GBB1_DROME
ID GBB1_DROME Reviewed; 340 AA.
AC P26308; Q9VXM8;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=Guanine nucleotide-binding protein subunit beta-1;
GN Name=Gbeta13F; Synonyms=Gb13F; ORFNames=CG10545;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RC STRAIN=Canton-S;
RX PubMed=3140235; DOI=10.1073/pnas.85.19.7134;
RA Yarfitz S., Provost N.M., Hurley J.B.;
RT "Cloning of a Drosophila melanogaster guanine nucleotide regulatory protein
RT beta-subunit gene and characterization of its expression during
RT development.";
RL Proc. Natl. Acad. Sci. U.S.A. 85:7134-7138(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
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 -!- TISSUE SPECIFICITY: In adults, expression is higher in the head than in
CC the body. {ECO:0000269|PubMed:3140235}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout development.
CC {ECO:0000269|PubMed:3140235}.
CC -!- SIMILARITY: Belongs to the WD repeat G protein beta family.
CC {ECO:0000305}.
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DR EMBL; M22567; AAB59247.1; -; Genomic_DNA.
DR EMBL; AE014298; AAF48530.1; -; Genomic_DNA.
DR EMBL; AY058566; AAL13795.1; -; mRNA.
DR PIR; A40489; RGFFBH.
DR RefSeq; NP_001303567.1; NM_001316638.2.
DR RefSeq; NP_525090.1; NM_080351.7.
DR RefSeq; NP_996459.1; NM_206736.2.
DR RefSeq; NP_996460.1; NM_206737.2.
DR RefSeq; NP_996461.1; NM_206738.3.
DR RefSeq; NP_996462.1; NM_206739.2.
DR AlphaFoldDB; P26308; -.
DR SMR; P26308; -.
DR BioGRID; 58892; 10.
DR DIP; DIP-18432N; -.
DR IntAct; P26308; 1.
DR STRING; 7227.FBpp0089182; -.
DR iPTMnet; P26308; -.
DR PaxDb; P26308; -.
DR PRIDE; P26308; -.
DR DNASU; 32544; -.
DR EnsemblMetazoa; FBtr0074107; FBpp0073921; FBgn0001105.
DR EnsemblMetazoa; FBtr0074108; FBpp0089182; FBgn0001105.
DR EnsemblMetazoa; FBtr0074110; FBpp0089184; FBgn0001105.
DR EnsemblMetazoa; FBtr0074111; FBpp0089185; FBgn0001105.
DR EnsemblMetazoa; FBtr0331597; FBpp0303987; FBgn0001105.
DR EnsemblMetazoa; FBtr0346794; FBpp0312372; FBgn0001105.
DR GeneID; 32544; -.
DR KEGG; dme:Dmel_CG10545; -.
DR CTD; 32544; -.
DR FlyBase; FBgn0001105; Gbeta13F.
DR VEuPathDB; VectorBase:FBgn0001105; -.
DR eggNOG; KOG0286; Eukaryota.
DR GeneTree; ENSGT01000000214413; -.
DR HOGENOM; CLU_000288_57_34_1; -.
DR InParanoid; P26308; -.
DR OMA; PLDSQWV; -.
DR OrthoDB; 704786at2759; -.
DR PhylomeDB; P26308; -.
DR Reactome; R-DME-1296041; Activation of G protein gated Potassium channels.
DR Reactome; R-DME-202040; G-protein activation.
DR Reactome; R-DME-2485179; Activation of the phototransduction cascade.
DR Reactome; R-DME-381753; Olfactory Signaling Pathway.
DR Reactome; R-DME-392170; ADP signalling through P2Y purinoceptor 12.
DR Reactome; R-DME-392451; G beta:gamma signalling through PI3Kgamma.
DR Reactome; R-DME-392851; Prostacyclin signalling through prostacyclin receptor.
DR Reactome; R-DME-400042; Adrenaline,noradrenaline inhibits insulin secretion.
DR Reactome; R-DME-4086398; Ca2+ pathway.
DR Reactome; R-DME-416476; G alpha (q) signalling events.
DR Reactome; R-DME-416482; G alpha (12/13) signalling events.
DR Reactome; R-DME-418217; G beta:gamma signalling through PLC beta.
DR Reactome; R-DME-418555; G alpha (s) signalling events.
DR Reactome; R-DME-418594; G alpha (i) signalling events.
DR Reactome; R-DME-418597; G alpha (z) signalling events.
DR Reactome; R-DME-428930; Thromboxane signalling through TP receptor.
DR Reactome; R-DME-500657; Presynaptic function of Kainate receptors.
DR Reactome; R-DME-6814122; Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding.
DR Reactome; R-DME-8964315; G beta:gamma signalling through BTK.
DR Reactome; R-DME-8964616; G beta:gamma signalling through CDC42.
DR Reactome; R-DME-9009391; Extra-nuclear estrogen signaling.
DR Reactome; R-DME-9717207; Sensory perception of sweet, bitter, and umami (glutamate) taste.
DR Reactome; R-DME-997272; Inhibition of voltage gated Ca2+ channels via Gbeta/gamma subunits.
DR BioGRID-ORCS; 32544; 0 hits in 1 CRISPR screen.
DR ChiTaRS; Gbeta13F; fly.
DR GenomeRNAi; 32544; -.
DR PRO; PR:P26308; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0001105; Expressed in eye disc (Drosophila) and 42 other tissues.
DR ExpressionAtlas; P26308; baseline and differential.
DR Genevisible; P26308; DM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005834; C:heterotrimeric G-protein complex; IDA:FlyBase.
DR GO; GO:0005886; C:plasma membrane; IDA:FlyBase.
DR GO; GO:0030159; F:signaling receptor complex adaptor activity; IBA:GO_Central.
DR GO; GO:0045176; P:apical protein localization; TAS:FlyBase.
DR GO; GO:0055059; P:asymmetric neuroblast division; IMP:FlyBase.
DR GO; GO:0061343; P:cell adhesion involved in heart morphogenesis; IMP:FlyBase.
DR GO; GO:0060027; P:convergent extension involved in gastrulation; IMP:FlyBase.
DR GO; GO:0003380; P:establishment or maintenance of cytoskeleton polarity involved in gastrulation; IMP:FlyBase.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IDA:FlyBase.
DR GO; GO:0048383; P:mesectoderm development; IMP:FlyBase.
DR GO; GO:0045879; P:negative regulation of smoothened signaling pathway; IGI:FlyBase.
DR GO; GO:0010470; P:regulation of gastrulation; IMP:FlyBase.
DR GO; GO:0043519; P:regulation of myosin II filament organization; IMP:FlyBase.
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; 6.
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 Phosphoprotein; Reference proteome; Repeat; Transducer; WD repeat.
FT CHAIN 1..340
FT /note="Guanine nucleotide-binding protein subunit beta-1"
FT /id="PRO_0000127715"
FT REPEAT 53..83
FT /note="WD 1"
FT REPEAT 95..125
FT /note="WD 2"
FT REPEAT 141..170
FT /note="WD 3"
FT REPEAT 182..212
FT /note="WD 4"
FT REPEAT 224..254
FT /note="WD 5"
FT REPEAT 268..298
FT /note="WD 6"
FT REPEAT 310..340
FT /note="WD 7"
FT MOD_RES 29
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
SQ SEQUENCE 340 AA; 37133 MW; 5A4B70DCB0A1C32C CRC64;
MNELDSLRQE AESLKNAIRD ARKAACDTSL LQAATSLEPI GRIQMRTRRT LRGHLAKIYA
MHWGNDSRNL VSASQDGKLI VWDSHTTNKV HAIPLRSSWV MTCAYAPSGS YVACGGLDNM
CSIYNLKTRE GNVRVSRELP GHGGYLSCCR FLDDNQIVTS SGDMSCGLWD IETGLQVTSF
LGHTGDVMAL SLAPQCKTFV SGACDASAKL WDIREGVCKQ TFPGHESDIN AVTFFPNGQA
FATGSDDATC RLFDIRADQE LAMYSHDNII CGITSVAFSK SGRLLLAGYD DFNCNVWDTM
KAERSGILAG HDNRVSCLGV TENGMAVATG SWDSFLRVWN
