UniProtKB - Q04631 (FNTA_RAT)
Protein
Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha
Gene
Fnta
Organism
Rattus norvegicus (Rat)
Status
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.4 Publications
Catalytic activityi
- (2E,6E)-farnesyl diphosphate + L-cysteinyl-[protein] = diphosphate + S-(2E,6E)-farnesyl-L-cysteinyl-[protein]4 PublicationsEC:2.5.1.584 Publications
- geranylgeranyl diphosphate + L-cysteinyl-[protein] = diphosphate + S-geranylgeranyl-L-cysteinyl-[protein]2 PublicationsEC:2.5.1.592 Publications
Cofactori
Mg2+By similarity
Activity regulationi
Activated by the AGRIN-induced phosphorylation which is mediated by MUSK.By similarity
GO - Molecular functioni
- acetylcholine receptor regulator activity Source: RGD
- alpha-tubulin binding Source: RGD
- CAAX-protein geranylgeranyltransferase activity Source: UniProtKB-EC
- microtubule binding Source: RGD
- protein farnesyltransferase activity Source: RGD
- protein geranylgeranyltransferase activity Source: UniProtKB
- Rab geranylgeranyltransferase activity Source: RGD
- receptor tyrosine kinase binding Source: RGD
GO - Biological processi
- negative regulation of apoptotic process Source: RGD
- negative regulation of nitric-oxide synthase biosynthetic process Source: RGD
- neurotransmitter receptor metabolic process Source: RGD
- positive regulation of cell cycle Source: RGD
- positive regulation of cell population proliferation Source: RGD
- positive regulation of deacetylase activity Source: RGD
- positive regulation of nitric-oxide synthase biosynthetic process Source: RGD
- positive regulation of tubulin deacetylation Source: RGD
- protein farnesylation Source: UniProtKB
- protein geranylgeranylation Source: UniProtKB
- response to cytokine Source: RGD
- response to inorganic substance Source: RGD
- response to organic cyclic compound Source: RGD
Keywordsi
Molecular function | Prenyltransferase, Transferase |
Ligand | Magnesium |
Enzyme and pathway databases
BRENDAi | 2.5.1.58, 5301 |
Reactomei | R-RNO-111465, Apoptotic cleavage of cellular proteins R-RNO-2514859, Inactivation, recovery and regulation of the phototransduction cascade R-RNO-9648002, RAS processing |
SABIO-RKi | Q04631 |
Names & Taxonomyi
Protein namesi | Recommended name: Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha (EC:2.5.1.584 Publications, EC:2.5.1.592 Publications)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 |
Organismi | Rattus norvegicus (Rat) |
Taxonomic identifieri | 10116 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Rattus |
Proteomesi |
|
Organism-specific databases
RGDi | 2625, Fnta |
Subcellular locationi
Cytoskeleton
- microtubule associated complex Source: RGD
Other locations
- CAAX-protein geranylgeranyltransferase complex Source: RGD
- cytoplasm Source: RGD
- protein farnesyltransferase complex Source: UniProtKB
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Initiator methioninei | RemovedBy similarity | |||
ChainiPRO_0000119748 | 2 – 377 | Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alphaAdd BLAST | 376 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 2 | N-acetylalanineBy similarity | 1 |
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
AcetylationProteomic databases
jPOSTi | Q04631 |
PaxDbi | Q04631 |
PRIDEi | Q04631 |
PTM databases
iPTMneti | Q04631 |
PhosphoSitePlusi | Q04631 |
Interactioni
Subunit structurei
Interacts with MUSK; the interaction is direct and mediates AGRIN-induced phosphorylation of FNTA (By similarity). Heterodimer of FNTA and FNTB (farnesyltransferase). Heterodimer of FNTA and PGGT1B (geranylgeranyltransferase).
By similarity16 PublicationsBinary interactionsi
Hide detailsQ04631
With | #Exp. | IntAct |
---|---|---|
Fntb [Q02293] | 16 | EBI-602447,EBI-602454 |
Ntrk2 [Q63604] | 4 | EBI-602447,EBI-7287667 |
Pggt1b [P53610] | 7 | EBI-602447,EBI-602610 |
KRAS - isoform 2B [P01116-2] from Homo sapiens. | 3 | EBI-602447,EBI-367427 |
GO - Molecular functioni
- alpha-tubulin binding Source: RGD
- microtubule binding Source: RGD
- receptor tyrosine kinase binding Source: RGD
Protein-protein interaction databases
BioGRIDi | 247357, 1 interactor |
ComplexPortali | CPX-2181, Protein farnesyltransferase complex |
CORUMi | Q04631 |
DIPi | DIP-6131N |
IntActi | Q04631, 9 interactors |
STRINGi | 10116.ENSRNOP00000019594 |
Chemistry databases
BindingDBi | Q04631 |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | Q04631 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | Q04631 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Repeati | 112 – 146 | PFTA 1Add BLAST | 35 | |
Repeati | 147 – 181 | PFTA 2Add BLAST | 35 | |
Repeati | 182 – 214 | PFTA 3Add BLAST | 33 | |
Repeati | 215 – 249 | PFTA 4Add BLAST | 35 | |
Repeati | 255 – 289 | PFTA 5Add BLAST | 35 |
Compositional bias
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Compositional biasi | 22 – 30 | Pro-rich | 9 |
Sequence similaritiesi
Belongs to the protein prenyltransferase subunit alpha family.Curated
Keywords - Domaini
RepeatPhylogenomic databases
eggNOGi | KOG0530, Eukaryota |
InParanoidi | Q04631 |
OrthoDBi | 1527547at2759 |
PhylomeDBi | Q04631 |
Family and domain databases
InterProi | View protein in InterPro IPR002088, Prenyl_trans_a |
Pfami | View protein in Pfam PF01239, PPTA, 5 hits |
PROSITEi | View protein in PROSITE PS51147, PFTA, 5 hits |
(1+)i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
This entry has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All
Q04631-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MAATEGVGES APGGEPGQPE QPPPPPPPPP AQQPQEEEMA AEAGEAAASP
60 70 80 90 100
MDDGFLSLDS PTYVLYRDRA EWADIDPVPQ NDGPSPVVQI IYSEKFRDVY
110 120 130 140 150
DYFRAVLQRD ERSERAFKLT RDAIELNAAN YTVWHFRRVL LRSLQKDLQE
160 170 180 190 200
EMNYIIAIIE EQPKNYQVWH HRRVLVEWLK DPSQELEFIA DILNQDAKNY
210 220 230 240 250
HAWQHRQWVI QEFRLWDNEL QYVDQLLKED VRNNSVWNQR HFVISNTTGY
260 270 280 290 300
SDRAVLEREV QYTLEMIKLV PHNESAWNYL KGILQDRGLS RYPNLLNQLL
310 320 330 340 350
DLQPSHSSPY LIAFLVDIYE DMLENQCDNK EDILNKALEL CEILAKEKDT
360 370
IRKEYWRYIG RSLQSKHSRE SDIPASV
Computationally mapped potential isoform sequencesi
There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basketQ5RKJ4 | Q5RKJ4_RAT | Farnesyltransferase, CAAX box, alph... | Fnta rCG_42999 | 377 | Annotation score: |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | M81225 mRNA Translation: AAA41833.1 |
PIRi | A41625 |
RefSeqi | NP_036979.1, NM_012847.1 |
Genome annotation databases
GeneIDi | 25318 |
KEGGi | rno:25318 |
UCSCi | RGD:2625, rat |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | M81225 mRNA Translation: AAA41833.1 |
PIRi | A41625 |
RefSeqi | NP_036979.1, NM_012847.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1D8D | X-ray | 2.00 | A | 1-377 | [»] | |
1D8E | X-ray | 3.00 | A | 1-377 | [»] | |
1FPP | X-ray | 2.75 | A | 1-377 | [»] | |
1FT1 | X-ray | 2.25 | A | 1-377 | [»] | |
1FT2 | X-ray | 3.40 | A | 55-369 | [»] | |
1FTI | model | - | A | 55-369 | [»] | |
1HZ7 | model | - | A | 116-247 | [»] | |
1JCR | X-ray | 2.00 | A | 1-377 | [»] | |
1JCS | X-ray | 2.20 | A | 1-377 | [»] | |
1KZO | X-ray | 2.20 | A | 1-377 | [»] | |
1KZP | X-ray | 2.10 | A | 1-377 | [»] | |
1KZR | model | - | A | 55-377 | [»] | |
1N4P | X-ray | 2.65 | A/C/E/G/I/K | 1-377 | [»] | |
1N4Q | X-ray | 2.40 | A/C/E/G/I/K | 1-377 | [»] | |
1N4R | X-ray | 2.80 | A/C/E/G/I/K | 1-377 | [»] | |
1N4S | X-ray | 2.60 | A/C/E/G/I/K | 1-377 | [»] | |
1N94 | X-ray | 3.50 | A | 55-369 | [»] | |
1N95 | X-ray | 2.30 | A | 55-369 | [»] | |
1N9A | X-ray | 3.20 | A | 55-369 | [»] | |
1NI1 | X-ray | 2.30 | A | 55-369 | [»] | |
1NL4 | X-ray | 2.70 | A | 55-366 | [»] | |
1O1R | X-ray | 2.30 | A | 1-377 | [»] | |
1O1S | X-ray | 2.30 | A | 1-377 | [»] | |
1O1T | X-ray | 2.10 | A | 1-377 | [»] | |
1O5M | X-ray | 2.30 | A | 1-377 | [»] | |
1QBQ | X-ray | 2.40 | A | 45-377 | [»] | |
1QE2 | model | - | A | 116-247 | [»] | |
1S64 | X-ray | 2.55 | A/C/E/G/I/K | 1-377 | [»] | |
1SA5 | X-ray | 2.60 | A | 1-377 | [»] | |
1TN7 | X-ray | 2.30 | A | 1-377 | [»] | |
1TN8 | X-ray | 2.25 | A | 1-377 | [»] | |
1TNB | X-ray | 2.85 | A/C/E/G/I/K | 1-377 | [»] | |
1TNO | X-ray | 2.70 | A/C/E/G/I/K | 1-377 | [»] | |
1TNU | X-ray | 2.70 | A/C/E/G/I/K | 1-377 | [»] | |
1TNY | X-ray | 2.70 | A/C/E/G/I/K | 1-377 | [»] | |
1TNZ | X-ray | 2.90 | A/C/E/G/I/K | 1-377 | [»] | |
1X81 | X-ray | 3.50 | A | 55-369 | [»] | |
2BED | X-ray | 2.70 | A | 54-366 | [»] | |
2FTI | model | - | A | 55-369 | [»] | |
2R2L | X-ray | 2.23 | A | 54-368 | [»] | |
2ZIR | X-ray | 2.40 | A | 1-377 | [»] | |
2ZIS | X-ray | 2.60 | A | 1-377 | [»] | |
3DPY | X-ray | 2.70 | A | 1-377 | [»] | |
3E30 | X-ray | 2.45 | A | 1-377 | [»] | |
3E32 | X-ray | 2.45 | A | 1-377 | [»] | |
3E33 | X-ray | 1.90 | A | 1-377 | [»] | |
3E34 | X-ray | 2.05 | A | 1-377 | [»] | |
3EU5 | X-ray | 2.80 | A | 1-377 | [»] | |
3EUV | X-ray | 2.75 | A | 1-377 | [»] | |
3FTI | model | - | A | 55-369 | [»] | |
3KSL | X-ray | 2.05 | A | 1-377 | [»] | |
3KSQ | X-ray | 2.10 | A | 1-377 | [»] | |
3PZ4 | X-ray | 2.10 | A | 1-377 | [»] | |
4GTM | X-ray | 2.20 | A | 1-377 | [»] | |
4GTO | X-ray | 2.15 | A | 1-377 | [»] | |
4GTP | X-ray | 2.75 | A | 1-377 | [»] | |
4GTQ | X-ray | 2.60 | A | 1-377 | [»] | |
4GTR | X-ray | 2.20 | A | 1-377 | [»] | |
SMRi | Q04631 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 247357, 1 interactor |
ComplexPortali | CPX-2181, Protein farnesyltransferase complex |
CORUMi | Q04631 |
DIPi | DIP-6131N |
IntActi | Q04631, 9 interactors |
STRINGi | 10116.ENSRNOP00000019594 |
Chemistry databases
BindingDBi | Q04631 |
ChEMBLi | CHEMBL2095197 CHEMBL2111479 |
PTM databases
iPTMneti | Q04631 |
PhosphoSitePlusi | Q04631 |
Proteomic databases
jPOSTi | Q04631 |
PaxDbi | Q04631 |
PRIDEi | Q04631 |
Genome annotation databases
GeneIDi | 25318 |
KEGGi | rno:25318 |
UCSCi | RGD:2625, rat |
Organism-specific databases
CTDi | 2339 |
RGDi | 2625, Fnta |
Phylogenomic databases
eggNOGi | KOG0530, Eukaryota |
InParanoidi | Q04631 |
OrthoDBi | 1527547at2759 |
PhylomeDBi | Q04631 |
Enzyme and pathway databases
BRENDAi | 2.5.1.58, 5301 |
Reactomei | R-RNO-111465, Apoptotic cleavage of cellular proteins R-RNO-2514859, Inactivation, recovery and regulation of the phototransduction cascade R-RNO-9648002, RAS processing |
SABIO-RKi | Q04631 |
Miscellaneous databases
EvolutionaryTracei | Q04631 |
PROi | PR:Q04631 |
Family and domain databases
InterProi | View protein in InterPro IPR002088, Prenyl_trans_a |
Pfami | View protein in Pfam PF01239, PPTA, 5 hits |
PROSITEi | View protein in PROSITE PS51147, PFTA, 5 hits |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | FNTA_RAT | |
Accessioni | Q04631Primary (citable) accession number: Q04631 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | October 1, 1993 |
Last sequence update: | October 1, 1993 | |
Last modified: | December 2, 2020 | |
This is version 156 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencing, Reference proteomeDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families