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Reviewed, UniProtKB/Swiss-Prot Q61239 (FNTA_MOUSE)

Last modified January 19, 2010. Version 69. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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
    Ras proteins prenyltransferase subunit alpha
    FTase-alpha
    Type I protein geranyl-geranyltransferase subunit alpha
      Short name=GGTase-I-alpha
Gene names
Name: Fnta
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMus

Protein attributes

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

Catalytic activity

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

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

Subunit structure

Heterodimer of an alpha and a beta subunit.

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

Sequences

Sequence LengthMass (Da)Tools
Q61239-1 [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].
+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.
UniGeneMm.3496

3D structure databases

SMRQ61239. Positions 55-377.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ61239.

PTM databases

PhosphoSiteQ61239.

Proteomic databases

PRIDEQ61239.

Genome annotation databases

EnsemblENSMUST00000016138; ENSMUSP00000016138; ENSMUSG00000015994; Mus musculus. [Genome view]
GeneID14272.
KEGGmmu:14272.
UCSCuc009lhi.1. mouse.

Organism-specific databases

CTD14272.
MGIMGI:104683. Fnta.

Phylogenomic databases

HOGENOMHBG623262.
HOVERGENQ61239.
InParanoidQ61239.
OMAVEWLRDP.
OrthoDBEOG9909VB.
PhylomeDBQ61239.

Enzyme and pathway databases

BRENDA2.5.1.58. 244.
2.5.1.59. 244.

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.
PfamPF01239. PPTA. 5 hits.
[Graphical view]
PROSITEPS51147. PFTA. 5 hits.
[Graphical view]
ProtoNetSearch...

Other Resources

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 19, 2010
This is version 69 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

MGD cross-references

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

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents