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Geranylgeranyl transferase type-2 subunit beta (EC 2.5.1.60) (Geranylgeranyl transferase type II subunit beta) (GGTase-II-beta) (Rab geranyl-geranyltransferase subunit beta) (Rab GG transferase beta) (Rab GGTase beta) (Rab geranylgeranyltransferase subunit beta) (Type II protein geranyl-geranyltransferase subunit beta)

 PGTB2_RAT               Reviewed;         331 AA.
Q08603;
01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
01-FEB-1995, sequence version 1.
22-NOV-2017, entry version 123.
RecName: Full=Geranylgeranyl transferase type-2 subunit beta;
EC=2.5.1.60;
AltName: Full=Geranylgeranyl transferase type II subunit beta;
Short=GGTase-II-beta;
AltName: Full=Rab geranyl-geranyltransferase subunit beta;
Short=Rab GG transferase beta;
Short=Rab GGTase beta;
AltName: Full=Rab geranylgeranyltransferase subunit beta;
AltName: Full=Type II protein geranyl-geranyltransferase subunit beta;
Name=Rabggtb; Synonyms=Ggtb;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, FUNCTION,
SUBUNIT, AND CATALYTIC ACTIVITY.
TISSUE=Brain;
PubMed=8505342;
Armstrong S.A., Seabra M.C., Suedhof T.C., Goldstein J.L., Brown M.S.;
"cDNA cloning and expression of the alpha and beta subunits of rat Rab
geranylgeranyl transferase.";
J. Biol. Chem. 268:12221-12229(1993).
[2]
SUBUNIT.
PubMed=11675392; DOI=10.1074/jbc.M108241200;
Thoma N.H., Iakovenko A., Goody R.S., Alexandrov K.;
"Phosphoisoprenoids modulate association of Rab
geranylgeranyltransferase with REP-1.";
J. Biol. Chem. 276:48637-48643(2001).
[3]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH RABGGTA AND ZINC
IONS, SUBUNIT, AND COFACTOR.
PubMed=10745007; DOI=10.1016/S0969-2126(00)00102-7;
Zhang H., Seabra M.C., Deisenhofer J.;
"Crystal structure of Rab geranylgeranyltransferase at 2.0 A
resolution.";
Structure 8:241-251(2000).
[4]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH ZINC IONS;
GERANYGERANYL PHOSPHATE ANALOG; RAB7A; RABGGTA AND CHM, SUBUNIT, AND
COFACTOR.
PubMed=12620235; DOI=10.1016/S1097-2765(03)00044-3;
Pylypenko O., Rak A., Reents R., Niculae A., Sidorovitch V.,
Cioaca M.D., Bessolitsyna E., Thomae N.H., Waldmann H.,
Schlichting I., Goody R.S., Alexandrov K.;
"Structure of Rab escort protein-1 in complex with Rab
geranylgeranyltransferase.";
Mol. Cell 11:483-494(2003).
[5]
X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) IN COMPLEX WITH RABGGTA;
INHIBITOR AND ZINC IONS, FUNCTION, SUBUNIT, COFACTOR, AND CATALYTIC
ACTIVITY.
PubMed=18399557; DOI=10.1002/anie.200705795;
Guo Z., Wu Y.W., Tan K.T., Bon R.S., Guiu-Rozas E., Delon C.,
Nguyen T.U., Wetzel S., Arndt S., Goody R.S., Blankenfeldt W.,
Alexandrov K., Waldmann H.;
"Development of selective RabGGTase inhibitors and crystal structure
of a RabGGTase-inhibitor complex.";
Angew. Chem. Int. Ed. Engl. 47:3747-3750(2008).
[6]
X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEXES WITH RABGGTA;
RAB7A; GERANYLGERANYL DIPHOSPHATE AND ZINC IONS, COFACTOR, SUBUNIT,
FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=18756270; DOI=10.1038/emboj.2008.164;
Guo Z., Wu Y.W., Das D., Delon C., Cramer J., Yu S., Thuns S.,
Lupilova N., Waldmann H., Brunsveld L., Goody R.S., Alexandrov K.,
Blankenfeldt W.;
"Structures of RabGGTase-substrate/product complexes provide insights
into the evolution of protein prenylation.";
EMBO J. 27:2444-2456(2008).
[7]
X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH RABGGTA; ZINC
IONS AND INHIBITOR, SUBUNIT, COFACTOR, FUNCTION, AND CATALYTIC
ACTIVITY.
PubMed=19894725; DOI=10.1021/jm901117d;
Tan K.T., Guiu-Rozas E., Bon R.S., Guo Z., Delon C., Wetzel S.,
Arndt S., Alexandrov K., Waldmann H., Goody R.S., Wu Y.W.,
Blankenfeldt W.;
"Design, synthesis, and characterization of peptide-based rab
geranylgeranyl transferase inhibitors.";
J. Med. Chem. 52:8025-8037(2009).
[8]
X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) IN COMPLEX WITH RABGGTA; ZINC
IONS, SUBUNIT, COFACTOR, CATALYTIC ACTIVITY, AND FUNCTION.
PubMed=22480322; DOI=10.1021/ja211305j;
Deraeve C., Guo Z., Bon R.S., Blankenfeldt W., DiLucrezia R., Wolf A.,
Menninger S., Stigter E.A., Wetzel S., Choidas A., Alexandrov K.,
Waldmann H., Goody R.S., Wu Y.W.;
"Psoromic acid is a selective and covalent Rab-prenylation inhibitor
targeting autoinhibited RabGGTase.";
J. Am. Chem. Soc. 134:7384-7391(2012).
[9]
X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) IN COMPLEX WITH RABGGTA; ZINC
IONS, SUBUNIT, COFACTOR, CATALYTIC ACTIVITY, AND FUNCTION.
PubMed=22963166; DOI=10.1021/jm300624s;
Stigter E.A., Guo Z., Bon R.S., Wu Y.W., Choidas A., Wolf A.,
Menninger S., Waldmann H., Blankenfeldt W., Goody R.S.;
"Development of selective, potent RabGGTase inhibitors.";
J. Med. Chem. 55:8330-8340(2012).
-!- FUNCTION: Catalyzes the transfer of a geranylgeranyl moiety from
geranylgeranyl diphosphate to both cysteines of Rab proteins with
the C-terminal sequence -XXCC, -XCXC and -CCXX, such as RAB1A,
RAB3A, RAB5A and RAB7A. {ECO:0000269|PubMed:18399557,
ECO:0000269|PubMed:18756270, ECO:0000269|PubMed:19894725,
ECO:0000269|PubMed:22480322, ECO:0000269|PubMed:22963166,
ECO:0000269|PubMed:8505342}.
-!- CATALYTIC ACTIVITY: Geranylgeranyl diphosphate + protein-cysteine
= S-geranylgeranyl-protein + diphosphate.
{ECO:0000269|PubMed:18399557, ECO:0000269|PubMed:18756270,
ECO:0000269|PubMed:19894725, ECO:0000269|PubMed:22480322,
ECO:0000269|PubMed:22963166, ECO:0000269|PubMed:8505342}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000269|PubMed:10745007,
ECO:0000269|PubMed:12620235, ECO:0000269|PubMed:18399557,
ECO:0000269|PubMed:18756270, ECO:0000269|PubMed:19894725,
ECO:0000269|PubMed:22480322, ECO:0000269|PubMed:22963166};
Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:10745007,
ECO:0000269|PubMed:12620235, ECO:0000269|PubMed:18399557,
ECO:0000269|PubMed:18756270, ECO:0000269|PubMed:19894725,
ECO:0000269|PubMed:22480322, ECO:0000269|PubMed:22963166};
-!- ENZYME REGULATION: The enzymatic reaction requires the aid of a
Rab escort protein (also called component A), such as CHM.
-!- SUBUNIT: Heterotrimer composed of RABGGTA, RABGGTB and CHM; within
this trimer, RABGGTA and RABGGTB form the catalytic component B,
while CHM (component A) mediates peptide substrate binding. The
Rab GGTase dimer (RGGT) interacts with CHM (component A) prior to
Rab protein binding; the association is stabilized by
geranylgeranyl pyrophosphate (GGpp). The CHM:RGGT:Rab complex is
destabilized by GGpp. Interaction of RABGGTB with prenylated
PTP4A2 precludes its association with RABGGTA and inhibits enzyme
activity. Interacts with CHODL. {ECO:0000250|UniProtKB:P53612,
ECO:0000269|PubMed:10745007, ECO:0000269|PubMed:11675392,
ECO:0000269|PubMed:12620235, ECO:0000269|PubMed:18399557,
ECO:0000269|PubMed:18756270, ECO:0000269|PubMed:19894725,
ECO:0000269|PubMed:22480322, ECO:0000269|PubMed:22963166,
ECO:0000269|PubMed:8505342}.
-!- TISSUE SPECIFICITY: Most abundant in the heart, brain, spleen and
liver. Less in the lung, muscle, kidney and testis; in these
tissues, more abundant than the subunit alpha.
-!- SIMILARITY: Belongs to the protein prenyltransferase subunit beta
family. {ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; L10416; AAA41999.1; -; mRNA.
EMBL; S62097; AAB27019.1; -; mRNA.
PIR; B45977; B45977.
RefSeq; NP_619715.1; NM_138708.2.
UniGene; Rn.107818; -.
PDB; 1DCE; X-ray; 2.00 A; B/D=1-331.
PDB; 1LTX; X-ray; 2.70 A; B=1-331.
PDB; 3C72; X-ray; 2.30 A; B=1-331.
PDB; 3DSS; X-ray; 1.80 A; B=1-331.
PDB; 3DST; X-ray; 1.90 A; B=1-331.
PDB; 3DSU; X-ray; 1.90 A; B=1-331.
PDB; 3DSV; X-ray; 2.10 A; B=1-331.
PDB; 3DSW; X-ray; 2.15 A; B=1-331.
PDB; 3DSX; X-ray; 2.10 A; B=1-331.
PDB; 3HXB; X-ray; 2.25 A; B=1-331.
PDB; 3HXC; X-ray; 1.95 A; B=1-331.
PDB; 3HXD; X-ray; 1.95 A; B=1-331.
PDB; 3HXE; X-ray; 1.95 A; B=1-331.
PDB; 3HXF; X-ray; 1.90 A; B=1-331.
PDB; 4EHM; X-ray; 2.20 A; B=2-331.
PDB; 4GTS; X-ray; 2.45 A; B=2-331.
PDB; 4GTT; X-ray; 2.05 A; B=2-331.
PDB; 4GTV; X-ray; 1.95 A; B=2-331.
PDBsum; 1DCE; -.
PDBsum; 1LTX; -.
PDBsum; 3C72; -.
PDBsum; 3DSS; -.
PDBsum; 3DST; -.
PDBsum; 3DSU; -.
PDBsum; 3DSV; -.
PDBsum; 3DSW; -.
PDBsum; 3DSX; -.
PDBsum; 3HXB; -.
PDBsum; 3HXC; -.
PDBsum; 3HXD; -.
PDBsum; 3HXE; -.
PDBsum; 3HXF; -.
PDBsum; 4EHM; -.
PDBsum; 4GTS; -.
PDBsum; 4GTT; -.
PDBsum; 4GTV; -.
ProteinModelPortal; Q08603; -.
SMR; Q08603; -.
DIP; DIP-6138N; -.
STRING; 10116.ENSRNOP00000061541; -.
PaxDb; Q08603; -.
PRIDE; Q08603; -.
GeneID; 25533; -.
KEGG; rno:25533; -.
CTD; 5876; -.
RGD; 3530; Rabggtb.
eggNOG; KOG0366; Eukaryota.
eggNOG; COG5029; LUCA.
HOVERGEN; HBG008182; -.
InParanoid; Q08603; -.
KO; K05956; -.
PhylomeDB; Q08603; -.
EvolutionaryTrace; Q08603; -.
PRO; PR:Q08603; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0005968; C:Rab-protein geranylgeranyltransferase complex; IDA:UniProtKB.
GO; GO:0019840; F:isoprenoid binding; IDA:CAFA.
GO; GO:0046982; F:protein heterodimerization activity; IDA:CAFA.
GO; GO:0004663; F:Rab geranylgeranyltransferase activity; IDA:UniProtKB.
GO; GO:0017137; F:Rab GTPase binding; IDA:UniProtKB.
GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
GO; GO:0006461; P:protein complex assembly; IMP:CAFA.
GO; GO:0018344; P:protein geranylgeranylation; IDA:UniProtKB.
CDD; cd02894; GGTase-II; 1.
InterPro; IPR001330; PFTB_repeat.
InterPro; IPR026873; Ptb1.
InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase.
Pfam; PF00432; Prenyltrans; 5.
SUPFAM; SSF48239; SSF48239; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Complete proteome;
Direct protein sequencing; Metal-binding; Phosphoprotein;
Prenyltransferase; Reference proteome; Repeat; Transferase; Zinc.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P53611}.
CHAIN 2 331 Geranylgeranyl transferase type-2 subunit
beta.
/FTId=PRO_0000119774.
REPEAT 20 61 PFTB 1.
REPEAT 68 109 PFTB 2.
REPEAT 116 157 PFTB 3.
REPEAT 164 205 PFTB 4.
REPEAT 212 253 PFTB 5.
REPEAT 260 302 PFTB 6.
REGION 190 192 Geranylgeranyl diphosphate binding.
REGION 232 244 Geranylgeranyl diphosphate binding.
METAL 238 238 Zinc; catalytic.
METAL 240 240 Zinc; catalytic.
METAL 290 290 Zinc; via tele nitrogen; catalytic.
MOD_RES 2 2 N-acetylglycine.
{ECO:0000250|UniProtKB:P53611}.
MOD_RES 3 3 Phosphothreonine.
{ECO:0000250|UniProtKB:P53611}.
HELIX 20 29 {ECO:0000244|PDB:3DSS}.
STRAND 32 34 {ECO:0000244|PDB:3DSS}.
HELIX 36 38 {ECO:0000244|PDB:3DSS}.
HELIX 40 45 {ECO:0000244|PDB:3DSS}.
HELIX 46 59 {ECO:0000244|PDB:3DSS}.
HELIX 63 65 {ECO:0000244|PDB:3DSS}.
HELIX 68 77 {ECO:0000244|PDB:3DSS}.
STRAND 85 88 {ECO:0000244|PDB:3DSS}.
HELIX 95 107 {ECO:0000244|PDB:3DSS}.
HELIX 111 113 {ECO:0000244|PDB:3DSS}.
HELIX 116 125 {ECO:0000244|PDB:3DSS}.
STRAND 133 136 {ECO:0000244|PDB:3DSS}.
HELIX 143 156 {ECO:0000244|PDB:3DSS}.
HELIX 159 161 {ECO:0000244|PDB:3DSS}.
HELIX 164 172 {ECO:0000244|PDB:3DSS}.
HELIX 191 203 {ECO:0000244|PDB:3DSS}.
HELIX 207 209 {ECO:0000244|PDB:3DSS}.
HELIX 212 220 {ECO:0000244|PDB:3DSS}.
STRAND 231 234 {ECO:0000244|PDB:1LTX}.
HELIX 239 251 {ECO:0000244|PDB:3DSS}.
HELIX 255 257 {ECO:0000244|PDB:3DSS}.
HELIX 260 269 {ECO:0000244|PDB:3DSS}.
TURN 273 275 {ECO:0000244|PDB:3DSS}.
STRAND 277 281 {ECO:0000244|PDB:3DSV}.
HELIX 288 300 {ECO:0000244|PDB:3DSS}.
TURN 311 313 {ECO:0000244|PDB:3DSS}.
STRAND 314 316 {ECO:0000244|PDB:3DSS}.
HELIX 317 323 {ECO:0000244|PDB:3DSS}.
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


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