Full text data of RIC8A
RIC8A
[Confidence: low (only semi-automatic identification from reviews)]
Synembryn-A (Protein Ric-8A)
Synembryn-A (Protein Ric-8A)
UniProt
Q9NPQ8
ID RIC8A_HUMAN Reviewed; 531 AA.
AC Q9NPQ8; Q0P508; Q2T9J1; Q7Z352; Q96EZ1; Q96SZ2; Q9H064; Q9H5H3;
read moreAC Q9H9E7;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 3.
DT 22-JAN-2014, entry version 86.
DE RecName: Full=Synembryn-A;
DE AltName: Full=Protein Ric-8A;
GN Name=RIC8A;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Uterus;
RX PubMed=11230166; DOI=10.1101/gr.GR1547R;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H.,
RA Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N.,
RA Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D.,
RA Wambutt R., Korn B., Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and
RT analysis of 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Teratocarcinoma;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RG The European IMAGE consortium;
RL Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Uterine endothelium;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
RA Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
RA FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
RA Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
RA Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
RA Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=Lymph, and Uterus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [8]
RP FUNCTION.
RX PubMed=16629901; DOI=10.1111/j.1365-2443.2006.00959.x;
RA Nishimura A., Okamoto M., Sugawara Y., Mizuno N., Yamauchi J.,
RA Itoh H.;
RT "Ric-8A potentiates Gq-mediated signal transduction by acting
RT downstream of G protein-coupled receptor in intact cells.";
RL Genes Cells 11:487-498(2006).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
RA Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
RA Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-436; THR-441; SER-523;
RP SER-524 AND SER-528, AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18318008; DOI=10.1002/pmic.200700884;
RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
RA Zou H., Gu J.;
RT "Large-scale phosphoproteome analysis of human liver tissue by
RT enrichment and fractionation of phosphopeptides with strong anion
RT exchange chromatography.";
RL Proteomics 8:1346-1361(2008).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-436 AND THR-441, AND
RP MASS SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-436; THR-441 AND
RP SER-502, AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-502, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
CC -!- FUNCTION: Guanine nucleotide exchange factor (GEF), which can
CC activate some, but not all, G-alpha proteins. Able to activate
CC GNAI1, GNAO1 and GNAQ, but not GNAS by exchanging bound GDP for
CC free GTP. Involved in regulation of microtubule pulling forces
CC during mitotic movement of chromosomes by stimulating G(i)-alpha
CC protein, possibly leading to release G(i)-alpha-GTP and NuMA
CC proteins from the NuMA-GPSM2-G(i)-alpha-GDP complex (By
CC similarity). Also acts as an activator for G(q)-alpha (GNAQ)
CC protein by enhancing the G(q)-coupled receptor-mediated ERK
CC activation.
CC -!- SUBUNIT: Interacts with GDP-bound G alpha proteins GNAI1, GNAO1
CC and GNAQ, and with GNA13 with lower affinity. Does not interact
CC with G-alpha proteins when they are in complex with subunits beta
CC and gamma. Interacts (via C-terminus) with RGS14; the interaction
CC stimulates the dissociation of the complex between RGS14 and the
CC active GTP-bound form of GNAI1 (By similarity).
CC -!- INTERACTION:
CC Q9UMX0:UBQLN1; NbExp=3; IntAct=EBI-717509, EBI-741480;
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Cell membrane (By
CC similarity). Note=Colocalizes with RIC8A in CA2 hippocampal
CC neurons. Colocalizes with GNAI1 and RGS14 at the plasma membrane
CC (By similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q9NPQ8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NPQ8-2; Sequence=VSP_018507;
CC Name=3;
CC IsoId=Q9NPQ8-3; Sequence=VSP_018508;
CC Name=4;
CC IsoId=Q9NPQ8-4; Sequence=VSP_039849;
CC -!- SIMILARITY: Belongs to the synembryn family.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB14282.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=BAB14282.1; Type=Frameshift; Positions=397;
CC Sequence=BAB15653.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=BAB55126.1; Type=Frameshift; Positions=48;
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DR EMBL; AL136935; CAB66869.1; -; mRNA.
DR EMBL; AK022870; BAB14282.1; ALT_SEQ; mRNA.
DR EMBL; AK027090; BAB15653.1; ALT_INIT; mRNA.
DR EMBL; AK027461; BAB55126.1; ALT_FRAME; mRNA.
DR EMBL; AL390088; CAB98211.1; -; mRNA.
DR EMBL; BX538115; CAD98025.1; -; mRNA.
DR EMBL; AC069287; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC011821; AAH11821.2; -; mRNA.
DR EMBL; BC111499; AAI11500.1; -; mRNA.
DR EMBL; BC121807; AAI21808.1; -; mRNA.
DR EMBL; BC121808; AAI21809.1; -; mRNA.
DR RefSeq; NP_001273063.1; NM_001286134.1.
DR RefSeq; NP_068751.4; NM_021932.5.
DR UniGene; Hs.592292; -.
DR ProteinModelPortal; Q9NPQ8; -.
DR SMR; Q9NPQ8; 373-407.
DR IntAct; Q9NPQ8; 10.
DR MINT; MINT-1422193; -.
DR PhosphoSite; Q9NPQ8; -.
DR DMDM; 308153562; -.
DR PaxDb; Q9NPQ8; -.
DR PRIDE; Q9NPQ8; -.
DR DNASU; 60626; -.
DR Ensembl; ENST00000325207; ENSP00000325941; ENSG00000177963.
DR Ensembl; ENST00000526104; ENSP00000432008; ENSG00000177963.
DR Ensembl; ENST00000527696; ENSP00000434833; ENSG00000177963.
DR GeneID; 60626; -.
DR KEGG; hsa:60626; -.
DR UCSC; uc001log.3; human.
DR CTD; 60626; -.
DR GeneCards; GC11P000200; -.
DR HGNC; HGNC:29550; RIC8A.
DR HPA; CAB046012; -.
DR HPA; HPA041491; -.
DR MIM; 609146; gene.
DR neXtProt; NX_Q9NPQ8; -.
DR PharmGKB; PA142671067; -.
DR eggNOG; NOG322219; -.
DR HOVERGEN; HBG054867; -.
DR InParanoid; Q9NPQ8; -.
DR OMA; LHQTHRL; -.
DR OrthoDB; EOG72JWG4; -.
DR ChiTaRS; RIC8A; human.
DR GeneWiki; RIC8A; -.
DR GenomeRNAi; 60626; -.
DR NextBio; 65465; -.
DR PRO; PR:Q9NPQ8; -.
DR ArrayExpress; Q9NPQ8; -.
DR Bgee; Q9NPQ8; -.
DR Genevestigator; Q9NPQ8; -.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:UniProtKB-KW.
DR GO; GO:0007193; P:adenylate cyclase-inhibiting G-protein coupled receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0071711; P:basement membrane organization; IEA:Ensembl.
DR GO; GO:0042074; P:cell migration involved in gastrulation; IEA:Ensembl.
DR GO; GO:0070586; P:cell-cell adhesion involved in gastrulation; IEA:Ensembl.
DR GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR GO; GO:0001944; P:vasculature development; IEA:Ensembl.
DR GO; GO:0008542; P:visual learning; IEA:Ensembl.
DR Gene3D; 1.25.10.10; -; 2.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR019318; Gua_nucleotide_exch_fac_Ric8.
DR InterPro; IPR008376; Synembryn.
DR Pfam; PF10165; Ric8; 1.
DR PRINTS; PR01802; SYNEMBRYN.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Complete proteome; Cytoplasm;
KW Guanine-nucleotide releasing factor; Membrane; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1 531 Synembryn-A.
FT /FTId=PRO_0000235890.
FT MOD_RES 436 436 Phosphoserine.
FT MOD_RES 441 441 Phosphothreonine.
FT MOD_RES 502 502 Phosphoserine.
FT MOD_RES 523 523 Phosphoserine.
FT MOD_RES 524 524 Phosphoserine.
FT MOD_RES 528 528 Phosphoserine.
FT VAR_SEQ 1 44 MEPRAVAEAVETGEEDVIMEALRSYNQEHSQSFTFDDAQQE
FT DRK -> MMPNRRTGRWVLAQGVKGQGRVAPGRRAWWSRSS
FT PCPQ (in isoform 2).
FT /FTId=VSP_018507.
FT VAR_SEQ 209 209 Missing (in isoform 4).
FT /FTId=VSP_039849.
FT VAR_SEQ 354 354 A -> AQGWPPP (in isoform 3).
FT /FTId=VSP_018508.
FT CONFLICT 48 48 E -> V (in Ref. 2; BAB55126).
FT CONFLICT 405 405 P -> L (in Ref. 4; CAD98025).
SQ SEQUENCE 531 AA; 59710 MW; 2BAF3E2791F6E021 CRC64;
MEPRAVAEAV ETGEEDVIME ALRSYNQEHS QSFTFDDAQQ EDRKRLAELL VSVLEQGLPP
SHRVIWLQSV RILSRDRNCL DPFTSRQSLQ ALACYADISV SEGSVPESAD MDVVLESLKC
LCNLVLSSPV AQMLAAEARL VVKLTERVGL YRERSFPHDV QFFDLRLLFL LTALRTDVRQ
QLFQELKGVR LLTDTLELTL GVTPEGNPPP TLLPSQETER AMEILKVLFN ITLDSIKGEV
DEEDAALYRH LGTLLRHCVM IATAGDRTEE FHGHAVNLLG NLPLKCLDVL LTLEPHGDST
EFMGVNMDVI RALLIFLEKR LHKTHRLKES VAPVLSVLTE CARMHRPARK FLKAQVLPPL
RDVRTRPEVG EMLRNKLVRL MTHLDTDVKR VAAEFLFVLC SESVPRFIKY TGYGNAAGLL
AARGLMAGGR PEGQYSEDED TDTDEYKEAK ASINPVTGRV EEKPPNPMEG MTEEQKEHEA
MKLVTMFDKL SRNRVIQPMG MSPRGHLTSL QDAMCETMEQ QLSSDPDSDP D
//
ID RIC8A_HUMAN Reviewed; 531 AA.
AC Q9NPQ8; Q0P508; Q2T9J1; Q7Z352; Q96EZ1; Q96SZ2; Q9H064; Q9H5H3;
read moreAC Q9H9E7;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 3.
DT 22-JAN-2014, entry version 86.
DE RecName: Full=Synembryn-A;
DE AltName: Full=Protein Ric-8A;
GN Name=RIC8A;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Uterus;
RX PubMed=11230166; DOI=10.1101/gr.GR1547R;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H.,
RA Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N.,
RA Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D.,
RA Wambutt R., Korn B., Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and
RT analysis of 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Teratocarcinoma;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RG The European IMAGE consortium;
RL Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Uterine endothelium;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
RA Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
RA FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
RA Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
RA Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
RA Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=Lymph, and Uterus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [8]
RP FUNCTION.
RX PubMed=16629901; DOI=10.1111/j.1365-2443.2006.00959.x;
RA Nishimura A., Okamoto M., Sugawara Y., Mizuno N., Yamauchi J.,
RA Itoh H.;
RT "Ric-8A potentiates Gq-mediated signal transduction by acting
RT downstream of G protein-coupled receptor in intact cells.";
RL Genes Cells 11:487-498(2006).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
RA Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
RA Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-436; THR-441; SER-523;
RP SER-524 AND SER-528, AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18318008; DOI=10.1002/pmic.200700884;
RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
RA Zou H., Gu J.;
RT "Large-scale phosphoproteome analysis of human liver tissue by
RT enrichment and fractionation of phosphopeptides with strong anion
RT exchange chromatography.";
RL Proteomics 8:1346-1361(2008).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-436 AND THR-441, AND
RP MASS SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-436; THR-441 AND
RP SER-502, AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-502, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
CC -!- FUNCTION: Guanine nucleotide exchange factor (GEF), which can
CC activate some, but not all, G-alpha proteins. Able to activate
CC GNAI1, GNAO1 and GNAQ, but not GNAS by exchanging bound GDP for
CC free GTP. Involved in regulation of microtubule pulling forces
CC during mitotic movement of chromosomes by stimulating G(i)-alpha
CC protein, possibly leading to release G(i)-alpha-GTP and NuMA
CC proteins from the NuMA-GPSM2-G(i)-alpha-GDP complex (By
CC similarity). Also acts as an activator for G(q)-alpha (GNAQ)
CC protein by enhancing the G(q)-coupled receptor-mediated ERK
CC activation.
CC -!- SUBUNIT: Interacts with GDP-bound G alpha proteins GNAI1, GNAO1
CC and GNAQ, and with GNA13 with lower affinity. Does not interact
CC with G-alpha proteins when they are in complex with subunits beta
CC and gamma. Interacts (via C-terminus) with RGS14; the interaction
CC stimulates the dissociation of the complex between RGS14 and the
CC active GTP-bound form of GNAI1 (By similarity).
CC -!- INTERACTION:
CC Q9UMX0:UBQLN1; NbExp=3; IntAct=EBI-717509, EBI-741480;
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Cell membrane (By
CC similarity). Note=Colocalizes with RIC8A in CA2 hippocampal
CC neurons. Colocalizes with GNAI1 and RGS14 at the plasma membrane
CC (By similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q9NPQ8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NPQ8-2; Sequence=VSP_018507;
CC Name=3;
CC IsoId=Q9NPQ8-3; Sequence=VSP_018508;
CC Name=4;
CC IsoId=Q9NPQ8-4; Sequence=VSP_039849;
CC -!- SIMILARITY: Belongs to the synembryn family.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB14282.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=BAB14282.1; Type=Frameshift; Positions=397;
CC Sequence=BAB15653.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=BAB55126.1; Type=Frameshift; Positions=48;
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DR EMBL; AL136935; CAB66869.1; -; mRNA.
DR EMBL; AK022870; BAB14282.1; ALT_SEQ; mRNA.
DR EMBL; AK027090; BAB15653.1; ALT_INIT; mRNA.
DR EMBL; AK027461; BAB55126.1; ALT_FRAME; mRNA.
DR EMBL; AL390088; CAB98211.1; -; mRNA.
DR EMBL; BX538115; CAD98025.1; -; mRNA.
DR EMBL; AC069287; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC011821; AAH11821.2; -; mRNA.
DR EMBL; BC111499; AAI11500.1; -; mRNA.
DR EMBL; BC121807; AAI21808.1; -; mRNA.
DR EMBL; BC121808; AAI21809.1; -; mRNA.
DR RefSeq; NP_001273063.1; NM_001286134.1.
DR RefSeq; NP_068751.4; NM_021932.5.
DR UniGene; Hs.592292; -.
DR ProteinModelPortal; Q9NPQ8; -.
DR SMR; Q9NPQ8; 373-407.
DR IntAct; Q9NPQ8; 10.
DR MINT; MINT-1422193; -.
DR PhosphoSite; Q9NPQ8; -.
DR DMDM; 308153562; -.
DR PaxDb; Q9NPQ8; -.
DR PRIDE; Q9NPQ8; -.
DR DNASU; 60626; -.
DR Ensembl; ENST00000325207; ENSP00000325941; ENSG00000177963.
DR Ensembl; ENST00000526104; ENSP00000432008; ENSG00000177963.
DR Ensembl; ENST00000527696; ENSP00000434833; ENSG00000177963.
DR GeneID; 60626; -.
DR KEGG; hsa:60626; -.
DR UCSC; uc001log.3; human.
DR CTD; 60626; -.
DR GeneCards; GC11P000200; -.
DR HGNC; HGNC:29550; RIC8A.
DR HPA; CAB046012; -.
DR HPA; HPA041491; -.
DR MIM; 609146; gene.
DR neXtProt; NX_Q9NPQ8; -.
DR PharmGKB; PA142671067; -.
DR eggNOG; NOG322219; -.
DR HOVERGEN; HBG054867; -.
DR InParanoid; Q9NPQ8; -.
DR OMA; LHQTHRL; -.
DR OrthoDB; EOG72JWG4; -.
DR ChiTaRS; RIC8A; human.
DR GeneWiki; RIC8A; -.
DR GenomeRNAi; 60626; -.
DR NextBio; 65465; -.
DR PRO; PR:Q9NPQ8; -.
DR ArrayExpress; Q9NPQ8; -.
DR Bgee; Q9NPQ8; -.
DR Genevestigator; Q9NPQ8; -.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:UniProtKB-KW.
DR GO; GO:0007193; P:adenylate cyclase-inhibiting G-protein coupled receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0071711; P:basement membrane organization; IEA:Ensembl.
DR GO; GO:0042074; P:cell migration involved in gastrulation; IEA:Ensembl.
DR GO; GO:0070586; P:cell-cell adhesion involved in gastrulation; IEA:Ensembl.
DR GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR GO; GO:0001944; P:vasculature development; IEA:Ensembl.
DR GO; GO:0008542; P:visual learning; IEA:Ensembl.
DR Gene3D; 1.25.10.10; -; 2.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR019318; Gua_nucleotide_exch_fac_Ric8.
DR InterPro; IPR008376; Synembryn.
DR Pfam; PF10165; Ric8; 1.
DR PRINTS; PR01802; SYNEMBRYN.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Complete proteome; Cytoplasm;
KW Guanine-nucleotide releasing factor; Membrane; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1 531 Synembryn-A.
FT /FTId=PRO_0000235890.
FT MOD_RES 436 436 Phosphoserine.
FT MOD_RES 441 441 Phosphothreonine.
FT MOD_RES 502 502 Phosphoserine.
FT MOD_RES 523 523 Phosphoserine.
FT MOD_RES 524 524 Phosphoserine.
FT MOD_RES 528 528 Phosphoserine.
FT VAR_SEQ 1 44 MEPRAVAEAVETGEEDVIMEALRSYNQEHSQSFTFDDAQQE
FT DRK -> MMPNRRTGRWVLAQGVKGQGRVAPGRRAWWSRSS
FT PCPQ (in isoform 2).
FT /FTId=VSP_018507.
FT VAR_SEQ 209 209 Missing (in isoform 4).
FT /FTId=VSP_039849.
FT VAR_SEQ 354 354 A -> AQGWPPP (in isoform 3).
FT /FTId=VSP_018508.
FT CONFLICT 48 48 E -> V (in Ref. 2; BAB55126).
FT CONFLICT 405 405 P -> L (in Ref. 4; CAD98025).
SQ SEQUENCE 531 AA; 59710 MW; 2BAF3E2791F6E021 CRC64;
MEPRAVAEAV ETGEEDVIME ALRSYNQEHS QSFTFDDAQQ EDRKRLAELL VSVLEQGLPP
SHRVIWLQSV RILSRDRNCL DPFTSRQSLQ ALACYADISV SEGSVPESAD MDVVLESLKC
LCNLVLSSPV AQMLAAEARL VVKLTERVGL YRERSFPHDV QFFDLRLLFL LTALRTDVRQ
QLFQELKGVR LLTDTLELTL GVTPEGNPPP TLLPSQETER AMEILKVLFN ITLDSIKGEV
DEEDAALYRH LGTLLRHCVM IATAGDRTEE FHGHAVNLLG NLPLKCLDVL LTLEPHGDST
EFMGVNMDVI RALLIFLEKR LHKTHRLKES VAPVLSVLTE CARMHRPARK FLKAQVLPPL
RDVRTRPEVG EMLRNKLVRL MTHLDTDVKR VAAEFLFVLC SESVPRFIKY TGYGNAAGLL
AARGLMAGGR PEGQYSEDED TDTDEYKEAK ASINPVTGRV EEKPPNPMEG MTEEQKEHEA
MKLVTMFDKL SRNRVIQPMG MSPRGHLTSL QDAMCETMEQ QLSSDPDSDP D
//
MIM
609146
*RECORD*
*FIELD* NO
609146
*FIELD* TI
*609146 RIC8, C. ELEGANS, HOMOLOG OF, A; RIC8A
;;SYNEMBRYN, C. ELEGANS, HOMOLOG OF, A
read more*FIELD* TX
CLONING
Using G-alpha proteins (see GNAS; 139320) as bait in a yeast 2-hybrid
screen of a rat brain cDNA library, Tall et al. (2003) cloned Ric8a, a
homolog of C. elegans Ric8/synembryn. Database analysis identified 3
splice variants of human RIC8A that encode deduced proteins of 531, 537,
and 401 amino acids. The 531-amino acid RIC8A isoform shares 87%
identity with rat Ric8a. The 537-amino acid protein is identical to the
531-amino acid protein except for a 6-amino acid insertion, including a
polyproline sequence, at codon 355. The variant encoding the 401-amino
acid protein is derived from a 1-bp insertion at codon 395 of the
transcript encoding the 531-amino acid protein. The resultant frameshift
leads to a protein with 5 different C-terminal amino acids and a new
stop codon that forms a consensus CAAX box for geranylgeranyl
modification.
GENE FUNCTION
By yeast 2-hybrid analysis, Tall et al. (2003) found that rat Ric8a
interacted with GNAI1 (139310), GNAO (139311), GNAQ (600998), and weakly
with GNA13 (604406). No interaction was observed with GNAS. Ric8a
interacted preferentially with wildtype GNAI1 compared with its
GTPase-defective counterpart. In detergent extracts of rat brain
membranes, Ric8a interacted with GNAI1, GNAI2 (139360), GNAI3 (139370),
GNAQ, and GNA13, but not with GNAS or G protein beta subunits (see GNB1;
139380). Tall et al. (2003) found that Ric8a preferentially interacted
with nucleotide-free GNAI1. Ric8a stimulated the rate of binding between
a nonhydrolyzable GTP analog and GNAQ, and it stimulated the
steady-state GTPase activity of GNAQ. However, Ric8a did not interact
with preformed G protein heterotrimers or facilitate their nucleotide
exchange. Beta-gamma dimers appeared to compete with Ric8a for binding
to G-alpha proteins.
Afshar et al. (2004) determined that C. elegans Ric8 is required for
proper asymmetric division of 1-cell-stage embryos. Spindle severing
experiments demonstrated that Ric8 was required for the generation of
substantial pulling forces on astral microtubules. Ric8 physically
interacted with 2 nematode G-alpha subunits that act in a partially
redundant manner in 1-cell-stage embryos. Ric8 behaved as a guanine
nucleotide exchange factor for the G-alpha protein Goa1.
GENE STRUCTURE
Tall et al. (2003) determined that the RIC8A gene contains at least 7
exons.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the RIC8A
gene to chromosome 11 (TMAP WI-19967).
*FIELD* RF
1. Afshar, K.; Willard, F. S.; Colombo, K.; Johnston, C. A.; McCudden,
C. R.; Siderovski, D. P.; Gonczy, P.: RIC-8 is required for GPR-1/2-dependent
G-alpha function during asymmetric division of C. elegans embryos. Cell 119:
219-230, 2004.
2. Tall, G. G.; Krumins, A. M.; Gilman, A. G.: Mammalian Ric-8A (synembryn)
is a heterotrimeric G-alpha protein guanine nucleotide exchange factor. J.
Biol. Chem. 278: 8356-8362, 2003.
*FIELD* CD
Patricia A. Hartz: 1/6/2005
*FIELD* ED
alopez: 09/08/2011
alopez: 6/14/2005
mgross: 1/6/2005
*RECORD*
*FIELD* NO
609146
*FIELD* TI
*609146 RIC8, C. ELEGANS, HOMOLOG OF, A; RIC8A
;;SYNEMBRYN, C. ELEGANS, HOMOLOG OF, A
read more*FIELD* TX
CLONING
Using G-alpha proteins (see GNAS; 139320) as bait in a yeast 2-hybrid
screen of a rat brain cDNA library, Tall et al. (2003) cloned Ric8a, a
homolog of C. elegans Ric8/synembryn. Database analysis identified 3
splice variants of human RIC8A that encode deduced proteins of 531, 537,
and 401 amino acids. The 531-amino acid RIC8A isoform shares 87%
identity with rat Ric8a. The 537-amino acid protein is identical to the
531-amino acid protein except for a 6-amino acid insertion, including a
polyproline sequence, at codon 355. The variant encoding the 401-amino
acid protein is derived from a 1-bp insertion at codon 395 of the
transcript encoding the 531-amino acid protein. The resultant frameshift
leads to a protein with 5 different C-terminal amino acids and a new
stop codon that forms a consensus CAAX box for geranylgeranyl
modification.
GENE FUNCTION
By yeast 2-hybrid analysis, Tall et al. (2003) found that rat Ric8a
interacted with GNAI1 (139310), GNAO (139311), GNAQ (600998), and weakly
with GNA13 (604406). No interaction was observed with GNAS. Ric8a
interacted preferentially with wildtype GNAI1 compared with its
GTPase-defective counterpart. In detergent extracts of rat brain
membranes, Ric8a interacted with GNAI1, GNAI2 (139360), GNAI3 (139370),
GNAQ, and GNA13, but not with GNAS or G protein beta subunits (see GNB1;
139380). Tall et al. (2003) found that Ric8a preferentially interacted
with nucleotide-free GNAI1. Ric8a stimulated the rate of binding between
a nonhydrolyzable GTP analog and GNAQ, and it stimulated the
steady-state GTPase activity of GNAQ. However, Ric8a did not interact
with preformed G protein heterotrimers or facilitate their nucleotide
exchange. Beta-gamma dimers appeared to compete with Ric8a for binding
to G-alpha proteins.
Afshar et al. (2004) determined that C. elegans Ric8 is required for
proper asymmetric division of 1-cell-stage embryos. Spindle severing
experiments demonstrated that Ric8 was required for the generation of
substantial pulling forces on astral microtubules. Ric8 physically
interacted with 2 nematode G-alpha subunits that act in a partially
redundant manner in 1-cell-stage embryos. Ric8 behaved as a guanine
nucleotide exchange factor for the G-alpha protein Goa1.
GENE STRUCTURE
Tall et al. (2003) determined that the RIC8A gene contains at least 7
exons.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the RIC8A
gene to chromosome 11 (TMAP WI-19967).
*FIELD* RF
1. Afshar, K.; Willard, F. S.; Colombo, K.; Johnston, C. A.; McCudden,
C. R.; Siderovski, D. P.; Gonczy, P.: RIC-8 is required for GPR-1/2-dependent
G-alpha function during asymmetric division of C. elegans embryos. Cell 119:
219-230, 2004.
2. Tall, G. G.; Krumins, A. M.; Gilman, A. G.: Mammalian Ric-8A (synembryn)
is a heterotrimeric G-alpha protein guanine nucleotide exchange factor. J.
Biol. Chem. 278: 8356-8362, 2003.
*FIELD* CD
Patricia A. Hartz: 1/6/2005
*FIELD* ED
alopez: 09/08/2011
alopez: 6/14/2005
mgross: 1/6/2005