PGTB2_MOUSE
ID PGTB2_MOUSE Reviewed; 339 AA.
AC P53612; A2RTE6;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Geranylgeranyl transferase type-2 subunit beta;
DE EC=2.5.1.60 {ECO:0000269|PubMed:21520375};
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;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=CD-1; TISSUE=Embryo;
RX PubMed=7544156;
RA Wei L.-N., Lee C.-H., Chinpaisal C., Copeland N.G., Gilbert D.J.,
RA Jenkins N.A., Hsu Y.-C.;
RT "Studies of cloning, chromosomal mapping, and embryonic expression of the
RT mouse Rab geranylgeranyl transferase beta subunit.";
RL Cell Growth Differ. 6:607-614(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND
RP INDUCTION.
RC STRAIN=CD-1; TISSUE=Embryo;
RX PubMed=9031634; DOI=10.1016/s0378-1119(96)00605-1;
RA Chinpaisal C., Lee C.-H., Wei L.-N.;
RT "Studies of the mouse Rab geranylgeranyl transferase beta subunit: gene
RT structure, expression and regulation.";
RL Gene 184:237-243(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP INTERACTION WITH CHODL.
RX PubMed=18161010; DOI=10.2478/s11658-007-0052-8;
RA Claessens A., Weyn C., Merregaert J.;
RT "The cytoplasmic domain of chondrolectin interacts with the beta-subunit of
RT Rab geranylgeranyl transferase.";
RL Cell. Mol. Biol. Lett. 13:250-259(2008).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Liver, Lung, and Pancreas;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 10-339 IN COMPLEX WITH ZINC AND
RP GERANYLGERANYL DIPHOSPHATE, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND
RP SUBUNIT.
RX PubMed=21520375; DOI=10.1002/anie.201101210;
RA Bon R.S., Guo Z., Stigter E.A., Wetzel S., Menninger S., Wolf A.,
RA Choidas A., Alexandrov K., Blankenfeldt W., Goody R.S., Waldmann H.;
RT "Structure-guided development of selective RabGGTase inhibitors.";
RL Angew. Chem. Int. Ed. Engl. 50:4957-4961(2011).
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:21520375}.
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:21520375};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:21520375};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:21520375};
CC -!- ACTIVITY REGULATION: The enzymatic reaction requires the aid of a Rab
CC escort protein (also called component A), such as CHM.
CC {ECO:0000250|UniProtKB:P53611}.
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:21520375). The
CC Rab GGTase dimer (RGGT) interacts with CHM (component A) prior to Rab
CC protein binding; the association is stabilized by geranylgeranyl
CC pyrophosphate (GGpp) (By similarity). The CHM:RGGT:Rab complex is
CC destabilized by GGpp (By similarity). Interaction of RABGGTB with
CC prenylated PTP4A2 precludes its association with RABGGTA and inhibits
CC enzyme activity (By similarity). Interacts with CHODL
CC (PubMed:18161010). Interacts with non-phosphorylated form of RAB8A;
CC phosphorylation of RAB8A at 'Thr-72' disrupts this interaction (By
CC similarity). {ECO:0000250|UniProtKB:P53611,
CC ECO:0000250|UniProtKB:Q08603, ECO:0000269|PubMed:18161010,
CC ECO:0000269|PubMed:21520375}.
CC -!- INTERACTION:
CC P53612; Q9CXM0: Chodl; NbExp=2; IntAct=EBI-9104297, EBI-13948582;
CC -!- TISSUE SPECIFICITY: Ubiquitous. Detected in all the major organs in
CC adult animals. {ECO:0000269|PubMed:9031634}.
CC -!- DEVELOPMENTAL STAGE: Specific expression was elevated in mid-gestation
CC stages, particularly developing liver and spinal cord.
CC {ECO:0000269|PubMed:9031634}.
CC -!- INDUCTION: Increased dramatically by cycloheximide (CHX) treatment
CC within a short time (as early as 2 hours). Actinomycin D was used to
CC determine the half-life, CHX treatment resulted in a dramatic increase
CC of the half-life from 8 hours to greater than 12 hours.
CC {ECO:0000269|PubMed:9031634}.
CC -!- SIMILARITY: Belongs to the protein prenyltransferase subunit beta
CC family. {ECO:0000305}.
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DR EMBL; U12922; AAB01502.1; -; mRNA.
DR EMBL; CH466532; EDL11902.1; -; Genomic_DNA.
DR EMBL; BC132473; AAI32474.1; -; mRNA.
DR EMBL; BC138547; AAI38548.1; -; mRNA.
DR CCDS; CCDS17923.1; -.
DR PIR; I49116; I49116.
DR PIR; JC6177; JC6177.
DR RefSeq; NP_035361.2; NM_011231.2.
DR PDB; 3PZ1; X-ray; 1.95 A; B=10-339.
DR PDB; 3PZ2; X-ray; 2.35 A; B=10-339.
DR PDB; 3PZ3; X-ray; 2.00 A; B=10-339.
DR PDBsum; 3PZ1; -.
DR PDBsum; 3PZ2; -.
DR PDBsum; 3PZ3; -.
DR AlphaFoldDB; P53612; -.
DR SMR; P53612; -.
DR BioGRID; 202555; 9.
DR ComplexPortal; CPX-2920; Protein geranylgeranyltransferase type II complex.
DR IntAct; P53612; 1.
DR STRING; 10090.ENSMUSP00000129481; -.
DR iPTMnet; P53612; -.
DR PhosphoSitePlus; P53612; -.
DR EPD; P53612; -.
DR MaxQB; P53612; -.
DR PaxDb; P53612; -.
DR PeptideAtlas; P53612; -.
DR PRIDE; P53612; -.
DR ProteomicsDB; 288135; -.
DR Antibodypedia; 19716; 72 antibodies from 23 providers.
DR DNASU; 19352; -.
DR Ensembl; ENSMUST00000167111; ENSMUSP00000129481; ENSMUSG00000038975.
DR GeneID; 19352; -.
DR KEGG; mmu:19352; -.
DR UCSC; uc008rug.2; mouse.
DR CTD; 5876; -.
DR MGI; MGI:99537; Rabggtb.
DR VEuPathDB; HostDB:ENSMUSG00000038975; -.
DR eggNOG; KOG0366; Eukaryota.
DR GeneTree; ENSGT00950000183128; -.
DR InParanoid; P53612; -.
DR OrthoDB; 1042804at2759; -.
DR PhylomeDB; P53612; -.
DR TreeFam; TF105762; -.
DR Reactome; R-MMU-6803205; TP53 regulates transcription of several additional cell death genes whose specific roles in p53-dependent apoptosis remain uncertain.
DR Reactome; R-MMU-8873719; RAB geranylgeranylation.
DR BioGRID-ORCS; 19352; 25 hits in 70 CRISPR screens.
DR ChiTaRS; Rabggtb; mouse.
DR EvolutionaryTrace; P53612; -.
DR PRO; PR:P53612; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; P53612; protein.
DR Bgee; ENSMUSG00000038975; Expressed in ectoplacental cone and 259 other tissues.
DR ExpressionAtlas; P53612; baseline and differential.
DR Genevisible; P53612; MM.
DR GO; GO:0005968; C:Rab-protein geranylgeranyltransferase complex; ISS:UniProtKB.
DR GO; GO:0019840; F:isoprenoid binding; ISO:MGI.
DR GO; GO:0004663; F:Rab geranylgeranyltransferase activity; ISS:UniProtKB.
DR GO; GO:0031267; F:small GTPase binding; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR GO; GO:0018344; P:protein geranylgeranylation; ISS:UniProtKB.
DR GO; GO:0018342; P:protein prenylation; IBA:GO_Central.
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 3D-structure; Metal-binding; Phosphoprotein; Prenyltransferase;
KW Reference proteome; Repeat; Transferase; Zinc.
FT CHAIN 1..339
FT /note="Geranylgeranyl transferase type-2 subunit beta"
FT /id="PRO_0000119773"
FT REPEAT 28..69
FT /note="PFTB 1"
FT REPEAT 76..117
FT /note="PFTB 2"
FT REPEAT 124..165
FT /note="PFTB 3"
FT REPEAT 172..213
FT /note="PFTB 4"
FT REPEAT 220..261
FT /note="PFTB 5"
FT REPEAT 268..310
FT /note="PFTB 6"
FT BINDING 198..200
FT /ligand="geranylgeranyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57533"
FT /evidence="ECO:0000250|UniProtKB:Q08603"
FT BINDING 240..243
FT /ligand="geranylgeranyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57533"
FT /evidence="ECO:0000269|PubMed:21520375"
FT BINDING 246
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:21520375"
FT BINDING 248
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:21520375"
FT BINDING 249..252
FT /ligand="geranylgeranyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57533"
FT /evidence="ECO:0000250|UniProtKB:Q08603"
FT BINDING 249
FT /ligand="geranylgeranyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57533"
FT /evidence="ECO:0000269|PubMed:21520375"
FT BINDING 298
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:21520375"
FT MOD_RES 11
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P53611"
FT CONFLICT 230
FT /note="R -> A (in Ref. 1; AAB01502)"
FT /evidence="ECO:0000305"
FT CONFLICT 236
FT /note="G -> A (in Ref. 1; AAB01502)"
FT /evidence="ECO:0000305"
FT CONFLICT 241
FT /note="P -> R (in Ref. 1; AAB01502)"
FT /evidence="ECO:0000305"
FT CONFLICT 267..268
FT /note="DR -> VS (in Ref. 1; AAB01502)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 339 AA; 37803 MW; 4765A39E5392B8B5 CRC64;
MGSLLFSWKG TQQKDVTIKS DAPDTLLLEK HADYIASYGS KKDDYEYCMS EYLRMSGVYW
GLTVMDLMGQ LHRMNREEIL VFIKSCQHEC GGISASIGHD PHLLYTLSAV QILTLYDSVH
VINVDKVVAY VQSLQKEDGS FAGDIWGEID TRFSFCAVAT LALLGKLDAI NVEKAIEFVL
SCMNFDGGFG CRPGSESHAG QIYCCTGFLA ITSQLHQVNS DLLGWWLCER QLPSGGLNGR
PEKLPDVCYS WWVLASLKII GRLHWIDREK LRSFILACQD EETGGFADRP GDMVDPFHTL
FGIAGLSLLG EEQIKPVSPV FCMPEEVLQR VNVQPELVS
