PGTB1_BOVIN
ID PGTB1_BOVIN Reviewed; 377 AA.
AC Q5EAD5;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Geranylgeranyl transferase type-1 subunit beta;
DE EC=2.5.1.59;
DE AltName: Full=Geranylgeranyl transferase type I subunit beta;
DE Short=GGTase-I-beta;
DE AltName: Full=Type I protein geranyl-geranyltransferase subunit beta;
GN Name=PGGT1B;
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).
CC -!- FUNCTION: Catalyzes the transfer of a geranyl-geranyl moiety from
CC geranyl-geranyl pyrophosphate to a cysteine at the fourth position from
CC the C-terminus of proteins having the C-terminal sequence Cys-
CC aliphatic-aliphatic-X. Known substrates include RAC1, RAC2, RAP1A and
CC RAP1B (By similarity). {ECO:0000250}.
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=2.5.1.59;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P53610};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P53610};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P18898};
CC -!- SUBUNIT: Heterodimer of FNTA and PGGT1B. PGGT1B mediates interaction
CC with substrate peptides (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein prenyltransferase subunit beta
CC family. {ECO:0000305}.
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DR EMBL; BT020634; AAX08651.1; -; mRNA.
DR RefSeq; NP_001015560.1; NM_001015560.1.
DR AlphaFoldDB; Q5EAD5; -.
DR SMR; Q5EAD5; -.
DR ComplexPortal; CPX-2169; Protein geranylgeranyl transferase type I complex.
DR STRING; 9913.ENSBTAP00000002466; -.
DR BindingDB; Q5EAD5; -.
DR ChEMBL; CHEMBL2096987; -.
DR PRIDE; Q5EAD5; -.
DR Ensembl; ENSBTAT00000002466; ENSBTAP00000002466; ENSBTAG00000001895.
DR GeneID; 509322; -.
DR KEGG; bta:509322; -.
DR CTD; 5229; -.
DR VEuPathDB; HostDB:ENSBTAG00000001895; -.
DR VGNC; VGNC:32788; PGGT1B.
DR eggNOG; KOG0367; Eukaryota.
DR GeneTree; ENSGT00950000183128; -.
DR InParanoid; Q5EAD5; -.
DR OMA; RWCLMRQ; -.
DR OrthoDB; 1042804at2759; -.
DR PRO; PR:Q5EAD5; -.
DR Proteomes; UP000009136; Chromosome 10.
DR Bgee; ENSBTAG00000001895; Expressed in oocyte and 108 other tissues.
DR GO; GO:0005953; C:CAAX-protein geranylgeranyltransferase complex; ISS:UniProtKB.
DR GO; GO:0004662; F:CAAX-protein geranylgeranyltransferase activity; ISS:UniProtKB.
DR GO; GO:0004661; F:protein geranylgeranyltransferase activity; 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; cd02895; GGTase-I; 1.
DR InterPro; IPR041960; GGTase_I_beta.
DR InterPro; IPR001330; PFTB_repeat.
DR InterPro; IPR045089; PGGT1B-like.
DR InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase.
DR PANTHER; PTHR11774; PTHR11774; 1.
DR Pfam; PF00432; Prenyltrans; 4.
DR SUPFAM; SSF48239; SSF48239; 1.
PE 2: Evidence at transcript level;
KW Magnesium; Metal-binding; Prenyltransferase; Reference proteome; Repeat;
KW Transferase; Zinc.
FT CHAIN 1..377
FT /note="Geranylgeranyl transferase type-1 subunit beta"
FT /id="PRO_0000244432"
FT REPEAT 144..186
FT /note="PFTB 1"
FT REPEAT 193..234
FT /note="PFTB 2"
FT REPEAT 245..284
FT /note="PFTB 3"
FT REPEAT 291..333
FT /note="PFTB 4"
FT BINDING 219..221
FT /ligand="geranylgeranyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57533"
FT /evidence="ECO:0000250|UniProtKB:P53610"
FT BINDING 263..266
FT /ligand="geranylgeranyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57533"
FT /evidence="ECO:0000250|UniProtKB:P53610"
FT BINDING 269
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P53610"
FT BINDING 271
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P53610"
FT BINDING 272..275
FT /ligand="geranylgeranyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57533"
FT /evidence="ECO:0000250|UniProtKB:P53610"
FT BINDING 321
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P53610"
SQ SEQUENCE 377 AA; 42481 MW; 1CF78FBD41131B70 CRC64;
MAATEDERPT GSGEGERLDF LRDRHVRFFQ RCLQVLPERY SSLETSRLTI AFFALSGLDM
LDSLDVVNKD DIIEWIYSLQ VLPTEDRSNL NRCGFRGSSY LGIPFNPSKN PGTAHPYDSG
HIAMTYTGLS CLVILGDDLS RVNKEACLAG LRALQLEDGS FCAVPEGSEN DMRFVYCASC
ICYMLNNWSG MDMKKAINYI RRSMSYDNGL AQGAGLESHG GSTFCGIASL CLMGKLEEVF
SEKELNRIKR WCIMRQQNGY HGRPNKPVDT CYSFWVGATL KLLKIFQYTN FEKNRNYILS
TQDRLVGGFA KWPDSHPDAL HAYFGICGLS LMEESGICKV HPALNVSTRT SERLRDLHQS
WKTKDSKQCS ENVHIST
