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Protein

Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha

Gene

Fnta

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein 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.4 Publications

Catalytic activityi

Farnesyl diphosphate + protein-cysteine = S-farnesyl protein + diphosphate.4 Publications
Geranylgeranyl diphosphate + protein-cysteine = S-geranylgeranyl-protein + diphosphate.2 Publications

Enzyme regulationi

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

GO - Molecular functioni

GO - Biological processi

  • negative regulation of apoptotic process Source: RGD
  • negative regulation of nitric-oxide synthase biosynthetic process Source: RGD
  • positive regulation of cell cycle Source: RGD
  • positive regulation of cell proliferation Source: RGD
  • positive regulation of nitric-oxide synthase biosynthetic process 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
Complete GO annotation...

Keywords - Molecular functioni

Prenyltransferase, Transferase

Enzyme and pathway databases

BRENDAi2.5.1.58. 5301.
SABIO-RKQ04631.

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
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi2625. Fnta.

Subcellular locationi

GO - Cellular componenti

  • CAAX-protein geranylgeranyltransferase complex Source: RGD
  • cytoplasm Source: RGD
  • protein farnesyltransferase complex Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL2111479.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00001197482 – 377Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alphaAdd BLAST376

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

PaxDbiQ04631.
PRIDEiQ04631.

PTM databases

iPTMnetiQ04631.
PhosphoSitePlusiQ04631.

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 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
FntbQ0229314EBI-602447,EBI-602454
KRASP01116-22EBI-602447,EBI-367427From a different organism.
Pggt1bP536105EBI-602447,EBI-602610

Protein-protein interaction databases

DIPiDIP-6131N.
IntActiQ04631. 8 interactors.
MINTiMINT-121907.
STRINGi10116.ENSRNOP00000019594.

Chemistry databases

BindingDBiQ04631.

Structurei

Secondary structure

1377
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi58 – 60Combined sources3
Helixi66 – 68Combined sources3
Helixi70 – 72Combined sources3
Beta strandi73 – 75Combined sources3
Beta strandi87 – 90Combined sources4
Helixi94 – 109Combined sources16
Helixi114 – 126Combined sources13
Helixi131 – 143Combined sources13
Helixi148 – 161Combined sources14
Helixi166 – 179Combined sources14
Turni182 – 184Combined sources3
Helixi185 – 195Combined sources11
Helixi200 – 213Combined sources14
Helixi216 – 218Combined sources3
Helixi219 – 229Combined sources11
Turni230 – 232Combined sources3
Helixi234 – 246Combined sources13
Beta strandi250 – 252Combined sources3
Helixi253 – 269Combined sources17
Beta strandi270 – 272Combined sources3
Helixi274 – 284Combined sources11
Turni285 – 287Combined sources3
Helixi289 – 291Combined sources3
Helixi293 – 300Combined sources8
Helixi303 – 306Combined sources4
Helixi309 – 324Combined sources16
Helixi330 – 346Combined sources17
Turni347 – 349Combined sources3
Helixi350 – 352Combined sources3
Helixi353 – 367Combined sources15
Turni369 – 372Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
3KSLX-ray2.05A1-377[»]
3KSQX-ray2.10A1-377[»]
3PZ4X-ray2.10A1-377[»]
4GTMX-ray2.20A1-377[»]
4GTOX-ray2.15A1-377[»]
4GTPX-ray2.75A1-377[»]
4GTQX-ray2.60A1-377[»]
4GTRX-ray2.20A1-377[»]
ProteinModelPortaliQ04631.
SMRiQ04631.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ04631.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati112 – 146PFTA 1Add BLAST35
Repeati147 – 181PFTA 2Add BLAST35
Repeati182 – 214PFTA 3Add BLAST33
Repeati215 – 249PFTA 4Add BLAST35
Repeati255 – 289PFTA 5Add BLAST35

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi22 – 30Pro-rich9

Sequence similaritiesi

Contains 5 PFTA repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG0530. Eukaryota.
COG5536. LUCA.
HOGENOMiHOG000188957.
HOVERGENiHBG004498.
InParanoidiQ04631.
KOiK05955.
PhylomeDBiQ04631.

Family and domain databases

InterProiIPR002088. Prenyl_trans_a.
[Graphical view]
PfamiPF01239. PPTA. 5 hits.
[Graphical view]
PROSITEiPS51147. PFTA. 5 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q04631-1 [UniParc]FASTAAdd to basket

« Hide

        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
Length:377
Mass (Da):44,049
Last modified:October 1, 1993 - v1
Checksum:iDFFFECC1B88BC080
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M81225 mRNA. Translation: AAA41833.1.
PIRiA41625.
RefSeqiNP_036979.1. NM_012847.1.
UniGeneiRn.5990.

Genome annotation databases

GeneIDi25318.
KEGGirno:25318.
UCSCiRGD:2625. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M81225 mRNA. Translation: AAA41833.1.
PIRiA41625.
RefSeqiNP_036979.1. NM_012847.1.
UniGeneiRn.5990.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
3KSLX-ray2.05A1-377[»]
3KSQX-ray2.10A1-377[»]
3PZ4X-ray2.10A1-377[»]
4GTMX-ray2.20A1-377[»]
4GTOX-ray2.15A1-377[»]
4GTPX-ray2.75A1-377[»]
4GTQX-ray2.60A1-377[»]
4GTRX-ray2.20A1-377[»]
ProteinModelPortaliQ04631.
SMRiQ04631.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-6131N.
IntActiQ04631. 8 interactors.
MINTiMINT-121907.
STRINGi10116.ENSRNOP00000019594.

Chemistry databases

BindingDBiQ04631.
ChEMBLiCHEMBL2111479.

PTM databases

iPTMnetiQ04631.
PhosphoSitePlusiQ04631.

Proteomic databases

PaxDbiQ04631.
PRIDEiQ04631.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi25318.
KEGGirno:25318.
UCSCiRGD:2625. rat.

Organism-specific databases

CTDi2339.
RGDi2625. Fnta.

Phylogenomic databases

eggNOGiKOG0530. Eukaryota.
COG5536. LUCA.
HOGENOMiHOG000188957.
HOVERGENiHBG004498.
InParanoidiQ04631.
KOiK05955.
PhylomeDBiQ04631.

Enzyme and pathway databases

BRENDAi2.5.1.58. 5301.
SABIO-RKQ04631.

Miscellaneous databases

EvolutionaryTraceiQ04631.
PROiQ04631.

Family and domain databases

InterProiIPR002088. Prenyl_trans_a.
[Graphical view]
PfamiPF01239. PPTA. 5 hits.
[Graphical view]
PROSITEiPS51147. PFTA. 5 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiFNTA_RAT
AccessioniPrimary (citable) accession number: Q04631
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: November 2, 2016
This is version 135 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.