FNTA_MOUSE
ID FNTA_MOUSE Reviewed; 377 AA.
AC Q61239; Q921F7;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha;
DE EC=2.5.1.58;
DE EC=2.5.1.59 {ECO:0000305|PubMed:14622576};
DE AltName: Full=CAAX farnesyltransferase subunit alpha;
DE AltName: Full=FTase-alpha;
DE AltName: Full=Ras proteins prenyltransferase subunit alpha;
DE AltName: Full=Type I protein geranyl-geranyltransferase subunit alpha;
DE Short=GGTase-I-alpha;
GN Name=Fnta;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7590362; DOI=10.1016/0378-1119(95)00445-c;
RA Shirasawa H., Kinoshita T., Shino Y., Mori K., Shimizu K., Simizu B.;
RT "Cloning and sequencing of the murine farnesyltransferase alpha-encoding
RT cDNA from a cell line which expresses the human papillomavirus type-16 E6
RT gene.";
RL Gene 164:373-374(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP FUNCTION IN NEUROMUSCULAR JUNCTION DEVELOPMENT, FUNCTION IN RAC1
RP ACTIVATION, CATALYTIC ACTIVITY, PHOSPHORYLATION, INTERACTION WITH MUSK,
RP ACTIVITY REGULATION, AND MUTAGENESIS OF LYS-164 AND TYR-200.
RX PubMed=14622576; DOI=10.1016/s0896-6273(03)00695-0;
RA Luo Z.G., Je H.S., Wang Q., Yang F., Dobbins G.C., Yang Z.H., Xiong W.C.,
RA Lu B., Mei L.;
RT "Implication of geranylgeranyltransferase I in synapse formation.";
RL Neuron 40:703-717(2003).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Lung, Pancreas, Spleen, and
RC Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Essential subunit of both the farnesyltransferase and the
CC geranylgeranyltransferase complex. Contributes to the transfer of a
CC farnesyl or geranylgeranyl moiety from farnesyl or geranylgeranyl
CC diphosphate to a cysteine at the fourth position from the C-terminus of
CC several proteins having the C-terminal sequence Cys-aliphatic-
CC aliphatic-X. May positively regulate neuromuscular junction development
CC downstream of MUSK via its function in RAC1 prenylation and activation.
CC {ECO:0000269|PubMed:14622576}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate + L-cysteinyl-[protein] =
CC diphosphate + S-(2E,6E)-farnesyl-L-cysteinyl-[protein];
CC Xref=Rhea:RHEA:13345, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:11535,
CC ChEBI:CHEBI:29950, ChEBI:CHEBI:33019, ChEBI:CHEBI:86019,
CC ChEBI:CHEBI:175763; EC=2.5.1.58;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=geranylgeranyl diphosphate + L-cysteinyl-[protein] =
CC diphosphate + S-geranylgeranyl-L-cysteinyl-[protein];
CC Xref=Rhea:RHEA:21240, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:11537,
CC ChEBI:CHEBI:29950, ChEBI:CHEBI:33019, ChEBI:CHEBI:57533,
CC ChEBI:CHEBI:86021; EC=2.5.1.59;
CC Evidence={ECO:0000305|PubMed:14622576};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P29703};
CC -!- ACTIVITY REGULATION: Activated by the AGRIN-induced phosphorylation
CC which is mediated by MUSK. {ECO:0000269|PubMed:14622576}.
CC -!- SUBUNIT: Heterodimer of FNTA and FNTB (farnesyltransferase).
CC Heterodimer of FNTA and PGGT1B (geranylgeranyltransferase). Interacts
CC with MUSK; the interaction is direct and mediates AGRIN-induced
CC phosphorylation of FNTA. {ECO:0000269|PubMed:14622576}.
CC -!- PTM: Phosphorylated. Phosphorylation is mediated by MUSK upon AGRIN
CC stimulation and results in the activation of FNTA.
CC {ECO:0000269|PubMed:14622576}.
CC -!- SIMILARITY: Belongs to the protein prenyltransferase subunit alpha
CC family. {ECO:0000305}.
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DR EMBL; D49744; BAA08578.1; -; mRNA.
DR EMBL; BC012711; AAH12711.1; -; mRNA.
DR CCDS; CCDS22205.1; -.
DR PIR; JC4368; JC4368.
DR RefSeq; NP_032059.1; NM_008033.3.
DR AlphaFoldDB; Q61239; -.
DR SMR; Q61239; -.
DR BioGRID; 199723; 4.
DR ComplexPortal; CPX-2185; Protein farnesyltransferase complex.
DR ComplexPortal; CPX-2949; Protein geranylgeranyl transferase type I complex.
DR STRING; 10090.ENSMUSP00000016138; -.
DR BindingDB; Q61239; -.
DR ChEMBL; CHEMBL2096912; -.
DR ChEMBL; CHEMBL3301421; -.
DR iPTMnet; Q61239; -.
DR PhosphoSitePlus; Q61239; -.
DR SwissPalm; Q61239; -.
DR EPD; Q61239; -.
DR jPOST; Q61239; -.
DR MaxQB; Q61239; -.
DR PaxDb; Q61239; -.
DR PRIDE; Q61239; -.
DR ProteomicsDB; 267611; -.
DR Antibodypedia; 1067; 311 antibodies from 33 providers.
DR DNASU; 14272; -.
DR Ensembl; ENSMUST00000016138; ENSMUSP00000016138; ENSMUSG00000015994.
DR GeneID; 14272; -.
DR KEGG; mmu:14272; -.
DR UCSC; uc009lhi.1; mouse.
DR CTD; 2339; -.
DR MGI; MGI:104683; Fnta.
DR VEuPathDB; HostDB:ENSMUSG00000015994; -.
DR eggNOG; KOG0530; Eukaryota.
DR GeneTree; ENSGT00550000074935; -.
DR HOGENOM; CLU_026582_1_1_1; -.
DR InParanoid; Q61239; -.
DR OMA; RRKYWQY; -.
DR OrthoDB; 1527547at2759; -.
DR PhylomeDB; Q61239; -.
DR TreeFam; TF313038; -.
DR BRENDA; 2.5.1.58; 3474.
DR BRENDA; 2.5.1.59; 3474.
DR Reactome; R-MMU-111465; Apoptotic cleavage of cellular proteins.
DR Reactome; R-MMU-2514859; Inactivation, recovery and regulation of the phototransduction cascade.
DR Reactome; R-MMU-9648002; RAS processing.
DR BioGRID-ORCS; 14272; 31 hits in 81 CRISPR screens.
DR ChiTaRS; Fnta; mouse.
DR PRO; PR:Q61239; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q61239; protein.
DR Bgee; ENSMUSG00000015994; Expressed in renal medulla collecting duct and 259 other tissues.
DR ExpressionAtlas; Q61239; baseline and differential.
DR Genevisible; Q61239; MM.
DR GO; GO:0005953; C:CAAX-protein geranylgeranyltransferase complex; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005875; C:microtubule associated complex; ISO:MGI.
DR GO; GO:0005965; C:protein farnesyltransferase complex; ISS:UniProtKB.
DR GO; GO:0030548; F:acetylcholine receptor regulator activity; IMP:MGI.
DR GO; GO:0043014; F:alpha-tubulin binding; ISO:MGI.
DR GO; GO:0004662; F:CAAX-protein geranylgeranyltransferase activity; ISO:MGI.
DR GO; GO:1901363; F:heterocyclic compound binding; ISO:MGI.
DR GO; GO:0008017; F:microtubule binding; ISO:MGI.
DR GO; GO:0042277; F:peptide binding; ISO:MGI.
DR GO; GO:0004660; F:protein farnesyltransferase activity; IDA:UniProtKB.
DR GO; GO:0004661; F:protein geranylgeranyltransferase activity; ISS:UniProtKB.
DR GO; GO:0004663; F:Rab geranylgeranyltransferase activity; IDA:UniProtKB.
DR GO; GO:0030971; F:receptor tyrosine kinase binding; IPI:UniProtKB.
DR GO; GO:0036094; F:small molecule binding; ISO:MGI.
DR GO; GO:0008270; F:zinc ion binding; ISO:MGI.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
DR GO; GO:0051771; P:negative regulation of nitric-oxide synthase biosynthetic process; ISO:MGI.
DR GO; GO:0045213; P:neurotransmitter receptor metabolic process; IMP:MGI.
DR GO; GO:0045787; P:positive regulation of cell cycle; ISO:MGI.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:MGI.
DR GO; GO:0090045; P:positive regulation of deacetylase activity; ISO:MGI.
DR GO; GO:0051770; P:positive regulation of nitric-oxide synthase biosynthetic process; ISO:MGI.
DR GO; GO:0090044; P:positive regulation of tubulin deacetylation; ISO:MGI.
DR GO; GO:0018343; P:protein farnesylation; ISS:UniProtKB.
DR GO; GO:0018344; P:protein geranylgeranylation; ISS:UniProtKB.
DR GO; GO:0034097; P:response to cytokine; ISO:MGI.
DR GO; GO:0010035; P:response to inorganic substance; ISO:MGI.
DR GO; GO:0014070; P:response to organic cyclic compound; ISO:MGI.
DR InterPro; IPR002088; Prenyl_trans_a.
DR Pfam; PF01239; PPTA; 5.
DR PROSITE; PS51147; PFTA; 5.
PE 1: Evidence at protein level;
KW Acetylation; Magnesium; Phosphoprotein; Prenyltransferase;
KW Reference proteome; Repeat; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P49354"
FT CHAIN 2..377
FT /note="Protein
FT farnesyltransferase/geranylgeranyltransferase type-1
FT subunit alpha"
FT /id="PRO_0000119747"
FT REPEAT 112..146
FT /note="PFTA 1"
FT REPEAT 147..181
FT /note="PFTA 2"
FT REPEAT 182..214
FT /note="PFTA 3"
FT REPEAT 215..249
FT /note="PFTA 4"
FT REPEAT 255..289
FT /note="PFTA 5"
FT REGION 1..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..34
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P49354"
FT MUTAGEN 164
FT /note="K->A: Inhibits prenylation activity. In myoblasts,
FT impaired insulin-induced RAC1 activation, possibly due to
FT impaired insulin-induced geranyl-geranyltransferase
FT activation. No effect on MUSK-binding."
FT /evidence="ECO:0000269|PubMed:14622576"
FT MUTAGEN 200
FT /note="Y->F: Inhibits prenylation activity. In myoblasts,
FT impaired insulin-induced RAC1 activation, possibly due to
FT impaired insulin-induced geranyl-geranyltransferase
FT activation. 68% decrease in MUSK-binding."
FT /evidence="ECO:0000269|PubMed:14622576"
FT CONFLICT 191
FT /note="D -> N (in Ref. 2; AAH12711)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 377 AA; 44013 MW; F3D60B9899F36D66 CRC64;
MAATEGVGES AAGGEPGQPE QPPPPPPPPP AQQPQEEEMA AEAGEAAASP MDDGFLSLDS
PTYVLYRDRA EWADIDPVPQ NDGPNPVVQI IYSEKFRDVY DYFRAVLQRD ERSERAFKLT
RDAIELNAAN YTVWHFRRVL LRSLQKDLQE EMNYITAIIE EQPKNYQVWH HRRVLVEWLK
DPSQELEFIA DILSQDAKNY HAWQHRQWVI QEFRLWDNEL QYVDQLLKED VRNNSVWNQR
HFVISNTTGY SDRAVLEREV QYTLEMIKLV PHNESAWNYL KGILQDRGLS RYPNLLNQLL
DLQPSHSSPY LIAFLVDVYE DMLENQCDNK EDILNKALEL CEILAKEKDT IRKEYWRYIG
RSLQSKHCRE SDIPASV
