PGTB1_MOUSE
ID PGTB1_MOUSE Reviewed; 377 AA.
AC Q8BUY9;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 123.
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 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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Head;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung, and Testis;
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).
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; AK081731; BAC38314.1; -; mRNA.
DR CCDS; CCDS29230.1; -.
DR RefSeq; NP_766215.1; NM_172627.3.
DR AlphaFoldDB; Q8BUY9; -.
DR SMR; Q8BUY9; -.
DR BioGRID; 230397; 1.
DR ComplexPortal; CPX-2949; Protein geranylgeranyl transferase type I complex.
DR STRING; 10090.ENSMUSP00000025354; -.
DR BindingDB; Q8BUY9; -.
DR ChEMBL; CHEMBL3301421; -.
DR iPTMnet; Q8BUY9; -.
DR PhosphoSitePlus; Q8BUY9; -.
DR EPD; Q8BUY9; -.
DR MaxQB; Q8BUY9; -.
DR PaxDb; Q8BUY9; -.
DR PRIDE; Q8BUY9; -.
DR ProteomicsDB; 288134; -.
DR Antibodypedia; 25414; 84 antibodies from 14 providers.
DR Ensembl; ENSMUST00000236216; ENSMUSP00000158214; ENSMUSG00000024477.
DR GeneID; 225467; -.
DR KEGG; mmu:225467; -.
DR UCSC; uc008evk.1; mouse.
DR CTD; 5229; -.
DR MGI; MGI:1917514; Pggt1b.
DR VEuPathDB; HostDB:ENSMUSG00000024477; -.
DR eggNOG; KOG0367; Eukaryota.
DR GeneTree; ENSGT00950000183128; -.
DR HOGENOM; CLU_028946_2_2_1; -.
DR InParanoid; Q8BUY9; -.
DR OMA; RWCLMRQ; -.
DR OrthoDB; 1042804at2759; -.
DR PhylomeDB; Q8BUY9; -.
DR TreeFam; TF105968; -.
DR BRENDA; 2.5.1.59; 3474.
DR BioGRID-ORCS; 225467; 31 hits in 75 CRISPR screens.
DR ChiTaRS; Pggt1b; mouse.
DR PRO; PR:Q8BUY9; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; Q8BUY9; protein.
DR Bgee; ENSMUSG00000024477; Expressed in manus and 220 other tissues.
DR ExpressionAtlas; Q8BUY9; baseline and differential.
DR Genevisible; Q8BUY9; MM.
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:1901363; F:heterocyclic compound binding; ISO:MGI.
DR GO; GO:0042277; F:peptide binding; ISO:MGI.
DR GO; GO:0004661; F:protein geranylgeranyltransferase activity; ISS:UniProtKB.
DR GO; GO:0036094; F:small molecule binding; ISO:MGI.
DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR GO; GO:0051771; P:negative regulation of nitric-oxide synthase biosynthetic process; ISO:MGI.
DR GO; GO:0045787; P:positive regulation of cell cycle; ISO:MGI.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:MGI.
DR GO; GO:0018344; P:protein geranylgeranylation; ISS:UniProtKB.
DR GO; GO:0018342; P:protein prenylation; IBA:GO_Central.
DR GO; GO:0034097; P:response to cytokine; ISO:MGI.
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 1: Evidence at protein 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_0000119770"
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; 42354 MW; 7046611ECFCFDAAB CRC64;
MATTEDDRLA GSGEGERLDF LRDRHVRFFQ RCLQVLPERY SSLETSRLTI AFFALSGLDM
LDSLDVVNKD DIIEWIYSLQ VLPTEDRSNL SRCGFRGSSY LGIPFNPSKN PGAAHPYDSG
HIAMTYTGLS CLIILGDDLG RVDKEACLAG LRALQLEDGS FCAVPEGSEN DMRFVYCASC
ICYMLNNWSG MDMKKAISYI RRSMSYDNGL AQGAGLESHG GSTFCGIASL CLMGKLEEVF
SEKELNRIKR WCIMRQQNGY HGRPNKPVDT CYSFWVGATL KLLKIFQYTN FEKNRNYILS
TQDRLVGGFA KWPDSHPDAL HAYFGICGLS LMEESGICKV HPALNVSTRT SERLRDLHQS
WKTKDSKQCS DNVHIAT
