ID   FNTB_RAT                Reviewed;         437 AA.
AC   Q02293;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   24-JAN-2024, entry version 188.
DE   RecName: Full=Protein farnesyltransferase subunit beta;
DE            Short=FTase-beta;
DE            EC=2.5.1.58 {ECO:0000269|PubMed:10673434, ECO:0000269|PubMed:18844669, ECO:0000269|PubMed:19219049, ECO:0000269|PubMed:19246009, ECO:0000269|PubMed:22963166};
DE   AltName: Full=CAAX farnesyltransferase subunit beta;
DE   AltName: Full=Ras proteins prenyltransferase subunit beta;
GN   Name=Fntb;
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=1855253; DOI=10.1016/0092-8674(91)90622-6;
RA   Chen W.-J., Andres D.A., Goldstein J.L., Russell D.W., Brown M.S.;
RT   "cDNA cloning and expression of the peptide-binding beta subunit of rat
RT   p21ras farnesyltransferase, the counterpart of yeast DPR1/RAM1.";
RL   Cell 66:327-334(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
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   X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) IN COMPLEX WITH ZINC.
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   [4]
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   [5]
RP   X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) IN COMPLEX WITH FNTA; FARNESYL
RP   DIPHOSPHATE AND ZINC IONS, SUBUNIT, AND COFACTOR.
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   [6]
RP   X-RAY CRYSTALLOGRAPHY (3.4 ANGSTROMS) IN COMPLEX WITH FNTA; FARNESYL
RP   DIPHOSPHATE AND ZINC IONS, COFACTOR, 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   [7]
RP   X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) IN COMPLEX WITH FNTA; ZINC IONS AND
RP   FARNESYL DIPHOSPHATE ANALOG, COFACTOR, AND 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   [8]
RP   X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH ZINC IONS; FNTA AND
RP   KRAS, INTERACTION WITH KRAS, CATALYTIC ACTIVITY, COFACTOR, FUNCTION, 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 FNTA AND
RP   GERANYLGERANYL DIPHOSPHATE, 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) IN COMPLEX WITH FNTA; FARNESYL
RP   DIPHOSPHATE AND ZINC IONS, SUBUNIT, AND COFACTOR.
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 1-427 IN COMPLEX WITH FNTA;
RP   GERANYLGERANYL DIPHOSPHATE AND ZINC IONS, COFACTOR, AND 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 (2.25 ANGSTROMS) IN COMPLEX WITH FNTA AND ZINC IONS,
RP   COFACTOR, 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   [13]
RP   X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) IN COMPLEX WITH FNTA; FARNESYL
RP   DIPHOSPHATE AND ZINC, COFACTOR, CATALYTIC ACTIVITY, AND SUBUNIT.
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   [14]
RP   X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH FNTA; FARNESYL
RP   DIPHOSPHATE AND ZINC IONS, CATALYTIC ACTIVITY, FUNCTION, COFACTOR, AND
RP   SUBUNIT.
RX   PubMed=19246009; DOI=10.1016/j.chembiol.2009.01.014;
RA   Hast M.A., Fletcher S., Cummings C.G., Pusateri E.E., Blaskovich M.A.,
RA   Rivas K., Gelb M.H., Van Voorhis W.C., Sebti S.M., Hamilton A.D.,
RA   Beese L.S.;
RT   "Structural basis for binding and selectivity of antimalarial and
RT   anticancer ethylenediamine inhibitors to protein farnesyltransferase.";
RL   Chem. Biol. 16:181-192(2009).
RN   [15]
RP   X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF 1-427 IN COMPLEX WITH FNTA AND
RP   ZINC IONS, SUBUNIT, COFACTOR, CATALYTIC ACTIVITY, AND 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   [16]
RP   X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH FNTA; FARNESYL
RP   DIPHOSPHATE AND ZINC, SUBUNIT, AND COFACTOR.
RX   PubMed=20056542; DOI=10.1016/j.bmcl.2009.12.013;
RA   Zhu H.Y., Cooper A.B., Desai J., Njoroge G., Kirschmeier P., Bishop W.R.,
RA   Strickland C., Hruza A., Doll R.J., Girijavallabhan V.M.;
RT   "Discovery of C-imidazole azaheptapyridine FPT inhibitors.";
RL   Bioorg. Med. Chem. Lett. 20:1134-1136(2010).
RN   [17]
RP   X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 1-427 IN COMPLEX WITH FNTA;
RP   FARNESYL DIPHOSPHATE AND ZINC IONS, SUBUNIT, COFACTOR, CATALYTIC ACTIVITY,
RP   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 the farnesyltransferase complex.
CC       Catalyzes the transfer of a farnesyl moiety from farnesyl diphosphate
CC       to a cysteine at the fourth position from the C-terminus of several
CC       proteins having the C-terminal sequence Cys-aliphatic-aliphatic-X.
CC       {ECO:0000269|PubMed:10673434, ECO:0000269|PubMed:19219049,
CC       ECO:0000269|PubMed:19246009, 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:10673434, ECO:0000269|PubMed:18844669,
CC         ECO:0000269|PubMed:19219049, ECO:0000269|PubMed:19246009,
CC         ECO:0000269|PubMed:22963166};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000269|PubMed:10673434, ECO:0000269|PubMed:12374986,
CC         ECO:0000269|PubMed:12667062, ECO:0000269|PubMed:15451670,
CC         ECO:0000269|PubMed:18844669, ECO:0000269|PubMed:19219049,
CC         ECO:0000269|PubMed:19246009, ECO:0000269|PubMed:20056542,
CC         ECO:0000269|PubMed:22963166, ECO:0000269|PubMed:9609683,
CC         ECO:0000269|PubMed:9657673, ECO:0000269|PubMed:9843427};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:10673434,
CC       ECO:0000269|PubMed:12374986, ECO:0000269|PubMed:12667062,
CC       ECO:0000269|PubMed:15451670, ECO:0000269|PubMed:18844669,
CC       ECO:0000269|PubMed:19219049, ECO:0000269|PubMed:19246009,
CC       ECO:0000269|PubMed:20056542, ECO:0000269|PubMed:22963166,
CC       ECO:0000269|PubMed:9609683, ECO:0000269|PubMed:9657673,
CC       ECO:0000269|PubMed:9843427};
CC   -!- SUBUNIT: Heterodimer of FNTA and FNTB. {ECO:0000269|PubMed:10673434,
CC       ECO:0000269|PubMed:11687658, ECO:0000269|PubMed:12374986,
CC       ECO:0000269|PubMed:12667062, ECO:0000269|PubMed:15451670,
CC       ECO:0000269|PubMed:18844669, ECO:0000269|PubMed:19219049,
CC       ECO:0000269|PubMed:19246009, ECO:0000269|PubMed:20056542,
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       Q02293; Q04631: Fnta; NbExp=16; IntAct=EBI-602454, EBI-602447;
CC   -!- SIMILARITY: Belongs to the protein prenyltransferase subunit beta
CC       family. {ECO:0000305}.
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DR   EMBL; M69056; AAA41176.1; -; mRNA.
DR   EMBL; BC087675; AAH87675.1; -; mRNA.
DR   PIR; A40037; A40037.
DR   RefSeq; NP_742031.1; NM_172034.2.
DR   PDB; 1D8D; X-ray; 2.00 A; B=1-437.
DR   PDB; 1D8E; X-ray; 3.00 A; B=1-437.
DR   PDB; 1FPP; X-ray; 2.75 A; B=1-437.
DR   PDB; 1FT1; X-ray; 2.25 A; B=1-437.
DR   PDB; 1FT2; X-ray; 3.40 A; B=22-422.
DR   PDB; 1JCR; X-ray; 2.00 A; B=1-437.
DR   PDB; 1JCS; X-ray; 2.20 A; B=1-437.
DR   PDB; 1KZO; X-ray; 2.20 A; B=1-437.
DR   PDB; 1KZP; X-ray; 2.10 A; B=1-437.
DR   PDB; 1N94; X-ray; 3.50 A; B=22-418.
DR   PDB; 1N95; X-ray; 2.30 A; B=22-423.
DR   PDB; 1N9A; X-ray; 3.20 A; B=22-423.
DR   PDB; 1NI1; X-ray; 2.30 A; B=22-423.
DR   PDB; 1NL4; X-ray; 2.70 A; B=23-423.
DR   PDB; 1O1R; X-ray; 2.30 A; B=1-427.
DR   PDB; 1O1S; X-ray; 2.30 A; B=1-427.
DR   PDB; 1O1T; X-ray; 2.10 A; B=1-427.
DR   PDB; 1O5M; X-ray; 2.30 A; B=1-437.
DR   PDB; 1QBQ; X-ray; 2.40 A; B=1-437.
DR   PDB; 1SA5; X-ray; 2.60 A; B=1-437.
DR   PDB; 1TN7; X-ray; 2.30 A; B=1-437.
DR   PDB; 1TN8; X-ray; 2.25 A; B=1-437.
DR   PDB; 1X81; X-ray; 3.50 A; B=22-418.
DR   PDB; 2BED; X-ray; 2.70 A; B=23-423.
DR   PDB; 2R2L; X-ray; 2.23 A; B=23-423.
DR   PDB; 2ZIR; X-ray; 2.40 A; B=1-437.
DR   PDB; 2ZIS; X-ray; 2.60 A; B=1-437.
DR   PDB; 3DPY; X-ray; 2.70 A; B=1-437.
DR   PDB; 3E30; X-ray; 2.45 A; B=1-437.
DR   PDB; 3E32; X-ray; 2.45 A; B=1-437.
DR   PDB; 3E33; X-ray; 1.90 A; B=1-437.
DR   PDB; 3E34; X-ray; 2.05 A; B=1-437.
DR   PDB; 3EU5; X-ray; 2.80 A; B=1-427.
DR   PDB; 3EUV; X-ray; 2.75 A; B=1-427.
DR   PDB; 3KSL; X-ray; 2.05 A; B=1-437.
DR   PDB; 3KSQ; X-ray; 2.10 A; B=1-437.
DR   PDB; 4GTM; X-ray; 2.20 A; B=1-427.
DR   PDB; 4GTO; X-ray; 2.15 A; B=1-427.
DR   PDB; 4GTP; X-ray; 2.75 A; B=1-427.
DR   PDB; 4GTQ; X-ray; 2.60 A; B=1-427.
DR   PDB; 4GTR; X-ray; 2.20 A; B=1-427.
DR   PDB; 7RN5; X-ray; 2.28 A; B=1-437.
DR   PDB; 7RNI; X-ray; 1.98 A; B=1-437.
DR   PDB; 8E9E; X-ray; 2.84 A; B=1-437.
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; 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; 1SA5; -.
DR   PDBsum; 1TN7; -.
DR   PDBsum; 1TN8; -.
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; 4GTM; -.
DR   PDBsum; 4GTO; -.
DR   PDBsum; 4GTP; -.
DR   PDBsum; 4GTQ; -.
DR   PDBsum; 4GTR; -.
DR   PDBsum; 7RN5; -.
DR   PDBsum; 7RNI; -.
DR   PDBsum; 8E9E; -.
DR   AlphaFoldDB; Q02293; -.
DR   SMR; Q02293; -.
DR   BioGRID; 249096; 1.
DR   ComplexPortal; CPX-2181; Protein farnesyltransferase complex.
DR   DIP; DIP-6132N; -.
DR   IntAct; Q02293; 1.
DR   STRING; 10116.ENSRNOP00000010588; -.
DR   BindingDB; Q02293; -.
DR   ChEMBL; CHEMBL2095197; -.
DR   iPTMnet; Q02293; -.
DR   PhosphoSitePlus; Q02293; -.
DR   jPOST; Q02293; -.
DR   PaxDb; 10116-ENSRNOP00000010588; -.
DR   Ensembl; ENSRNOT00000010588.5; ENSRNOP00000010588.3; ENSRNOG00000007660.5.
DR   Ensembl; ENSRNOT00055035360; ENSRNOP00055028662; ENSRNOG00055020713.
DR   Ensembl; ENSRNOT00060052814; ENSRNOP00060043901; ENSRNOG00060030412.
DR   Ensembl; ENSRNOT00065033869; ENSRNOP00065027091; ENSRNOG00065020087.
DR   GeneID; 64511; -.
DR   KEGG; rno:64511; -.
DR   UCSC; RGD:620119; rat.
DR   AGR; RGD:620119; -.
DR   CTD; 2342; -.
DR   RGD; 620119; Fntb.
DR   eggNOG; KOG0365; Eukaryota.
DR   GeneTree; ENSGT00950000183128; -.
DR   HOGENOM; CLU_028946_0_1_1; -.
DR   InParanoid; Q02293; -.
DR   OMA; WCIYWIL; -.
DR   OrthoDB; 5478505at2759; -.
DR   PhylomeDB; Q02293; -.
DR   TreeFam; TF353162; -.
DR   BRENDA; 2.5.1.58; 5301.
DR   BRENDA; 2.5.1.59; 5301.
DR   Reactome; R-RNO-2514859; Inactivation, recovery and regulation of the phototransduction cascade.
DR   Reactome; R-RNO-9648002; RAS processing.
DR   SABIO-RK; Q02293; -.
DR   EvolutionaryTrace; Q02293; -.
DR   PRO; PR:Q02293; -.
DR   Proteomes; UP000002494; Chromosome 6.
DR   Bgee; ENSRNOG00000007660; Expressed in cerebellum and 20 other cell types or tissues.
DR   GO; GO:0005875; C:microtubule associated complex; ISO:RGD.
DR   GO; GO:0005965; C:protein farnesyltransferase complex; ISS:UniProtKB.
DR   GO; GO:0004311; F:farnesyltranstransferase activity; ISO:RGD.
DR   GO; GO:0004660; F:protein farnesyltransferase activity; IDA:RGD.
DR   GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR   GO; GO:0008283; P:cell population proliferation; ISO:RGD.
DR   GO; GO:0048144; P:fibroblast proliferation; ISO:RGD.
DR   GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0008285; P:negative regulation of cell population proliferation; 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:0048146; P:positive regulation of fibroblast proliferation; ISO:RGD.
DR   GO; GO:0051770; P:positive regulation of nitric-oxide synthase biosynthetic process; IMP:RGD.
DR   GO; GO:0018343; P:protein farnesylation; ISS:UniProtKB.
DR   GO; GO:0048145; P:regulation of fibroblast proliferation; ISO:RGD.
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   GO; GO:0042060; P:wound healing; ISO:RGD.
DR   CDD; cd02893; FTase; 1.
DR   Gene3D; 1.50.10.20; -; 1.
DR   InterPro; IPR026872; FTB.
DR   InterPro; IPR001330; PFTB_repeat.
DR   InterPro; IPR045089; PGGT1B-like.
DR   InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase.
DR   PANTHER; PTHR11774; GERANYLGERANYL TRANSFERASE TYPE BETA SUBUNIT; 1.
DR   PANTHER; PTHR11774:SF6; PROTEIN FARNESYLTRANSFERASE SUBUNIT BETA; 1.
DR   Pfam; PF00432; Prenyltrans; 5.
DR   SFLD; SFLDG01015; Prenyltransferase_Like_1; 1.
DR   SUPFAM; SSF48239; Terpenoid cyclases/Protein prenyltransferases; 1.
DR   Genevisible; Q02293; RN.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Lipid metabolism; Metal-binding;
KW   Phosphoprotein; Prenyltransferase; Reference proteome; Repeat; Transferase;
KW   Zinc.
FT   CHAIN           1..437
FT                   /note="Protein farnesyltransferase subunit beta"
FT                   /id="PRO_0000119763"
FT   REPEAT          123..164
FT                   /note="PFTB 1"
FT   REPEAT          174..215
FT                   /note="PFTB 2"
FT   REPEAT          222..263
FT                   /note="PFTB 3"
FT   REPEAT          270..312
FT                   /note="PFTB 4"
FT   REPEAT          332..374
FT                   /note="PFTB 5"
FT   BINDING         248..251
FT                   /ligand="(2E,6E)-farnesyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:175763"
FT   BINDING         291..294
FT                   /ligand="(2E,6E)-farnesyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:175763"
FT   BINDING         297
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000269|PubMed:18844669,
FT                   ECO:0000269|PubMed:20056542, ECO:0000269|PubMed:9065406"
FT   BINDING         299
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000269|PubMed:18844669,
FT                   ECO:0000269|PubMed:20056542, ECO:0000269|PubMed:9065406"
FT   BINDING         300..303
FT                   /ligand="(2E,6E)-farnesyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:175763"
FT   BINDING         362
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000269|PubMed:18844669,
FT                   ECO:0000269|PubMed:20056542, ECO:0000269|PubMed:9065406"
FT   SITE            102
FT                   /note="Important for selectivity against geranylgeranyl
FT                   diphosphate"
FT                   /evidence="ECO:0000250|UniProtKB:P49356"
FT   MOD_RES         432
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8K2I1"
FT   MOD_RES         436
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8K2I1"
FT   HELIX           24..26
FT                   /evidence="ECO:0007829|PDB:3E33"
FT   HELIX           28..33
FT                   /evidence="ECO:0007829|PDB:3E33"
FT   HELIX           43..65
FT                   /evidence="ECO:0007829|PDB:3E33"
FT   HELIX           75..85
FT                   /evidence="ECO:0007829|PDB:3E33"
FT   HELIX           91..96
FT                   /evidence="ECO:0007829|PDB:3E33"
FT   HELIX           100..113
FT                   /evidence="ECO:0007829|PDB:3E33"
FT   HELIX           120..133
FT                   /evidence="ECO:0007829|PDB:3E33"
FT   STRAND          138..143
FT                   /evidence="ECO:0007829|PDB:3E33"
FT   HELIX           150..163
FT                   /evidence="ECO:0007829|PDB:3E33"
FT   HELIX           166..171
FT                   /evidence="ECO:0007829|PDB:3E33"
FT   HELIX           174..184
FT                   /evidence="ECO:0007829|PDB:3E33"
FT   STRAND          191..194
FT                   /evidence="ECO:0007829|PDB:3E33"
FT   HELIX           201..213
FT                   /evidence="ECO:0007829|PDB:3E33"
FT   TURN            219..224
FT                   /evidence="ECO:0007829|PDB:3E33"
FT   HELIX           225..232
FT                   /evidence="ECO:0007829|PDB:3E33"
FT   STRAND          237..239
FT                   /evidence="ECO:0007829|PDB:3E33"
FT   HELIX           249..261
FT                   /evidence="ECO:0007829|PDB:3E33"
FT   HELIX           265..267
FT                   /evidence="ECO:0007829|PDB:3E33"
FT   HELIX           270..278
FT                   /evidence="ECO:0007829|PDB:3E33"
FT   TURN            283..285
FT                   /evidence="ECO:0007829|PDB:3E33"
FT   STRAND          287..291
FT                   /evidence="ECO:0007829|PDB:3E33"
FT   HELIX           300..303
FT                   /evidence="ECO:0007829|PDB:3E33"
FT   TURN            304..306
FT                   /evidence="ECO:0007829|PDB:3E33"
FT   HELIX           307..317
FT                   /evidence="ECO:0007829|PDB:3E33"
FT   STRAND          321..323
FT                   /evidence="ECO:0007829|PDB:1NI1"
FT   STRAND          325..327
FT                   /evidence="ECO:0007829|PDB:1NI1"
FT   HELIX           332..342
FT                   /evidence="ECO:0007829|PDB:3E33"
FT   STRAND          348..350
FT                   /evidence="ECO:0007829|PDB:1FT1"
FT   STRAND          352..355
FT                   /evidence="ECO:0007829|PDB:1N94"
FT   HELIX           360..374
FT                   /evidence="ECO:0007829|PDB:3E33"
FT   STRAND          375..378
FT                   /evidence="ECO:0007829|PDB:3E33"
FT   STRAND          381..384
FT                   /evidence="ECO:0007829|PDB:3E33"
FT   HELIX           390..392
FT                   /evidence="ECO:0007829|PDB:3E33"
FT   TURN            399..401
FT                   /evidence="ECO:0007829|PDB:3E33"
FT   HELIX           405..415
FT                   /evidence="ECO:0007829|PDB:3E33"
FT   HELIX           424..426
FT                   /evidence="ECO:0007829|PDB:1FT1"
FT   HELIX           434..436
FT                   /evidence="ECO:0007829|PDB:1FT1"
SQ   SEQUENCE   437 AA;  48673 MW;  41A9D6D79CD319A8 CRC64;
     MASSSSFTYY CPPSSSPVWS EPLYSLRPEH ARERLQDDSV ETVTSIEQAK VEEKIQEVFS
     SYKFNHLVPR LVLQREKHFH YLKRGLRQLT DAYECLDASR PWLCYWILHS LELLDEPIPQ
     IVATDVCQFL ELCQSPDGGF GGGPGQYPHL APTYAAVNAL CIIGTEEAYN VINREKLLQY
     LYSLKQPDGS FLMHVGGEVD VRSAYCAASV ASLTNIITPD LFEGTAEWIA RCQNWEGGIG
     GVPGMEAHGG YTFCGLAALV ILKKERSLNL KSLLQWVTSR QMRFEGGFQG RCNKLVDGCY
     SFWQAGLLPL LHRALHAQGD PALSMSHWMF HQQALQEYIL MCCQCPAGGL LDKPGKSRDF
     YHTCYCLSGL SIAQHFGSGA MLHDVVMGVP ENVLQPTHPV YNIGPDKVIQ ATTHFLQKPV
     PGFEECEDAV TSDPATD
//