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Protein

Synembryn

Gene

ric8a

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Guanine nucleotide exchange factor (GEF), which can activate some, but not all, G-alpha proteins independently of G-protein coupled receptors. Acts by exchanging bound GDP for free GTP. Plays a key role in asymmetric spindle positioning, a step for asymmetric cell division that generates cell diversity during development by activating G(i) alpha protein independently of G-protein coupled receptors. In addition to its GEF activity, it plays an essential role in cortical subcellular localization of heterotrimeric G proteins, suggesting it acts as a facilitator of G-alpha function through control of its membrane targeting and/or assembling of associated components rather than a GEF. Also required during gastrulation and sensory organ precursors (SOP) formation.3 Publications

GO - Molecular functioni

GO - Biological processi

  • asymmetric cell division Source: UniProtKB
  • asymmetric protein localization Source: UniProtKB
  • establishment of mitotic spindle localization Source: UniProtKB
  • establishment or maintenance of cell polarity Source: UniProtKB
  • gastrulation involving germ band extension Source: UniProtKB
  • G-protein coupled receptor signaling pathway Source: GO_Central
  • neuroblast division Source: UniProtKB
  • protein stabilization Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Guanine-nucleotide releasing factor

Keywords - Biological processi

Gastrulation

Names & Taxonomyi

Protein namesi
Recommended name:
Synembryn
Alternative name(s):
Protein Ric-8
Gene namesi
Name:ric8a
Synonyms:l(1)G0397, Ric8
ORF Names:CG15797
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome X

Organism-specific databases

FlyBaseiFBgn0028292. ric8a.

Subcellular locationi

GO - Cellular componenti

  • cell cortex Source: UniProtKB-SubCell
  • cytoplasm Source: UniProtKB
  • cytosol Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 573573SynembrynPRO_0000235905Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei477 – 4771Phosphoserine1 Publication
Modified residuei478 – 4781Phosphoserine1 Publication
Modified residuei480 – 4801Phosphoserine1 Publication
Modified residuei483 – 4831Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ9W358.

PTM databases

iPTMnetiQ9W358.

Expressioni

Tissue specificityi

Ubiquitous.1 Publication

Developmental stagei

Expressed both maternally and zygotically.1 Publication

Gene expression databases

BgeeiQ9W358.
ExpressionAtlasiQ9W358. differential.
GenevisibleiQ9W358. DM.

Interactioni

Subunit structurei

Interacts with GDP-bound G(i)-alpha protein G-i-alpha-65A. Does not interact with G-alpha proteins when they are in complex with subunits beta and gamma.2 Publications

GO - Molecular functioni

  • G-protein alpha-subunit binding Source: UniProtKB

Protein-protein interaction databases

BioGridi58324. 3 interactions.
IntActiQ9W358. 1 interaction.
MINTiMINT-876454.
STRINGi7227.FBpp0071252.

Structurei

3D structure databases

ProteinModelPortaliQ9W358.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the synembryn family.Curated

Phylogenomic databases

eggNOGiKOG4464. Eukaryota.
ENOG410XSCJ. LUCA.
InParanoidiQ9W358.
OMAiPMGMSPR.
OrthoDBiEOG72JWG4.
PhylomeDBiQ9W358.

Family and domain databases

InterProiIPR016024. ARM-type_fold.
IPR019318. Gua_nucleotide_exch_fac_Ric8.
IPR008376. Synembryn.
[Graphical view]
PfamiPF10165. Ric8. 1 hit.
[Graphical view]
PRINTSiPR01802. SYNEMBRYN.
SUPFAMiSSF48371. SSF48371. 3 hits.

Sequencei

Sequence statusi: Complete.

Q9W358-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
METEHLKRLE AKEADHIPAI LDEFNTKNAD LLVFDSFRTD NLWHELWLAI
60 70 80 90 100
FGILDDQRLS HLHTQCLNTV RILTRDEFSL QTNYIEQEVN TLLKLARIEA
110 120 130 140 150
GSLKLPATPD ELKQEEREEP QLEPSQAQSE VIAEALKCLC NLVYQSSDCR
160 170 180 190 200
RQCLRQHCLD AILKRVASSM RHPCALEYYD MKLLFLLTAL EPAARSRLQI
210 220 230 240 250
DLNGLTYMTK WLDDKLGEDS VGEEQLNIIC ELLKVMFNVT SAPDKSPNEY
260 270 280 290 300
EIQSLHLTGV LRELLLRFGD LATEKDRAVV THAINLLTNI SGSCLTELTL
310 320 330 340 350
RCSNAELESH KEREQDNEKE KDTEAGAGAK PRECCSQCFE KRNVRSLDVL
360 370 380 390 400
LRYLRQSLAQ QEAEASSHEL LSPVLTVLVK CARSDRVMRH YLRQEILPPL
410 420 430 440 450
RDVSQRPEVG QELRNHLCRF LTLPAMILRD LSAELLFVLC KENVGRMIKY
460 470 480 490 500
TGYGNAAGLF AKRGILDCRR VEGTDYSSDS EDSDTEEYKQ QQQGINPVLG
510 520 530 540 550
CVEPRSKSHL DDISEEQKEY EAMQLVNLIE QLRQGGIVKP AMIDKDGRPQ
560 570
PLEHILQLQE ELPQQQLDQK RKT
Length:573
Mass (Da):65,602
Last modified:June 1, 2003 - v2
Checksum:i1E9CF9EE90C957B2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014298 Genomic DNA. Translation: AAF46477.2.
BT004873 mRNA. Translation: AAO45229.1.
RefSeqiNP_001285048.1. NM_001298119.1.
NP_572550.2. NM_132322.4.
UniGeneiDm.6684.

Genome annotation databases

EnsemblMetazoaiFBtr0071317; FBpp0071252; FBgn0028292.
FBtr0346166; FBpp0311994; FBgn0028292.
GeneIDi31874.
KEGGidme:Dmel_CG15797.
UCSCiCG15797-RA. d. melanogaster.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014298 Genomic DNA. Translation: AAF46477.2.
BT004873 mRNA. Translation: AAO45229.1.
RefSeqiNP_001285048.1. NM_001298119.1.
NP_572550.2. NM_132322.4.
UniGeneiDm.6684.

3D structure databases

ProteinModelPortaliQ9W358.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi58324. 3 interactions.
IntActiQ9W358. 1 interaction.
MINTiMINT-876454.
STRINGi7227.FBpp0071252.

PTM databases

iPTMnetiQ9W358.

Proteomic databases

PaxDbiQ9W358.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0071317; FBpp0071252; FBgn0028292.
FBtr0346166; FBpp0311994; FBgn0028292.
GeneIDi31874.
KEGGidme:Dmel_CG15797.
UCSCiCG15797-RA. d. melanogaster.

Organism-specific databases

CTDi60626.
FlyBaseiFBgn0028292. ric8a.

Phylogenomic databases

eggNOGiKOG4464. Eukaryota.
ENOG410XSCJ. LUCA.
InParanoidiQ9W358.
OMAiPMGMSPR.
OrthoDBiEOG72JWG4.
PhylomeDBiQ9W358.

Miscellaneous databases

GenomeRNAii31874.
PROiQ9W358.

Gene expression databases

BgeeiQ9W358.
ExpressionAtlasiQ9W358. differential.
GenevisibleiQ9W358. DM.

Family and domain databases

InterProiIPR016024. ARM-type_fold.
IPR019318. Gua_nucleotide_exch_fac_Ric8.
IPR008376. Synembryn.
[Graphical view]
PfamiPF10165. Ric8. 1 hit.
[Graphical view]
PRINTSiPR01802. SYNEMBRYN.
SUPFAMiSSF48371. SSF48371. 3 hits.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  2. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Embryo.
  4. "Drosophila Ric-8 regulates Galphai cortical localization to promote Galphai-dependent planar orientation of the mitotic spindle during asymmetric cell division."
    David N.B., Martin C.A., Segalen M., Rosenfeld F., Schweisguth F., Bellaiche Y.
    Nat. Cell Biol. 7:1083-1090(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  5. "Ric-8 controls Drosophila neural progenitor asymmetric division by regulating heterotrimeric G proteins."
    Wang H., Ng K.H., Qian H., Siderovski D.P., Chia W., Yu F.
    Nat. Cell Biol. 7:1091-1098(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, INTERACTION WITH G-I-ALPHA-65A.
  6. "Drosophila Ric-8 is essential for plasma-membrane localization of heterotrimeric G proteins."
    Hampoelz B., Hoeller O., Bowman S.K., Dunican D., Knoblich J.A.
    Nat. Cell Biol. 7:1099-1105(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH G-I-ALPHA-65A.
  7. "Phosphoproteome analysis of Drosophila melanogaster embryos."
    Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.
    J. Proteome Res. 7:1675-1682(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-477; SER-478; SER-480 AND SER-483, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Embryo.

Entry informationi

Entry nameiRIC8_DROME
AccessioniPrimary (citable) accession number: Q9W358
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 16, 2006
Last sequence update: June 1, 2003
Last modified: July 6, 2016
This is version 109 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.