FNTB_SCHPO
ID FNTB_SCHPO Reviewed; 382 AA.
AC O13782;
DT 06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Protein farnesyltransferase subunit beta;
DE Short=FTase-beta;
DE EC=2.5.1.58 {ECO:0000269|PubMed:10617635};
DE AltName: Full=CAAX farnesyltransferase subunit beta;
DE AltName: Full=Ras proteins prenyltransferase subunit beta;
GN Name=cpp1; ORFNames=SPAC17G6.04c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP SUBUNIT.
RX PubMed=10617635; DOI=10.1074/jbc.275.1.429;
RA Yang W., Urano J., Tamanoi F.;
RT "Protein farnesylation is critical for maintaining normal cell morphology
RT and canavanine resistance in Schizosaccharomyces pombe.";
RL J. Biol. Chem. 275:429-438(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
CC -!- FUNCTION: Catalyzes the transfer of a farnesyl moiety from farnesyl
CC diphosphate to a cysteine at the fourth position from the C-terminus of
CC several proteins. The beta(cpp1) subunit is responsible for peptide-
CC binding. {ECO:0000269|PubMed:10617635}.
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:10617635};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13346;
CC Evidence={ECO:0000269|PubMed:10617635};
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 an alpha(cwp1) and a beta(cpp1) subunit.
CC {ECO:0000269|PubMed:10617635}.
CC -!- SIMILARITY: Belongs to the protein prenyltransferase subunit beta
CC family. {ECO:0000305}.
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DR EMBL; CU329670; CAB16215.1; -; Genomic_DNA.
DR PIR; T37836; T37836.
DR RefSeq; NP_594251.1; NM_001019674.2.
DR AlphaFoldDB; O13782; -.
DR SMR; O13782; -.
DR BioGRID; 278844; 13.
DR STRING; 4896.SPAC17G6.04c.1; -.
DR MaxQB; O13782; -.
DR PaxDb; O13782; -.
DR EnsemblFungi; SPAC17G6.04c.1; SPAC17G6.04c.1:pep; SPAC17G6.04c.
DR GeneID; 2542380; -.
DR KEGG; spo:SPAC17G6.04c; -.
DR PomBase; SPAC17G6.04c; cpp1.
DR VEuPathDB; FungiDB:SPAC17G6.04c; -.
DR eggNOG; KOG0365; Eukaryota.
DR HOGENOM; CLU_028946_0_2_1; -.
DR InParanoid; O13782; -.
DR OMA; WCIYWIL; -.
DR PhylomeDB; O13782; -.
DR Reactome; R-SPO-9648002; RAS processing.
DR PRO; PR:O13782; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0005965; C:protein farnesyltransferase complex; IPI:PomBase.
DR GO; GO:0004660; F:protein farnesyltransferase activity; IDA:PomBase.
DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR GO; GO:0018343; P:protein farnesylation; IBA:GO_Central.
DR GO; GO:0072659; P:protein localization to plasma membrane; IC:PomBase.
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 1: Evidence at protein level;
KW Metal-binding; Prenyltransferase; Reference proteome; Repeat; Transferase;
KW Zinc.
FT CHAIN 1..382
FT /note="Protein farnesyltransferase subunit beta"
FT /id="PRO_0000119767"
FT REPEAT 78..119
FT /note="PFTB 1"
FT REPEAT 129..170
FT /note="PFTB 2"
FT REPEAT 178..219
FT /note="PFTB 3"
FT REPEAT 226..268
FT /note="PFTB 4"
FT REPEAT 286..328
FT /note="PFTB 5"
FT BINDING 204..207
FT /ligand="(2E,6E)-farnesyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:175763"
FT /evidence="ECO:0000250|UniProtKB:P49356"
FT BINDING 247..250
FT /ligand="(2E,6E)-farnesyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:175763"
FT /evidence="ECO:0000250|UniProtKB:P49356"
FT BINDING 253
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P49356"
FT BINDING 255
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P49356"
FT BINDING 256..259
FT /ligand="(2E,6E)-farnesyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:175763"
FT /evidence="ECO:0000250|UniProtKB:P49356"
FT BINDING 316
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P49356"
FT SITE 58
FT /note="Important for selectivity against geranylgeranyl
FT diphosphate"
FT /evidence="ECO:0000250|UniProtKB:P49356"
SQ SEQUENCE 382 AA; 42189 MW; C3F2705D93F84203 CRC64;
MDELSETQVM QNETATAVLP LLNGESQSFN LQKHLKYLTK MLDPLPSPFT VLDASRAWMV
YWELSSLAIL GKLDSSVCER AISSVRQLKG PSGGFCGGNG QDEHLLSTYA SILSICLCDS
TDAYSLIERD RLYDWLFSLK NPDGSFRVNN EGESDARSVY AAVCVSSLVG ISMDDPLFEG
TLQWLCKCQT YEGGLSGVPY AEAHGGYTFC ALAAIALLGG LDNLNEIKLS TWLVQRQDPA
LYGFSGRSNK LVDGCYSWWV GASHVIVASG YGSASHKSLP NLFYNPEKLL GYILQCCQST
SGGLRDKPPK RPDQYHTCYC LLGLSSIAYD YRYHTSDGWS YKPSILHSSL SSLLPAHPIY
CVPFGFEERI KSYFLSQESS KF
