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 01-MAY-2013, entry version 111. 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; Sciurognathi; 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 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 MASS SPECTROMETRY. RA Lubec G., Chen W.-Q.; RL Submitted (FEB-2007) to UniProtKB. 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 PTH1R (via C-terminus) (By CC similarity). CC -!- PTM: Phosphorylation at His-266 by NDKB contributes to G protein CC activation by increasing the high energetic phosphate transfer CC onto GDP (By similarity). CC -!- SIMILARITY: Belongs to the WD repeat G protein beta family. CC -!- SIMILARITY: Contains 7 WD repeats. 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 IPI; IPI00212655; -. DR RefSeq; NP_112249.2; NM_030987.2. DR UniGene; Rn.126047; -. DR PDB; 3SN6; X-ray; 3.20 A; B=2-340. DR PDBsum; 3SN6; -. DR ProteinModelPortal; P54311; -. DR DIP; DIP-37029N; -. DR IntAct; P54311; 1. DR MINT; MINT-1795773; -. DR PhosphoSite; 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; COG2319; -. DR GeneTree; ENSGT00550000074331; -. DR HOGENOM; HOG000176356; -. DR HOVERGEN; HBG000188; -. DR InParanoid; P54311; -. DR KO; K04536; -. DR OMA; CMLWDIE; -. DR OrthoDB; EOG4HX51D; -. DR EvolutionaryTrace; P54311; -. DR NextBio; 603199; -. DR ArrayExpress; P54311; -. DR Genevestigator; P54311; -. DR GermOnline; ENSRNOG00000016638; Rattus norvegicus. 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:0001917; C:photoreceptor inner segment; IDA:RGD. DR GO; GO:0042622; C:photoreceptor outer segment membrane; IDA:RGD. DR GO; GO:0003924; F:GTPase activity; IEA:Compara. DR GO; GO:0004871; F:signal transducer activity; IEA:UniProtKB-KW. DR GO; GO:0010659; P:cardiac muscle cell apoptotic process; IDA:MGI. DR GO; GO:0008283; P:cell proliferation; IEA:Compara. DR GO; GO:0071456; P:cellular response to hypoxia; IDA:MGI. DR GO; GO:0007204; P:elevation of cytosolic calcium ion concentration; IMP:RGD. 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:Compara. DR GO; GO:0060041; P:retina development in camera-type eye; IEA:Compara. DR GO; GO:0050909; P:sensory perception of taste; IEA:Compara. 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. DR InterPro; IPR001680; WD40_repeat. DR InterPro; IPR019775; WD40_repeat_CS. DR InterPro; IPR017986; WD40_repeat_dom. DR Pfam; PF00400; WD40; 7. DR PIRSF; PIRSF002394; GN-bd_beta; 1. DR PRINTS; PR00319; GPROTEINB. DR PRINTS; PR00320; GPROTEINBRPT. DR SMART; SM00320; WD40; 7. DR SUPFAM; SSF50978; WD40_like; 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. 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. FT MOD_RES 266 266 Phosphohistidine (By similarity). FT CONFLICT 208 208 A -> V (in Ref. 2; AAD00650). FT CONFLICT 277 277 S -> P (in Ref. 2; AAD00650). FT CONFLICT 287 287 A -> G (in Ref. 2; AAD00650). FT CONFLICT 301 301 K -> N (in Ref. 2; AAD00650). FT CONFLICT 307 307 V -> D (in Ref. 1; AAC72249). FT HELIX 3 24 FT HELIX 30 33 FT STRAND 35 37 FT STRAND 47 52 FT STRAND 58 63 FT STRAND 67 74 FT STRAND 77 83 FT TURN 84 87 FT STRAND 88 94 FT STRAND 96 98 FT STRAND 100 105 FT STRAND 109 116 FT STRAND 121 126 FT STRAND 129 132 FT STRAND 135 139 FT STRAND 146 161 FT STRAND 166 170 FT TURN 171 174 FT STRAND 175 180 FT STRAND 187 192 FT STRAND 196 203 FT STRAND 208 212 FT TURN 213 215 FT STRAND 217 222 FT STRAND 229 234 FT STRAND 238 245 FT STRAND 250 254 FT TURN 255 258 FT STRAND 259 264 FT STRAND 273 278 FT STRAND 280 282 FT STRAND 284 289 FT STRAND 294 298 FT TURN 299 301 FT STRAND 303 308 FT STRAND 315 320 FT STRAND 327 331 FT STRAND 334 339 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 //