PGTB2_YEAST
ID PGTB2_YEAST Reviewed; 325 AA.
AC P20133; D6W4H7; P32433;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 3.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Geranylgeranyl transferase type-2 subunit beta;
DE EC=2.5.1.60;
DE AltName: Full=Geranylgeranyl transferase type II subunit beta;
DE Short=GGTase-II-beta;
DE AltName: Full=Type II protein geranyl-geranyltransferase subunit beta;
DE Short=PGGT;
DE AltName: Full=YPT1/SEC4 proteins geranylgeranyltransferase subunit beta;
GN Name=BET2; OrderedLocusNames=YPR176C; ORFNames=P9705.12;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2204247; DOI=10.1002/yea.320060407;
RA Petersen-Bjoern S., Harrington T.R., Friesen J.D.;
RT "An essential gene in Saccharomyces cerevisiae shares an upstream
RT regulatory element with PRP4.";
RL Yeast 6:345-352(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1903184; DOI=10.1038/351158a0;
RA Rossi G., Jiang Y., Newman A.P., Ferro-Novick S.;
RT "Dependence of Ypt1 and Sec4 membrane attachment on Bet2.";
RL Nature 351:158-161(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(1997).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-187.
RX PubMed=2528686; DOI=10.1128/mcb.9.9.3698-3709.1989;
RA Petersen-Bjoern S., Soltyk A., Beggs J.D., Friesen J.D.;
RT "PRP4 (RNA4) from Saccharomyces cerevisiae: its gene product is associated
RT with the U4/U6 small nuclear ribonucleoprotein particle.";
RL Mol. Cell. Biol. 9:3698-3709(1989).
RN [7]
RP CHARACTERIZATION.
RX PubMed=8232542; DOI=10.1038/366084a0;
RA Jiang Y., Rossi G., Ferro-Novick S.;
RT "Bet2p and Mad2p are components of a prenyltransferase that adds
RT geranylgeranyl onto Ypt1p and Sec4p.";
RL Nature 366:84-86(1993).
RN [8]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
CC -!- FUNCTION: Catalyzes the transfer of a geranyl-geranyl moiety from
CC geranyl-geranyl pyrophosphate to proteins having the C-terminal -XCC or
CC -XCXC, where both cysteines may become modified. Acts on YPT1 and SEC4.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=geranylgeranyl diphosphate + L-cysteinyl-[protein] =
CC diphosphate + S-geranylgeranyl-L-cysteinyl-[protein];
CC Xref=Rhea:RHEA:21240, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:11537,
CC ChEBI:CHEBI:29950, ChEBI:CHEBI:33019, ChEBI:CHEBI:57533,
CC ChEBI:CHEBI:86021; EC=2.5.1.60;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit.
CC -!- INTERACTION:
CC P20133; Q00618: BET4; NbExp=3; IntAct=EBI-3559, EBI-3573;
CC -!- MISCELLANEOUS: Present with 1520 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the protein prenyltransferase subunit beta
CC family. {ECO:0000305}.
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DR EMBL; M29585; AAA66939.1; -; Genomic_DNA.
DR EMBL; M26597; AAA79331.1; -; Genomic_DNA.
DR EMBL; U25842; AAB68110.1; -; Genomic_DNA.
DR EMBL; AY558067; AAS56393.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11593.1; -; Genomic_DNA.
DR PIR; S59834; S59834.
DR RefSeq; NP_015502.1; NM_001184273.1.
DR AlphaFoldDB; P20133; -.
DR SMR; P20133; -.
DR BioGRID; 36349; 357.
DR ComplexPortal; CPX-1636; Protein geranylgeranyltransferase type II complex.
DR DIP; DIP-2214N; -.
DR IntAct; P20133; 3.
DR STRING; 4932.YPR176C; -.
DR MaxQB; P20133; -.
DR PaxDb; P20133; -.
DR PRIDE; P20133; -.
DR EnsemblFungi; YPR176C_mRNA; YPR176C; YPR176C.
DR GeneID; 856306; -.
DR KEGG; sce:YPR176C; -.
DR SGD; S000006380; BET2.
DR VEuPathDB; FungiDB:YPR176C; -.
DR eggNOG; KOG0366; Eukaryota.
DR GeneTree; ENSGT00950000183128; -.
DR HOGENOM; CLU_028946_3_0_1; -.
DR InParanoid; P20133; -.
DR OMA; VKRCQCP; -.
DR BioCyc; YEAST:MON3O-1; -.
DR Reactome; R-SCE-6803205; TP53 regulates transcription of several additional cell death genes whose specific roles in p53-dependent apoptosis remain uncertain.
DR Reactome; R-SCE-8873719; RAB geranylgeranylation.
DR PRO; PR:P20133; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; P20133; protein.
DR GO; GO:0005829; C:cytosol; HDA:SGD.
DR GO; GO:0005968; C:Rab-protein geranylgeranyltransferase complex; IDA:SGD.
DR GO; GO:0004663; F:Rab geranylgeranyltransferase activity; IDA:SGD.
DR GO; GO:0031267; F:small GTPase binding; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IMP:SGD.
DR GO; GO:0018344; P:protein geranylgeranylation; IDA:SGD.
DR GO; GO:0018342; P:protein prenylation; IBA:GO_Central.
DR GO; GO:0006612; P:protein targeting to membrane; IMP:SGD.
DR CDD; cd02894; GGTase-II; 1.
DR InterPro; IPR001330; PFTB_repeat.
DR InterPro; IPR045089; PGGT1B-like.
DR InterPro; IPR026873; Ptb1.
DR InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase.
DR PANTHER; PTHR11774; PTHR11774; 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..325
FT /note="Geranylgeranyl transferase type-2 subunit beta"
FT /id="PRO_0000119777"
FT REPEAT 9..50
FT /note="PFTB 1"
FT REPEAT 57..99
FT /note="PFTB 2"
FT REPEAT 109..150
FT /note="PFTB 3"
FT REPEAT 157..198
FT /note="PFTB 4"
FT REPEAT 208..249
FT /note="PFTB 5"
FT REPEAT 256..298
FT /note="PFTB 6"
FT BINDING 183..185
FT /ligand="geranylgeranyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57533"
FT /evidence="ECO:0000250"
FT BINDING 228..240
FT /ligand="geranylgeranyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57533"
FT /evidence="ECO:0000250"
FT BINDING 234
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 236
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 286
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT CONFLICT 22
FT /note="K -> N (in Ref. 1 and 5)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 325 AA; 36666 MW; 6A9C44DFBE62AAFC CRC64;
MSGSLTLLKE KHIRYIESLD TKKHNFEYWL TEHLRLNGIY WGLTALCVLD SPETFVKEEV
ISFVLSCWDD KYGAFAPFPR HDAHLLTTLS AVQILATYDA LDVLGKDRKV RLISFIRGNQ
LEDGSFQGDR FGEVDTRFVY TALSALSILG ELTSEVVDPA VDFVLKCYNF DGGFGLCPNA
ESHAAQAFTC LGALAIANKL DMLSDDQLEE IGWWLCERQL PEGGLNGRPS KLPDVCYSWW
VLSSLAIIGR LDWINYEKLT EFILKCQDEK KGGISDRPEN EVDVFHTVFG VAGLSLMGYD
NLVPIDPIYC MPKSVTSKFK KYPYK
