ID RIC8A_HUMAN Reviewed; 531 AA. AC Q9NPQ8; Q0P508; Q2T9J1; Q7Z352; Q96EZ1; Q96SZ2; Q9H064; Q9H5H3; Q9H9E7; DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot. DT 05-OCT-2010, sequence version 3. DT 27-MAR-2024, entry version 160. 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; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC 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., Lauber J., RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B., RA Klein M., Poustka A.; RT "Towards a catalog of human genes and proteins: sequencing and analysis of RT 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., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., 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., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA 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., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA 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., Bloom T., RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G., RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., RA Hattori M., Rogers J., Lander E.S., 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 project: RT 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., Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling RT 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., Itoh H.; RT "Ric-8A potentiates Gq-mediated signal transduction by acting downstream of RT 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, Hurov K.E., RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., RA 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 the RT 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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. 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 enrichment RT and fractionation of phosphopeptides with strong anion exchange RT chromatography."; RL Proteomics 8:1346-1361(2008). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-436 AND THR-441, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. 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 SER-502, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. 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., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT 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., Buerckstuemmer T., RA 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 IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-436; THR-441 AND SER-502, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [18] RP INTERACTION WITH NCS1. RX PubMed=25074811; DOI=10.1242/jcs.152603; RA Romero-Pozuelo J., Dason J.S., Mansilla A., Banos-Mateos S., Sardina J.L., RA Chaves-Sanjuan A., Jurado-Gomez J., Santana E., Atwood H.L., RA Hernandez-Hernandez A., Sanchez-Barrena M.J., Ferrus A.; RT "The guanine-exchange factor Ric8a binds to the Ca sensor NCS-1 to regulate RT synapse number and neurotransmitter release."; RL J. Cell Sci. 127:4246-4259(2014). RN [19] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-441; SER-523 AND SER-524, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [20] RP INTERACTION WITH NCS1. RX PubMed=28119500; DOI=10.1073/pnas.1611089114; RA Mansilla A., Chaves-Sanjuan A., Campillo N.E., Semelidou O., RA Martinez-Gonzalez L., Infantes L., Gonzalez-Rubio J.M., Gil C., Conde S., RA Skoulakis E.M., Ferrus A., Martinez A., Sanchez-Barrena M.J.; RT "Interference of the complex between NCS-1 and Ric8a with phenothiazines RT regulates synaptic function and is an approach for fragile X syndrome."; RL Proc. Natl. Acad. Sci. U.S.A. 114:E999-E1008(2017). RN [21] RP INTERACTION WITH NCS1. RX PubMed=29966094; DOI=10.1021/acs.jmedchem.8b00088; RA Roca C., Martinez-Gonzalez L., Daniel-Mozo M., Sastre J., Infantes L., RA Mansilla A., Chaves-Sanjuan A., Gonzalez-Rubio J.M., Gil C., Canada F.J., RA Martinez A., Sanchez-Barrena M.J., Campillo N.E.; RT "Deciphering the Inhibition of the Neuronal Calcium Sensor 1 and the RT Guanine Exchange Factor Ric8a with a Small Phenothiazine Molecule for the RT Rational Generation of Therapeutic Synapse Function Regulators."; RL J. Med. Chem. 61:5910-5921(2018). CC -!- FUNCTION: Guanine nucleotide exchange factor (GEF), which can activate CC some, but not all, G-alpha proteins. Able to activate GNAI1, GNAO1 and CC GNAQ, but not GNAS by exchanging bound GDP for free GTP. Involved in CC regulation of microtubule pulling forces during mitotic movement of CC chromosomes by stimulating G(i)-alpha protein, possibly leading to CC release G(i)-alpha-GTP and NuMA proteins from the NuMA-GPSM2-G(i)- CC alpha-GDP complex (By similarity). Also acts as an activator for G(q)- CC alpha (GNAQ) protein by enhancing the G(q)-coupled receptor-mediated CC ERK activation. {ECO:0000250, ECO:0000269|PubMed:16629901}. CC -!- SUBUNIT: Interacts with GDP-bound G alpha proteins GNAI1, GNAO1 and CC GNAQ, and with GNA13 with lower affinity. Does not interact with G- CC alpha proteins when they are in complex with subunits beta and gamma. CC Interacts (via C-terminus) with RGS14; the interaction stimulates the CC dissociation of the complex between RGS14 and the active GTP-bound form CC of GNAI1 (By similarity). Interacts with NCS1; interaction is favored CC in the absence of Ca(2+) and myristoylation of NCS1 is not required CC (PubMed:25074811, PubMed:28119500, PubMed:29966094). CC {ECO:0000250|UniProtKB:Q80ZG1, ECO:0000269|PubMed:25074811, CC ECO:0000269|PubMed:28119500, ECO:0000269|PubMed:29966094}. CC -!- INTERACTION: CC Q9NPQ8; Q9UMX0: UBQLN1; NbExp=4; IntAct=EBI-717509, EBI-741480; CC Q9NPQ8-4; Q13733-2: ATP1A4; NbExp=3; IntAct=EBI-9091816, EBI-12356439; CC Q9NPQ8-4; Q12805: EFEMP1; NbExp=3; IntAct=EBI-9091816, EBI-536772; CC Q9NPQ8-4; P13473-2: LAMP2; NbExp=3; IntAct=EBI-9091816, EBI-21591415; CC Q9NPQ8-4; Q7Z6G3-2: NECAB2; NbExp=3; IntAct=EBI-9091816, EBI-10172876; CC Q9NPQ8-4; Q86Y26: NUTM1; NbExp=3; IntAct=EBI-9091816, EBI-10178410; CC Q9NPQ8-4; Q9UNF0: PACSIN2; NbExp=3; IntAct=EBI-9091816, EBI-742503; CC Q9NPQ8-4; Q9UI14: RABAC1; NbExp=3; IntAct=EBI-9091816, EBI-712367; CC Q9NPQ8-4; O00560: SDCBP; NbExp=3; IntAct=EBI-9091816, EBI-727004; CC Q9NPQ8-4; Q9Y371: SH3GLB1; NbExp=8; IntAct=EBI-9091816, EBI-2623095; CC Q9NPQ8-4; Q96QE2: SLC2A13; NbExp=3; IntAct=EBI-9091816, EBI-18082698; CC Q9NPQ8-4; Q9UMX0: UBQLN1; NbExp=3; IntAct=EBI-9091816, EBI-741480; CC Q9NPQ8-4; Q9UMX0-2: UBQLN1; NbExp=3; IntAct=EBI-9091816, EBI-10173939; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q80ZG1}. Cell CC membrane {ECO:0000250|UniProtKB:Q80ZG1}. Note=Colocalizes with RGS14 in CC CA2 hippocampal neurons. Colocalizes with GNAI1 and RGS14 at the plasma CC membrane (By similarity). {ECO:0000250}. 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. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAB14282.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC Sequence=BAB14282.1; Type=Frameshift; Evidence={ECO:0000305}; CC Sequence=BAB15653.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC Sequence=BAB55126.1; Type=Frameshift; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 CCDS; CCDS65982.1; -. [Q9NPQ8-1] DR CCDS; CCDS7690.1; -. [Q9NPQ8-3] DR RefSeq; NP_001273063.1; NM_001286134.1. [Q9NPQ8-1] DR RefSeq; NP_068751.4; NM_021932.5. [Q9NPQ8-3] DR RefSeq; XP_016873596.1; XM_017018107.1. DR AlphaFoldDB; Q9NPQ8; -. DR SMR; Q9NPQ8; -. DR BioGRID; 121946; 98. DR IntAct; Q9NPQ8; 43. DR MINT; Q9NPQ8; -. DR STRING; 9606.ENSP00000325941; -. DR ChEMBL; CHEMBL4296100; -. DR GlyGen; Q9NPQ8; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q9NPQ8; -. DR MetOSite; Q9NPQ8; -. DR PhosphoSitePlus; Q9NPQ8; -. DR BioMuta; RIC8A; -. DR DMDM; 308153562; -. DR EPD; Q9NPQ8; -. DR jPOST; Q9NPQ8; -. DR MassIVE; Q9NPQ8; -. DR MaxQB; Q9NPQ8; -. DR PaxDb; 9606-ENSP00000325941; -. DR PeptideAtlas; Q9NPQ8; -. DR ProteomicsDB; 82040; -. [Q9NPQ8-1] DR ProteomicsDB; 82041; -. [Q9NPQ8-2] DR ProteomicsDB; 82042; -. [Q9NPQ8-3] DR ProteomicsDB; 82043; -. [Q9NPQ8-4] DR Pumba; Q9NPQ8; -. DR Antibodypedia; 22381; 340 antibodies from 36 providers. DR DNASU; 60626; -. DR Ensembl; ENST00000325207.9; ENSP00000325941.5; ENSG00000177963.15. [Q9NPQ8-3] DR Ensembl; ENST00000526104.6; ENSP00000432008.1; ENSG00000177963.15. [Q9NPQ8-1] DR Ensembl; ENST00000527696.5; ENSP00000434833.1; ENSG00000177963.15. [Q9NPQ8-2] DR GeneID; 60626; -. DR KEGG; hsa:60626; -. DR MANE-Select; ENST00000526104.6; ENSP00000432008.1; NM_001286134.2; NP_001273063.1. DR UCSC; uc001lof.5; human. [Q9NPQ8-1] DR AGR; HGNC:29550; -. DR CTD; 60626; -. DR DisGeNET; 60626; -. DR GeneCards; RIC8A; -. DR HGNC; HGNC:29550; RIC8A. DR HPA; ENSG00000177963; Low tissue specificity. DR MIM; 609146; gene. DR neXtProt; NX_Q9NPQ8; -. DR OpenTargets; ENSG00000177963; -. DR PharmGKB; PA142671067; -. DR VEuPathDB; HostDB:ENSG00000177963; -. DR eggNOG; KOG4464; Eukaryota. DR GeneTree; ENSGT00390000014700; -. DR HOGENOM; CLU_018602_1_0_1; -. DR InParanoid; Q9NPQ8; -. DR OMA; NADPIFT; -. DR OrthoDB; 5357832at2759; -. DR PhylomeDB; Q9NPQ8; -. DR TreeFam; TF314907; -. DR PathwayCommons; Q9NPQ8; -. DR SignaLink; Q9NPQ8; -. DR BioGRID-ORCS; 60626; 101 hits in 1159 CRISPR screens. DR ChiTaRS; RIC8A; human. DR GeneWiki; RIC8A; -. DR GenomeRNAi; 60626; -. DR Pharos; Q9NPQ8; Tbio. DR PRO; PR:Q9NPQ8; -. DR Proteomes; UP000005640; Chromosome 11. DR RNAct; Q9NPQ8; Protein. DR Bgee; ENSG00000177963; Expressed in stromal cell of endometrium and 194 other cell types or tissues. DR ExpressionAtlas; Q9NPQ8; baseline and differential. DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB. DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB. DR GO; GO:0001965; F:G-protein alpha-subunit binding; IBA:GO_Central. DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IBA:GO_Central. 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:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central. 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; Leucine-rich Repeat Variant; 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; SYNEMBRYN; 1. DR PANTHER; PTHR12425:SF4; SYNEMBRYN-A; 1. DR Pfam; PF10165; Ric8; 1. DR PRINTS; PR01802; SYNEMBRYN. DR SUPFAM; SSF48371; ARM repeat; 1. DR Genevisible; Q9NPQ8; HS. PE 1: Evidence at protein level; KW Alternative splicing; Cell membrane; Cytoplasm; KW Guanine-nucleotide releasing factor; Membrane; Phosphoprotein; KW Reference proteome. FT CHAIN 1..531 FT /note="Synembryn-A" FT /id="PRO_0000235890" FT MOD_RES 436 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163" FT MOD_RES 441 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569" FT MOD_RES 443 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q3TIR3" FT MOD_RES 502 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163" FT MOD_RES 523 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:24275569" FT MOD_RES 524 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:24275569" FT MOD_RES 528 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT VAR_SEQ 1..44 FT /note="MEPRAVAEAVETGEEDVIMEALRSYNQEHSQSFTFDDAQQEDRK -> MMPN FT RRTGRWVLAQGVKGQGRVAPGRRAWWSRSSPCPQ (in isoform 2)" FT /evidence="ECO:0000303|PubMed:17974005" FT /id="VSP_018507" FT VAR_SEQ 209 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_039849" FT VAR_SEQ 354 FT /note="A -> AQGWPPP (in isoform 3)" FT /evidence="ECO:0000303|PubMed:11230166" FT /id="VSP_018508" FT CONFLICT 48 FT /note="E -> V (in Ref. 2; BAB55126)" FT /evidence="ECO:0000305" FT CONFLICT 405 FT /note="P -> L (in Ref. 4; CAD98025)" FT /evidence="ECO:0000305" 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 //