Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha

Gene

Fnta

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: -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

Keywordsi

Molecular functionPrenyltransferase, Transferase

Enzyme and pathway databases

BRENDAi2.5.1.58 5301
SABIO-RKiQ04631

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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi

Organism-specific databases

RGDi2625 Fnta

Subcellular locationi

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

Show more details

Protein-protein interaction databases

CORUMiQ04631
DIPiDIP-6131N
IntActiQ04631, 9 interactors
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

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG0530 Eukaryota
COG5536 LUCA
HOGENOMiHOG000188957
HOVERGENiHBG004498
InParanoidiQ04631
KOiK05955
PhylomeDBiQ04631

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.

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

Entry informationi

Entry nameiFNTA_RAT
AccessioniPrimary (citable) accession number: Q04631
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: May 23, 2018
This is version 142 of the entry and version 1 of the sequence. See 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

Cookie policy

We would like to use anonymized google analytics cookies to gather statistics on how uniprot.org is used in aggregate. Learn more

UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health