RIC8_DROME
ID RIC8_DROME Reviewed; 573 AA.
AC Q9W358;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 2.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Synembryn;
DE AltName: Full=Protein Ric-8;
GN Name=ric8a; Synonyms=l(1)G0397, Ric8; ORFNames=CG15797;
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 [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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M.,
RA Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A.,
RA Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A.,
RA Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S.,
RA Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.;
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=16228010; DOI=10.1038/ncb1319;
RA David N.B., Martin C.A., Segalen M., Rosenfeld F., Schweisguth F.,
RA Bellaiche Y.;
RT "Drosophila Ric-8 regulates Galphai cortical localization to promote
RT Galphai-dependent planar orientation of the mitotic spindle during
RT asymmetric cell division.";
RL Nat. Cell Biol. 7:1083-1090(2005).
RN [5]
RP FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND INTERACTION WITH
RP G-I-ALPHA-65A.
RX PubMed=16228012; DOI=10.1038/ncb1317;
RA Wang H., Ng K.H., Qian H., Siderovski D.P., Chia W., Yu F.;
RT "Ric-8 controls Drosophila neural progenitor asymmetric division by
RT regulating heterotrimeric G proteins.";
RL Nat. Cell Biol. 7:1091-1098(2005).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH G-I-ALPHA-65A.
RX PubMed=16228011; DOI=10.1038/ncb1318;
RA Hampoelz B., Hoeller O., Bowman S.K., Dunican D., Knoblich J.A.;
RT "Drosophila Ric-8 is essential for plasma-membrane localization of
RT heterotrimeric G proteins.";
RL Nat. Cell Biol. 7:1099-1105(2005).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-477; SER-478; SER-480 AND
RP SER-483, AND IDENTIFICATION BY 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 exchange factor (GEF), which can activate
CC some, but not all, G-alpha proteins independently of G-protein coupled
CC receptors. Acts by exchanging bound GDP for free GTP. Plays a key role
CC in asymmetric spindle positioning, a step for asymmetric cell division
CC that generates cell diversity during development by activating G(i)
CC alpha protein independently of G-protein coupled receptors. In addition
CC to its GEF activity, it plays an essential role in cortical subcellular
CC localization of heterotrimeric G proteins, suggesting it acts as a
CC facilitator of G-alpha function through control of its membrane
CC targeting and/or assembling of associated components rather than a GEF.
CC Also required during gastrulation and sensory organ precursors (SOP)
CC formation. {ECO:0000269|PubMed:16228010, ECO:0000269|PubMed:16228011,
CC ECO:0000269|PubMed:16228012}.
CC -!- SUBUNIT: Interacts with GDP-bound G(i)-alpha protein G-i-alpha-65A.
CC Does not interact with G-alpha proteins when they are in complex with
CC subunits beta and gamma. {ECO:0000269|PubMed:16228011,
CC ECO:0000269|PubMed:16228012}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cell cortex
CC {ECO:0000269|PubMed:16228010, ECO:0000269|PubMed:16228011}.
CC Note=Localizes to the cell cortex.
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:16228012}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC {ECO:0000269|PubMed:16228012}.
CC -!- SIMILARITY: Belongs to the synembryn family. {ECO:0000305}.
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DR EMBL; AE014298; AAF46477.2; -; Genomic_DNA.
DR EMBL; BT004873; AAO45229.1; -; mRNA.
DR RefSeq; NP_001285048.1; NM_001298119.1.
DR RefSeq; NP_572550.2; NM_132322.4.
DR AlphaFoldDB; Q9W358; -.
DR SMR; Q9W358; -.
DR BioGRID; 58324; 7.
DR IntAct; Q9W358; 1.
DR STRING; 7227.FBpp0071252; -.
DR iPTMnet; Q9W358; -.
DR PaxDb; Q9W358; -.
DR PRIDE; Q9W358; -.
DR EnsemblMetazoa; FBtr0071317; FBpp0071252; FBgn0028292.
DR EnsemblMetazoa; FBtr0346166; FBpp0311994; FBgn0028292.
DR GeneID; 31874; -.
DR KEGG; dme:Dmel_CG15797; -.
DR UCSC; CG15797-RA; d. melanogaster.
DR CTD; 60626; -.
DR FlyBase; FBgn0028292; ric8a.
DR VEuPathDB; VectorBase:FBgn0028292; -.
DR eggNOG; KOG4464; Eukaryota.
DR HOGENOM; CLU_018602_1_0_1; -.
DR InParanoid; Q9W358; -.
DR OMA; NADPIFT; -.
DR OrthoDB; 1110075at2759; -.
DR PhylomeDB; Q9W358; -.
DR SignaLink; Q9W358; -.
DR BioGRID-ORCS; 31874; 1 hit in 3 CRISPR screens.
DR GenomeRNAi; 31874; -.
DR PRO; PR:Q9W358; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0028292; Expressed in egg cell and 23 other tissues.
DR ExpressionAtlas; Q9W358; baseline and differential.
DR Genevisible; Q9W358; DM.
DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0001965; F:G-protein alpha-subunit binding; IPI:UniProtKB.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; ISS:UniProtKB.
DR GO; GO:0008356; P:asymmetric cell division; IMP:UniProtKB.
DR GO; GO:0040001; P:establishment of mitotic spindle localization; IMP:UniProtKB.
DR GO; GO:0007163; P:establishment or maintenance of cell polarity; IMP:UniProtKB.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0010004; P:gastrulation involving germ band extension; IMP:UniProtKB.
DR GO; GO:0055057; P:neuroblast division; IMP:UniProtKB.
DR GO; GO:0008104; P:protein localization; IMP:UniProtKB.
DR GO; GO:0050821; P:protein stabilization; IMP:UniProtKB.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR019318; Gua_nucleotide_exch_fac_Ric8.
DR InterPro; IPR008376; Synembryn.
DR PANTHER; PTHR12425; PTHR12425; 1.
DR Pfam; PF10165; Ric8; 1.
DR PRINTS; PR01802; SYNEMBRYN.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Developmental protein; Gastrulation;
KW Guanine-nucleotide releasing factor; Phosphoprotein; Reference proteome.
FT CHAIN 1..573
FT /note="Synembryn"
FT /id="PRO_0000235905"
FT REGION 308..329
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 473..493
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 308..328
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 473..488
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 477
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 478
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 480
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 483
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
SQ SEQUENCE 573 AA; 65602 MW; 1E9CF9EE90C957B2 CRC64;
METEHLKRLE AKEADHIPAI LDEFNTKNAD LLVFDSFRTD NLWHELWLAI FGILDDQRLS
HLHTQCLNTV RILTRDEFSL QTNYIEQEVN TLLKLARIEA GSLKLPATPD ELKQEEREEP
QLEPSQAQSE VIAEALKCLC NLVYQSSDCR RQCLRQHCLD AILKRVASSM RHPCALEYYD
MKLLFLLTAL EPAARSRLQI DLNGLTYMTK WLDDKLGEDS VGEEQLNIIC ELLKVMFNVT
SAPDKSPNEY EIQSLHLTGV LRELLLRFGD LATEKDRAVV THAINLLTNI SGSCLTELTL
RCSNAELESH KEREQDNEKE KDTEAGAGAK PRECCSQCFE KRNVRSLDVL LRYLRQSLAQ
QEAEASSHEL LSPVLTVLVK CARSDRVMRH YLRQEILPPL RDVSQRPEVG QELRNHLCRF
LTLPAMILRD LSAELLFVLC KENVGRMIKY TGYGNAAGLF AKRGILDCRR VEGTDYSSDS
EDSDTEEYKQ QQQGINPVLG CVEPRSKSHL DDISEEQKEY EAMQLVNLIE QLRQGGIVKP
AMIDKDGRPQ PLEHILQLQE ELPQQQLDQK RKT
