GNB5_RAT
ID GNB5_RAT Reviewed; 353 AA.
AC P62882; O35354; P54314; Q5FWS8; Q91WB3;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 112.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RA Levay K., Slepak V.Z.;
RL Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
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 5 subunit.";
RL Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 11-198, AND TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RX PubMed=9622245; DOI=10.1016/s0306-4522(97)00623-4;
RA Betty M., Harnish S.W., Rhodes K.J., Cockett M.I.;
RT "Distribution of heterotrimeric G-protein beta and gamma subunits in the
RT rat brain.";
RL Neuroscience 85:475-486(1998).
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). Interacts with RGS6 and RGS7 (By similarity).
CC {ECO:0000250|UniProtKB:O14775, ECO:0000250|UniProtKB:P62881}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:P62881}.
CC -!- TISSUE SPECIFICITY: Detected in brain. {ECO:0000269|PubMed:9622245}.
CC -!- SIMILARITY: Belongs to the WD repeat G protein beta family.
CC {ECO:0000305}.
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DR EMBL; AF001953; AAB59974.1; -; mRNA.
DR EMBL; AY552803; AAS59141.1; -; mRNA.
DR EMBL; BC089221; AAH89221.1; -; mRNA.
DR EMBL; AF022086; AAB82553.1; -; mRNA.
DR RefSeq; NP_113958.1; NM_031770.3.
DR AlphaFoldDB; P62882; -.
DR SMR; P62882; -.
DR BioGRID; 249765; 1.
DR CORUM; P62882; -.
DR IntAct; P62882; 2.
DR MINT; P62882; -.
DR STRING; 10116.ENSRNOP00000066690; -.
DR PhosphoSitePlus; P62882; -.
DR jPOST; P62882; -.
DR PaxDb; P62882; -.
DR PRIDE; P62882; -.
DR GeneID; 83579; -.
DR KEGG; rno:83579; -.
DR UCSC; RGD:620759; rat.
DR CTD; 10681; -.
DR RGD; 620759; Gnb5.
DR eggNOG; KOG0286; Eukaryota.
DR InParanoid; P62882; -.
DR OrthoDB; 704786at2759; -.
DR PhylomeDB; P62882; -.
DR Reactome; R-RNO-1296041; Activation of G protein gated Potassium channels.
DR Reactome; R-RNO-202040; G-protein activation.
DR Reactome; R-RNO-2514859; Inactivation, recovery and regulation of the phototransduction cascade.
DR Reactome; R-RNO-381676; Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
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-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-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-6814122; Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding.
DR Reactome; R-RNO-8964616; G beta:gamma signalling through CDC42.
DR Reactome; R-RNO-997272; Inhibition of voltage gated Ca2+ channels via Gbeta/gamma subunits.
DR PRO; PR:P62882; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0044297; C:cell body; IDA:RGD.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0005834; C:heterotrimeric G-protein complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0098793; C:presynapse; ISO:RGD.
DR GO; GO:0032991; C:protein-containing complex; IDA:RGD.
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; IPI:RGD.
DR GO; GO:0005096; F:GTPase activator activity; ISO:RGD.
DR GO; GO:0030159; F:signaling receptor complex adaptor activity; IBA:GO_Central.
DR GO; GO:1990603; P:dark adaptation; ISO:RGD.
DR GO; GO:0007212; P:dopamine receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISO:RGD.
DR GO; GO:0036367; P:light adaption; ISO:RGD.
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:RGD.
DR GO; GO:0007165; P:signal transduction; TAS:RGD.
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 2: Evidence at transcript level;
KW Membrane; Reference proteome; Repeat; Transducer; WD repeat.
FT CHAIN 1..353
FT /note="Guanine nucleotide-binding protein subunit beta-5"
FT /id="PRO_0000127709"
FT REPEAT 61..100
FT /note="WD 1"
FT REPEAT 103..142
FT /note="WD 2"
FT REPEAT 151..192
FT /note="WD 3"
FT REPEAT 194..236
FT /note="WD 4"
FT REPEAT 237..276
FT /note="WD 5"
FT REPEAT 278..320
FT /note="WD 6"
FT REPEAT 323..352
FT /note="WD 7"
SQ SEQUENCE 353 AA; 38732 MW; 30FCF51C125A024D CRC64;
MATDGLHENE TLASLKSEAE SLKGKLEEER AKLHDVELHQ VAERVEALGQ FVMKTRRTLK
GHGNKVLCMD WCKDKRRIVS SSQDGKVIVW DSFTTNKEHA VTMPCTWVMA CAYAPSGCAI
ACGGLDNKCS VYPLTFDKNE NMAAKKKSVA MHTNYLSACS FTNSDMQILT ASGDGTCALW
DVESGQLLQS FHGHGADVLC LDLAPSETGN TFVSGGCDKK AMVWDMRSGQ CVQAFETHES
DVNSVRYYPS GDAFASGSDD ATCRLYDLRA DREVAIYSKE SIIFGASSVD FSLSGRLLFA
GYNDYTINVW DVLKGSRVSI LFGHENRVST LRVSPDGTAF CSGSWDHTLR VWA
