FNTA_RAT
ID FNTA_RAT Reviewed; 377 AA.
AC Q04631;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha;
DE EC=2.5.1.58 {ECO:0000269|PubMed:12657282, ECO:0000269|PubMed:18844669, ECO:0000269|PubMed:19219049, ECO:0000269|PubMed:22963166};
DE EC=2.5.1.59 {ECO:0000269|PubMed:14609943, ECO:0000269|PubMed:19219049};
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Brain;
RX PubMed=1763049; DOI=10.1073/pnas.88.24.11368;
RA Chen W.-J., Andres D.A., Goldstein J.L., Brown M.S.;
RT "Cloning and expression of a cDNA encoding the alpha subunit of rat p21ras
RT protein farnesyltransferase.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:11368-11372(1991).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS), AND SUBUNIT.
RX PubMed=9065406; DOI=10.1126/science.275.5307.1800;
RA Park H.-W., Boduluri S.R., Mooomaw J.F., Casey P.J., Beese L.S.;
RT "Crystal structure of protein farnesyltransferase at 2.25-A resolution.";
RL Science 275:1800-1804(1997).
RN [3]
RP ERRATUM OF PUBMED:9065406.
RA Park H.-W., Boduluri S.R., Mooomaw J.F., Casey P.J., Beese L.S.;
RL Science 276:21-21(1997).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF 1-377 IN COMPLEX WITH FNTB, AND
RP SUBUNIT.
RX PubMed=9609683; DOI=10.1021/bi980531o;
RA Dunten P., Kammlott U., Crowther R., Weber D., Palermo R., Birktoft J.;
RT "Protein farnesyltransferase: structure and implications for substrate
RT binding.";
RL Biochemistry 37:7907-7912(1998).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (3.4 ANGSTROMS)IN COMPLEX WITH FNTB, AND SUBUNIT.
RX PubMed=9657673; DOI=10.1021/bi980708e;
RA Long S.B., Casey P.J., Beese L.S.;
RT "Cocrystal structure of protein farnesyltransferase complexed with a
RT farnesyl diphosphate substrate.";
RL Biochemistry 37:9612-9618(1998).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 45-377 IN COMPLEX WITH FNTB, AND
RP SUBUNIT.
RX PubMed=9843427; DOI=10.1021/bi981197z;
RA Strickland C.L., Windsor W.T., Syto R., Wang L., Bond R., Wu Z.,
RA Schwartz J., Le H.V., Beese L.S., Weber P.C.;
RT "Crystal structure of farnesyl protein transferase complexed with a CaaX
RT peptide and farnesyl diphosphate analogue.";
RL Biochemistry 37:16601-16611(1998).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 1-377 IN COMPLEX WITH FNTB, AND
RP SUBUNIT.
RX PubMed=10377218; DOI=10.1021/jm990030g;
RA Strickland C.L., Weber P.C., Windsor W.T., Wu Z., Le H.V., Albanese M.M.,
RA Alvarez C.S., Cesarz D., del Rosario J., Deskus J., Mallams A.K.,
RA Njoroge F.G., Piwinski J.J., Remiszewski S., Rossman R.R., Taveras A.G.,
RA Vibulbhan B., Doll R.J., Girijavallabhan V.M., Ganguly A.K.;
RT "Tricyclic farnesyl protein transferase inhibitors: crystallographic and
RT calorimetric studies of structure-activity relationships.";
RL J. Med. Chem. 42:2125-2135(1999).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 1-377 IN COMPLEX WITH FNTB, AND
RP SUBUNIT.
RX PubMed=10673434; DOI=10.1016/s0969-2126(00)00096-4;
RA Long S.B., Casey P.J., Beese L.S.;
RT "The basis for K-Ras4B binding specificity to protein farnesyltransferase
RT revealed by 2 A resolution ternary complex structures.";
RL Structure 8:209-222(2000).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH FNTB, AND SUBUNIT.
RX PubMed=11687658; DOI=10.1073/pnas.241407898;
RA Long S.B., Hancock P.J., Kral A.M., Hellinga H.W., Beese L.S.;
RT "The crystal structure of human protein farnesyltransferase reveals the
RT basis for inhibition by CaaX tetrapeptides and their mimetics.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:12948-12953(2001).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 1-377 IN COMPLEX WITH FNTB, AND
RP SUBUNIT.
RX PubMed=12374986; DOI=10.1038/nature00986;
RA Long S.B., Casey P.J., Beese L.S.;
RT "Reaction path of protein farnesyltransferase at atomic resolution.";
RL Nature 419:645-650(2002).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 1-377 IN COMPLEX WITH FNTB, AND
RP SUBUNIT.
RX PubMed=12667062; DOI=10.1021/bi0266838;
RA Turek-Etienne T.C., Strickland C.L., Distefano M.D.;
RT "Biochemical and structural studies with prenyl diphosphate analogues
RT provide insights into isoprenoid recognition by protein farnesyl
RT transferase.";
RL Biochemistry 42:3716-3724(2003).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 55-369 IN COMPLEX WITH FNTB,
RP SUBUNIT, AND CATALYTIC ACTIVITY.
RX PubMed=12657282; DOI=10.1016/s0960-894x(03)00095-7;
RA Gwaltney S.L., O'Connor S.J., Nelson L.T., Sullivan G.M., Imade H.,
RA Wang W., Hasvold L., Li Q., Cohen J., Gu W.Z., Tahir S.K., Bauch J.,
RA Marsh K., Ng S.C., Frost D.J., Zhang H., Muchmore S., Jakob C.G., Stoll V.,
RA Hutchins C., Rosenberg S.H., Sham H.L.;
RT "Aryl tetrahydropyridine inhibitors of farnesyltransferase: glycine,
RT phenylalanine and histidine derivatives.";
RL Bioorg. Med. Chem. Lett. 13:1359-1362(2003).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) IN COMPLEX WITH PGGT1B, SUBUNIT,
RP CATALYTIC ACTIVITY, AND FUNCTION.
RX PubMed=14609943; DOI=10.1093/emboj/cdg571;
RA Taylor J.S., Reid T.S., Terry K.L., Casey P.J., Beese L.S.;
RT "Structure of mammalian protein geranylgeranyltransferase type-I.";
RL EMBO J. 22:5963-5974(2003).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) IN COMPLEX WITH FNTB, AND SUBUNIT.
RX PubMed=15170324; DOI=10.1021/bi049723b;
RA Reid T.S., Beese L.S.;
RT "Crystal structures of the anticancer clinical candidates R115777
RT (Tipifarnib) and BMS-214662 complexed with protein farnesyltransferase
RT suggest a mechanism of FTI selectivity.";
RL Biochemistry 43:6877-6884(2004).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) IN COMPLEX WITH FNTB, AND SUBUNIT.
RX PubMed=15451670; DOI=10.1016/j.jmb.2004.08.056;
RA Reid T.S., Terry K.L., Casey P.J., Beese L.S.;
RT "Crystallographic analysis of CaaX prenyltransferases complexed with
RT substrates defines rules of protein substrate selectivity.";
RL J. Mol. Biol. 343:417-433(2004).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) IN COMPLEX WITH FNTB, SUBUNIT,
RP CATALYTIC ACTIVITY, AND FUNCTION.
RX PubMed=18844669; DOI=10.1111/j.1747-0285.2008.00698.x;
RA DeGraw A.J., Hast M.A., Xu J., Mullen D., Beese L.S., Barany G.,
RA Distefano M.D.;
RT "Caged protein prenyltransferase substrates: tools for understanding
RT protein prenylation.";
RL Chem. Biol. Drug Des. 72:171-181(2008).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS), SUBUNIT, CATALYTIC ACTIVITY, AND
RP FUNCTION.
RX PubMed=19219049; DOI=10.1038/nchembio.149;
RA Nguyen U.T., Guo Z., Delon C., Wu Y., Deraeve C., Franzel B., Bon R.S.,
RA Blankenfeldt W., Goody R.S., Waldmann H., Wolters D., Alexandrov K.;
RT "Analysis of the eukaryotic prenylome by isoprenoid affinity tagging.";
RL Nat. Chem. Biol. 5:227-235(2009).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) IN COMPLEX WITH FNTB, SUBUNIT,
RP CATALYTIC ACTIVITY, AND FUNCTION.
RX PubMed=22963166; DOI=10.1021/jm300624s;
RA Stigter E.A., Guo Z., Bon R.S., Wu Y.W., Choidas A., Wolf A., Menninger S.,
RA Waldmann H., Blankenfeldt W., Goody R.S.;
RT "Development of selective, potent RabGGTase inhibitors.";
RL J. Med. Chem. 55:8330-8340(2012).
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:14609943, ECO:0000269|PubMed:18844669,
CC ECO:0000269|PubMed:19219049, ECO:0000269|PubMed:22963166}.
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 Evidence={ECO:0000269|PubMed:12657282, ECO:0000269|PubMed:18844669,
CC ECO:0000269|PubMed:19219049, ECO:0000269|PubMed:22963166};
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:0000269|PubMed:14609943, ECO:0000269|PubMed:19219049};
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: Interacts with MUSK; the interaction is direct and mediates
CC AGRIN-induced phosphorylation of FNTA (By similarity). Heterodimer of
CC FNTA and FNTB (farnesyltransferase). Heterodimer of FNTA and PGGT1B
CC (geranylgeranyltransferase). {ECO:0000250, ECO:0000269|PubMed:10377218,
CC ECO:0000269|PubMed:10673434, ECO:0000269|PubMed:11687658,
CC ECO:0000269|PubMed:12374986, ECO:0000269|PubMed:12657282,
CC ECO:0000269|PubMed:12667062, ECO:0000269|PubMed:14609943,
CC ECO:0000269|PubMed:15170324, ECO:0000269|PubMed:15451670,
CC ECO:0000269|PubMed:18844669, ECO:0000269|PubMed:19219049,
CC ECO:0000269|PubMed:22963166, ECO:0000269|PubMed:9065406,
CC ECO:0000269|PubMed:9609683, ECO:0000269|PubMed:9657673,
CC ECO:0000269|PubMed:9843427}.
CC -!- INTERACTION:
CC Q04631; Q02293: Fntb; NbExp=16; IntAct=EBI-602447, EBI-602454;
CC Q04631; Q63604: Ntrk2; NbExp=4; IntAct=EBI-602447, EBI-7287667;
CC Q04631; P53610: Pggt1b; NbExp=7; IntAct=EBI-602447, EBI-602610;
CC Q04631; P01116-2: KRAS; Xeno; NbExp=3; IntAct=EBI-602447, EBI-367427;
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}.
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DR EMBL; M81225; AAA41833.1; -; mRNA.
DR PIR; A41625; A41625.
DR RefSeq; NP_036979.1; NM_012847.1.
DR PDB; 1D8D; X-ray; 2.00 A; A=1-377.
DR PDB; 1D8E; X-ray; 3.00 A; A=1-377.
DR PDB; 1FPP; X-ray; 2.75 A; A=1-377.
DR PDB; 1FT1; X-ray; 2.25 A; A=1-377.
DR PDB; 1FT2; X-ray; 3.40 A; A=55-369.
DR PDB; 1JCR; X-ray; 2.00 A; A=1-377.
DR PDB; 1JCS; X-ray; 2.20 A; A=1-377.
DR PDB; 1KZO; X-ray; 2.20 A; A=1-377.
DR PDB; 1KZP; X-ray; 2.10 A; A=1-377.
DR PDB; 1N4P; X-ray; 2.65 A; A/C/E/G/I/K=1-377.
DR PDB; 1N4Q; X-ray; 2.40 A; A/C/E/G/I/K=1-377.
DR PDB; 1N4R; X-ray; 2.80 A; A/C/E/G/I/K=1-377.
DR PDB; 1N4S; X-ray; 2.60 A; A/C/E/G/I/K=1-377.
DR PDB; 1N94; X-ray; 3.50 A; A=55-369.
DR PDB; 1N95; X-ray; 2.30 A; A=55-369.
DR PDB; 1N9A; X-ray; 3.20 A; A=55-369.
DR PDB; 1NI1; X-ray; 2.30 A; A=55-369.
DR PDB; 1NL4; X-ray; 2.70 A; A=55-366.
DR PDB; 1O1R; X-ray; 2.30 A; A=1-377.
DR PDB; 1O1S; X-ray; 2.30 A; A=1-377.
DR PDB; 1O1T; X-ray; 2.10 A; A=1-377.
DR PDB; 1O5M; X-ray; 2.30 A; A=1-377.
DR PDB; 1QBQ; X-ray; 2.40 A; A=45-377.
DR PDB; 1S64; X-ray; 2.55 A; A/C/E/G/I/K=1-377.
DR PDB; 1SA5; X-ray; 2.60 A; A=1-377.
DR PDB; 1TN7; X-ray; 2.30 A; A=1-377.
DR PDB; 1TN8; X-ray; 2.25 A; A=1-377.
DR PDB; 1TNB; X-ray; 2.85 A; A/C/E/G/I/K=1-377.
DR PDB; 1TNO; X-ray; 2.70 A; A/C/E/G/I/K=1-377.
DR PDB; 1TNU; X-ray; 2.70 A; A/C/E/G/I/K=1-377.
DR PDB; 1TNY; X-ray; 2.70 A; A/C/E/G/I/K=1-377.
DR PDB; 1TNZ; X-ray; 2.90 A; A/C/E/G/I/K=1-377.
DR PDB; 1X81; X-ray; 3.50 A; A=55-369.
DR PDB; 2BED; X-ray; 2.70 A; A=54-366.
DR PDB; 2R2L; X-ray; 2.23 A; A=54-368.
DR PDB; 2ZIR; X-ray; 2.40 A; A=1-377.
DR PDB; 2ZIS; X-ray; 2.60 A; A=1-377.
DR PDB; 3DPY; X-ray; 2.70 A; A=1-377.
DR PDB; 3E30; X-ray; 2.45 A; A=1-377.
DR PDB; 3E32; X-ray; 2.45 A; A=1-377.
DR PDB; 3E33; X-ray; 1.90 A; A=1-377.
DR PDB; 3E34; X-ray; 2.05 A; A=1-377.
DR PDB; 3EU5; X-ray; 2.80 A; A=1-377.
DR PDB; 3EUV; X-ray; 2.75 A; A=1-377.
DR PDB; 3KSL; X-ray; 2.05 A; A=1-377.
DR PDB; 3KSQ; X-ray; 2.10 A; A=1-377.
DR PDB; 3PZ4; X-ray; 2.10 A; A=1-377.
DR PDB; 4GTM; X-ray; 2.20 A; A=1-377.
DR PDB; 4GTO; X-ray; 2.15 A; A=1-377.
DR PDB; 4GTP; X-ray; 2.75 A; A=1-377.
DR PDB; 4GTQ; X-ray; 2.60 A; A=1-377.
DR PDB; 4GTR; X-ray; 2.20 A; A=1-377.
DR PDB; 7RN5; X-ray; 2.28 A; A=1-377.
DR PDB; 7RNI; X-ray; 1.98 A; A=1-377.
DR PDBsum; 1D8D; -.
DR PDBsum; 1D8E; -.
DR PDBsum; 1FPP; -.
DR PDBsum; 1FT1; -.
DR PDBsum; 1FT2; -.
DR PDBsum; 1JCR; -.
DR PDBsum; 1JCS; -.
DR PDBsum; 1KZO; -.
DR PDBsum; 1KZP; -.
DR PDBsum; 1N4P; -.
DR PDBsum; 1N4Q; -.
DR PDBsum; 1N4R; -.
DR PDBsum; 1N4S; -.
DR PDBsum; 1N94; -.
DR PDBsum; 1N95; -.
DR PDBsum; 1N9A; -.
DR PDBsum; 1NI1; -.
DR PDBsum; 1NL4; -.
DR PDBsum; 1O1R; -.
DR PDBsum; 1O1S; -.
DR PDBsum; 1O1T; -.
DR PDBsum; 1O5M; -.
DR PDBsum; 1QBQ; -.
DR PDBsum; 1S64; -.
DR PDBsum; 1SA5; -.
DR PDBsum; 1TN7; -.
DR PDBsum; 1TN8; -.
DR PDBsum; 1TNB; -.
DR PDBsum; 1TNO; -.
DR PDBsum; 1TNU; -.
DR PDBsum; 1TNY; -.
DR PDBsum; 1TNZ; -.
DR PDBsum; 1X81; -.
DR PDBsum; 2BED; -.
DR PDBsum; 2R2L; -.
DR PDBsum; 2ZIR; -.
DR PDBsum; 2ZIS; -.
DR PDBsum; 3DPY; -.
DR PDBsum; 3E30; -.
DR PDBsum; 3E32; -.
DR PDBsum; 3E33; -.
DR PDBsum; 3E34; -.
DR PDBsum; 3EU5; -.
DR PDBsum; 3EUV; -.
DR PDBsum; 3KSL; -.
DR PDBsum; 3KSQ; -.
DR PDBsum; 3PZ4; -.
DR PDBsum; 4GTM; -.
DR PDBsum; 4GTO; -.
DR PDBsum; 4GTP; -.
DR PDBsum; 4GTQ; -.
DR PDBsum; 4GTR; -.
DR PDBsum; 7RN5; -.
DR PDBsum; 7RNI; -.
DR AlphaFoldDB; Q04631; -.
DR SMR; Q04631; -.
DR BioGRID; 247357; 1.
DR ComplexPortal; CPX-2181; Protein farnesyltransferase complex.
DR CORUM; Q04631; -.
DR DIP; DIP-6131N; -.
DR IntAct; Q04631; 9.
DR STRING; 10116.ENSRNOP00000019594; -.
DR BindingDB; Q04631; -.
DR ChEMBL; CHEMBL2095197; -.
DR ChEMBL; CHEMBL2111479; -.
DR iPTMnet; Q04631; -.
DR PhosphoSitePlus; Q04631; -.
DR jPOST; Q04631; -.
DR PaxDb; Q04631; -.
DR PRIDE; Q04631; -.
DR GeneID; 25318; -.
DR KEGG; rno:25318; -.
DR UCSC; RGD:2625; rat.
DR CTD; 2339; -.
DR RGD; 2625; Fnta.
DR eggNOG; KOG0530; Eukaryota.
DR InParanoid; Q04631; -.
DR OrthoDB; 1527547at2759; -.
DR PhylomeDB; Q04631; -.
DR BRENDA; 2.5.1.58; 5301.
DR BRENDA; 2.5.1.59; 5301.
DR Reactome; R-RNO-111465; Apoptotic cleavage of cellular proteins.
DR Reactome; R-RNO-2514859; Inactivation, recovery and regulation of the phototransduction cascade.
DR Reactome; R-RNO-9648002; RAS processing.
DR SABIO-RK; Q04631; -.
DR EvolutionaryTrace; Q04631; -.
DR PRO; PR:Q04631; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005953; C:CAAX-protein geranylgeranyltransferase complex; IDA:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005875; C:microtubule associated complex; ISO:RGD.
DR GO; GO:0005965; C:protein farnesyltransferase complex; ISS:UniProtKB.
DR GO; GO:0030548; F:acetylcholine receptor regulator activity; ISO:RGD.
DR GO; GO:0043014; F:alpha-tubulin binding; ISO:RGD.
DR GO; GO:0004662; F:CAAX-protein geranylgeranyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0008017; F:microtubule binding; ISO:RGD.
DR GO; GO:0004660; F:protein farnesyltransferase activity; IDA:RGD.
DR GO; GO:0004661; F:protein geranylgeranyltransferase activity; ISS:UniProtKB.
DR GO; GO:0004663; F:Rab geranylgeranyltransferase activity; ISO:RGD.
DR GO; GO:0030971; F:receptor tyrosine kinase binding; ISO:RGD.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:RGD.
DR GO; GO:0051771; P:negative regulation of nitric-oxide synthase biosynthetic process; IMP:RGD.
DR GO; GO:0045213; P:neurotransmitter receptor metabolic process; ISO:RGD.
DR GO; GO:0045787; P:positive regulation of cell cycle; IMP:RGD.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:RGD.
DR GO; GO:0090045; P:positive regulation of deacetylase activity; ISO:RGD.
DR GO; GO:0051770; P:positive regulation of nitric-oxide synthase biosynthetic process; IMP:RGD.
DR GO; GO:0090044; P:positive regulation of tubulin deacetylation; ISO:RGD.
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; IMP:RGD.
DR GO; GO:0010035; P:response to inorganic substance; IMP:RGD.
DR GO; GO:0014070; P:response to organic cyclic compound; IMP:RGD.
DR InterPro; IPR002088; Prenyl_trans_a.
DR Pfam; PF01239; PPTA; 5.
DR PROSITE; PS51147; PFTA; 5.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Direct protein sequencing; Magnesium;
KW Prenyltransferase; 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_0000119748"
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 16..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 STRAND 58..60
FT /evidence="ECO:0007829|PDB:1N94"
FT HELIX 66..68
FT /evidence="ECO:0007829|PDB:3E33"
FT HELIX 70..72
FT /evidence="ECO:0007829|PDB:3E33"
FT STRAND 73..75
FT /evidence="ECO:0007829|PDB:2ZIS"
FT STRAND 87..90
FT /evidence="ECO:0007829|PDB:3E33"
FT HELIX 94..109
FT /evidence="ECO:0007829|PDB:3E33"
FT HELIX 114..126
FT /evidence="ECO:0007829|PDB:3E33"
FT HELIX 131..143
FT /evidence="ECO:0007829|PDB:3E33"
FT HELIX 148..161
FT /evidence="ECO:0007829|PDB:3E33"
FT HELIX 166..179
FT /evidence="ECO:0007829|PDB:3E33"
FT TURN 182..184
FT /evidence="ECO:0007829|PDB:1NL4"
FT HELIX 185..195
FT /evidence="ECO:0007829|PDB:3E33"
FT HELIX 200..213
FT /evidence="ECO:0007829|PDB:3E33"
FT HELIX 216..218
FT /evidence="ECO:0007829|PDB:1FPP"
FT HELIX 219..229
FT /evidence="ECO:0007829|PDB:3E33"
FT TURN 230..232
FT /evidence="ECO:0007829|PDB:1N94"
FT HELIX 234..246
FT /evidence="ECO:0007829|PDB:3E33"
FT STRAND 250..252
FT /evidence="ECO:0007829|PDB:7RNI"
FT HELIX 253..269
FT /evidence="ECO:0007829|PDB:3E33"
FT STRAND 270..272
FT /evidence="ECO:0007829|PDB:1N4P"
FT HELIX 274..284
FT /evidence="ECO:0007829|PDB:3E33"
FT TURN 285..287
FT /evidence="ECO:0007829|PDB:3E33"
FT HELIX 289..291
FT /evidence="ECO:0007829|PDB:3E33"
FT HELIX 293..300
FT /evidence="ECO:0007829|PDB:3E33"
FT HELIX 303..306
FT /evidence="ECO:0007829|PDB:3E33"
FT HELIX 309..324
FT /evidence="ECO:0007829|PDB:3E33"
FT HELIX 330..346
FT /evidence="ECO:0007829|PDB:3E33"
FT TURN 347..349
FT /evidence="ECO:0007829|PDB:7RN5"
FT HELIX 350..352
FT /evidence="ECO:0007829|PDB:3E33"
FT HELIX 353..367
FT /evidence="ECO:0007829|PDB:3E33"
FT TURN 369..372
FT /evidence="ECO:0007829|PDB:3E33"
SQ SEQUENCE 377 AA; 44049 MW; DFFFECC1B88BC080 CRC64;
MAATEGVGES APGGEPGQPE QPPPPPPPPP AQQPQEEEMA AEAGEAAASP MDDGFLSLDS
PTYVLYRDRA EWADIDPVPQ NDGPSPVVQI IYSEKFRDVY DYFRAVLQRD ERSERAFKLT
RDAIELNAAN YTVWHFRRVL LRSLQKDLQE EMNYIIAIIE EQPKNYQVWH HRRVLVEWLK
DPSQELEFIA DILNQDAKNY HAWQHRQWVI QEFRLWDNEL QYVDQLLKED VRNNSVWNQR
HFVISNTTGY SDRAVLEREV QYTLEMIKLV PHNESAWNYL KGILQDRGLS RYPNLLNQLL
DLQPSHSSPY LIAFLVDIYE DMLENQCDNK EDILNKALEL CEILAKEKDT IRKEYWRYIG
RSLQSKHSRE SDIPASV
