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   02-SEP-2026, entry version 151.
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.
CC       {ECO:0000250|UniProtKB:P49356}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-cysteinyl-[protein] + (2E,6E)-farnesyl diphosphate = S-
CC         (2E,6E)-farnesyl-L-cysteinyl-[protein] + diphosphate;
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:0000250|UniProtKB:P49356};
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|UniProtKB:P49356}.
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   FunCoup; P49355; 4334.
DR   STRING; 9913.ENSBTAP00000007751; -.
DR   BindingDB; P49355; -.
DR   ChEMBL; CHEMBL2095178; -.
DR   DrugCentral; P49355; -.
DR   PaxDb; 9913-ENSBTAP00000007751; -.
DR   GeneID; 327686; -.
DR   KEGG; bta:327686; -.
DR   CTD; 2342; -.
DR   VEuPathDB; HostDB:ENSBTAG00000005897; -.
DR   eggNOG; KOG0365; Eukaryota.
DR   HOGENOM; CLU_028946_0_1_1; -.
DR   InParanoid; P49355; -.
DR   OMA; WCIYWIL; -.
DR   OrthoDB; 10261146at2759; -.
DR   Reactome; R-BTA-2514859; Inactivation, recovery and regulation of the phototransduction cascade.
DR   Reactome; R-BTA-9648002; RAS processing.
DR   Reactome; R-BTA-9953170; GBP-mediated host defense.
DR   PRO; PR:P49355; -.
DR   Proteomes; UP000009136; Chromosome 10.
DR   Bgee; ENSBTAG00000005897; Expressed in pons and 103 other cell types or tissues.
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:0018343; P:protein farnesylation; ISS:UniProtKB.
DR   CDD; cd02893; FTase; 1.
DR   FunFam; 1.50.10.20:FF:000007; Protein farnesyltransferase subunit beta; 1.
DR   Gene3D; 1.50.10.20; -; 1.
DR   InterPro; IPR026872; FTB.
DR   InterPro; IPR045089; PGGT1B-like.
DR   InterPro; IPR001330; Prenyltrans.
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; 1.
DR   SFLD; SFLDG01015; Prenyltransferase_Like_1; 1.
DR   SUPFAM; SSF48239; Terpenoid cyclases/Protein prenyltransferases; 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
//