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 27-MAR-2024, entry version 168. 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|UniProtKB:Q61239}. CC -!- SUBUNIT: Heterodimer of FNTA and FNTB (farnesyltransferase) CC (PubMed:10377218, PubMed:10673434, PubMed:11687658, PubMed:12374986, CC PubMed:12657282, PubMed:12667062, PubMed:15170324, PubMed:15451670, CC PubMed:18844669, PubMed:19219049, PubMed:22963166, PubMed:9065406, CC PubMed:9609683, PubMed:9657673, PubMed:9843427). Heterodimer of FNTA CC and PGGT1B (geranylgeranyltransferase) (PubMed:14609943). CC {ECO:0000269|PubMed:10377218, ECO:0000269|PubMed:10673434, CC ECO:0000269|PubMed:11687658, ECO:0000269|PubMed:12374986, CC ECO:0000269|PubMed:12657282, ECO:0000269|PubMed:12667062, CC ECO:0000269|PubMed:14609943, ECO:0000269|PubMed:15170324, CC ECO:0000269|PubMed:15451670, ECO:0000269|PubMed:18844669, CC ECO:0000269|PubMed:19219049, ECO:0000269|PubMed:22963166, CC ECO:0000269|PubMed:9065406, ECO:0000269|PubMed:9609683, CC ECO:0000269|PubMed:9657673, 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|UniProtKB:Q61239}. CC -!- SIMILARITY: Belongs to the protein prenyltransferase subunit alpha CC family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 PDB; 8E9E; X-ray; 2.84 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 PDBsum; 8E9E; -. 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; 10116-ENSRNOP00000019594; -. DR GeneID; 25318; -. DR KEGG; rno:25318; -. DR UCSC; RGD:2625; rat. DR AGR; RGD:2625; -. DR CTD; 2339; -. DR RGD; 2625; Fnta. DR eggNOG; KOG0530; Eukaryota. DR InParanoid; Q04631; -. DR OrthoDB; 20949at2759; -. 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; IBA:GO_Central. DR GO; GO:0005875; C:microtubule associated complex; ISO:RGD. DR GO; GO:0005965; C:protein farnesyltransferase complex; ISS:UniProtKB. 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:0060090; F:molecular adaptor activity; 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:0007167; P:enzyme-linked receptor protein signaling pathway; 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: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:0051770; P:positive regulation of nitric-oxide synthase biosynthetic process; IMP:RGD. DR GO; GO:0035022; P:positive regulation of Rac protein signal transduction; ISO:RGD. DR GO; GO:1904395; P:positive regulation of skeletal muscle acetylcholine-gated channel clustering; ISO: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 Gene3D; 1.25.40.120; Protein prenylyltransferase; 1. DR InterPro; IPR002088; Prenyl_trans_a. DR PANTHER; PTHR11129; PROTEIN FARNESYLTRANSFERASE ALPHA SUBUNIT/RAB GERANYLGERANYL TRANSFERASE ALPHA SUBUNIT; 1. DR PANTHER; PTHR11129:SF1; PROTEIN FARNESYLTRANSFERASE_GERANYLGERANYLTRANSFERASE TYPE-1 SUBUNIT ALPHA; 1. DR Pfam; PF01239; PPTA; 5. DR SUPFAM; SSF48439; Protein prenylyltransferase; 1. 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 //