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 05-DEC-2018, entry version 161. 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; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; OC Muroidea; Muridae; 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; 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 RT project: 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 RP 257-280, 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 RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22673903; DOI=10.1038/ncomms1871; RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., RA Lundby C., Olsen J.V.; RT "Quantitative maps of protein phosphorylation sites across 14 RT different rat organs and tissues."; RL Nat. Commun. 3:876-876(2012). CC -!- FUNCTION: Guanine nucleotide-binding proteins (G proteins) are CC involved as a modulator or transducer in various transmembrane CC signaling systems. The beta and gamma chains are required for the CC GTPase activity, for replacement of GDP by GTP, and for G protein- CC effector interaction. CC -!- SUBUNIT: G proteins are composed of 3 units, alpha, beta and CC gamma. Interacts with ARHGEF18 and RASD2. The heterodimer formed CC by GNB1 and GNG2 interacts with ARHGEF5 (By similarity). CC {ECO:0000250|UniProtKB:P62873}. CC -!- INTERACTION: CC 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 CC onto 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 UniGene; Rn.126047; -. 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 PDBsum; 3SN6; -. DR PDBsum; 5TDH; -. DR PDBsum; 5VAI; -. DR PDBsum; 6CMO; -. DR ProteinModelPortal; P54311; -. DR SMR; P54311; -. DR BioGrid; 246567; 5. DR CORUM; P54311; -. DR DIP; DIP-37029N; -. DR IntAct; P54311; 7. DR MINT; P54311; -. DR STRING; 10116.ENSRNOP00000044340; -. DR iPTMnet; P54311; -. DR PhosphoSitePlus; P54311; -. DR PaxDb; P54311; -. DR PRIDE; P54311; -. DR Ensembl; ENSRNOT00000041789; ENSRNOP00000044340; ENSRNOG00000016638. DR GeneID; 24400; -. DR KEGG; rno:24400; -. DR CTD; 2782; -. DR RGD; 2718; Gnb1. DR eggNOG; KOG0286; Eukaryota. DR eggNOG; ENOG410XQUX; LUCA. DR GeneTree; ENSGT00940000153602; -. DR HOGENOM; HOG000176356; -. DR HOVERGEN; HBG000188; -. DR InParanoid; P54311; -. DR KO; K04536; -. DR OMA; TCNVWDT; -. DR OrthoDB; EOG091G0A7T; -. 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-392170; ADP signalling through P2Y purinoceptor 12. DR Reactome; R-RNO-392451; G beta:gamma signalling through PI3Kgamma. DR Reactome; R-RNO-392851; Prostacyclin signalling through prostacyclin receptor. 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-416482; G alpha (12/13) signalling events. DR Reactome; R-RNO-418217; G beta:gamma signalling through PLC beta. DR Reactome; R-RNO-418555; G alpha (s) signalling events. DR Reactome; R-RNO-418592; ADP signalling through P2Y purinoceptor 1. 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-500657; Presynaptic function of Kainate receptors. DR Reactome; R-RNO-6814122; Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding. 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 10 organ(s), highest expression level in brain. DR Genevisible; P54311; RN. DR GO; GO:0044297; C:cell body; IDA:RGD. DR GO; GO:0030425; C:dendrite; IDA:RGD. DR GO; GO:0005834; C:heterotrimeric G-protein complex; IDA:RGD. DR GO; GO:0043209; C:myelin sheath; IEA:Ensembl. DR GO; GO:0001917; C:photoreceptor inner segment; IDA:RGD. DR GO; GO:0042622; C:photoreceptor outer segment membrane; IDA:RGD. DR GO; GO:0047391; F:alkylglycerophosphoethanolamine phosphodiesterase activity; IDA:MGI. DR GO; GO:0003924; F:GTPase activity; IEA:Ensembl. DR GO; GO:0051020; F:GTPase binding; IEA:Ensembl. DR GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl. 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 proliferation; IEA:Ensembl. 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; IEA:Ensembl. DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IMP:RGD. DR GO; GO:0070208; P:protein heterotrimerization; IDA:MGI. DR GO; GO:0060041; P:retina development in camera-type eye; IEA:Ensembl. DR GO; GO:0050909; P:sensory perception of taste; IEA:Ensembl. 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; IPR017986; WD40_repeat_dom. 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; Complete proteome; KW Direct protein sequencing; Phosphoprotein; Reference proteome; Repeat; KW Transducer; WD repeat. FT INIT_MET 1 1 Removed. {ECO:0000269|Ref.6}. FT CHAIN 2 340 Guanine nucleotide-binding protein FT G(I)/G(S)/G(T) subunit beta-1. FT /FTId=PRO_0000127690. FT REPEAT 53 83 WD 1. FT REPEAT 95 125 WD 2. FT REPEAT 141 170 WD 3. FT REPEAT 182 212 WD 4. FT REPEAT 224 254 WD 5. FT REPEAT 268 298 WD 6. FT REPEAT 310 340 WD 7. FT MOD_RES 2 2 N-acetylserine. {ECO:0000269|Ref.6}. FT MOD_RES 2 2 Phosphoserine. FT {ECO:0000244|PubMed:22673903}. FT MOD_RES 266 266 Phosphohistidine. FT {ECO:0000250|UniProtKB:P62871}. FT CONFLICT 208 208 A -> V (in Ref. 2; AAD00650). FT {ECO:0000305}. FT CONFLICT 277 277 S -> P (in Ref. 2; AAD00650). FT {ECO:0000305}. FT CONFLICT 287 287 A -> G (in Ref. 2; AAD00650). FT {ECO:0000305}. FT CONFLICT 301 301 K -> N (in Ref. 2; AAD00650). FT {ECO:0000305}. FT CONFLICT 307 307 V -> D (in Ref. 1; AAC72249). FT {ECO:0000305}. FT HELIX 2 25 {ECO:0000244|PDB:5TDH}. FT HELIX 30 33 {ECO:0000244|PDB:5TDH}. FT TURN 34 36 {ECO:0000244|PDB:5TDH}. FT STRAND 47 51 {ECO:0000244|PDB:5TDH}. FT STRAND 58 63 {ECO:0000244|PDB:5TDH}. FT STRAND 67 74 {ECO:0000244|PDB:5TDH}. FT TURN 75 77 {ECO:0000244|PDB:5TDH}. FT STRAND 78 83 {ECO:0000244|PDB:5TDH}. FT TURN 84 87 {ECO:0000244|PDB:5TDH}. FT STRAND 88 94 {ECO:0000244|PDB:5TDH}. FT STRAND 96 98 {ECO:0000244|PDB:5TDH}. FT STRAND 102 105 {ECO:0000244|PDB:5TDH}. FT STRAND 109 115 {ECO:0000244|PDB:5TDH}. FT STRAND 121 125 {ECO:0000244|PDB:5TDH}. FT STRAND 129 132 {ECO:0000244|PDB:3SN6}. FT STRAND 134 139 {ECO:0000244|PDB:5TDH}. FT STRAND 146 153 {ECO:0000244|PDB:5TDH}. FT STRAND 156 161 {ECO:0000244|PDB:5TDH}. FT STRAND 166 170 {ECO:0000244|PDB:5TDH}. FT TURN 171 174 {ECO:0000244|PDB:5TDH}. FT STRAND 175 180 {ECO:0000244|PDB:5TDH}. FT STRAND 187 192 {ECO:0000244|PDB:5TDH}. FT STRAND 196 203 {ECO:0000244|PDB:5TDH}. FT STRAND 208 212 {ECO:0000244|PDB:5TDH}. FT TURN 213 216 {ECO:0000244|PDB:5TDH}. FT STRAND 217 222 {ECO:0000244|PDB:5TDH}. FT STRAND 229 234 {ECO:0000244|PDB:5TDH}. FT STRAND 238 245 {ECO:0000244|PDB:5TDH}. FT STRAND 250 254 {ECO:0000244|PDB:5TDH}. FT TURN 255 258 {ECO:0000244|PDB:5TDH}. FT STRAND 259 264 {ECO:0000244|PDB:5TDH}. FT STRAND 273 278 {ECO:0000244|PDB:5TDH}. FT STRAND 280 282 {ECO:0000244|PDB:5TDH}. FT STRAND 284 289 {ECO:0000244|PDB:5TDH}. FT STRAND 294 298 {ECO:0000244|PDB:5TDH}. FT TURN 299 301 {ECO:0000244|PDB:5TDH}. FT STRAND 304 308 {ECO:0000244|PDB:5TDH}. FT STRAND 315 320 {ECO:0000244|PDB:5TDH}. FT STRAND 327 331 {ECO:0000244|PDB:5TDH}. FT STRAND 336 339 {ECO:0000244|PDB:5TDH}. 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 //