GBB1_MOUSE
ID GBB1_MOUSE Reviewed; 340 AA.
AC P62874; P04697; P04901;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1;
DE AltName: Full=Transducin beta chain 1;
GN Name=Gnb1;
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 TISSUE=Adrenal gland;
RA Qiu R., Schimmer B.P.;
RL Submitted (JUN-1995) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/Sv; TISSUE=Liver;
RX PubMed=11913780; DOI=10.3109/10425170109084458;
RA Kitanaka J., Wang X., Kitanaka N., Hembree C.M., Uhl G.R.;
RT "Genomic organization of the murine G protein beta subunit genes and
RT related processed pseudogenes.";
RL DNA Seq. 12:345-354(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [4]
RP PROTEIN SEQUENCE OF 24-42; 58-96; 138-150; 198-209 AND 284-301, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain, and Hippocampus;
RA Lubec G., Klug S., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, 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: Guanine nucleotide-binding proteins (G proteins) are involved
CC as a modulator or transducer in various transmembrane signaling
CC systems. The beta and gamma chains are required for the GTPase
CC activity, for replacement of GDP by GTP, and for G protein-effector
CC interaction (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: G proteins are composed of 3 units, alpha, beta and gamma (By
CC similarity). The heterodimer formed by GNB1 and GNG2 interacts with
CC ARHGEF5 (By similarity). The heterodimer formed by GNB1 and GNG2
CC interacts with GRK2 (By similarity). Interacts with ARHGEF18 and RASD2
CC (By similarity). {ECO:0000250|UniProtKB:P62871,
CC ECO:0000250|UniProtKB:P62873}.
CC -!- PTM: Phosphorylation at His-266 by NDKB contributes to G protein
CC activation by increasing the high energetic phosphate transfer onto
CC GDP. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the WD repeat G protein beta family.
CC {ECO:0000305}.
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DR EMBL; U29055; AAC52905.1; -; mRNA.
DR EMBL; AB042854; BAB63904.1; -; Genomic_DNA.
DR EMBL; BC013058; AAH13058.1; -; mRNA.
DR CCDS; CCDS19030.1; -.
DR PIR; JC5057; JC5057.
DR RefSeq; NP_001153488.1; NM_001160016.1.
DR RefSeq; NP_001153489.1; NM_001160017.1.
DR RefSeq; NP_032168.1; NM_008142.4.
DR RefSeq; XP_017175466.1; XM_017319977.1.
DR PDB; 6K41; EM; 2.90 A; B=2-340.
DR PDB; 6K42; EM; 4.10 A; B=2-340.
DR PDB; 6RMV; X-ray; 1.94 A; A=1-340.
DR PDBsum; 6K41; -.
DR PDBsum; 6K42; -.
DR PDBsum; 6RMV; -.
DR AlphaFoldDB; P62874; -.
DR SMR; P62874; -.
DR BioGRID; 199976; 62.
DR CORUM; P62874; -.
DR IntAct; P62874; 22.
DR MINT; P62874; -.
DR STRING; 10090.ENSMUSP00000030940; -.
DR iPTMnet; P62874; -.
DR PhosphoSitePlus; P62874; -.
DR SwissPalm; P62874; -.
DR EPD; P62874; -.
DR jPOST; P62874; -.
DR PaxDb; P62874; -.
DR PeptideAtlas; P62874; -.
DR PRIDE; P62874; -.
DR ProteomicsDB; 272935; -.
DR Antibodypedia; 26613; 253 antibodies from 31 providers.
DR DNASU; 14688; -.
DR Ensembl; ENSMUST00000030940; ENSMUSP00000030940; ENSMUSG00000029064.
DR Ensembl; ENSMUST00000105616; ENSMUSP00000101241; ENSMUSG00000029064.
DR Ensembl; ENSMUST00000165335; ENSMUSP00000130123; ENSMUSG00000029064.
DR Ensembl; ENSMUST00000176637; ENSMUSP00000135091; ENSMUSG00000029064.
DR GeneID; 14688; -.
DR KEGG; mmu:14688; -.
DR UCSC; uc008wdp.2; mouse.
DR CTD; 2782; -.
DR MGI; MGI:95781; Gnb1.
DR VEuPathDB; HostDB:ENSMUSG00000029064; -.
DR eggNOG; KOG0286; Eukaryota.
DR GeneTree; ENSGT01000000214413; -.
DR HOGENOM; CLU_000288_57_34_1; -.
DR InParanoid; P62874; -.
DR OMA; PLDSQWV; -.
DR OrthoDB; 704786at2759; -.
DR PhylomeDB; P62874; -.
DR TreeFam; TF106149; -.
DR Reactome; R-MMU-1296041; Activation of G protein gated Potassium channels.
DR Reactome; R-MMU-202040; G-protein activation.
DR Reactome; R-MMU-2485179; Activation of the phototransduction cascade.
DR Reactome; R-MMU-381676; Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
DR Reactome; R-MMU-381753; Olfactory Signaling Pathway.
DR Reactome; R-MMU-381771; Synthesis, secretion, and inactivation of Glucagon-like Peptide-1 (GLP-1).
DR Reactome; R-MMU-392170; ADP signalling through P2Y purinoceptor 12.
DR Reactome; R-MMU-392451; G beta:gamma signalling through PI3Kgamma.
DR Reactome; R-MMU-392851; Prostacyclin signalling through prostacyclin receptor.
DR Reactome; R-MMU-400042; Adrenaline,noradrenaline inhibits insulin secretion.
DR Reactome; R-MMU-4086398; Ca2+ pathway.
DR Reactome; R-MMU-416476; G alpha (q) signalling events.
DR Reactome; R-MMU-416482; G alpha (12/13) signalling events.
DR Reactome; R-MMU-418217; G beta:gamma signalling through PLC beta.
DR Reactome; R-MMU-418555; G alpha (s) signalling events.
DR Reactome; R-MMU-418592; ADP signalling through P2Y purinoceptor 1.
DR Reactome; R-MMU-418594; G alpha (i) signalling events.
DR Reactome; R-MMU-418597; G alpha (z) signalling events.
DR Reactome; R-MMU-420092; Glucagon-type ligand receptors.
DR Reactome; R-MMU-428930; Thromboxane signalling through TP receptor.
DR Reactome; R-MMU-432040; Vasopressin regulates renal water homeostasis via Aquaporins.
DR Reactome; R-MMU-456926; Thrombin signalling through proteinase activated receptors (PARs).
DR Reactome; R-MMU-500657; Presynaptic function of Kainate receptors.
DR Reactome; R-MMU-6814122; Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding.
DR Reactome; R-MMU-8964315; G beta:gamma signalling through BTK.
DR Reactome; R-MMU-8964616; G beta:gamma signalling through CDC42.
DR Reactome; R-MMU-9009391; Extra-nuclear estrogen signaling.
DR Reactome; R-MMU-9634597; GPER1 signaling.
DR Reactome; R-MMU-9717207; Sensory perception of sweet, bitter, and umami (glutamate) taste.
DR Reactome; R-MMU-997272; Inhibition of voltage gated Ca2+ channels via Gbeta/gamma subunits.
DR BioGRID-ORCS; 14688; 7 hits in 75 CRISPR screens.
DR ChiTaRS; Gnb1; mouse.
DR PRO; PR:P62874; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; P62874; protein.
DR Bgee; ENSMUSG00000029064; Expressed in retinal neural layer and 260 other tissues.
DR ExpressionAtlas; P62874; baseline and differential.
DR Genevisible; P62874; MM.
DR GO; GO:0044297; C:cell body; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0030425; C:dendrite; ISO:MGI.
DR GO; GO:0005834; C:heterotrimeric G-protein complex; IPI:MGI.
DR GO; GO:0043209; C:myelin sheath; HDA:UniProtKB.
DR GO; GO:0001917; C:photoreceptor inner segment; ISO:MGI.
DR GO; GO:0001750; C:photoreceptor outer segment; IDA:MGI.
DR GO; GO:0042622; C:photoreceptor outer segment membrane; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0047391; F:alkylglycerophosphoethanolamine phosphodiesterase activity; ISO:MGI.
DR GO; GO:0003924; F:GTPase activity; ISO:MGI.
DR GO; GO:0051020; F:GTPase binding; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0030159; F:signaling receptor complex adaptor activity; IBA:GO_Central.
DR GO; GO:0030507; F:spectrin binding; ISO:MGI.
DR GO; GO:0010659; P:cardiac muscle cell apoptotic process; ISO:MGI.
DR GO; GO:0008283; P:cell population proliferation; IDA:MGI.
DR GO; GO:0071456; P:cellular response to hypoxia; ISO:MGI.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IDA:MGI.
DR GO; GO:0007200; P:phospholipase C-activating G protein-coupled receptor signaling pathway; IDA:MGI.
DR GO; GO:0007603; P:phototransduction, visible light; ISO:MGI.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; ISO:MGI.
DR GO; GO:0060041; P:retina development in camera-type eye; IMP:MGI.
DR GO; GO:0050909; P:sensory perception of taste; IDA:MGI.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR001632; Gprotein_B.
DR InterPro; IPR016346; Guanine_nucleotide-bd_bsu.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR19850; PTHR19850; 1.
DR Pfam; PF00400; WD40; 7.
DR PRINTS; PR00319; GPROTEINB.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 3.
DR PROSITE; PS50082; WD_REPEATS_2; 6.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Direct protein sequencing; Phosphoprotein;
KW Reference proteome; Repeat; Transducer; WD repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P62873"
FT CHAIN 2..340
FT /note="Guanine nucleotide-binding protein G(I)/G(S)/G(T)
FT subunit beta-1"
FT /id="PRO_0000127688"
FT REPEAT 53..83
FT /note="WD 1"
FT REPEAT 95..125
FT /note="WD 2"
FT REPEAT 141..170
FT /note="WD 3"
FT REPEAT 182..212
FT /note="WD 4"
FT REPEAT 224..254
FT /note="WD 5"
FT REPEAT 268..298
FT /note="WD 6"
FT REPEAT 310..340
FT /note="WD 7"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:P62873"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P62873"
FT MOD_RES 266
FT /note="Phosphohistidine"
FT /evidence="ECO:0000250|UniProtKB:P62871"
FT HELIX 6..25
FT /evidence="ECO:0007829|PDB:6RMV"
FT HELIX 30..33
FT /evidence="ECO:0007829|PDB:6RMV"
FT TURN 34..36
FT /evidence="ECO:0007829|PDB:6RMV"
FT STRAND 46..51
FT /evidence="ECO:0007829|PDB:6RMV"
FT STRAND 58..63
FT /evidence="ECO:0007829|PDB:6RMV"
FT STRAND 67..74
FT /evidence="ECO:0007829|PDB:6RMV"
FT STRAND 77..83
FT /evidence="ECO:0007829|PDB:6RMV"
FT TURN 84..86
FT /evidence="ECO:0007829|PDB:6RMV"
FT STRAND 89..94
FT /evidence="ECO:0007829|PDB:6RMV"
FT STRAND 100..105
FT /evidence="ECO:0007829|PDB:6RMV"
FT STRAND 109..116
FT /evidence="ECO:0007829|PDB:6RMV"
FT STRAND 121..127
FT /evidence="ECO:0007829|PDB:6RMV"
FT STRAND 129..131
FT /evidence="ECO:0007829|PDB:6RMV"
FT STRAND 134..139
FT /evidence="ECO:0007829|PDB:6RMV"
FT STRAND 146..153
FT /evidence="ECO:0007829|PDB:6RMV"
FT STRAND 156..161
FT /evidence="ECO:0007829|PDB:6RMV"
FT TURN 162..164
FT /evidence="ECO:0007829|PDB:6K41"
FT STRAND 166..170
FT /evidence="ECO:0007829|PDB:6RMV"
FT TURN 171..174
FT /evidence="ECO:0007829|PDB:6RMV"
FT STRAND 175..180
FT /evidence="ECO:0007829|PDB:6RMV"
FT STRAND 187..192
FT /evidence="ECO:0007829|PDB:6RMV"
FT STRAND 196..203
FT /evidence="ECO:0007829|PDB:6RMV"
FT STRAND 208..212
FT /evidence="ECO:0007829|PDB:6RMV"
FT TURN 213..215
FT /evidence="ECO:0007829|PDB:6RMV"
FT STRAND 218..222
FT /evidence="ECO:0007829|PDB:6RMV"
FT STRAND 229..234
FT /evidence="ECO:0007829|PDB:6RMV"
FT STRAND 238..245
FT /evidence="ECO:0007829|PDB:6RMV"
FT STRAND 250..254
FT /evidence="ECO:0007829|PDB:6RMV"
FT TURN 255..258
FT /evidence="ECO:0007829|PDB:6RMV"
FT STRAND 259..264
FT /evidence="ECO:0007829|PDB:6RMV"
FT STRAND 273..278
FT /evidence="ECO:0007829|PDB:6RMV"
FT STRAND 282..292
FT /evidence="ECO:0007829|PDB:6RMV"
FT STRAND 294..298
FT /evidence="ECO:0007829|PDB:6RMV"
FT TURN 299..301
FT /evidence="ECO:0007829|PDB:6RMV"
FT STRAND 304..308
FT /evidence="ECO:0007829|PDB:6RMV"
FT STRAND 315..320
FT /evidence="ECO:0007829|PDB:6RMV"
FT STRAND 322..325
FT /evidence="ECO:0007829|PDB:6K41"
FT STRAND 327..331
FT /evidence="ECO:0007829|PDB:6RMV"
FT STRAND 336..340
FT /evidence="ECO:0007829|PDB:6RMV"
SQ SEQUENCE 340 AA; 37377 MW; 896CBD32D2686598 CRC64;
MSELDQLRQE AEQLKNQIRD ARKACADATL SQITNNIDPV GRIQMRTRRT LRGHLAKIYA
MHWGTDSRLL VSASQDGKLI IWDSYTTNKV HAIPLRSSWV MTCAYAPSGN YVACGGLDNI
CSIYNLKTRE GNVRVSRELA GHTGYLSCCR FLDDNQIVTS SGDTTCALWD IETGQQTTTF
TGHTGDVMSL SLAPDTRLFV SGACDASAKL WDVREGMCRQ TFTGHESDIN AICFFPNGNA
FATGSDDATC RLFDLRADQE LMTYSHDNII CGITSVSFSK SGRLLLAGYD DFNCNVWDAL
KADRAGVLAG HDNRVSCLGV TDDGMAVATG SWDSFLKIWN
