GBB4_MOUSE
ID GBB4_MOUSE Reviewed; 340 AA.
AC P29387; Q3TJJ1; Q8R475; Q9JHX8;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Guanine nucleotide-binding protein subunit beta-4;
DE AltName: Full=Transducin beta chain 4;
GN Name=Gnb4;
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].
RX PubMed=1543505; DOI=10.1016/0006-291x(92)91650-f;
RA von Weizsaecker E., Strathmann M.P., Simon M.I.;
RT "Diversity among the beta subunits of heterotrimeric GTP-binding proteins:
RT characterization of a novel beta-subunit cDNA.";
RL Biochem. Biophys. Res. Commun. 183:350-356(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=10970423; DOI=10.1111/j.1469-7793.2000.00203.x;
RA Arnot M.I., Stotz S.C., Jarvis S.E., Zamponi G.W.;
RT "Differential modulation of N-type 1B and P/Q-type 1A calcium channels by
RT different G protein subunit isoforms.";
RL J. Physiol. (Lond.) 527:203-212(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J;
RX PubMed=11842130; DOI=10.1152/physiolgenomics.00085.2001;
RA Ruiz-Velasco V., Ikeda S.R., Puhl H.L. III;
RT "Cloning, tissue distribution, and functional expression of the human G
RT protein beta 4-subunit.";
RL Physiol. Genomics 8:41-50(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Bone marrow, Placenta, and Vagina;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Mammary gland;
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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Lung, Pancreas, and Spleen;
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).
CC -!- FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved
CC as a modulator or transducer in various transmembrane signaling
CC systems. The beta and gamma chains are required for the GTPase
CC activity, for replacement of GDP by GTP, and for G protein-effector
CC interaction.
CC -!- SUBUNIT: G proteins are composed of 3 units, alpha, beta and gamma.
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; S86124; AAB21609.1; -; mRNA.
DR EMBL; M87286; AAA37756.1; -; mRNA.
DR EMBL; M63658; AAA37664.1; -; mRNA.
DR EMBL; AF277893; AAF82124.1; -; mRNA.
DR EMBL; AF501886; AAM15922.1; -; mRNA.
DR EMBL; AK036816; BAC29589.1; -; mRNA.
DR EMBL; AK152227; BAE31054.1; -; mRNA.
DR EMBL; AK167416; BAE39504.1; -; mRNA.
DR EMBL; BC028753; AAH28753.1; -; mRNA.
DR CCDS; CCDS17297.1; -.
DR PIR; JS0669; RGMSB4.
DR RefSeq; NP_001334991.1; NM_001348062.1.
DR RefSeq; NP_001335033.1; NM_001348104.1.
DR RefSeq; NP_038559.2; NM_013531.5.
DR RefSeq; XP_006535466.1; XM_006535403.3.
DR AlphaFoldDB; P29387; -.
DR SMR; P29387; -.
DR BioGRID; 199980; 2.
DR DIP; DIP-604N; -.
DR IntAct; P29387; 1.
DR STRING; 10090.ENSMUSP00000121127; -.
DR iPTMnet; P29387; -.
DR PhosphoSitePlus; P29387; -.
DR SwissPalm; P29387; -.
DR REPRODUCTION-2DPAGE; P29387; -.
DR EPD; P29387; -.
DR jPOST; P29387; -.
DR MaxQB; P29387; -.
DR PaxDb; P29387; -.
DR PeptideAtlas; P29387; -.
DR PRIDE; P29387; -.
DR ProteomicsDB; 265730; -.
DR Antibodypedia; 18788; 171 antibodies from 25 providers.
DR DNASU; 14696; -.
DR Ensembl; ENSMUST00000108234; ENSMUSP00000103869; ENSMUSG00000027669.
DR Ensembl; ENSMUST00000155737; ENSMUSP00000121127; ENSMUSG00000027669.
DR GeneID; 14696; -.
DR KEGG; mmu:14696; -.
DR UCSC; uc008owl.1; mouse.
DR CTD; 59345; -.
DR MGI; MGI:104581; Gnb4.
DR VEuPathDB; HostDB:ENSMUSG00000027669; -.
DR eggNOG; KOG0286; Eukaryota.
DR GeneTree; ENSGT01000000214413; -.
DR HOGENOM; CLU_000288_57_34_1; -.
DR InParanoid; P29387; -.
DR OMA; GDTNCAL; -.
DR OrthoDB; 704786at2759; -.
DR PhylomeDB; P29387; -.
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-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; 14696; 2 hits in 71 CRISPR screens.
DR ChiTaRS; Gnb4; mouse.
DR PRO; PR:P29387; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; P29387; protein.
DR Bgee; ENSMUSG00000027669; Expressed in semi-lunar valve and 259 other tissues.
DR ExpressionAtlas; P29387; baseline and differential.
DR Genevisible; P29387; MM.
DR GO; GO:0044297; C:cell body; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005834; C:heterotrimeric G-protein complex; IPI:MGI.
DR GO; GO:0043209; C:myelin sheath; HDA:UniProtKB.
DR GO; GO:0003924; F:GTPase activity; ISA:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0030159; F:signaling receptor complex adaptor activity; IBA:GO_Central.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
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; 7.
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 Acetylation; Phosphoprotein; Reference proteome; Repeat; Transducer;
KW WD repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9HAV0"
FT CHAIN 2..340
FT /note="Guanine nucleotide-binding protein subunit beta-4"
FT /id="PRO_0000127703"
FT REPEAT 53..92
FT /note="WD 1"
FT REPEAT 95..134
FT /note="WD 2"
FT REPEAT 141..179
FT /note="WD 3"
FT REPEAT 182..221
FT /note="WD 4"
FT REPEAT 224..263
FT /note="WD 5"
FT REPEAT 268..307
FT /note="WD 6"
FT REPEAT 310..339
FT /note="WD 7"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HAV0"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P62873"
FT MOD_RES 266
FT /note="Phosphohistidine"
FT /evidence="ECO:0000250|UniProtKB:P62871"
FT CONFLICT 132
FT /note="N -> D (in Ref. 1; AAB21609/AAA37756/AAA37664)"
FT /evidence="ECO:0000305"
FT CONFLICT 140
FT /note="P -> A (in Ref. 1; AAB21609/AAA37756/AAA37664)"
FT /evidence="ECO:0000305"
FT CONFLICT 238
FT /note="G -> V (in Ref. 3; AAM15922)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 340 AA; 37379 MW; F06827EBC2F0E966 CRC64;
MSELEQLRQE AEQLRNQIQD ARKACNDATL VQITSNMDSV GRIQMRTRRT LRGHLAKIYA
MHWGYDSRLL VSASQDGKLI IWDSYTTNKM HAIPLRSSWV MTCAYAPSGN YVACGGLDNI
CSIYNLKTRE GNVRVSRELP GHTGYLSCCR FLDDGQIITS SGDTTCALWD IETGQQTTTF
TGHSGDVMSL SLSPDLKTFV SGACDASSKL WDIRDGMCRQ SFTGHISDIN AVSFFPSGYA
FATGSDDATC RLFDLRADQE LLLYSHDNII CGITSVAFSK SGRLLLAGYD DFNCSVWDAL
KGGRSGVLAG HDNRVSCLGV TDDGMAVATG SWDSFLRIWN
