ID GNB5_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 24-JAN-2024, entry version 160. 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; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY, AND SUBCELLULAR RP LOCATION. RC TISSUE=Brain; RX PubMed=8071339; DOI=10.1016/s0021-9258(17)31768-4; RA Watson A.J., Katz A., Simon M.I.; RT "A fifth member of the mammalian G-protein beta-subunit family. Expression RT in brain and activation of the beta 2 isotype of phospholipase C."; RL J. Biol. Chem. 269:22150-22156(1994). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, AND TISSUE RP SPECIFICITY. RX PubMed=8910430; DOI=10.1074/jbc.271.45.28154; 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 project: RT 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 protein, RT 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 expression."; RL Cell 143:1174-1189(2010). RN [8] RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 43-395 IN COMPLEX WITH RGS9, AND RP INTERACTION WITH RGS9. RX PubMed=18204463; DOI=10.1038/nsmb.1377; RA Cheever M.L., Snyder J.T., Gershburg S., Siderovski D.P., Harden T.K., RA Sondek J.; RT "Crystal structure of the multifunctional Gbeta5-RGS9 complex."; RL Nat. Struct. Mol. Biol. 15:155-162(2008). RN [9] RP INTERACTION WITH GPR158. RX PubMed=31311860; DOI=10.1074/jbc.ra119.007533; RA Song C., Orlandi C., Sutton L.P., Martemyanov K.A.; RT "The signaling proteins GPR158 and RGS7 modulate excitability of L2/3 RT pyramidal neurons and control A-type potassium channel in the prelimbic RT cortex."; RL J. Biol. Chem. 294:13145-13157(2019). RN [10] {ECO:0007744|PDB:7SHF} RP STRUCTURE BY ELECTRON MICROSCOPY (3.40 ANGSTROMS) OF 43-395 IN COMPLEX WITH RP GPR158 AND RGS7, AND INTERACTION WITH RGS7 AND GPR158. RX PubMed=34793198; DOI=10.1126/science.abl4732; RA Patil D.N., Singh S., Laboute T., Strutzenberg T.S., Qiu X., Wu D., RA Novick S.J., Robinson C.V., Griffin P.R., Hunt J.F., Izard T., Singh A.K., RA Martemyanov K.A.; RT "Cryo-EM structure of human GPR158 receptor coupled to the RGS7-Gbeta5 RT signaling complex."; RL Science 375:86-91(2022). CC -!- FUNCTION: Enhances GTPase-activating protein (GAP) activity of CC regulator of G protein signaling (RGS) proteins, such as RGS7 and RGS9, CC hence involved in the termination of the signaling initiated by the G CC protein coupled receptors (GPCRs) by accelerating the GTP hydrolysis on CC the G-alpha subunits, thereby promoting their inactivation (By CC similarity). Increases RGS7 GTPase-activating protein (GAP) activity, CC thereby regulating mood and cognition (By similarity). Increases RGS9 CC GTPase-activating protein (GAP) activity, hence contributes to the CC deactivation of G protein signaling initiated by D(2) dopamine CC receptors (By similarity). May play an important role in neuronal CC signaling, including in the parasympathetic, but not sympathetic, CC control of heart rate (By similarity). {ECO:0000250|UniProtKB:A1L271, CC ECO:0000250|UniProtKB:O14775}. CC -!- SUBUNIT: Component of a complex composed of RGS9 (isoform RGS9-1), GNB5 CC and RGS9BP; within this complex, the presence of GNB5 stabilizes both CC itself and RGS9 and increases RGS9 GTPase-activating protein (GAP) CC activity (PubMed:12119397, PubMed:16908407, PubMed:18204463). Interacts CC with RGS7, forming the RGS7-GNB5 complex; within this complex, the CC presence of GNB5 increases RGS7 GTPase-activating protein (GAP) CC activity (PubMed:31311860, PubMed:34793198). Interacts with GPR158; CC promotes the GTPase activator activity of the RGS7-GNB5 complex in CC absence of glycine, in contrast GTPase activator activity of the RGS7- CC GNB5 complex is inhibited in presence of glycine (PubMed:31311860, CC PubMed:34793198). Interacts with RGS6 (By similarity). CC {ECO:0000250|UniProtKB:O14775, ECO:0000269|PubMed:12119397, CC ECO:0000269|PubMed:16908407, ECO:0000269|PubMed:18204463, CC ECO:0000269|PubMed:31311860, ECO:0000269|PubMed:34793198}. CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:8071339, CC ECO:0000269|PubMed:8910430}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; Synonyms=Long, Beta-5L, Gbeta5L; CC IsoId=P62881-1, P54314-1; Sequence=Displayed; CC Name=2; CC IsoId=P62881-2, P54314-2; Sequence=VSP_008766; CC -!- TISSUE SPECIFICITY: Isoform 1 is only detected in retina CC (PubMed:8910430). Isoform 2 is detected in brain (at protein level) CC (PubMed:8071339). Isoform 2 is detected in brain (PubMed:8071339). CC {ECO:0000269|PubMed:8071339, ECO:0000269|PubMed:8910430}. 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; L34290; AAA93084.1; -; mRNA. DR EMBL; U69145; AAC52886.1; -; mRNA. DR EMBL; BC016135; AAH16135.1; -; mRNA. DR CCDS; CCDS40692.1; -. DR CCDS; CCDS90626.1; -. [P62881-2] 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 PDB; 2PBI; X-ray; 1.95 A; B/D=43-395. DR PDB; 6N9G; X-ray; 2.13 A; C/D=43-395. DR PDB; 7SHF; EM; 3.40 A; D=43-395. DR PDBsum; 2PBI; -. DR PDBsum; 6N9G; -. DR PDBsum; 7SHF; -. DR AlphaFoldDB; P62881; -. DR EMDB; EMD-25126; -. DR SMR; P62881; -. DR BioGRID; 199981; 23. DR CORUM; P62881; -. DR DIP; DIP-264N; -. DR IntAct; P62881; 2. DR STRING; 10090.ENSMUSP00000149938; -. DR iPTMnet; P62881; -. DR PhosphoSitePlus; P62881; -. DR SwissPalm; P62881; -. DR MaxQB; P62881; -. DR PaxDb; 10090-ENSMUSP00000076155; -. DR PeptideAtlas; P62881; -. DR ProteomicsDB; 271413; -. DR ProteomicsDB; 271414; -. [P62881-2] DR Pumba; P62881; -. DR Antibodypedia; 24930; 336 antibodies from 32 providers. DR DNASU; 14697; -. DR Ensembl; ENSMUST00000076889.7; ENSMUSP00000076155.7; ENSMUSG00000032192.10. [P62881-1] DR Ensembl; ENSMUST00000213990.2; ENSMUSP00000149938.2; ENSMUSG00000032192.10. [P62881-1] DR Ensembl; ENSMUST00000215875.2; ENSMUSP00000150492.2; ENSMUSG00000032192.10. [P62881-2] DR GeneID; 14697; -. DR KEGG; mmu:14697; -. DR UCSC; uc009qry.2; mouse. DR AGR; MGI:101848; -. DR CTD; 10681; -. DR MGI; MGI:101848; Gnb5. DR VEuPathDB; HostDB:ENSMUSG00000032192; -. DR eggNOG; KOG0286; Eukaryota. DR GeneTree; ENSGT01000000214413; -. DR HOGENOM; CLU_000288_57_34_1; -. DR InParanoid; P62881; -. DR OrthoDB; 102097at2759; -. DR PhylomeDB; P62881; -. DR TreeFam; TF106149; -. DR Reactome; R-MMU-1296041; Activation of G protein gated Potassium channels. DR Reactome; R-MMU-202040; G-protein activation. 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-392170; ADP signalling through P2Y purinoceptor 12. DR Reactome; R-MMU-392451; G beta:gamma signalling through PI3Kgamma. DR Reactome; R-MMU-392851; Prostacyclin signalling through prostacyclin receptor. DR Reactome; R-MMU-400042; Adrenaline,noradrenaline inhibits insulin secretion. DR Reactome; R-MMU-4086398; Ca2+ pathway. DR Reactome; R-MMU-416476; G alpha (q) signalling events. DR Reactome; R-MMU-416482; G alpha (12/13) signalling events. DR Reactome; R-MMU-418217; G beta:gamma signalling through PLC beta. DR Reactome; R-MMU-418555; G alpha (s) signalling events. DR Reactome; R-MMU-418592; ADP signalling through P2Y purinoceptor 1. DR Reactome; R-MMU-418594; G alpha (i) signalling events. DR Reactome; R-MMU-418597; G alpha (z) signalling events. DR Reactome; R-MMU-420092; Glucagon-type ligand receptors. DR Reactome; R-MMU-428930; Thromboxane signalling through TP receptor. DR Reactome; R-MMU-432040; Vasopressin regulates renal water homeostasis via Aquaporins. DR Reactome; R-MMU-456926; Thrombin signalling through proteinase activated receptors (PARs). DR Reactome; R-MMU-500657; Presynaptic function of Kainate receptors. DR Reactome; R-MMU-6814122; Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding. DR Reactome; R-MMU-8964315; G beta:gamma signalling through BTK. DR Reactome; R-MMU-8964616; G beta:gamma signalling through CDC42. DR Reactome; R-MMU-9009391; Extra-nuclear estrogen signaling. DR Reactome; R-MMU-9634597; GPER1 signaling. DR Reactome; R-MMU-997272; Inhibition of voltage gated Ca2+ channels via Gbeta/gamma subunits. DR BioGRID-ORCS; 14697; 3 hits in 80 CRISPR screens. DR ChiTaRS; Gnb5; mouse. DR EvolutionaryTrace; P62881; -. DR PRO; PR:P62881; -. DR Proteomes; UP000000589; Chromosome 9. DR RNAct; P62881; Protein. DR Bgee; ENSMUSG00000032192; Expressed in retinal neural layer and 261 other cell types or tissues. DR ExpressionAtlas; P62881; baseline and differential. DR GO; GO:0044297; C:cell body; ISO:MGI. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005829; C:cytosol; ISO:MGI. DR GO; GO:0005834; C:heterotrimeric G-protein complex; IBA:GO_Central. DR GO; GO:0043209; C:myelin sheath; HDA:UniProtKB. DR GO; GO:0005634; C:nucleus; IDA:MGI. DR GO; GO:0005886; C:plasma membrane; IDA:MGI. DR GO; GO:0098793; C:presynapse; IDA:SynGO. DR GO; GO:0032991; C:protein-containing complex; ISO:MGI. DR GO; GO:0031682; F:G-protein gamma-subunit binding; ISS:CAFA. DR GO; GO:0032794; F:GTPase activating protein binding; ISO:MGI. DR GO; GO:0005096; F:GTPase activator activity; ISO:MGI. DR GO; GO:0051087; F:protein-folding chaperone binding; ISS:CAFA. DR GO; GO:0030159; F:signaling receptor complex adaptor activity; IBA:GO_Central. DR GO; GO:1990603; P:dark adaptation; IDA:MGI. DR GO; GO:0007212; P:dopamine receptor signaling pathway; ISS:UniProtKB. DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IDA:MGI. DR GO; GO:0036367; P:light adaption; IDA:MGI. DR GO; GO:1901386; P:negative regulation of voltage-gated calcium channel activity; ISS:CAFA. DR CDD; cd00200; WD40; 1. DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 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; IPR019775; WD40_repeat_CS. DR InterPro; IPR036322; WD40_repeat_dom_sf. DR InterPro; IPR001680; WD40_rpt. DR PANTHER; PTHR19850; GUANINE NUCLEOTIDE-BINDING PROTEIN BETA G PROTEIN BETA; 1. DR PANTHER; PTHR19850:SF36; GUANINE NUCLEOTIDE-BINDING PROTEIN SUBUNIT BETA-5; 1. 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 repeat-like; 1. DR PROSITE; PS00678; WD_REPEATS_1; 3. DR PROSITE; PS50082; WD_REPEATS_2; 6. DR PROSITE; PS50294; WD_REPEATS_REGION; 1. DR Genevisible; P62881; MM. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Direct protein sequencing; Membrane; KW Reference proteome; Repeat; Transducer; WD repeat. FT CHAIN 1..395 FT /note="Guanine nucleotide-binding protein subunit beta-5" FT /id="PRO_0000127706" FT REPEAT 103..142 FT /note="WD 1" FT REPEAT 145..184 FT /note="WD 2" FT REPEAT 193..234 FT /note="WD 3" FT REPEAT 236..278 FT /note="WD 4" FT REPEAT 279..318 FT /note="WD 5" FT REPEAT 320..362 FT /note="WD 6" FT REPEAT 365..394 FT /note="WD 7" FT VAR_SEQ 1..42 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:8071339" FT /id="VSP_008766" FT HELIX 52..73 FT /evidence="ECO:0007829|PDB:2PBI" FT HELIX 80..83 FT /evidence="ECO:0007829|PDB:2PBI" FT TURN 84..86 FT /evidence="ECO:0007829|PDB:2PBI" FT STRAND 97..102 FT /evidence="ECO:0007829|PDB:2PBI" FT STRAND 108..113 FT /evidence="ECO:0007829|PDB:2PBI" FT STRAND 117..124 FT /evidence="ECO:0007829|PDB:2PBI" FT STRAND 127..133 FT /evidence="ECO:0007829|PDB:2PBI" FT TURN 134..136 FT /evidence="ECO:0007829|PDB:2PBI" FT STRAND 139..144 FT /evidence="ECO:0007829|PDB:2PBI" FT STRAND 146..148 FT /evidence="ECO:0007829|PDB:2PBI" FT STRAND 152..155 FT /evidence="ECO:0007829|PDB:2PBI" FT STRAND 159..166 FT /evidence="ECO:0007829|PDB:2PBI" FT STRAND 169..175 FT /evidence="ECO:0007829|PDB:2PBI" FT STRAND 179..182 FT /evidence="ECO:0007829|PDB:6N9G" FT HELIX 185..187 FT /evidence="ECO:0007829|PDB:2PBI" FT STRAND 189..193 FT /evidence="ECO:0007829|PDB:2PBI" FT STRAND 198..203 FT /evidence="ECO:0007829|PDB:2PBI" FT STRAND 205..214 FT /evidence="ECO:0007829|PDB:2PBI" FT STRAND 217..223 FT /evidence="ECO:0007829|PDB:2PBI" FT TURN 224..226 FT /evidence="ECO:0007829|PDB:2PBI" FT STRAND 229..234 FT /evidence="ECO:0007829|PDB:2PBI" FT STRAND 240..245 FT /evidence="ECO:0007829|PDB:2PBI" FT STRAND 253..258 FT /evidence="ECO:0007829|PDB:2PBI" FT STRAND 263..267 FT /evidence="ECO:0007829|PDB:2PBI" FT TURN 268..270 FT /evidence="ECO:0007829|PDB:2PBI" FT STRAND 273..277 FT /evidence="ECO:0007829|PDB:2PBI" FT STRAND 284..289 FT /evidence="ECO:0007829|PDB:2PBI" FT STRAND 293..300 FT /evidence="ECO:0007829|PDB:2PBI" FT STRAND 305..309 FT /evidence="ECO:0007829|PDB:2PBI" FT TURN 310..313 FT /evidence="ECO:0007829|PDB:2PBI" FT STRAND 314..319 FT /evidence="ECO:0007829|PDB:2PBI" FT STRAND 328..333 FT /evidence="ECO:0007829|PDB:2PBI" FT STRAND 337..344 FT /evidence="ECO:0007829|PDB:2PBI" FT STRAND 349..353 FT /evidence="ECO:0007829|PDB:2PBI" FT TURN 354..356 FT /evidence="ECO:0007829|PDB:2PBI" FT STRAND 358..363 FT /evidence="ECO:0007829|PDB:2PBI" FT STRAND 370..375 FT /evidence="ECO:0007829|PDB:2PBI" FT STRAND 382..386 FT /evidence="ECO:0007829|PDB:2PBI" FT STRAND 389..394 FT /evidence="ECO:0007829|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 //