NameProtein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha
Synonyms
  • 2.5.1.58
  • CAAX farnesyltransferase subunit alpha
  • FTase-alpha
  • GGTase-I-alpha
  • Ras proteins prenyltransferase subunit alpha
  • Type I protein geranyl-geranyltransferase subunit alpha
Gene NameFNTA
OrganismHuman
Amino acid sequence
>lcl|BSEQ0004661|Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha
MAATEGVGEAAQGGEPGQPAQPPPQPHPPPPQQQHKEEMAAEAGEAVASPMDDGFVSLDS
PSYVLYRDRAEWADIDPVPQNDGPNPVVQIIYSDKFRDVYDYFRAVLQRDERSERAFKLT
RDAIELNAANYTVWHFRRVLLKSLQKDLHEEMNYITAIIEEQPKNYQVWHHRRVLVEWLR
DPSQELEFIADILNQDAKNYHAWQHRQWVIQEFKLWDNELQYVDQLLKEDVRNNSVWNQR
YFVISNTTGYNDRAVLEREVQYTLEMIKLVPHNESAWNYLKGILQDRGLSKYPNLLNQLL
DLQPSHSSPYLIAFLVDIYEDMLENQCDNKEDILNKALELCEILAKEKDTIRKEYWRYIG
RSLQSKHSTENDSPTNVQQ
Number of residues379
Molecular Weight44408.32
Theoretical pI4.72
GO Classification
Functions
  • protein geranylgeranyltransferase activity
  • alpha-tubulin binding
  • microtubule binding
  • acetylcholine receptor regulator activity
  • CAAX-protein geranylgeranyltransferase activity
  • protein farnesyltransferase activity
  • Rab geranylgeranyltransferase activity
Processes
  • positive regulation of tubulin deacetylation
  • protein farnesylation
  • protein geranylgeranylation
  • apoptotic process
  • regulation of rhodopsin mediated signaling pathway
  • phototransduction, visible light
  • rhodopsin mediated signaling pathway
  • transforming growth factor beta receptor signaling pathway
  • cellular component disassembly involved in execution phase of apoptosis
  • neurotransmitter receptor metabolic process
  • programmed cell death
  • positive regulation of deacetylase activity
Components
  • cytosol
  • CAAX-protein geranylgeranyltransferase complex
  • protein farnesyltransferase complex
  • cytoplasm
  • microtubule associated complex
General FunctionRab geranylgeranyltransferase activity
Specific FunctionEssential subunit of both the farnesyltransferase and the geranylgeranyltransferase complex. Contributes to the transfer of a farnesyl or geranylgeranyl moiety from farnesyl or geranylgeranyl diphosphate to a cysteine at the fourth position from the C-terminus of several proteins having the C-terminal sequence Cys-aliphatic-aliphatic-X. May positively regulate neuromuscular junction development downstream of MUSK via its function in RAC1 prenylation and activation.
Pfam Domain Function
Transmembrane RegionsNot Available
GenBank Protein IDNot Available
UniProtKB IDP49354
UniProtKB Entry NameFNTA_HUMAN
Cellular LocationNot Available
Gene sequence
>lcl|BSEQ0011702|Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha (FNTA)
ATGGCGGCCACCGAGGGGGTCGGGGAGGCTGCGCAAGGGGGCGAGCCCGGGCAGCCGGCG
CAACCCCCGCCCCAGCCGCACCCACCGCCGCCCCAGCAGCAGCACAAGGAAGAGATGGCG
GCCGAGGCTGGGGAAGCCGTGGCGTCCCCCATGGACGACGGGTTTGTGAGCCTGGACTCG
CCCTCCTATGTCCTGTACAGGGACAGAGCAGAATGGGCTGATATAGATCCGGTGCCGCAG
AATGATGGCCCCAATCCCGTGGTCCAGATCATTTATAGTGACAAATTTAGAGATGTTTAT
GATTACTTCCGAGCTGTCCTGCAGCGTGATGAAAGAAGTGAACGAGCTTTTAAGCTAACC
CGGGATGCTATTGAGTTAAATGCAGCCAATTATACAGTGTGGCATTTCCGGAGAGTTCTT
TTGAAGTCACTTCAGAAGGATCTACATGAGGAAATGAACTACATCACTGCAATAATTGAG
GAGCAGCCCAAAAACTATCAAGTTTGGCATCATAGGCGAGTATTAGTGGAATGGCTAAGA
GATCCATCTCAGGAGCTTGAATTTATTGCTGATATTCTTAATCAGGATGCAAAGAATTAT
CATGCCTGGCAGCATCGACAATGGGTTATTCAGGAATTTAAACTTTGGGATAATGAGCTG
CAGTATGTGGACCAACTTCTGAAAGAGGATGTGAGAAATAACTCTGTCTGGAACCAAAGA
TACTTCGTTATTTCTAACACCACTGGCTACAATGATCGTGCTGTATTGGAGAGAGAAGTC
CAATACACTCTGGAAATGATTAAACTAGTACCACATAATGAAAGTGCATGGAACTATTTG
AAAGGGATTTTGCAGGATCGTGGTCTTTCCAAATATCCTAATCTGTTAAATCAATTACTT
GATTTACAACCAAGTCATAGTTCCCCCTACCTAATTGCCTTTCTTGTGGATATCTATGAA
GACATGCTAGAAAATCAGTGTGACAATAAGGAAGACATTCTTAATAAAGCATTAGAGTTA
TGTGAAATCCTAGCTAAAGAAAAGGACACTATAAGAAAGGAATATTGGAGATACATTGGA
AGATCCCTTCAAAGCAAACACAGCACAGAAAATGACTCACCAACAAATGTACAGCAATAA
GenBank Gene IDL10413
GeneCard IDNot Available
GenAtlas IDFNTA
HGNC IDHGNC:3782
Chromosome Location8
Locus8p11
References
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  2. Andres DA, Goldstein JL, Ho YK, Brown MS: Mutational analysis of alpha-subunit of protein farnesyltransferase. Evidence for a catalytic role. J Biol Chem. 1993 Jan 15;268(2):1383-90. 8419339
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