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Protein

Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha

Gene

FNTA

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: -Experimental evidence at transcript leveli

Functioni

Essential 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 (By similarity).By similarity

Catalytic activityi

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

Enzyme regulationi

Activated by the AGRIN-induced phosphorylation which is mediated by MUSK.By similarity

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionPrenyltransferase, Transferase

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:FNTA
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Unplaced

Subcellular locationi

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL2096987

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00001197452 – 375Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alphaAdd BLAST374

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineBy similarity1

Post-translational modificationi

Phosphorylated. Phosphorylation is mediated by MUSK upon AGRIN stimulation and results in the activation of FNTA (By similarity).By similarity

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP29702
PRIDEiP29702

Interactioni

Subunit structurei

Heterodimer of FNTA and FNTB (farnesyltransferase). Heterodimer of FNTA and PGGT1B (geranylgeranyltransferase). Interacts with MUSK; the interaction is direct and mediates AGRIN-induced phosphorylation of FNTA (By similarity).By similarity

Protein-protein interaction databases

ComplexPortaliCPX-2162 Protein farnesyltransferase complex
CPX-2169 Protein geranylgeranyl transferase type I complex
STRINGi9913.ENSBTAP00000004159

Chemistry databases

BindingDBiP29702

Structurei

3D structure databases

ProteinModelPortaliP29702
SMRiP29702
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati108 – 142PFTA 1Add BLAST35
Repeati143 – 176PFTA 2Add BLAST34
Repeati177 – 211PFTA 3Add BLAST35
Repeati212 – 245PFTA 4Add BLAST34
Repeati251 – 285PFTA 5Add BLAST35

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi16 – 37Pro-richAdd BLAST22

Sequence similaritiesi

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG0530 Eukaryota
COG5536 LUCA
HOGENOMiHOG000188957
HOVERGENiHBG004498
InParanoidiP29702
KOiK05955

Family and domain databases

InterProiView protein in InterPro
IPR002088 Prenyl_trans_a
PfamiView protein in Pfam
PF01239 PPTA, 5 hits
PROSITEiView protein in PROSITE
PS51147 PFTA, 5 hits

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P29702-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAADGVGEA AQGGDPGQPE PPPPPQPHPP PPPPQPPQEE AAAASPIDDG
60 70 80 90 100
FLSLDSPTYV LYRDRPEWAD IDPVPQNDGP NPVVQIIYSE KFQDVYDYFR
110 120 130 140 150
AVLQRDERSE RAFKLTRDAI ELNAANYTVW HFRRVLLKSL QKDLHEEMNY
160 170 180 190 200
ISAIIEEQPK NYQVWHHRRV LVEWLRDPSQ ELEFIADILT QDAKNYHAWQ
210 220 230 240 250
HRQWVIQEFK LWDNELQYVD QLLKEDVRNN SVWNQRYFVI SNTTGYNDRA
260 270 280 290 300
ILEREVQYTL EMIKLVPHNE SAWNYLKGIL QDRGLSKYPN LLNQLLDLQP
310 320 330 340 350
SHSSPYLIAF LVDIYEDMLE NQCDNKEDIL NKALELCEIL AKEKDTIRKE
360 370
YWRYIGRSLQ SKHSTESDPP TNVQQ
Length:375
Mass (Da):43,845
Last modified:June 13, 2006 - v2
Checksum:i7253AD4CED67296C
GO

Sequence cautioni

The sequence AAA30529 differs from that shown. Reason: Erroneous initiation.Curated
The sequence AAI12663 differs from that shown. Contaminating sequence. Potential poly-A sequence.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti47I → M in AAA30529 (PubMed:1918005).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC112662 mRNA Translation: AAI12663.1 Sequence problems.
M74083 mRNA Translation: AAA30529.1 Different initiation.
PIRiA41013
RefSeqiNP_803464.2, NM_177498.3
UniGeneiBt.407

Genome annotation databases

GeneIDi281169
KEGGibta:281169

Similar proteinsi

Entry informationi

Entry nameiFNTA_BOVIN
AccessioniPrimary (citable) accession number: P29702
Secondary accession number(s): Q2KIF0
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: June 13, 2006
Last modified: June 20, 2018
This is version 106 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

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