FNTB_MOUSE
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 03-AUG-2022, entry version 135.
DE RecName: Full=Protein farnesyltransferase subunit beta;
DE Short=FTase-beta;
DE EC=2.5.1.58;
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, Spleen,
RC 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 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: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; Q8K2I1; -.
DR PeptideAtlas; Q8K2I1; -.
DR PRIDE; Q8K2I1; -.
DR ProteomicsDB; 267612; -.
DR DNASU; 110606; -.
DR Ensembl; ENSMUST00000041008; ENSMUSP00000035498; ENSMUSG00000033373.
DR GeneID; 110606; -.
DR KEGG; mmu:110606; -.
DR UCSC; uc007nyu.1; mouse.
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; 1042804at2759; -.
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; 27 hits in 77 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 210 other tissues.
DR ExpressionAtlas; Q8K2I1; baseline and differential.
DR Genevisible; Q8K2I1; MM.
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:0042277; F:peptide binding; ISO: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:0018342; P:protein prenylation; IBA:GO_Central.
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 InterPro; IPR026872; FTB.
DR InterPro; IPR001330; PFTB_repeat.
DR InterPro; IPR045089; PGGT1B-like.
DR InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase.
DR PANTHER; PTHR11774; PTHR11774; 1.
DR PANTHER; PTHR11774:SF6; PTHR11774:SF6; 1.
DR Pfam; PF00432; Prenyltrans; 5.
DR SUPFAM; SSF48239; SSF48239; 1.
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
