RIC8A_HUMAN
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 03-AUG-2022, entry version 151.
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 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).
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). {ECO:0000250}.
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}. Cell membrane
CC {ECO:0000250}. Note=Colocalizes with RIC8A in CA2 hippocampal neurons.
CC Colocalizes with GNAI1 and RGS14 at the plasma membrane (By
CC 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};
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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 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; 87.
DR IntAct; Q9NPQ8; 41.
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; Q9NPQ8; -.
DR PeptideAtlas; Q9NPQ8; -.
DR PRIDE; Q9NPQ8; -.
DR ProteomicsDB; 82040; -. [Q9NPQ8-1]
DR ProteomicsDB; 82041; -. [Q9NPQ8-2]
DR ProteomicsDB; 82042; -. [Q9NPQ8-3]
DR ProteomicsDB; 82043; -. [Q9NPQ8-4]
DR Antibodypedia; 22381; 295 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 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; 1110075at2759; -.
DR PhylomeDB; Q9NPQ8; -.
DR TreeFam; TF314907; -.
DR PathwayCommons; Q9NPQ8; -.
DR SignaLink; Q9NPQ8; -.
DR BioGRID-ORCS; 60626; 84 hits in 1082 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 192 other tissues.
DR ExpressionAtlas; Q9NPQ8; baseline and differential.
DR Genevisible; Q9NPQ8; HS.
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; -; 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 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
