ID   FNTB_MOUSE              Reviewed;         437 AA.
AC   Q8K2I1;
DT   25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   24-JAN-2024, entry version 142.
DE   RecName: Full=Protein farnesyltransferase subunit beta;
DE            Short=FTase-beta;
DE            EC=2.5.1.58 {ECO:0000269|PubMed:21520375};
DE   AltName: Full=CAAX farnesyltransferase subunit beta;
DE   AltName: Full=Ras proteins prenyltransferase subunit beta;
GN   Name=Fntb;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=129; TISSUE=Mammary tumor;
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   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-432 AND THR-436, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Pancreas,
RC   Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [3]
RP   FUNCTION.
RX   PubMed=17652517; DOI=10.1073/pnas.0704212104;
RA   Coffinier C., Hudon S.E., Farber E.A., Chang S.Y., Hrycyna C.A.,
RA   Young S.G., Fong L.G.;
RT   "HIV protease inhibitors block the zinc metalloproteinase ZMPSTE24 and lead
RT   to an accumulation of prelamin A in cells.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:13432-13437(2007).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 2-427 IN COMPLEX WITH FNTA AND
RP   ZINC IONS, SUBUNIT, CATALYTIC ACTIVITY, FUNCTION, AND COFACTOR.
RX   PubMed=21520375; DOI=10.1002/anie.201101210;
RA   Bon R.S., Guo Z., Stigter E.A., Wetzel S., Menninger S., Wolf A.,
RA   Choidas A., Alexandrov K., Blankenfeldt W., Goody R.S., Waldmann H.;
RT   "Structure-guided development of selective RabGGTase inhibitors.";
RL   Angew. Chem. Int. Ed. Engl. 50:4957-4961(2011).
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:17652517, ECO:0000269|PubMed:21520375}.
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:21520375};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000269|PubMed:21520375};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:21520375};
CC   -!- SUBUNIT: Heterodimer of FNTA and FNTB. {ECO:0000269|PubMed:21520375}.
CC   -!- SIMILARITY: Belongs to the protein prenyltransferase subunit beta
CC       family. {ECO:0000305}.
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DR   EMBL; BC031417; AAH31417.1; -; mRNA.
DR   CCDS; CCDS25998.1; -.
DR   RefSeq; NP_666039.1; NM_145927.2.
DR   PDB; 3PZ4; X-ray; 2.10 A; B=2-427.
DR   PDBsum; 3PZ4; -.
DR   AlphaFoldDB; Q8K2I1; -.
DR   SMR; Q8K2I1; -.
DR   BioGRID; 225746; 8.
DR   ComplexPortal; CPX-2185; Protein farnesyltransferase complex.
DR   STRING; 10090.ENSMUSP00000035498; -.
DR   BindingDB; Q8K2I1; -.
DR   ChEMBL; CHEMBL2096912; -.
DR   iPTMnet; Q8K2I1; -.
DR   PhosphoSitePlus; Q8K2I1; -.
DR   EPD; Q8K2I1; -.
DR   MaxQB; Q8K2I1; -.
DR   PaxDb; 10090-ENSMUSP00000035498; -.
DR   PeptideAtlas; Q8K2I1; -.
DR   ProteomicsDB; 267612; -.
DR   Pumba; Q8K2I1; -.
DR   DNASU; 110606; -.
DR   Ensembl; ENSMUST00000041008.10; ENSMUSP00000035498.10; ENSMUSG00000033373.17.
DR   GeneID; 110606; -.
DR   KEGG; mmu:110606; -.
DR   UCSC; uc007nyu.1; mouse.
DR   AGR; MGI:1861305; -.
DR   CTD; 2342; -.
DR   MGI; MGI:1861305; Fntb.
DR   VEuPathDB; HostDB:ENSMUSG00000033373; -.
DR   eggNOG; KOG0365; Eukaryota.
DR   GeneTree; ENSGT00950000183128; -.
DR   HOGENOM; CLU_028946_0_1_1; -.
DR   InParanoid; Q8K2I1; -.
DR   OMA; WCIYWIL; -.
DR   OrthoDB; 5478505at2759; -.
DR   PhylomeDB; Q8K2I1; -.
DR   TreeFam; TF353162; -.
DR   BRENDA; 2.5.1.58; 3474.
DR   Reactome; R-MMU-2514859; Inactivation, recovery and regulation of the phototransduction cascade.
DR   Reactome; R-MMU-9648002; RAS processing.
DR   BioGRID-ORCS; 110606; 28 hits in 82 CRISPR screens.
DR   ChiTaRS; Fntb; mouse.
DR   PRO; PR:Q8K2I1; -.
DR   Proteomes; UP000000589; Chromosome 12.
DR   RNAct; Q8K2I1; Protein.
DR   Bgee; ENSMUSG00000033373; Expressed in yolk sac and 213 other cell types or tissues.
DR   ExpressionAtlas; Q8K2I1; baseline and differential.
DR   GO; GO:0005875; C:microtubule associated complex; ISO:MGI.
DR   GO; GO:0005965; C:protein farnesyltransferase complex; ISS:UniProtKB.
DR   GO; GO:0004311; F:farnesyltranstransferase activity; IMP:MGI.
DR   GO; GO:0004660; F:protein farnesyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR   GO; GO:0008283; P:cell population proliferation; IMP:MGI.
DR   GO; GO:0048144; P:fibroblast proliferation; IMP:MGI.
DR   GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0008285; P:negative regulation of cell population proliferation; IMP:MGI.
DR   GO; GO:0045787; P:positive regulation of cell cycle; ISO:MGI.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:MGI.
DR   GO; GO:0048146; P:positive regulation of fibroblast proliferation; IMP:MGI.
DR   GO; GO:0051770; P:positive regulation of nitric-oxide synthase biosynthetic process; ISO:MGI.
DR   GO; GO:0018343; P:protein farnesylation; ISS:UniProtKB.
DR   GO; GO:0048145; P:regulation of fibroblast proliferation; IMP:MGI.
DR   GO; GO:0034097; P:response to cytokine; ISO:MGI.
DR   GO; GO:0010035; P:response to inorganic substance; ISO:MGI.
DR   GO; GO:0014070; P:response to organic cyclic compound; ISO:MGI.
DR   GO; GO:0042060; P:wound healing; IMP:MGI.
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; Q8K2I1; MM.
PE   1: Evidence at protein level;
KW   3D-structure; Lipid metabolism; Metal-binding; Phosphoprotein;
KW   Prenyltransferase; Reference proteome; Repeat; Transferase; Zinc.
FT   CHAIN           1..437
FT                   /note="Protein farnesyltransferase subunit beta"
FT                   /id="PRO_0000119762"
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                   /evidence="ECO:0000250|UniProtKB:P49356"
FT   BINDING         291..294
FT                   /ligand="(2E,6E)-farnesyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:175763"
FT                   /evidence="ECO:0000250|UniProtKB:P49356"
FT   BINDING         297
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P49356"
FT   BINDING         299
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P49356"
FT   BINDING         300..303
FT                   /ligand="(2E,6E)-farnesyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:175763"
FT                   /evidence="ECO:0000250|UniProtKB:P49356"
FT   BINDING         362
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P49356"
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:0007744|PubMed:21183079"
FT   MOD_RES         436
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
SQ   SEQUENCE   437 AA;  48820 MW;  42B780B356136950 CRC64;
     MASSSSFTYY CPPSSSPVWS EPLYSLRPEH VRERLQDDSV ETVTSIEQAK VEEKIQEVFS
     SYKFNHLVPR LILQREKHFH 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 MLHDMVMGVP ENVLQPTHPV YNIGPEKVIQ ATTHFLQKPV
     PGFEECEDEV TSDPATD
//