PGTB2_BOVIN
ID PGTB2_BOVIN Reviewed; 331 AA.
AC Q5E9B3; A6QLG2;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Geranylgeranyl transferase type-2 subunit beta;
DE EC=2.5.1.60 {ECO:0000250|UniProtKB:P53611};
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal medulla;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
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:0000250|UniProtKB:P53611}.
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:0000250|UniProtKB:P53611};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q08603};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:Q08603};
CC -!- ACTIVITY REGULATION: The enzymatic reaction requires the aid of a Rab
CC escort protein (also called component A).
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. 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 The CHM:RGGT:Rab complex is destabilized by GGpp. Interaction of
CC RABGGTB with prenylated PTP4A2 precludes its association with RABGGTA
CC and inhibits enzyme activity (By similarity). Interacts with CHODL (By
CC similarity). 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:P53612}.
CC -!- SIMILARITY: Belongs to the protein prenyltransferase subunit beta
CC family. {ECO:0000305}.
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DR EMBL; BT021007; AAX09024.1; -; mRNA.
DR EMBL; BC147953; AAI47954.1; -; mRNA.
DR RefSeq; NP_001015646.1; NM_001015646.1.
DR AlphaFoldDB; Q5E9B3; -.
DR SMR; Q5E9B3; -.
DR STRING; 9913.ENSBTAP00000024551; -.
DR PaxDb; Q5E9B3; -.
DR Ensembl; ENSBTAT00000024551; ENSBTAP00000024551; ENSBTAG00000018447.
DR GeneID; 533276; -.
DR KEGG; bta:533276; -.
DR CTD; 5876; -.
DR VEuPathDB; HostDB:ENSBTAG00000018447; -.
DR VGNC; VGNC:33671; RABGGTB.
DR eggNOG; KOG0366; Eukaryota.
DR GeneTree; ENSGT00950000183128; -.
DR InParanoid; Q5E9B3; -.
DR OMA; VKRCQCP; -.
DR OrthoDB; 1042804at2759; -.
DR Proteomes; UP000009136; Chromosome 3.
DR Bgee; ENSBTAG00000018447; Expressed in rectus femoris and 104 other tissues.
DR GO; GO:0005968; C:Rab-protein geranylgeranyltransferase complex; ISS:UniProtKB.
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 2: Evidence at transcript level;
KW Acetylation; Metal-binding; Phosphoprotein; Prenyltransferase;
KW Reference proteome; Repeat; Transferase; 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_0000244433"
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:0000250|UniProtKB:Q08603"
FT BINDING 238
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q08603"
FT BINDING 240
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q08603"
FT BINDING 241..244
FT /ligand="geranylgeranyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57533"
FT /evidence="ECO:0000250|UniProtKB:Q08603"
FT BINDING 290
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q08603"
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"
SQ SEQUENCE 331 AA; 36972 MW; CB554CA9B22D334A CRC64;
MGTPQKDVII KSDAPDTLLL EKHADYIASY GSKKDDYEYC MSEYLRMSGI YWGLTVMDLM
GQLHRMNREE ILTFIKSCQH ECGGISASIG HDPHLLYTLS AVQILTLYDS INVIDINKVV
EYVQSLQKED GSFAGDIWGE IDTRFSFCAV ATLALLGKLD AINVEKAIEF VLSCMNFDGG
FGCRPGSESH AGQIYCCTGF LAITSQLHQV NSDLLGWWLC ERQLPSGGLN GRPEKLPDVC
YSWWVLASLK IIGRLHWIDR EKLRSFILAC QDEETGGFAD RPGDMVDPFH TLFGIAGLSL
LGEEQIKPVS PVFCMPEEVL RRVNVQPELV S
