RIC8A_MOUSE
ID RIC8A_MOUSE Reviewed; 530 AA.
AC Q3TIR3; Q3TEY3; Q99JW0; Q9ERR6;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 2.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Synembryn-A;
DE AltName: Full=Protein Ric-8A;
GN Name=Ric8a; Synonyms=Ric8;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10985349; DOI=10.1016/s0896-6273(00)00037-4;
RA Miller K.G., Emerson M.D., McManus J.R., Rand J.B.;
RT "RIC-8 (Synembryn): a novel conserved protein that is required for Gq alpha
RT signaling in the C. elegans nervous system.";
RL Neuron 27:289-299(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, DBA/2J, and NOD; TISSUE=Aorta, Testis, and Vein;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 [4]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=12971991; DOI=10.1016/s1567-133x(03)00119-4;
RA Tonissoo T., Meier R., Talts K., Plaas M., Karis A.;
RT "Expression of ric-8 (synembryn) gene in the nervous system of developing
RT and adult mouse.";
RL Gene Expr. Patterns 3:591-594(2003).
RN [5]
RP DISRUPTION PHENOTYPE.
RX PubMed=16221497; DOI=10.1016/j.bbr.2005.08.025;
RA Tonissoo T., Koks S., Meier R., Raud S., Plaas M., Vasar E., Karis A.;
RT "Heterozygous mice with Ric-8 mutation exhibit impaired spatial memory and
RT decreased anxiety.";
RL Behav. Brain Res. 167:42-48(2006).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-435, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-435; THR-440 AND THR-442, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [8]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=21158412; DOI=10.1021/bi101910n;
RA Vellano C.P., Shu F.J., Ramineni S., Yates C.K., Tall G.G., Hepler J.R.;
RT "Activation of the regulator of G protein signaling 14-Galphai1-GDP
RT signaling complex is regulated by resistance to inhibitors of
RT cholinesterase-8A.";
RL Biochemistry 50:752-762(2011).
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. Also acts as an activator for G(q)-alpha (GNAQ)
CC protein by enhancing the G(q)-coupled receptor-mediated ERK activation
CC (By similarity). {ECO:0000250}.
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane
CC {ECO:0000250}. Note=Colocalizes with GNAI1 and RGS14 at the plasma
CC membrane (By similarity). Colocalizes with RIC8A in CA2 hippocampal
CC neurons. {ECO:0000250, ECO:0000269|PubMed:21158412}.
CC -!- TISSUE SPECIFICITY: Expressed in neurons and neurites of the CA1 and
CC CA2 subregions of the hippocampus (at protein level). In adult brain,
CC it is expressed in the neocortex, hippocampus and cerebellum as well as
CC in the pineal gland and ependymal layer. {ECO:0000269|PubMed:12971991,
CC ECO:0000269|PubMed:21158412}.
CC -!- DEVELOPMENTAL STAGE: During the early development (9.5-12.0 dpc) it is
CC expressed in the developing nervous system such as the cranial ganglia,
CC neural tube, sympathetic chain and dorsal root ganglia. Also found in
CC the lens, vomeronasal organ and endolymphatic sac.
CC {ECO:0000269|PubMed:12971991}.
CC -!- DISRUPTION PHENOTYPE: Death during early embryonic development.
CC Heterozygous mice exhibit impaired spatial memory and decreased
CC anxiety. {ECO:0000269|PubMed:16221497}.
CC -!- SIMILARITY: Belongs to the synembryn family. {ECO:0000305}.
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DR EMBL; AF288813; AAG10200.1; -; mRNA.
DR EMBL; AK031466; BAC27418.1; -; mRNA.
DR EMBL; AK080192; BAC37844.1; -; mRNA.
DR EMBL; AK155282; BAE33163.1; -; mRNA.
DR EMBL; AK167746; BAE39783.1; -; mRNA.
DR EMBL; AK169367; BAE41115.1; -; mRNA.
DR EMBL; BC022917; AAH22917.1; -; mRNA.
DR CCDS; CCDS21988.1; -.
DR RefSeq; NP_444424.1; NM_053194.4.
DR AlphaFoldDB; Q3TIR3; -.
DR SMR; Q3TIR3; -.
DR BioGRID; 221670; 9.
DR IntAct; Q3TIR3; 1.
DR STRING; 10090.ENSMUSP00000026558; -.
DR iPTMnet; Q3TIR3; -.
DR PhosphoSitePlus; Q3TIR3; -.
DR SwissPalm; Q3TIR3; -.
DR EPD; Q3TIR3; -.
DR jPOST; Q3TIR3; -.
DR MaxQB; Q3TIR3; -.
DR PaxDb; Q3TIR3; -.
DR PeptideAtlas; Q3TIR3; -.
DR PRIDE; Q3TIR3; -.
DR ProteomicsDB; 255338; -.
DR ABCD; Q3TIR3; 3 sequenced antibodies.
DR Antibodypedia; 22381; 295 antibodies from 36 providers.
DR DNASU; 101489; -.
DR Ensembl; ENSMUST00000026558; ENSMUSP00000026558; ENSMUSG00000025485.
DR GeneID; 101489; -.
DR KEGG; mmu:101489; -.
DR UCSC; uc009kij.1; mouse.
DR CTD; 60626; -.
DR MGI; MGI:2141866; Ric8a.
DR VEuPathDB; HostDB:ENSMUSG00000025485; -.
DR eggNOG; KOG4464; Eukaryota.
DR GeneTree; ENSGT00390000014700; -.
DR HOGENOM; CLU_018602_1_0_1; -.
DR InParanoid; Q3TIR3; -.
DR OMA; NADPIFT; -.
DR OrthoDB; 1110075at2759; -.
DR PhylomeDB; Q3TIR3; -.
DR TreeFam; TF314907; -.
DR BioGRID-ORCS; 101489; 21 hits in 75 CRISPR screens.
DR PRO; PR:Q3TIR3; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q3TIR3; protein.
DR Bgee; ENSMUSG00000025485; Expressed in paneth cell and 263 other tissues.
DR ExpressionAtlas; Q3TIR3; baseline and differential.
DR Genevisible; Q3TIR3; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0001965; F:G-protein alpha-subunit binding; ISO:MGI.
DR GO; GO:0005096; F:GTPase activator activity; ISO:MGI.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; ISO:MGI.
DR GO; GO:0007193; P:adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway; IDA:MGI.
DR GO; GO:0071711; P:basement membrane organization; IMP:MGI.
DR GO; GO:0042074; P:cell migration involved in gastrulation; IMP:MGI.
DR GO; GO:0070586; P:cell-cell adhesion involved in gastrulation; IMP:MGI.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0007369; P:gastrulation; IMP:MGI.
DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR GO; GO:0008277; P:regulation of G protein-coupled receptor signaling pathway; ISO:MGI.
DR GO; GO:0009416; P:response to light stimulus; IMP:MGI.
DR GO; GO:0001944; P:vasculature development; IMP:MGI.
DR GO; GO:0008542; P:visual learning; IMP:MGI.
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 Cell membrane; Cytoplasm; Guanine-nucleotide releasing factor; Membrane;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..530
FT /note="Synembryn-A"
FT /id="PRO_0000235892"
FT MOD_RES 435
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 440
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 442
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 501
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NPQ8"
FT MOD_RES 522
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NPQ8"
FT MOD_RES 523
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NPQ8"
FT MOD_RES 527
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NPQ8"
FT CONFLICT 87
FT /note="Q -> R (in Ref. 2; BAE41115)"
FT /evidence="ECO:0000305"
FT CONFLICT 274
FT /note="T -> A (in Ref. 2; BAE39783)"
FT /evidence="ECO:0000305"
FT CONFLICT 449
FT /note="K -> E (in Ref. 2; BAE39783)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 530 AA; 59847 MW; D23AFC0442CCC815 CRC64;
MEPRAVADAL ETGEEDAVTE ALRSFNREHS QSFTFDDAQQ EDRKRLAKLL VSVLEQGLSP
KHRVTWLQTI RILSRDRSCL DSFASRQSLH ALACYADITV SEEPIPQSPD MDVLLESLKC
LCNLVLSSPT AQMLAAEARL VVRLAERVGL YRKRSYPHEV QFFDLRLLFL LTALRTDVRQ
QLFQELHGVR LLTDALELTL GVAPKENPPV MLPAQETERA MEILKVLFNI TFDSVKREVD
EEDAALYRYL GTLLRHCVMV EAAGDRTEEF HGHTVNLLGN LPLKCLDVLL ALELHEGSLE
FMGVNMDVIS ALLAFLEKRL HQTHRLKECV APVLNVLTEC ARMHRPARKF LKAQVLPPLR
DVRTRPEVGD LLRNKLVRLM THLDTDVKRV AAEFLFVLCS ESVPRFIKYT GYGNAAGLLA
ARGLMAGGRP EGQYSEDEDT DTEEYREAKA SINPVTGRVE EKPPNPMEGM TEEQKEHEAM
KLVNMFDKLS RHRVIQPMGM SPRGHLTSLQ DAMCETMEGQ LSSDPDSDPD
