RIC8B_MOUSE
ID RIC8B_MOUSE Reviewed; 520 AA.
AC Q80XE1; Q58L65;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 2.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Synembryn-B;
DE AltName: Full=Protein Ric-8B;
GN Name=Ric8b;
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] (ISOFORMS 1 AND 2), FUNCTION, TISSUE
RP SPECIFICITY, AND INTERACTION WITH GNAL.
RC STRAIN=C57BL/6J; TISSUE=Olfactory epithelium;
RX PubMed=15829631; DOI=10.1523/jneurosci.4595-04.2005;
RA Von Dannecker L.E.C., Mercadante A.F., Malnic B.;
RT "Ric-8B, an olfactory putative GTP exchange factor, amplifies signal
RT transduction through the olfactory-specific G-protein Galphaolf.";
RL J. Neurosci. 25:3793-3800(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Head;
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] (ISOFORM 1).
RC TISSUE=Eye;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-468 AND THR-473, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, and Lung;
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).
CC -!- FUNCTION: Guanine nucleotide exchange factor (GEF), which can activate
CC some, but not all, G-alpha proteins by exchanging bound GDP for free
CC GTP (By similarity). Able to potentiate G(olf)-alpha-dependent cAMP
CC accumulation suggesting that it may be an important component for
CC odorant signal transduction. {ECO:0000250,
CC ECO:0000269|PubMed:15829631}.
CC -!- SUBUNIT: Interacts with GDP-bound G alpha proteins GNAI1, GNAL, GNAS
CC and GNAQ. Does not interact with G-alpha proteins when they are in
CC complex with subunits beta and gamma. {ECO:0000269|PubMed:15829631}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cell cortex {ECO:0000250}.
CC Note=Localizes to the cell cortex. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=2;
CC IsoId=Q80XE1-2; Sequence=Displayed;
CC Name=1;
CC IsoId=Q80XE1-1; Sequence=VSP_039867;
CC -!- TISSUE SPECIFICITY: Predominantly expressed in the mature olfactory
CC sensory neurons and also in a few regions in the brain.
CC {ECO:0000269|PubMed:15829631}.
CC -!- SIMILARITY: Belongs to the synembryn family. {ECO:0000305}.
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DR EMBL; AY940666; AAX46315.1; -; mRNA.
DR EMBL; AY940667; AAX46316.1; -; mRNA.
DR EMBL; AK132369; BAE21130.1; -; mRNA.
DR EMBL; BC051080; AAH51080.1; -; mRNA.
DR CCDS; CCDS24084.1; -. [Q80XE1-2]
DR CCDS; CCDS24085.1; -. [Q80XE1-1]
DR RefSeq; NP_001013459.1; NM_001013441.2. [Q80XE1-2]
DR RefSeq; NP_898995.1; NM_183172.2. [Q80XE1-1]
DR AlphaFoldDB; Q80XE1; -.
DR SMR; Q80XE1; -.
DR BioGRID; 231877; 7.
DR STRING; 10090.ENSMUSP00000046981; -.
DR iPTMnet; Q80XE1; -.
DR PhosphoSitePlus; Q80XE1; -.
DR EPD; Q80XE1; -.
DR jPOST; Q80XE1; -.
DR MaxQB; Q80XE1; -.
DR PeptideAtlas; Q80XE1; -.
DR PRIDE; Q80XE1; -.
DR ProteomicsDB; 253132; -. [Q80XE1-2]
DR ProteomicsDB; 253133; -. [Q80XE1-1]
DR Antibodypedia; 45122; 61 antibodies from 17 providers.
DR DNASU; 237422; -.
DR Ensembl; ENSMUST00000038523; ENSMUSP00000046981; ENSMUSG00000035620. [Q80XE1-1]
DR Ensembl; ENSMUST00000095385; ENSMUSP00000093032; ENSMUSG00000035620. [Q80XE1-2]
DR GeneID; 237422; -.
DR KEGG; mmu:237422; -.
DR UCSC; uc007gkx.2; mouse. [Q80XE1-1]
DR UCSC; uc007gky.2; mouse. [Q80XE1-2]
DR CTD; 55188; -.
DR MGI; MGI:2682307; Ric8b.
DR VEuPathDB; HostDB:ENSMUSG00000035620; -.
DR eggNOG; KOG4464; Eukaryota.
DR GeneTree; ENSGT00390000014700; -.
DR HOGENOM; CLU_018602_1_0_1; -.
DR InParanoid; Q80XE1; -.
DR OMA; EDNHQFR; -.
DR OrthoDB; 1110075at2759; -.
DR PhylomeDB; Q80XE1; -.
DR TreeFam; TF314907; -.
DR BioGRID-ORCS; 237422; 5 hits in 72 CRISPR screens.
DR ChiTaRS; Ric8b; mouse.
DR PRO; PR:Q80XE1; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q80XE1; protein.
DR Bgee; ENSMUSG00000035620; Expressed in olfactory epithelium and 222 other tissues.
DR ExpressionAtlas; Q80XE1; baseline and differential.
DR Genevisible; Q80XE1; MM.
DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
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:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
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; 2.
DR Pfam; PF10165; Ric8; 1.
DR PRINTS; PR01802; SYNEMBRYN.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Guanine-nucleotide releasing factor;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..520
FT /note="Synembryn-B"
FT /id="PRO_0000235900"
FT MOD_RES 468
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 473
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 484
FT /note="K -> NINLITGHLEEPMPNPIDEMTEEQKEYEAMKLVNMLDKLSR (in
FT isoform 1)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:15829631"
FT /id="VSP_039867"
SQ SEQUENCE 520 AA; 58683 MW; 79FACBB0C462F7A3 CRC64;
MDEERALYIV RAGEAGAIER VLRDYSDKHR ATFKFESADE DKRKKLCEGI FKVLVKEVPT
TCQVSCLEVL RILSRDKKIL VPVTTKENMQ ILLRLAKLHE SDDSLEKVSE FPVIVESLKC
LCNIVFNSQM AQQLSLELNL AAKLCNLLRK CKDRKFINDI KCFDLRLLFV LSLLHTDIRS
QLRYELQGLP LLTQILESAF SIKWTDEYES AIDHNGPPLS PQETDCAIEA LKALFNVTVD
SWKVHKESDS HQFRVMAAVL RHCLLIVGPT EDKTEELHSN AVNLLSNVPV SCLDVLICPL
THEETAQEAA TLDELPSDKT TEKDTALKNS TMVYNGMNME AIHVLLNFME KRIDKGSSYR
EGLTPVLSLL TECSRAHRNI RKFLKDQVLP PLRDVTNRPE VGSTVRNKLV RLMTHVDLGV
KQIAAEFLFV LCKERVDSLL KYTGYGNAAG LLAARGLLAG GRGDNWYSED EDTDTEEYKN
AKPKEELLKP MGLKPDGTIT PLEEALSQYS VIEETSSDTD
