FNTA_BOVIN
ID FNTA_BOVIN Reviewed; 375 AA.
AC P29702; Q2KIF0;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2006, sequence version 2.
DT 25-MAY-2022, entry version 121.
DE RecName: Full=Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha;
DE EC=2.5.1.58;
DE EC=2.5.1.59;
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-249.
RC STRAIN=Hereford; TISSUE=Testis;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 36-375.
RX PubMed=1918005; DOI=10.1016/s0021-9258(18)55146-2;
RA Kohl N.E., Diehl R.E., Schaber M.D., Rands E., Soderman D.D., He B.,
RA Moores S.L., Pompliano D.L., Ferro-Novick S., Powers S., Thomas K.A.,
RA Gibbs J.B.;
RT "Structural homology among mammalian and Saccharomyces cerevisiae
RT isoprenyl-protein transferases.";
RL J. Biol. Chem. 266:18884-18888(1991).
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 (By similarity). {ECO:0000250}.
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 -!- 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:0000250}.
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 (By similarity). {ECO:0000250}.
CC -!- PTM: Phosphorylated. Phosphorylation is mediated by MUSK upon AGRIN
CC stimulation and results in the activation of FNTA (By similarity).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein prenyltransferase subunit alpha
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA30529.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAI12663.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
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DR EMBL; BC112662; AAI12663.1; ALT_SEQ; mRNA.
DR EMBL; M74083; AAA30529.1; ALT_INIT; mRNA.
DR PIR; A41013; A41013.
DR RefSeq; NP_803464.2; NM_177498.3.
DR AlphaFoldDB; P29702; -.
DR SMR; P29702; -.
DR ComplexPortal; CPX-2162; Protein farnesyltransferase complex.
DR ComplexPortal; CPX-2169; Protein geranylgeranyl transferase type I complex.
DR STRING; 9913.ENSBTAP00000004159; -.
DR BindingDB; P29702; -.
DR ChEMBL; CHEMBL2095178; -.
DR ChEMBL; CHEMBL2096987; -.
DR DrugCentral; P29702; -.
DR PaxDb; P29702; -.
DR PRIDE; P29702; -.
DR GeneID; 281169; -.
DR KEGG; bta:281169; -.
DR CTD; 2339; -.
DR eggNOG; KOG0530; Eukaryota.
DR InParanoid; P29702; -.
DR OrthoDB; 1527547at2759; -.
DR PRO; PR:P29702; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005953; C:CAAX-protein geranylgeranyltransferase complex; ISS:UniProtKB.
DR GO; GO:0005965; C:protein farnesyltransferase complex; ISS:UniProtKB.
DR GO; GO:0004662; F:CAAX-protein geranylgeranyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0004660; F:protein farnesyltransferase activity; ISS:UniProtKB.
DR GO; GO:0004661; F:protein geranylgeranyltransferase activity; ISS:UniProtKB.
DR GO; GO:0018343; P:protein farnesylation; ISS:UniProtKB.
DR GO; GO:0018344; P:protein geranylgeranylation; ISS:UniProtKB.
DR InterPro; IPR002088; Prenyl_trans_a.
DR Pfam; PF01239; PPTA; 5.
DR PROSITE; PS51147; PFTA; 5.
PE 2: Evidence at transcript level;
KW Acetylation; Magnesium; Prenyltransferase; Reference proteome; Repeat;
KW Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P49354"
FT CHAIN 2..375
FT /note="Protein
FT farnesyltransferase/geranylgeranyltransferase type-1
FT subunit alpha"
FT /id="PRO_0000119745"
FT REPEAT 108..142
FT /note="PFTA 1"
FT REPEAT 143..176
FT /note="PFTA 2"
FT REPEAT 177..211
FT /note="PFTA 3"
FT REPEAT 212..245
FT /note="PFTA 4"
FT REPEAT 251..285
FT /note="PFTA 5"
FT REGION 1..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..40
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 CONFLICT 47
FT /note="I -> M (in Ref. 2; AAA30529)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 375 AA; 43845 MW; 7253AD4CED67296C CRC64;
MAAADGVGEA AQGGDPGQPE PPPPPQPHPP PPPPQPPQEE AAAASPIDDG FLSLDSPTYV
LYRDRPEWAD IDPVPQNDGP NPVVQIIYSE KFQDVYDYFR AVLQRDERSE RAFKLTRDAI
ELNAANYTVW HFRRVLLKSL QKDLHEEMNY ISAIIEEQPK NYQVWHHRRV LVEWLRDPSQ
ELEFIADILT QDAKNYHAWQ HRQWVIQEFK LWDNELQYVD QLLKEDVRNN SVWNQRYFVI
SNTTGYNDRA ILEREVQYTL EMIKLVPHNE SAWNYLKGIL QDRGLSKYPN LLNQLLDLQP
SHSSPYLIAF LVDIYEDMLE NQCDNKEDIL NKALELCEIL AKEKDTIRKE YWRYIGRSLQ
SKHSTESDPP TNVQQ
