ID PGTB2_RAT Reviewed; 331 AA. AC Q08603; DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1995, sequence version 1. DT 24-JAN-2024, entry version 146. DE RecName: Full=Geranylgeranyl transferase type-2 subunit beta; DE EC=2.5.1.60 {ECO:0000269|PubMed:18399557, ECO:0000269|PubMed:18756270, ECO:0000269|PubMed:19894725, ECO:0000269|PubMed:22480322, ECO:0000269|PubMed:22963166, ECO:0000269|PubMed:8505342}; DE AltName: Full=Geranylgeranyl transferase type II subunit beta; DE Short=GGTase-II-beta; DE AltName: Full=Rab geranyl-geranyltransferase subunit beta; DE Short=Rab GG transferase beta; DE Short=Rab GGTase beta; DE AltName: Full=Rab geranylgeranyltransferase subunit beta; DE AltName: Full=Type II protein geranyl-geranyltransferase subunit beta; GN Name=Rabggtb; Synonyms=Ggtb; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, SUBUNIT, RP CATALYTIC ACTIVITY, AND TISSUE SPECIFICITY. RC TISSUE=Brain; RX PubMed=8505342; DOI=10.1016/s0021-9258(19)50329-5; RA Armstrong S.A., Seabra M.C., Suedhof T.C., Goldstein J.L., Brown M.S.; RT "cDNA cloning and expression of the alpha and beta subunits of rat Rab RT geranylgeranyl transferase."; RL J. Biol. Chem. 268:12221-12229(1993). RN [2] RP SUBUNIT, AND ACTIVITY REGULATION. RX PubMed=11675392; DOI=10.1074/jbc.m108241200; RA Thoma N.H., Iakovenko A., Goody R.S., Alexandrov K.; RT "Phosphoisoprenoids modulate association of Rab geranylgeranyltransferase RT with REP-1."; RL J. Biol. Chem. 276:48637-48643(2001). RN [3] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH RABGGTA AND ZINC RP IONS, SUBUNIT, AND COFACTOR. RX PubMed=10745007; DOI=10.1016/s0969-2126(00)00102-7; RA Zhang H., Seabra M.C., Deisenhofer J.; RT "Crystal structure of Rab geranylgeranyltransferase at 2.0 A resolution."; RL Structure 8:241-251(2000). RN [4] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH ZINC IONS; RP GERANYGERANYL PHOSPHATE ANALOG; RAB7A; RABGGTA AND CHM, SUBUNIT, AND RP COFACTOR. RX PubMed=12620235; DOI=10.1016/s1097-2765(03)00044-3; RA Pylypenko O., Rak A., Reents R., Niculae A., Sidorovitch V., Cioaca M.D., RA Bessolitsyna E., Thomae N.H., Waldmann H., Schlichting I., Goody R.S., RA Alexandrov K.; RT "Structure of Rab escort protein-1 in complex with Rab RT geranylgeranyltransferase."; RL Mol. Cell 11:483-494(2003). RN [5] RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) IN COMPLEX WITH RABGGTA; INHIBITOR RP AND ZINC IONS, FUNCTION, SUBUNIT, COFACTOR, AND CATALYTIC ACTIVITY. RX PubMed=18399557; DOI=10.1002/anie.200705795; RA Guo Z., Wu Y.W., Tan K.T., Bon R.S., Guiu-Rozas E., Delon C., Nguyen T.U., RA Wetzel S., Arndt S., Goody R.S., Blankenfeldt W., Alexandrov K., RA Waldmann H.; RT "Development of selective RabGGTase inhibitors and crystal structure of a RT RabGGTase-inhibitor complex."; RL Angew. Chem. Int. Ed. Engl. 47:3747-3750(2008). RN [6] RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEXES WITH RABGGTA; RAB7A; RP GERANYLGERANYL DIPHOSPHATE AND ZINC IONS, COFACTOR, SUBUNIT, FUNCTION, AND RP CATALYTIC ACTIVITY. RX PubMed=18756270; DOI=10.1038/emboj.2008.164; RA Guo Z., Wu Y.W., Das D., Delon C., Cramer J., Yu S., Thuns S., Lupilova N., RA Waldmann H., Brunsveld L., Goody R.S., Alexandrov K., Blankenfeldt W.; RT "Structures of RabGGTase-substrate/product complexes provide insights into RT the evolution of protein prenylation."; RL EMBO J. 27:2444-2456(2008). RN [7] RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH RABGGTA; ZINC IONS RP AND INHIBITOR, SUBUNIT, COFACTOR, FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=19894725; DOI=10.1021/jm901117d; RA Tan K.T., Guiu-Rozas E., Bon R.S., Guo Z., Delon C., Wetzel S., Arndt S., RA Alexandrov K., Waldmann H., Goody R.S., Wu Y.W., Blankenfeldt W.; RT "Design, synthesis, and characterization of peptide-based rab RT geranylgeranyl transferase inhibitors."; RL J. Med. Chem. 52:8025-8037(2009). RN [8] RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) IN COMPLEX WITH RABGGTA; ZINC IONS, RP SUBUNIT, COFACTOR, CATALYTIC ACTIVITY, AND FUNCTION. RX PubMed=22480322; DOI=10.1021/ja211305j; RA Deraeve C., Guo Z., Bon R.S., Blankenfeldt W., DiLucrezia R., Wolf A., RA Menninger S., Stigter E.A., Wetzel S., Choidas A., Alexandrov K., RA Waldmann H., Goody R.S., Wu Y.W.; RT "Psoromic acid is a selective and covalent Rab-prenylation inhibitor RT targeting autoinhibited RabGGTase."; RL J. Am. Chem. Soc. 134:7384-7391(2012). RN [9] RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) IN COMPLEX WITH RABGGTA; ZINC IONS, RP SUBUNIT, COFACTOR, CATALYTIC ACTIVITY, AND FUNCTION. RX PubMed=22963166; DOI=10.1021/jm300624s; RA Stigter E.A., Guo Z., Bon R.S., Wu Y.W., Choidas A., Wolf A., Menninger S., RA Waldmann H., Blankenfeldt W., Goody R.S.; RT "Development of selective, potent RabGGTase inhibitors."; RL J. Med. Chem. 55:8330-8340(2012). CC -!- FUNCTION: Catalyzes the transfer of a geranylgeranyl moiety from CC geranylgeranyl diphosphate to both cysteines of Rab proteins with the CC C-terminal sequence -XXCC, -XCXC and -CCXX, such as RAB1A, RAB3A, RAB5A CC and RAB7A. {ECO:0000269|PubMed:18399557, ECO:0000269|PubMed:18756270, CC ECO:0000269|PubMed:19894725, ECO:0000269|PubMed:22480322, CC ECO:0000269|PubMed:22963166, ECO:0000269|PubMed:8505342}. 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 Evidence={ECO:0000269|PubMed:18399557, ECO:0000269|PubMed:18756270, CC ECO:0000269|PubMed:19894725, ECO:0000269|PubMed:22480322, CC ECO:0000269|PubMed:22963166, ECO:0000269|PubMed:8505342}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000269|PubMed:10745007, ECO:0000269|PubMed:12620235, CC ECO:0000269|PubMed:18399557, ECO:0000269|PubMed:18756270, CC ECO:0000269|PubMed:19894725, ECO:0000269|PubMed:22480322, CC ECO:0000269|PubMed:22963166}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:10745007, CC ECO:0000269|PubMed:12620235, ECO:0000269|PubMed:18399557, CC ECO:0000269|PubMed:18756270, ECO:0000269|PubMed:19894725, CC ECO:0000269|PubMed:22480322, ECO:0000269|PubMed:22963166}; CC -!- ACTIVITY REGULATION: The enzymatic reaction requires the aid of a Rab CC escort protein (also called component A), such as CHM. CC {ECO:0000269|PubMed:11675392}. CC -!- SUBUNIT: Heterotrimer composed of RABGGTA, RABGGTB and CHM; within this CC trimer, RABGGTA and RABGGTB form the catalytic component B, while CHM CC (component A) mediates peptide substrate binding (PubMed:10745007, CC PubMed:12620235, PubMed:18399557, PubMed:18756270, PubMed:19894725, CC PubMed:22480322, PubMed:8505342, PubMed:22963166). The Rab GGTase dimer CC (RGGT) interacts with CHM (component A) prior to Rab protein binding; CC the association is stabilized by geranylgeranyl pyrophosphate (GGpp) CC (PubMed:11675392). The CHM:RGGT:Rab complex is destabilized by GGpp CC (PubMed:11675392). Interaction of RABGGTB with prenylated PTP4A2 CC precludes its association with RABGGTA and inhibits enzyme activity (By CC similarity). Interacts with CHODL (By similarity). Interacts with non- CC phosphorylated form of RAB8A; phosphorylation of RAB8A at 'Thr-72' CC disrupts this interaction (By similarity). CC {ECO:0000250|UniProtKB:P53611, ECO:0000250|UniProtKB:P53612, CC ECO:0000269|PubMed:10745007, ECO:0000269|PubMed:11675392, CC ECO:0000269|PubMed:12620235, ECO:0000269|PubMed:18399557, CC ECO:0000269|PubMed:18756270, ECO:0000269|PubMed:19894725, CC ECO:0000269|PubMed:22480322, ECO:0000269|PubMed:22963166, CC ECO:0000269|PubMed:8505342}. CC -!- TISSUE SPECIFICITY: Most abundant in the heart, brain, spleen and CC liver. Less in the lung, muscle, kidney and testis; in these tissues, CC more abundant than the subunit alpha. {ECO:0000269|PubMed:8505342}. CC -!- SIMILARITY: Belongs to the protein prenyltransferase subunit beta CC family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; L10416; AAA41999.1; -; mRNA. DR EMBL; S62097; AAB27019.1; -; mRNA. DR PIR; B45977; B45977. DR RefSeq; NP_619715.1; NM_138708.2. DR PDB; 1DCE; X-ray; 2.00 A; B/D=1-331. DR PDB; 1LTX; X-ray; 2.70 A; B=1-331. DR PDB; 3C72; X-ray; 2.30 A; B=1-331. DR PDB; 3DSS; X-ray; 1.80 A; B=1-331. DR PDB; 3DST; X-ray; 1.90 A; B=1-331. DR PDB; 3DSU; X-ray; 1.90 A; B=1-331. DR PDB; 3DSV; X-ray; 2.10 A; B=1-331. DR PDB; 3DSW; X-ray; 2.15 A; B=1-331. DR PDB; 3DSX; X-ray; 2.10 A; B=1-331. DR PDB; 3HXB; X-ray; 2.25 A; B=1-331. DR PDB; 3HXC; X-ray; 1.95 A; B=1-331. DR PDB; 3HXD; X-ray; 1.95 A; B=1-331. DR PDB; 3HXE; X-ray; 1.95 A; B=1-331. DR PDB; 3HXF; X-ray; 1.90 A; B=1-331. DR PDB; 4EHM; X-ray; 2.20 A; B=2-331. DR PDB; 4GTS; X-ray; 2.45 A; B=2-331. DR PDB; 4GTT; X-ray; 2.05 A; B=2-331. DR PDB; 4GTV; X-ray; 1.95 A; B=2-331. DR PDBsum; 1DCE; -. DR PDBsum; 1LTX; -. DR PDBsum; 3C72; -. DR PDBsum; 3DSS; -. DR PDBsum; 3DST; -. DR PDBsum; 3DSU; -. DR PDBsum; 3DSV; -. DR PDBsum; 3DSW; -. DR PDBsum; 3DSX; -. DR PDBsum; 3HXB; -. DR PDBsum; 3HXC; -. DR PDBsum; 3HXD; -. DR PDBsum; 3HXE; -. DR PDBsum; 3HXF; -. DR PDBsum; 4EHM; -. DR PDBsum; 4GTS; -. DR PDBsum; 4GTT; -. DR PDBsum; 4GTV; -. DR AlphaFoldDB; Q08603; -. DR SMR; Q08603; -. DR ComplexPortal; CPX-2249; Protein geranylgeranyltransferase type II complex. DR DIP; DIP-6138N; -. DR STRING; 10116.ENSRNOP00000061541; -. DR BindingDB; Q08603; -. DR ChEMBL; CHEMBL4523995; -. DR PhosphoSitePlus; Q08603; -. DR PaxDb; 10116-ENSRNOP00000061541; -. DR Ensembl; ENSRNOT00055048677; ENSRNOP00055040007; ENSRNOG00055028089. DR Ensembl; ENSRNOT00060002411; ENSRNOP00060001571; ENSRNOG00060001576. DR Ensembl; ENSRNOT00065020650; ENSRNOP00065015891; ENSRNOG00065012661. DR GeneID; 25533; -. DR KEGG; rno:25533; -. DR AGR; RGD:3530; -. DR CTD; 5876; -. DR RGD; 3530; Rabggtb. DR eggNOG; KOG0366; Eukaryota. DR InParanoid; Q08603; -. DR OrthoDB; 5478505at2759; -. DR PhylomeDB; Q08603; -. DR Reactome; R-RNO-6803205; TP53 regulates transcription of several additional cell death genes whose specific roles in p53-dependent apoptosis remain uncertain. DR Reactome; R-RNO-8873719; RAB geranylgeranylation. DR EvolutionaryTrace; Q08603; -. DR PRO; PR:Q08603; -. DR Proteomes; UP000002494; Unplaced. DR GO; GO:0005968; C:Rab-protein geranylgeranyltransferase complex; IDA:UniProtKB. DR GO; GO:0019840; F:isoprenoid binding; IDA:CAFA. DR GO; GO:0004663; F:Rab geranylgeranyltransferase activity; IDA:UniProtKB. DR GO; GO:0031267; F:small GTPase binding; IDA:UniProtKB. DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB. DR GO; GO:0018344; P:protein geranylgeranylation; IDA:UniProtKB. DR CDD; cd02894; GGTase-II; 1. DR Gene3D; 1.50.10.20; -; 1. DR InterPro; IPR001330; PFTB_repeat. DR InterPro; IPR045089; PGGT1B-like. DR InterPro; IPR026873; Ptb1. DR InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase. DR PANTHER; PTHR11774; GERANYLGERANYL TRANSFERASE TYPE BETA SUBUNIT; 1. DR PANTHER; PTHR11774:SF11; GERANYLGERANYL TRANSFERASE TYPE-2 SUBUNIT BETA; 1. DR Pfam; PF00432; Prenyltrans; 5. DR SUPFAM; SSF48239; Terpenoid cyclases/Protein prenyltransferases; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Direct protein sequencing; Metal-binding; KW Phosphoprotein; Prenyltransferase; Reference proteome; Repeat; Transferase; KW Zinc. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000250|UniProtKB:P53611" FT CHAIN 2..331 FT /note="Geranylgeranyl transferase type-2 subunit beta" FT /id="PRO_0000119774" FT REPEAT 20..61 FT /note="PFTB 1" FT REPEAT 68..109 FT /note="PFTB 2" FT REPEAT 116..157 FT /note="PFTB 3" FT REPEAT 164..205 FT /note="PFTB 4" FT REPEAT 212..253 FT /note="PFTB 5" FT REPEAT 260..302 FT /note="PFTB 6" FT BINDING 190..192 FT /ligand="geranylgeranyl diphosphate" FT /ligand_id="ChEBI:CHEBI:57533" FT /evidence="ECO:0000269|PubMed:18756270, FT ECO:0007744|PDB:3DST, ECO:0007744|PDB:3DSX" FT BINDING 238 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000269|PubMed:18399557, FT ECO:0000269|PubMed:18756270, ECO:0000269|PubMed:19894725, FT ECO:0000269|PubMed:22480322, ECO:0000269|PubMed:22963166" FT BINDING 240 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000269|PubMed:18399557, FT ECO:0000269|PubMed:18756270, ECO:0000269|PubMed:19894725, FT ECO:0000269|PubMed:22480322, ECO:0000269|PubMed:22963166" FT BINDING 241..244 FT /ligand="geranylgeranyl diphosphate" FT /ligand_id="ChEBI:CHEBI:57533" FT /evidence="ECO:0007744|PDB:3DST, ECO:0007744|PDB:3DSV" FT BINDING 290 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000269|PubMed:18399557, FT ECO:0000269|PubMed:18756270, ECO:0000269|PubMed:19894725, FT ECO:0000269|PubMed:22480322, ECO:0000269|PubMed:22963166" FT MOD_RES 2 FT /note="N-acetylglycine" FT /evidence="ECO:0000250|UniProtKB:P53611" FT MOD_RES 3 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P53611" FT HELIX 20..29 FT /evidence="ECO:0007829|PDB:3DSS" FT STRAND 32..34 FT /evidence="ECO:0007829|PDB:3DSS" FT HELIX 36..38 FT /evidence="ECO:0007829|PDB:3DSS" FT HELIX 40..45 FT /evidence="ECO:0007829|PDB:3DSS" FT HELIX 46..59 FT /evidence="ECO:0007829|PDB:3DSS" FT HELIX 63..65 FT /evidence="ECO:0007829|PDB:3DSS" FT HELIX 68..77 FT /evidence="ECO:0007829|PDB:3DSS" FT STRAND 85..88 FT /evidence="ECO:0007829|PDB:3DSS" FT HELIX 95..107 FT /evidence="ECO:0007829|PDB:3DSS" FT HELIX 111..113 FT /evidence="ECO:0007829|PDB:3DSS" FT HELIX 116..125 FT /evidence="ECO:0007829|PDB:3DSS" FT STRAND 133..136 FT /evidence="ECO:0007829|PDB:3DSS" FT HELIX 143..156 FT /evidence="ECO:0007829|PDB:3DSS" FT HELIX 159..161 FT /evidence="ECO:0007829|PDB:3DSS" FT HELIX 164..172 FT /evidence="ECO:0007829|PDB:3DSS" FT HELIX 191..203 FT /evidence="ECO:0007829|PDB:3DSS" FT HELIX 207..209 FT /evidence="ECO:0007829|PDB:3DSS" FT HELIX 212..220 FT /evidence="ECO:0007829|PDB:3DSS" FT STRAND 231..234 FT /evidence="ECO:0007829|PDB:1LTX" FT HELIX 239..251 FT /evidence="ECO:0007829|PDB:3DSS" FT HELIX 255..257 FT /evidence="ECO:0007829|PDB:3DSS" FT HELIX 260..269 FT /evidence="ECO:0007829|PDB:3DSS" FT TURN 273..275 FT /evidence="ECO:0007829|PDB:3DSS" FT STRAND 278..281 FT /evidence="ECO:0007829|PDB:3HXF" FT HELIX 288..300 FT /evidence="ECO:0007829|PDB:3DSS" FT TURN 311..313 FT /evidence="ECO:0007829|PDB:3DSS" FT STRAND 314..316 FT /evidence="ECO:0007829|PDB:3DSS" FT HELIX 317..323 FT /evidence="ECO:0007829|PDB:3DSS" SQ SEQUENCE 331 AA; 36856 MW; 4B12DEC0245979D6 CRC64; MGTQQKDVTI KSDAPDTLLL EKHADYIASY GSKKDDYEYC MSEYLRMSGV YWGLTVMDLM GQLHRMNKEE ILVFIKSCQH ECGGVSASIG HDPHLLYTLS AVQILTLYDS IHVINVDKVV AYVQSLQKED GSFAGDIWGE IDTRFSFCAV ATLALLGKLD AINVEKAIEF VLSCMNFDGG FGCRPGSESH AGQIYCCTGF LAITSQLHQV NSDLLGWWLC ERQLPSGGLN GRPEKLPDVC YSWWVLASLK IIGRLHWIDR EKLRSFILAC QDEETGGFAD RPGDMVDPFH TLFGIAGLSL LGEEQIKPVS PVFCMPEEVL QRVNVQPELV S //