ID GBB2_DROME Reviewed; 346 AA.
AC P29829; Q9VW29;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2004, sequence version 3.
DT 27-MAR-2024, entry version 182.
DE RecName: Full=Guanine nucleotide-binding protein subunit beta-2;
GN Name=Gbeta76C;
GN Synonyms=Gb76C, Gbe {ECO:0000312|FlyBase:FBgn0004623},
GN Gbetae {ECO:0000312|FlyBase:FBgn0004623};
GN ORFNames=CG8770 {ECO:0000312|FlyBase:FBgn0004623};
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 [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC TISSUE=Eye;
RX PubMed=1910788; DOI=10.1016/0896-6273(91)90295-b;
RA Yarfitz S., Niemi G.A., McConnell J.L., Fitch C.L., Hurley J.B.;
RT "A G beta protein in the Drosophila compound eye is different from that in
RT the brain.";
RL Neuron 7:429-438(1991).
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=Head;
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 SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=10608815; DOI=10.1074/jbc.274.53.37605;
RA Schulz S., Huber A., Schwab K., Paulsen R.;
RT "A novel Ggamma isolated from Drosophila constitutes a visual G protein
RT gamma subunit of the fly compound eye.";
RL J. Biol. Chem. 274:37605-37610(1999).
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 Interacts with Ggamma30A/Guanine nucleotide-binding protein subunit
CC gamma-e (By similarity). {ECO:0000250|UniProtKB:Q9NFZ1}.
CC -!- INTERACTION:
CC P29829; Q9NFZ3: Ggamma30A; NbExp=2; IntAct=EBI-128499, EBI-2695634;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10608815}. Cell
CC projection, axon {ECO:0000269|PubMed:10608815}. Cell projection,
CC rhabdomere {ECO:0000269|PubMed:10608815}.
CC -!- TISSUE SPECIFICITY: Expressed exclusively in photoreceptor cells in the
CC compound eye (at protein level). {ECO:0000269|PubMed:10608815,
CC ECO:0000269|PubMed:1910788}.
CC -!- DEVELOPMENTAL STAGE: Expressed in adult heads but not in adult bodies
CC (PubMed:1910788). Not expressed in embryos, larvae or pupae
CC (PubMed:1910788). {ECO:0000269|PubMed:1910788}.
CC -!- SIMILARITY: Belongs to the WD repeat G protein beta family.
CC {ECO:0000305}.
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DR EMBL; M76593; AAA73103.1; -; mRNA.
DR EMBL; AE014296; AAF49124.1; -; Genomic_DNA.
DR EMBL; AY118886; AAM50746.1; -; mRNA.
DR PIR; JU0269; RGFFB.
DR RefSeq; NP_523720.2; NM_078996.3.
DR AlphaFoldDB; P29829; -.
DR SMR; P29829; -.
DR BioGRID; 65418; 6.
DR IntAct; P29829; 5.
DR STRING; 7227.FBpp0074717; -.
DR PaxDb; 7227-FBpp0074717; -.
DR DNASU; 40148; -.
DR EnsemblMetazoa; FBtr0074949; FBpp0074717; FBgn0004623.
DR GeneID; 40148; -.
DR KEGG; dme:Dmel_CG8770; -.
DR AGR; FB:FBgn0004623; -.
DR CTD; 40148; -.
DR FlyBase; FBgn0004623; Gbeta76C.
DR VEuPathDB; VectorBase:FBgn0004623; -.
DR eggNOG; KOG0286; Eukaryota.
DR GeneTree; ENSGT01000000214413; -.
DR HOGENOM; CLU_000288_57_34_1; -.
DR InParanoid; P29829; -.
DR OMA; NSVCYHP; -.
DR OrthoDB; 102097at2759; -.
DR PhylomeDB; P29829; -.
DR Reactome; R-DME-1296041; Activation of G protein gated Potassium channels.
DR Reactome; R-DME-4086398; Ca2+ pathway.
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-6814122; Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding.
DR Reactome; R-DME-8964616; G beta:gamma signalling through CDC42.
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; 40148; 0 hits in 1 CRISPR screen.
DR ChiTaRS; Gbeta76C; fly.
DR GenomeRNAi; 40148; -.
DR PRO; PR:P29829; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0004623; Expressed in head capsule and 10 other cell types or tissues.
DR Genevisible; P29829; DM.
DR GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR GO; GO:0005834; C:heterotrimeric G-protein complex; IDA:FlyBase.
DR GO; GO:0016028; C:rhabdomere; IDA:FlyBase.
DR GO; GO:0016004; F:phospholipase activator activity; IMP:FlyBase.
DR GO; GO:0046982; F:protein heterodimerization activity; IPI:FlyBase.
DR GO; GO:0030159; F:signaling receptor complex adaptor activity; IBA:GO_Central.
DR GO; GO:0016059; P:deactivation of rhodopsin mediated signaling; IMP:FlyBase.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IDA:FlyBase.
DR GO; GO:0045879; P:negative regulation of smoothened signaling pathway; IGI:FlyBase.
DR GO; GO:0007602; P:phototransduction; IDA:FlyBase.
DR GO; GO:0016056; P:rhodopsin mediated signaling pathway; IMP:FlyBase.
DR GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
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; 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:SF43; GUANINE NUCLEOTIDE-BINDING PROTEIN SUBUNIT BETA-2; 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; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 4.
DR PROSITE; PS50294; WD_REPEATS_REGION; 3.
PE 1: Evidence at protein level;
KW Cell projection; Cytoplasm; Reference proteome; Repeat;
KW Sensory transduction; Transducer; Vision; WD repeat.
FT CHAIN 1..346
FT /note="Guanine nucleotide-binding protein subunit beta-2"
FT /id="PRO_0000127716"
FT REPEAT 57..96
FT /note="WD 1"
FT /evidence="ECO:0000255"
FT REPEAT 99..138
FT /note="WD 2"
FT /evidence="ECO:0000255"
FT REPEAT 147..185
FT /note="WD 3"
FT /evidence="ECO:0000255"
FT REPEAT 188..227
FT /note="WD 4"
FT /evidence="ECO:0000255"
FT REPEAT 230..269
FT /note="WD 5"
FT /evidence="ECO:0000255"
FT REPEAT 274..313
FT /note="WD 6"
FT /evidence="ECO:0000255"
FT REPEAT 316..346
FT /note="WD 7"
FT /evidence="ECO:0000255"
FT CONFLICT 116
FT /note="V -> E (in Ref. 1; AAA73103)"
FT /evidence="ECO:0000305"
FT CONFLICT 136
FT /note="S -> P (in Ref. 1; AAA73103)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 346 AA; 38336 MW; E9B22D937EC3A707 CRC64;
MPKIDPETQK LYDEINGMIQ KFKDDQKSKA DCTLADKCGD MGDVPKIRFS SKKILKGHIN
KVNSVHFAGD SRHCVTGSLD GKLIIWDTWT ANKVQIIPLR SAWVMTVAFS PSGNFVACGG
MDNQCTVYDV NNRDASGVAK MVKELMGYEG FLSSCRFLDD GHLITGSGDM KICHWDLEKG
VKTMDFNGHA GDIAGLSLSP DMKTYITGSV DKTAKLWDVR EEGHKQMFFG HDMDVSSVCY
HPSGFGFASC SEDQTARMYD LRADQQIAQY EPPQKNTGFT SCALSTSGRY LMCGGIEGNV
HSWDTMKQRH TGTLSGHENR ITCISLCPNG MCLASTSWDQ QVRLWL
//