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Database: UniProt
Entry: P29829
LinkDB: P29829
Original site: P29829 
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
//
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