ID GBB5_MOUSE Reviewed; 395 AA. AC P62881; O35354; P54314; Q91WB3; DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot. DT 16-AUG-2004, sequence version 1. DT 16-SEP-2015, entry version 111. DE RecName: Full=Guanine nucleotide-binding protein subunit beta-5; DE AltName: Full=Gbeta5; DE AltName: Full=Transducin beta chain 5; GN Name=Gnb5; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). RC TISSUE=Brain; RX PubMed=8071339; RA Watson A.J., Katz A., Simon M.I.; RT "A fifth member of the mammalian G-protein beta-subunit family. RT Expression in brain and activation of the beta 2 isotype of RT phospholipase C."; RL J. Biol. Chem. 269:22150-22156(1994). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY. RX PubMed=8910430; DOI=10.1074/jbc.271.45.28271; RA Watson A.J., Aragay A.M., Slepak V.Z., Simon M.I.; RT "A novel form of the G protein beta subunit Gbeta5 is specifically RT expressed in the vertebrate retina."; RL J. Biol. Chem. 271:28154-28160(1996). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Eye, and Retina; 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 [4] RP PROTEIN SEQUENCE OF 75-86 AND 322-338, AND IDENTIFICATION BY MASS RP SPECTROMETRY. RC TISSUE=Hippocampus; RA Lubec G., Klug S.; RL Submitted (MAR-2007) to UniProtKB. RN [5] RP INTERACTION WITH RGS9 AND RGS9BP. RC STRAIN=C57BL/6 X 129; TISSUE=Retina; RX PubMed=12119397; DOI=10.1073/pnas.152094799; RA Hu G., Wensel T.G.; RT "R9AP, a membrane anchor for the photoreceptor GTPase accelerating RT protein, RGS9-1."; RL Proc. Natl. Acad. Sci. U.S.A. 99:9755-9760(2002). RN [6] RP INTERACTION WITH RGS9 AND RGS9BP. RX PubMed=16908407; DOI=10.1016/j.neuron.2006.07.010; RA Krispel C.M., Chen D., Melling N., Chen Y.-J., Martemyanov K.A., RA Quillinan N., Arshavsky V.Y., Wensel T.G., Chen C.-K., Burns M.E.; RT "RGS expression rate-limits recovery of rod photoresponses."; RL Neuron 51:409-416(2006). RN [7] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain; 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 RT expression."; RL Cell 143:1174-1189(2010). 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. Component of the RGS9-1-Gbeta5 complex composed of RGS9 CC (isoform RGS9-1), Gbeta5 (GNB5) and RGS9BP. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; Synonyms=Long, Beta-5L, Gbeta5L; CC IsoId=P62881-1, P54314-1; CC Sequence=Displayed; CC Name=2; CC IsoId=P62881-2, P54314-2; CC Sequence=VSP_008766; CC -!- TISSUE SPECIFICITY: Brain and at much reduced levels in kidney. CC Isoform 1 is retinal specific. {ECO:0000269|PubMed:8910430}. CC -!- SIMILARITY: Belongs to the WD repeat G protein beta family. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 7 WD repeats. {ECO:0000255|PROSITE- CC ProRule:PRU00221}. 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; L34290; AAA93084.1; -; mRNA. DR EMBL; U69145; AAC52886.1; -; mRNA. DR EMBL; BC016135; AAH16135.1; -; mRNA. DR CCDS; CCDS40692.1; -. DR PIR; A54969; A54969. DR RefSeq; NP_034443.1; NM_010313.2. [P62881-1] DR RefSeq; NP_619733.1; NM_138719.5. [P62881-2] DR UniGene; Mm.17604; -. DR PDB; 2PBI; X-ray; 1.95 A; B/D=43-395. DR PDBsum; 2PBI; -. DR ProteinModelPortal; P62881; -. DR SMR; P62881; 43-395. DR BioGrid; 199981; 1. DR DIP; DIP-264N; -. DR IntAct; P62881; 3. DR MINT; MINT-4095704; -. DR STRING; 10090.ENSMUSP00000076155; -. DR PhosphoSite; P62881; -. DR MaxQB; P62881; -. DR PaxDb; P62881; -. DR PRIDE; P62881; -. DR Ensembl; ENSMUST00000076889; ENSMUSP00000076155; ENSMUSG00000032192. [P62881-1] DR GeneID; 14697; -. DR KEGG; mmu:14697; -. DR UCSC; uc009qry.2; mouse. DR CTD; 10681; -. DR MGI; MGI:101848; Gnb5. DR eggNOG; COG2319; -. DR GeneTree; ENSGT00760000119239; -. DR HOGENOM; HOG000176356; -. DR HOVERGEN; HBG000188; -. DR InParanoid; P62881; -. DR KO; K04539; -. DR OMA; YCSTCAE; -. DR OrthoDB; EOG7GN2N5; -. DR PhylomeDB; P62881; -. DR TreeFam; TF106149; -. DR Reactome; R-MMU-2514859; Inactivation, recovery and regulation of the phototransduction cascade. DR Reactome; R-MMU-381676; Glucagon-like Peptide-1 (GLP1) regulates insulin secretion. DR Reactome; R-MMU-400042; Adrenaline,noradrenaline inhibits insulin secretion. DR Reactome; R-MMU-420092; Glucagon-type ligand receptors. DR Reactome; R-MMU-432040; Vasopressin regulates renal water homeostasis via Aquaporins. DR ChiTaRS; Gnb5; mouse. DR EvolutionaryTrace; P62881; -. DR NextBio; 286651; -. DR PRO; PR:P62881; -. DR Proteomes; UP000000589; Chromosome 9. DR Bgee; P62881; -. DR Genevisible; P62881; MM. DR GO; GO:0043209; C:myelin sheath; IDA:UniProtKB. DR GO; GO:0005634; C:nucleus; IDA:MGI. DR GO; GO:0001917; C:photoreceptor inner segment; IDA:MGI. DR GO; GO:0001750; C:photoreceptor outer segment; IDA:MGI. DR GO; GO:0005886; C:plasma membrane; IDA:MGI. DR GO; GO:0051087; F:chaperone binding; ISS:UniProtKB. DR GO; GO:0031682; F:G-protein gamma-subunit binding; ISS:UniProtKB. DR GO; GO:0004871; F:signal transducer activity; IEA:UniProtKB-KW. DR GO; GO:0007186; P:G-protein coupled receptor signaling pathway; IDA:MGI. DR GO; GO:1901386; P:negative regulation of voltage-gated calcium channel activity; ISS:UniProtKB. 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 PANTHER; PTHR19850; PTHR19850; 1. DR Pfam; PF00400; WD40; 4. 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; Alternative splicing; Complete proteome; KW Direct protein sequencing; Reference proteome; Repeat; Transducer; KW WD repeat. FT CHAIN 1 395 Guanine nucleotide-binding protein FT subunit beta-5. FT /FTId=PRO_0000127706. FT REPEAT 103 142 WD 1. FT REPEAT 145 184 WD 2. FT REPEAT 193 234 WD 3. FT REPEAT 236 278 WD 4. FT REPEAT 279 318 WD 5. FT REPEAT 320 362 WD 6. FT REPEAT 365 394 WD 7. FT VAR_SEQ 1 42 Missing (in isoform 2). FT {ECO:0000303|PubMed:8071339}. FT /FTId=VSP_008766. FT HELIX 52 73 {ECO:0000244|PDB:2PBI}. FT HELIX 80 83 {ECO:0000244|PDB:2PBI}. FT TURN 84 86 {ECO:0000244|PDB:2PBI}. FT STRAND 97 102 {ECO:0000244|PDB:2PBI}. FT STRAND 108 113 {ECO:0000244|PDB:2PBI}. FT STRAND 117 124 {ECO:0000244|PDB:2PBI}. FT STRAND 127 133 {ECO:0000244|PDB:2PBI}. FT TURN 134 136 {ECO:0000244|PDB:2PBI}. FT STRAND 139 144 {ECO:0000244|PDB:2PBI}. FT STRAND 146 148 {ECO:0000244|PDB:2PBI}. FT STRAND 152 155 {ECO:0000244|PDB:2PBI}. FT STRAND 159 166 {ECO:0000244|PDB:2PBI}. FT STRAND 169 175 {ECO:0000244|PDB:2PBI}. FT HELIX 185 187 {ECO:0000244|PDB:2PBI}. FT STRAND 189 193 {ECO:0000244|PDB:2PBI}. FT STRAND 198 203 {ECO:0000244|PDB:2PBI}. FT STRAND 205 214 {ECO:0000244|PDB:2PBI}. FT STRAND 217 223 {ECO:0000244|PDB:2PBI}. FT TURN 224 226 {ECO:0000244|PDB:2PBI}. FT STRAND 229 234 {ECO:0000244|PDB:2PBI}. FT STRAND 240 245 {ECO:0000244|PDB:2PBI}. FT STRAND 253 258 {ECO:0000244|PDB:2PBI}. FT STRAND 263 267 {ECO:0000244|PDB:2PBI}. FT TURN 268 270 {ECO:0000244|PDB:2PBI}. FT STRAND 273 277 {ECO:0000244|PDB:2PBI}. FT STRAND 284 289 {ECO:0000244|PDB:2PBI}. FT STRAND 293 300 {ECO:0000244|PDB:2PBI}. FT STRAND 305 309 {ECO:0000244|PDB:2PBI}. FT TURN 310 313 {ECO:0000244|PDB:2PBI}. FT STRAND 314 319 {ECO:0000244|PDB:2PBI}. FT STRAND 328 333 {ECO:0000244|PDB:2PBI}. FT STRAND 337 344 {ECO:0000244|PDB:2PBI}. FT STRAND 349 353 {ECO:0000244|PDB:2PBI}. FT TURN 354 356 {ECO:0000244|PDB:2PBI}. FT STRAND 358 363 {ECO:0000244|PDB:2PBI}. FT STRAND 370 375 {ECO:0000244|PDB:2PBI}. FT STRAND 382 386 {ECO:0000244|PDB:2PBI}. FT STRAND 389 394 {ECO:0000244|PDB:2PBI}. SQ SEQUENCE 395 AA; 43565 MW; 972A41AAEC4CB3F8 CRC64; MCDQTFLVNV FGSCDKCFKQ RALRPVFKKS QQLNYCSTCA EIMATDGLHE NETLASLKSE AESLKGKLEE ERAKLHDVEL HQVAERVEAL GQFVMKTRRT LKGHGNKVLC MDWCKDKRRI VSSSQDGKVI VWDSFTTNKE HAVTMPCTWV MACAYAPSGC AIACGGLDNK CSVYPLTFDK NENMAAKKKS VAMHTNYLSA CSFTNSDMQI LTASGDGTCA LWDVESGQLL QSFHGHGADV LCLDLAPSET GNTFVSGGCD KKAMVWDMRS GQCVQAFETH ESDVNSVRYY PSGDAFASGS DDATCRLYDL RADREVAIYS KESIIFGASS VDFSLSGRLL FAGYNDYTIN VWDVLKGSRV SILFGHENRV STLRVSPDGT AFCSGSWDHT LRVWA //