GNB5_MOUSE
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 03-AUG-2022, entry version 152.
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).
CC -!- FUNCTION: Enhances GTPase-activating protein (GAP) activity of
CC regulator of G protein signaling (RGS) proteins, hence involved in the
CC termination of the signaling initiated by the G protein coupled
CC receptors (GPCRs) by accelerating the GTP hydrolysis on the G-alpha
CC subunits, thereby promoting their inactivation (Probable). Increases
CC RGS9 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, ECO:0000305}.
CC -!- SUBUNIT: Component of a complex composed of RGS9, GNB5 and RGS9BP;
CC within this complex, the presence of GNB5 stabilizes both itself and
CC RGS9 and increases RGS9 GTPase-activating protein (GAP) activity (By
CC similarity) (PubMed:12119397, PubMed:16908407, PubMed:18204463).
CC Interacts with RGS6 and RGS7 (By similarity).
CC {ECO:0000250|UniProtKB:O14775, ECO:0000269|PubMed:12119397,
CC ECO:0000269|PubMed:16908407, ECO:0000269|PubMed:18204463}.
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;
CC Sequence=Displayed;
CC Name=2;
CC IsoId=P62881-2, P54314-2;
CC 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}.
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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 SMR; P62881; -.
DR BioGRID; 199981; 20.
DR CORUM; P62881; -.
DR DIP; DIP-264N; -.
DR IntAct; P62881; 2.
DR STRING; 10090.ENSMUSP00000076155; -.
DR iPTMnet; P62881; -.
DR PhosphoSitePlus; P62881; -.
DR MaxQB; P62881; -.
DR PaxDb; P62881; -.
DR PeptideAtlas; P62881; -.
DR PRIDE; P62881; -.
DR ProteomicsDB; 271413; -.
DR ProteomicsDB; 271414; -. [P62881-2]
DR Antibodypedia; 24930; 309 antibodies from 32 providers.
DR DNASU; 14697; -.
DR Ensembl; ENSMUST00000076889; ENSMUSP00000076155; ENSMUSG00000032192. [P62881-1]
DR Ensembl; ENSMUST00000213990; ENSMUSP00000149938; ENSMUSG00000032192. [P62881-1]
DR Ensembl; ENSMUST00000215875; ENSMUSP00000150492; ENSMUSG00000032192. [P62881-2]
DR GeneID; 14697; -.
DR KEGG; mmu:14697; -.
DR UCSC; uc009qry.2; mouse.
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; 704786at2759; -.
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; 2 hits in 75 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 258 other tissues.
DR ExpressionAtlas; P62881; baseline and differential.
DR Genevisible; P62881; MM.
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:0051087; F:chaperone binding; ISS:CAFA.
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: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 GO; GO:0043547; P:positive regulation of GTPase activity; ISO:MGI.
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; 5.
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; 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
