FNTB_BOVIN
ID FNTB_BOVIN Reviewed; 437 AA.
AC P49355; A4FUX0; Q9TS25;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 136.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=8494894; DOI=10.1021/bi00070a028;
RA Omer C.A., Kral A.M., Diehl R.E., Prendergast G.C., Powers S., Allen C.M.,
RA Gibbs J.B., Kohl N.E.;
RT "Characterization of recombinant human farnesyl-protein transferase:
RT cloning, expression, farnesyl diphosphate binding, and functional homology
RT with yeast prenyl-protein transferases.";
RL Biochemistry 32:5167-5176(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Hippocampus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
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 (By
CC similarity). {ECO:0000250}.
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 -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P49356};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P49356};
CC -!- SUBUNIT: Heterodimer of FNTA and FNTB. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein prenyltransferase subunit beta
CC family. {ECO:0000305}.
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DR EMBL; L00633; AAA30524.1; -; mRNA.
DR EMBL; BC123393; AAI23394.1; -; mRNA.
DR PIR; C49274; C49274.
DR RefSeq; NP_786999.1; NM_175805.3.
DR AlphaFoldDB; P49355; -.
DR SMR; P49355; -.
DR ComplexPortal; CPX-2162; Protein farnesyltransferase complex.
DR STRING; 9913.ENSBTAP00000007751; -.
DR BindingDB; P49355; -.
DR ChEMBL; CHEMBL2095178; -.
DR DrugCentral; P49355; -.
DR PaxDb; P49355; -.
DR PRIDE; P49355; -.
DR Ensembl; ENSBTAT00000007751; ENSBTAP00000007751; ENSBTAG00000005897.
DR GeneID; 327686; -.
DR KEGG; bta:327686; -.
DR CTD; 2342; -.
DR VEuPathDB; HostDB:ENSBTAG00000005897; -.
DR VGNC; VGNC:108986; FNTB.
DR eggNOG; KOG0365; Eukaryota.
DR GeneTree; ENSGT00950000183128; -.
DR HOGENOM; CLU_028946_0_1_1; -.
DR InParanoid; P49355; -.
DR OMA; WCIYWIL; -.
DR OrthoDB; 1042804at2759; -.
DR TreeFam; TF353162; -.
DR PRO; PR:P49355; -.
DR Proteomes; UP000009136; Chromosome 10.
DR Bgee; ENSBTAG00000005897; Expressed in pons and 103 other tissues.
DR GO; GO:0005875; C:microtubule associated complex; IEA:Ensembl.
DR GO; GO:0005965; C:protein farnesyltransferase complex; ISS:UniProtKB.
DR GO; GO:0004660; F:protein farnesyltransferase activity; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0018343; P:protein farnesylation; ISS:UniProtKB.
DR GO; GO:0018342; P:protein prenylation; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Lipid metabolism; Metal-binding; Phosphoprotein; Prenyltransferase;
KW Reference proteome; Repeat; Transferase; Zinc.
FT CHAIN 1..437
FT /note="Protein farnesyltransferase subunit beta"
FT /id="PRO_0000119760"
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 436
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8K2I1"
SQ SEQUENCE 437 AA; 48768 MW; CE09DFA86AC6AB64 CRC64;
MASPSSFTYC CPPSSSPIWS EPLYSLRPEH ARERLQDDSV ETVTSIEQAK VEEKIQEVFS
SYKFNHLVPR LVLQREKHFH YLKRGLRQLT DAYECLDASR PWLCYWILHS LELLDEPIPQ
MVATDVCQFL ELCQSPEGGF GGGPGQYPHL APTYAAVNAL CIIGTEEAYD VINREKLLQY
LYSLKQPDGS FLMHDGGEVD VRSAYCAASV ASLTNIITPD LFEGTAEWIA RCQNWEGGIG
GVPGMEAHGG YTFCGLAALV ILKKERSLNL KSLLQWVTSR QMRFEGGFQG RCNKLVDGCY
SFWQAGLLPL LHRALHAQGD PALSMSRWMF HQQALQEYIL MCCQCPTGGL LDKPGKSRDF
YHTCYCLSGL SIAQHFGSGA MLHDVVLGVP ENALQPTHPV YNIGPDKVIQ ATMHFLQKPV
PGFEEHEDEA SAEPATD
