ENZYME REGULATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		D49744 mRNA. Translation: BAA08578.1.
BC012711 mRNA. Translation: AAH12711.1.
IPIIPI00118904.
PIRJC4368.
RefSeqNP_032059.1. NM_008033.3.
UniGeneMm.3496.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3PZ4X-ray2.10A1-377[»]
ProteinModelPortalQ61239.
SMRQ61239. Positions 54-367.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ61239.

PTM databases

PhosphoSiteQ61239.

Proteomic databases

PRIDEQ61239.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000016138; ENSMUSP00000016138; ENSMUSG00000015994.
GeneID14272.
KEGGmmu:14272.

Organism-specific databases

CTD2339.
MGIMGI:104683. Fnta.

Phylogenomic databases

GeneTreeENSGT00550000074935.
HOGENOMHBG623262.
HOVERGENHBG004498.
InParanoidQ61239.
OMAVEWLRDP.
OrthoDBEOG46DM39.
PhylomeDBQ61239.

Gene expression databases

ArrayExpressQ61239.
BgeeQ61239.
CleanExMM_FNTA.
GenevestigatorQ61239.
GermOnlineENSMUSG00000015994. Mus musculus.

Family and domain databases

InterProIPR002088. Prenyl_trans_a.
IPR008940. Prenyltransferase.
[Graphical view]
Gene3DG3DSA:1.25.40.120. Prenyl_trans. 1 hit.
KOK05955.
PfamPF01239. PPTA. 5 hits.
[Graphical view]
PROSITEPS51147. PFTA. 5 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio285645.
SOURCESearch...

Entry information

Entry nameFNTA_MOUSE
AccessionPrimary (citable) accession number: Q61239
Secondary accession number(s): Q921F7
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: January 25, 2012
This is version 84 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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