UniProt functional annotation for Q04631



	UniProt functional annotation for Q04631

UniProt code: Q04631.

Organism: Rattus norvegicus (Rat).

Taxonomy: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Rattus.

Function: 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. {ECO:0000269|PubMed:14609943, ECO:0000269|PubMed:18844669, ECO:0000269|PubMed:19219049, ECO:0000269|PubMed:22963166}.

Catalytic activity: Reaction=(2E,6E)-farnesyl diphosphate + L-cysteinyl-[protein] = diphosphate + S-(2E,6E)-farnesyl-L-cysteinyl-[protein]; Xref=Rhea:RHEA:13345, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:11535, ChEBI:CHEBI:29950, ChEBI:CHEBI:33019, ChEBI:CHEBI:86019, ChEBI:CHEBI:175763; EC=2.5.1.58; Evidence={ECO:0000269|PubMed:12657282, ECO:0000269|PubMed:18844669, ECO:0000269|PubMed:19219049, ECO:0000269|PubMed:22963166};

Catalytic activity: Reaction=geranylgeranyl diphosphate + L-cysteinyl-[protein] = diphosphate + S-geranylgeranyl-L-cysteinyl-[protein]; Xref=Rhea:RHEA:21240, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:11537, ChEBI:CHEBI:29950, ChEBI:CHEBI:33019, ChEBI:CHEBI:57533, ChEBI:CHEBI:86021; EC=2.5.1.59; Evidence={ECO:0000269|PubMed:14609943, ECO:0000269|PubMed:19219049};

Cofactor: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P29703};

Activity regulation: Activated by the AGRIN-induced phosphorylation which is mediated by MUSK. {ECO:0000250}.

Subunit: 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). {ECO:0000250, ECO:0000269|PubMed:10377218, ECO:0000269|PubMed:10673434, ECO:0000269|PubMed:11687658, ECO:0000269|PubMed:12374986, ECO:0000269|PubMed:12657282, ECO:0000269|PubMed:12667062, ECO:0000269|PubMed:14609943, ECO:0000269|PubMed:15170324, ECO:0000269|PubMed:15451670, ECO:0000269|PubMed:18844669, ECO:0000269|PubMed:19219049, ECO:0000269|PubMed:22963166, ECO:0000269|PubMed:9065406, ECO:0000269|PubMed:9609683, ECO:0000269|PubMed:9657673, ECO:0000269|PubMed:9843427}.

Ptm: Phosphorylated. Phosphorylation is mediated by MUSK upon AGRIN stimulation and results in the activation of FNTA (By similarity). {ECO:0000250}.

Similarity: Belongs to the protein prenyltransferase subunit alpha family. {ECO:0000305}.

Annotations taken from UniProtKB at the EBI.


Organism:		Rattus norvegicus (Rat).
Taxonomy:		Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Rattus.



Function:		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. {ECO:0000269\|PubMed:14609943, ECO:0000269\|PubMed:18844669, ECO:0000269\|PubMed:19219049, ECO:0000269\|PubMed:22963166}.


Catalytic activity:		Reaction=(2E,6E)-farnesyl diphosphate + L-cysteinyl-[protein] = diphosphate + S-(2E,6E)-farnesyl-L-cysteinyl-[protein]; Xref=Rhea:RHEA:13345, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:11535, ChEBI:CHEBI:29950, ChEBI:CHEBI:33019, ChEBI:CHEBI:86019, ChEBI:CHEBI:175763; EC=2.5.1.58; Evidence={ECO:0000269\|PubMed:12657282, ECO:0000269\|PubMed:18844669, ECO:0000269\|PubMed:19219049, ECO:0000269\|PubMed:22963166};
Catalytic activity:		Reaction=geranylgeranyl diphosphate + L-cysteinyl-[protein] = diphosphate + S-geranylgeranyl-L-cysteinyl-[protein]; Xref=Rhea:RHEA:21240, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:11537, ChEBI:CHEBI:29950, ChEBI:CHEBI:33019, ChEBI:CHEBI:57533, ChEBI:CHEBI:86021; EC=2.5.1.59; Evidence={ECO:0000269\|PubMed:14609943, ECO:0000269\|PubMed:19219049};
Cofactor:		Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250\|UniProtKB:P29703};
Activity regulation:		Activated by the AGRIN-induced phosphorylation which is mediated by MUSK. {ECO:0000250}.
Subunit:		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). {ECO:0000250, ECO:0000269\|PubMed:10377218, ECO:0000269\|PubMed:10673434, ECO:0000269\|PubMed:11687658, ECO:0000269\|PubMed:12374986, ECO:0000269\|PubMed:12657282, ECO:0000269\|PubMed:12667062, ECO:0000269\|PubMed:14609943, ECO:0000269\|PubMed:15170324, ECO:0000269\|PubMed:15451670, ECO:0000269\|PubMed:18844669, ECO:0000269\|PubMed:19219049, ECO:0000269\|PubMed:22963166, ECO:0000269\|PubMed:9065406, ECO:0000269\|PubMed:9609683, ECO:0000269\|PubMed:9657673, ECO:0000269\|PubMed:9843427}.
Ptm:		Phosphorylated. Phosphorylation is mediated by MUSK upon AGRIN stimulation and results in the activation of FNTA (By similarity). {ECO:0000250}.
Similarity:		Belongs to the protein prenyltransferase subunit alpha family. {ECO:0000305}.