Skip Header

Contribute Send feedback
Read comments (?) or add your own

P29702 (FNTA_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 78. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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
OrganismBos taurus (Bovine)
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length375 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. 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 375374Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha
PRO_0000119745

Regions

Repeat108 – 14235PFTA 1
Repeat143 – 17634PFTA 2
Repeat177 – 21135PFTA 3
Repeat212 – 24534PFTA 4
Repeat251 – 28535PFTA 5
Compositional bias16 – 3722Pro-rich

Amino acid modifications

Modified residue21N-acetylalanine By similarity

Experimental info

Sequence conflict471I → M in AAA30529. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P29702 [UniParc].

Last modified June 13, 2006. Version 2.
Checksum: 7253AD4CED67296C

FASTA37543,845
        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 

« Hide

References

« Hide '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.
IPIIPI00706713.
PIRA41013.
RefSeqNP_803464.2. NM_177498.3.
UniGeneBt.407.

3D structure databases

ProteinModelPortalP29702.
SMRP29702. Positions 51-365.
ModBaseSearch...

Protein-protein interaction databases

STRINGP29702.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID281169.
KEGGbta:281169.

Organism-specific databases

CTD2339.

Phylogenomic databases

HOVERGENHBG004498.
InParanoidP29702.
OrthoDBEOG46DM39.
PhylomeDBP29702.

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...

Entry information

Entry nameFNTA_BOVIN
AccessionPrimary (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 statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families