GBB1_RAT
ID GBB1_RAT Reviewed; 340 AA.
AC P54311; Q6Q8B1; Q9QWG8;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 185.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RA Kuroda S., Tokunaga C., Konishi H., Kikkawa U.;
RL Submitted (AUG-1995) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley;
RX PubMed=9221795; DOI=10.1523/jneurosci.17-15-05993.1997;
RA Wang X.B., Funada M., Imai Y., Revay R.S., Ujike H., Vandenbergh D.J.,
RA Uhl G.R.;
RT "rGbeta1: a psychostimulant-regulated gene essential for establishing
RT cocaine sensitization.";
RL J. Neurosci. 17:5993-6000(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Wistar; TISSUE=Brain;
RA Puhl H.L. III, Ikeda S.R.;
RT "Cloning and characterization of the rat G-protein beta 1 subunit.";
RL Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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 PROTEIN SEQUENCE OF 58-78; 90-96; 138-150; 198-209; 284-301 AND 257-280,
RP AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain, and Hippocampus;
RA Lubec G., Diao W., Afjehi-Sadat L., Chen W.-Q., Kang S.U.;
RL Submitted (JUL-2007) to UniProtKB.
RN [6]
RP ACETYLATION AT SER-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RA Lubec G., Chen W.-Q.;
RL Submitted (FEB-2007) to UniProtKB.
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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.
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 -!- INTERACTION:
CC P54311; Q5BJU7: Wasf1; NbExp=2; IntAct=EBI-917779, EBI-7269229;
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; U34958; AAC72249.1; -; mRNA.
DR EMBL; U88324; AAD00650.1; -; mRNA.
DR EMBL; AY552805; AAS59143.1; -; mRNA.
DR EMBL; BC078809; AAH78809.1; -; mRNA.
DR RefSeq; NP_112249.2; NM_030987.2.
DR RefSeq; XP_006239579.1; XM_006239517.3.
DR RefSeq; XP_008762557.1; XM_008764335.2.
DR RefSeq; XP_017448634.1; XM_017593145.1.
DR RefSeq; XP_017448635.1; XM_017593146.1.
DR RefSeq; XP_017448636.1; XM_017593147.1.
DR RefSeq; XP_017448637.1; XM_017593148.1.
DR RefSeq; XP_017448638.1; XM_017593149.1.
DR PDB; 3SN6; X-ray; 3.20 A; B=2-340.
DR PDB; 5TDH; X-ray; 3.00 A; B/J=1-340.
DR PDB; 5VAI; EM; 4.10 A; B=2-340.
DR PDB; 6CMO; EM; 4.50 A; B=2-340.
DR PDB; 6LPB; EM; 3.90 A; B=2-340.
DR PDB; 6NBF; EM; 3.00 A; B=2-340.
DR PDB; 6NBH; EM; 3.50 A; B=2-340.
DR PDB; 6NBI; EM; 4.00 A; B=2-340.
DR PDB; 6WWZ; EM; 3.34 A; B=2-340.
DR PDB; 7BW0; EM; 3.90 A; B=2-340.
DR PDB; 7CZ5; EM; 2.60 A; B=2-340.
DR PDB; 7D3S; EM; 2.90 A; B=2-340.
DR PDB; 7DH5; EM; 3.16 A; B=2-340.
DR PDB; 7DTY; EM; 2.98 A; B=2-340.
DR PDB; 7DUQ; EM; 2.50 A; B=2-340.
DR PDB; 7DUR; EM; 3.30 A; B=2-340.
DR PDB; 7DW9; EM; 2.60 A; B=2-340.
DR PDB; 7EIB; EM; 3.00 A; C=2-340.
DR PDB; 7EVM; EM; 2.50 A; B=2-340.
DR PDB; 7F16; EM; 2.80 A; B=2-340.
DR PDB; 7F2O; EM; 2.90 A; B=2-340.
DR PDB; 7FIG; EM; 3.90 A; B=2-340.
DR PDB; 7FIH; EM; 3.20 A; B=2-340.
DR PDB; 7FII; EM; 4.30 A; B=2-340.
DR PDB; 7FIM; EM; 3.40 A; B=2-340.
DR PDB; 7FIN; EM; 3.10 A; B=2-340.
DR PDB; 7FIY; EM; 3.40 A; B=2-340.
DR PDB; 7LJC; EM; 3.00 A; B=2-340.
DR PDB; 7LJD; EM; 3.20 A; B=2-340.
DR PDB; 7MBX; EM; 1.95 A; B=1-340.
DR PDB; 7MBY; EM; 2.44 A; B=1-340.
DR PDB; 7PIU; EM; 2.58 A; B=2-340.
DR PDB; 7PIV; EM; 2.86 A; B=2-340.
DR PDB; 7T6S; EM; 3.00 A; B=2-340.
DR PDB; 7T6T; EM; 3.20 A; B=2-340.
DR PDB; 7T6U; EM; 2.90 A; B=2-340.
DR PDB; 7T6V; EM; 3.10 A; B=2-340.
DR PDB; 7V35; EM; 3.40 A; B=2-340.
DR PDB; 7V9L; EM; 2.60 A; B=2-340.
DR PDB; 7V9M; EM; 3.29 A; B=2-340.
DR PDB; 7VAB; EM; 3.20 A; B=2-340.
DR PDB; 7VBH; EM; 3.00 A; B=2-340.
DR PDB; 7VBI; EM; 3.00 A; B=2-340.
DR PDB; 7VGY; EM; 3.10 A; C=2-340.
DR PDB; 7VGZ; EM; 3.30 A; D=2-340.
DR PDB; 7VH0; EM; 3.46 A; C=2-340.
DR PDBsum; 3SN6; -.
DR PDBsum; 5TDH; -.
DR PDBsum; 5VAI; -.
DR PDBsum; 6CMO; -.
DR PDBsum; 6LPB; -.
DR PDBsum; 6NBF; -.
DR PDBsum; 6NBH; -.
DR PDBsum; 6NBI; -.
DR PDBsum; 6WWZ; -.
DR PDBsum; 7BW0; -.
DR PDBsum; 7CZ5; -.
DR PDBsum; 7D3S; -.
DR PDBsum; 7DH5; -.
DR PDBsum; 7DTY; -.
DR PDBsum; 7DUQ; -.
DR PDBsum; 7DUR; -.
DR PDBsum; 7DW9; -.
DR PDBsum; 7EIB; -.
DR PDBsum; 7EVM; -.
DR PDBsum; 7F16; -.
DR PDBsum; 7F2O; -.
DR PDBsum; 7FIG; -.
DR PDBsum; 7FIH; -.
DR PDBsum; 7FII; -.
DR PDBsum; 7FIM; -.
DR PDBsum; 7FIN; -.
DR PDBsum; 7FIY; -.
DR PDBsum; 7LJC; -.
DR PDBsum; 7LJD; -.
DR PDBsum; 7MBX; -.
DR PDBsum; 7MBY; -.
DR PDBsum; 7PIU; -.
DR PDBsum; 7PIV; -.
DR PDBsum; 7T6S; -.
DR PDBsum; 7T6T; -.
DR PDBsum; 7T6U; -.
DR PDBsum; 7T6V; -.
DR PDBsum; 7V35; -.
DR PDBsum; 7V9L; -.
DR PDBsum; 7V9M; -.
DR PDBsum; 7VAB; -.
DR PDBsum; 7VBH; -.
DR PDBsum; 7VBI; -.
DR PDBsum; 7VGY; -.
DR PDBsum; 7VGZ; -.
DR PDBsum; 7VH0; -.
DR AlphaFoldDB; P54311; -.
DR SMR; P54311; -.
DR BioGRID; 246567; 8.
DR CORUM; P54311; -.
DR DIP; DIP-37029N; -.
DR IntAct; P54311; 9.
DR MINT; P54311; -.
DR STRING; 10116.ENSRNOP00000044340; -.
DR iPTMnet; P54311; -.
DR PhosphoSitePlus; P54311; -.
DR jPOST; P54311; -.
DR PaxDb; P54311; -.
DR PRIDE; P54311; -.
DR ABCD; P54311; 3 sequenced antibodies.
DR Ensembl; ENSRNOT00000041789; ENSRNOP00000044340; ENSRNOG00000016638.
DR GeneID; 24400; -.
DR KEGG; rno:24400; -.
DR CTD; 2782; -.
DR RGD; 2718; Gnb1.
DR eggNOG; KOG0286; Eukaryota.
DR GeneTree; ENSGT01000000214413; -.
DR HOGENOM; CLU_000288_57_34_1; -.
DR InParanoid; P54311; -.
DR OMA; PLDSQWV; -.
DR OrthoDB; 704786at2759; -.
DR PhylomeDB; P54311; -.
DR TreeFam; TF106149; -.
DR Reactome; R-RNO-1296041; Activation of G protein gated Potassium channels.
DR Reactome; R-RNO-202040; G-protein activation.
DR Reactome; R-RNO-2485179; Activation of the phototransduction cascade.
DR Reactome; R-RNO-381676; Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
DR Reactome; R-RNO-381753; Olfactory Signaling Pathway.
DR Reactome; R-RNO-381771; Synthesis, secretion, and inactivation of Glucagon-like Peptide-1 (GLP-1).
DR Reactome; R-RNO-392170; ADP signalling through P2Y purinoceptor 12.
DR Reactome; R-RNO-392451; G beta:gamma signalling through PI3Kgamma.
DR Reactome; R-RNO-400042; Adrenaline,noradrenaline inhibits insulin secretion.
DR Reactome; R-RNO-4086398; Ca2+ pathway.
DR Reactome; R-RNO-416476; G alpha (q) signalling events.
DR Reactome; R-RNO-418594; G alpha (i) signalling events.
DR Reactome; R-RNO-418597; G alpha (z) signalling events.
DR Reactome; R-RNO-420092; Glucagon-type ligand receptors.
DR Reactome; R-RNO-428930; Thromboxane signalling through TP receptor.
DR Reactome; R-RNO-432040; Vasopressin regulates renal water homeostasis via Aquaporins.
DR Reactome; R-RNO-456926; Thrombin signalling through proteinase activated receptors (PARs).
DR Reactome; R-RNO-6814122; Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding.
DR Reactome; R-RNO-8964616; G beta:gamma signalling through CDC42.
DR Reactome; R-RNO-9717207; Sensory perception of sweet, bitter, and umami (glutamate) taste.
DR Reactome; R-RNO-997272; Inhibition of voltage gated Ca2+ channels via Gbeta/gamma subunits.
DR EvolutionaryTrace; P54311; -.
DR PRO; PR:P54311; -.
DR Proteomes; UP000002494; Chromosome 5.
DR Bgee; ENSRNOG00000016638; Expressed in frontal cortex and 19 other tissues.
DR Genevisible; P54311; RN.
DR GO; GO:0044297; C:cell body; IDA:RGD.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0030425; C:dendrite; IDA:RGD.
DR GO; GO:0005834; C:heterotrimeric G-protein complex; IDA:RGD.
DR GO; GO:0001917; C:photoreceptor inner segment; IDA:RGD.
DR GO; GO:0001750; C:photoreceptor outer segment; ISO:RGD.
DR GO; GO:0042622; C:photoreceptor outer segment membrane; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0047391; F:alkylglycerophosphoethanolamine phosphodiesterase activity; IDA:MGI.
DR GO; GO:0003924; F:GTPase activity; ISO:RGD.
DR GO; GO:0051020; F:GTPase binding; ISO:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:RGD.
DR GO; GO:0030159; F:signaling receptor complex adaptor activity; IBA:GO_Central.
DR GO; GO:0030507; F:spectrin binding; IDA:MGI.
DR GO; GO:0010659; P:cardiac muscle cell apoptotic process; IDA:MGI.
DR GO; GO:0008283; P:cell population proliferation; ISO:RGD.
DR GO; GO:0071456; P:cellular response to hypoxia; IDA:MGI.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IMP:RGD.
DR GO; GO:0007200; P:phospholipase C-activating G protein-coupled receptor signaling pathway; ISO:RGD.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IMP:RGD.
DR GO; GO:0060041; P:retina development in camera-type eye; ISO:RGD.
DR GO; GO:0050909; P:sensory perception of taste; ISO:RGD.
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:0000269|Ref.6"
FT CHAIN 2..340
FT /note="Guanine nucleotide-binding protein G(I)/G(S)/G(T)
FT subunit beta-1"
FT /id="PRO_0000127690"
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:0000269|Ref.6"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 266
FT /note="Phosphohistidine"
FT /evidence="ECO:0000250|UniProtKB:P62871"
FT CONFLICT 208
FT /note="A -> V (in Ref. 2; AAD00650)"
FT /evidence="ECO:0000305"
FT CONFLICT 277
FT /note="S -> P (in Ref. 2; AAD00650)"
FT /evidence="ECO:0000305"
FT CONFLICT 287
FT /note="A -> G (in Ref. 2; AAD00650)"
FT /evidence="ECO:0000305"
FT CONFLICT 301
FT /note="K -> N (in Ref. 2; AAD00650)"
FT /evidence="ECO:0000305"
FT CONFLICT 307
FT /note="V -> D (in Ref. 1; AAC72249)"
FT /evidence="ECO:0000305"
FT HELIX 3..24
FT /evidence="ECO:0007829|PDB:7MBX"
FT HELIX 30..33
FT /evidence="ECO:0007829|PDB:7MBX"
FT HELIX 34..36
FT /evidence="ECO:0007829|PDB:7MBX"
FT STRAND 46..51
FT /evidence="ECO:0007829|PDB:7MBX"
FT STRAND 58..63
FT /evidence="ECO:0007829|PDB:7MBX"
FT STRAND 67..74
FT /evidence="ECO:0007829|PDB:7MBX"
FT TURN 75..77
FT /evidence="ECO:0007829|PDB:7MBX"
FT STRAND 78..83
FT /evidence="ECO:0007829|PDB:7MBX"
FT TURN 84..87
FT /evidence="ECO:0007829|PDB:7MBX"
FT STRAND 88..94
FT /evidence="ECO:0007829|PDB:7MBX"
FT STRAND 96..98
FT /evidence="ECO:0007829|PDB:7MBX"
FT STRAND 100..105
FT /evidence="ECO:0007829|PDB:7MBX"
FT STRAND 109..116
FT /evidence="ECO:0007829|PDB:7MBX"
FT STRAND 121..127
FT /evidence="ECO:0007829|PDB:7MBX"
FT STRAND 129..132
FT /evidence="ECO:0007829|PDB:7MBX"
FT STRAND 134..139
FT /evidence="ECO:0007829|PDB:7MBX"
FT STRAND 146..161
FT /evidence="ECO:0007829|PDB:7MBX"
FT STRAND 162..164
FT /evidence="ECO:0007829|PDB:7LJC"
FT STRAND 166..170
FT /evidence="ECO:0007829|PDB:7MBX"
FT TURN 171..174
FT /evidence="ECO:0007829|PDB:7MBX"
FT STRAND 175..180
FT /evidence="ECO:0007829|PDB:7MBX"
FT STRAND 187..192
FT /evidence="ECO:0007829|PDB:7MBX"
FT STRAND 196..203
FT /evidence="ECO:0007829|PDB:7MBX"
FT STRAND 206..212
FT /evidence="ECO:0007829|PDB:7MBX"
FT TURN 213..215
FT /evidence="ECO:0007829|PDB:7MBX"
FT STRAND 218..223
FT /evidence="ECO:0007829|PDB:7MBX"
FT STRAND 229..234
FT /evidence="ECO:0007829|PDB:7MBX"
FT STRAND 238..245
FT /evidence="ECO:0007829|PDB:7MBX"
FT STRAND 246..248
FT /evidence="ECO:0007829|PDB:7MBY"
FT STRAND 250..254
FT /evidence="ECO:0007829|PDB:7MBX"
FT TURN 255..258
FT /evidence="ECO:0007829|PDB:7MBX"
FT STRAND 259..264
FT /evidence="ECO:0007829|PDB:7MBX"
FT STRAND 273..278
FT /evidence="ECO:0007829|PDB:7MBX"
FT STRAND 280..282
FT /evidence="ECO:0007829|PDB:7MBX"
FT STRAND 284..289
FT /evidence="ECO:0007829|PDB:7MBX"
FT STRAND 290..292
FT /evidence="ECO:0007829|PDB:7DH5"
FT STRAND 294..298
FT /evidence="ECO:0007829|PDB:7MBX"
FT TURN 299..301
FT /evidence="ECO:0007829|PDB:7MBX"
FT STRAND 304..308
FT /evidence="ECO:0007829|PDB:7MBX"
FT STRAND 315..320
FT /evidence="ECO:0007829|PDB:7MBX"
FT STRAND 322..325
FT /evidence="ECO:0007829|PDB:7MBY"
FT STRAND 327..331
FT /evidence="ECO:0007829|PDB:7MBX"
FT STRAND 336..340
FT /evidence="ECO:0007829|PDB:7MBX"
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
