DP00558: Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha [Isoform 1]FASTA viewXML view

General information
DisProt:DP00558
Name:Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha [Isoform 1]
Synonym(s):FNTA_HUMAN
EC=2.5.1.58
EC=2.5.1.59
CAAX farnesyltransferase subunit alpha
Ras proteins prenyltransferase subunit alpha
FTase-alpha
Type I protein geranyl-geranyltransferase subunit alpha
GGTase-I-alpha
First appeared in release:Release 4.0 (06/23/2008)
UniProt:P49354-1
UniGene:Hs.370312
SwissProt: FNTA_HUMAN
TrEMBL:  
NCBI (GI): 1346694
Source organism:Homo sapiens (Human)
Sequence length:379
Percent disordered:14%
Homologues: 


Native sequence

        10         20         30         40         50         60
         |          |          |          |          |          |
MAATEGVGEA AQGGEPGQPA QPPPQPHPPP PQQQHKEEMA AEAGEAVASP MDDGFVSLDS - 60
PSYVLYRDRA EWADIDPVPQ NDGPNPVVQI IYSDKFRDVY DYFRAVLQRD ERSERAFKLT - 120
RDAIELNAAN YTVWHFRRVL LKSLQKDLHE EMNYITAIIE EQPKNYQVWH HRRVLVEWLR - 180
DPSQELEFIA DILNQDAKNY HAWQHRQWVI QEFKLWDNEL QYVDQLLKED VRNNSVWNQR - 240
YFVISNTTGY NDRAVLEREV QYTLEMIKLV PHNESAWNYL KGILQDRGLS KYPNLLNQLL - 300
DLQPSHSSPY LIAFLVDIYE DMLENQCDNK EDILNKALEL CEILAKEKDT IRKEYWRYIG - 360
RSLQSKHSTE NDSPTNVQQ



Functional narrative    

Attaches farnesyl lipid groups to the cysteine residue on the C-terminal tetrapeptide on many signal transduction proteins. 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.

Region 1: 1-54

Map of ordered and disordered regions







Note: 'Mouse' over a region to see the start and stop residues. Click on a region to see detailed information.


Region 1
Type:Disordered
Name:Alpha Subunit
Location:1 - 54
Length:54
Region sequence:

MAATEGVGEAAQGGEPGQPAQPPPQPHPPPPQQQHKEEMAAEAGEAVASPMDDG

Modification type: Native
PDB: 1JCQ:A
Structural/functional type: Function arises via an order to disorder transition
Functional classes: Modification site
Molecular assembly
Functional subclasses: Substrate/ligand binding
Detection methods:
  1. X-ray crystallography (290 K; pH: 5.7; )
References:
There are no documents referencing this region.
Comments:
 



References

  1. Long SB, Hancock PJ, Kral AM, Hellinga HW, Beese LS. "The crystal structure of human protein farnesyltransferase reveals the basis for inhibition by CaaX tetrapeptides and their mimetics." Proc Natl Acad Sci U S A. 2001; 98(23): 12948-53. PubMed: 11687658


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