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Reviewed, UniProtKB/Swiss-Prot Q04631 (FNTA_RAT)

Last modified January 19, 2010. Version 84. 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 · Binary interactions · 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
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

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.

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. Ref.5

Sequence similarities

Belongs to the protein prenyltransferase subunit alpha family.

Contains 5 PFTA repeats.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

FntbQ022937EBI-602447,EBI-602454

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 377376Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha
PRO_0000119748

Regions

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

Amino acid modifications

Modified residue21N-acetylalanine By similarity

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
Q04631-1 [UniParc].

Last modified October 1, 1993. Version 1.
Checksum: DFFFECC1B88BC080

FASTA37744,049
        10         20         30         40         50         60 
MAATEGVGES APGGEPGQPE QPPPPPPPPP AQQPQEEEMA AEAGEAAASP MDDGFLSLDS 

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

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

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

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

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

       370 
RSLQSKHSRE SDIPASV 

« Hide

References

[1]"Cloning and expression of a cDNA encoding the alpha subunit of rat p21ras protein farnesyltransferase."
Chen W.-J., Andres D.A., Goldstein J.L., Brown M.S.
Proc. Natl. Acad. Sci. U.S.A. 88:11368-11372(1991) [PubMed: 1763049] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
Tissue: Brain.
[2]"Crystal structure of protein farnesyltransferase at 2.25-A resolution."
Park H.-W., Boduluri S.R., Mooomaw J.F., Casey P.J., Beese L.S.
Science 275:1800-1804(1997) [PubMed: 9065406] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS).
[3]Erratum
Park H.-W., Boduluri S.R., Mooomaw J.F., Casey P.J., Beese L.S.
Science 276:21-21(1997)
[4]"Cocrystal structure of protein farnesyltransferase complexed with a farnesyl diphosphate substrate."
Long S.B., Casey P.J., Beese L.S.
Biochemistry 37:9612-9618(1998) [PubMed: 9657673] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.4 ANGSTROMS).
[5]"The crystal structure of human protein farnesyltransferase reveals the basis for inhibition by CaaX tetrapeptides and their mimetics."
Long S.B., Hancock P.J., Kral A.M., Hellinga H.W., Beese L.S.
Proc. Natl. Acad. Sci. U.S.A. 98:12948-12953(2001) [PubMed: 11687658] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH BETA SUBUNIT AND GERANYLGERANYL DIPHOSPHATE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M81225 mRNA. Translation: AAA41833.1.
IPIIPI00188070.
PIRA41625.
RefSeqNP_036979.1.
UniGeneRn.5990

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1D8DX-ray2.00A1-377[»]
1D8EX-ray3.00A1-377[»]
1FPPX-ray2.75A1-377[»]
1FT1X-ray2.25A1-377[»]
1FT2X-ray3.40A55-369[»]
1FTImodel-A55-369[»]
1HZ7model-A116-247[»]
1JCRX-ray2.00A1-377[»]
1JCSX-ray2.20A1-377[»]
1KZOX-ray2.20A1-377[»]
1KZPX-ray2.10A1-377[»]
1KZRmodel-A55-377[»]
1N4PX-ray2.65A/C/E/G/I/K1-377[»]
1N4QX-ray2.40A/C/E/G/I/K1-377[»]
1N4RX-ray2.80A/C/E/G/I/K1-377[»]
1N4SX-ray2.60A/C/E/G/I/K1-377[»]
1N94X-ray3.50A55-369[»]
1N95X-ray2.30A55-369[»]
1N9AX-ray3.20A55-369[»]
1NI1X-ray2.30A55-369[»]
1NL4X-ray2.70A55-366[»]
1O1RX-ray2.30A1-377[»]
1O1SX-ray2.30A1-377[»]
1O1TX-ray2.10A1-377[»]
1O5MX-ray2.30A1-377[»]
1QBQX-ray2.40A45-377[»]
1QE2model-A116-247[»]
1S64X-ray2.55A/C/E/G/I/K1-377[»]
1SA5X-ray2.60A1-377[»]
1TN7X-ray2.30A1-377[»]
1TN8X-ray2.25A1-377[»]
1TNBX-ray2.85A/C/E/G/I/K1-377[»]
1TNOX-ray2.70A/C/E/G/I/K1-377[»]
1TNUX-ray2.70A/C/E/G/I/K1-377[»]
1TNYX-ray2.70A/C/E/G/I/K1-377[»]
1TNZX-ray2.90A/C/E/G/I/K1-377[»]
1X81X-ray3.50A55-369[»]
2BEDX-ray2.70A54-366[»]
2FTImodel-A55-369[»]
2R2LX-ray2.23A54-368[»]
2ZIRX-ray2.40A1-377[»]
2ZISX-ray2.60A1-377[»]
3DPYX-ray2.70A1-377[»]
3E30X-ray2.45A1-377[»]
3E32X-ray2.45A1-377[»]
3E33X-ray1.90A1-377[»]
3E34X-ray2.05A1-377[»]
3EU5X-ray2.80A1-377[»]
3EUVX-ray2.75A1-377[»]
3FTImodel-A55-369[»]
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-6131N.
IntActQ04631. 9 interactions.
STRINGQ04631.

Genome annotation databases

EnsemblENSRNOT00000019594; ENSRNOP00000019594; ENSRNOG00000014462; Rattus norvegicus. [Genome view]
GeneID25318.
KEGGrno:25318.
UCSCNM_012847. rat.

Organism-specific databases

CTD25318.
RGD2625. Fnta.

Phylogenomic databases

HOVERGENQ04631.
InParanoidQ04631.
PhylomeDBQ04631.

Enzyme and pathway databases

BRENDA2.5.1.58. 248.
2.5.1.59. 248.

Gene expression databases

ArrayExpressQ04631.
GenevestigatorQ04631.
GermOnlineENSRNOG00000014462. Rattus norvegicus.

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

NextBio606153.

Entry information

Entry nameFNTA_RAT
AccessionPrimary (citable) accession number: Q04631
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: January 19, 2010
This is version 84 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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