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 25-MAY-2022, entry version 184. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 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; 7V9M; EM; 3.29 A; B=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; 7LJC; -. DR PDBsum; 7LJD; -. DR PDBsum; 7MBX; -. DR PDBsum; 7MBY; -. DR PDBsum; 7PIU; -. DR PDBsum; 7PIV; -. DR PDBsum; 7V9M; -. 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 21 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 //