RIC3_MOUSE
ID RIC3_MOUSE Reviewed; 367 AA.
AC Q8BPM6; Q6PCM7; Q8C4G2;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 2.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Protein RIC-3;
DE AltName: Full=Resistant to inhibitor of cholinesterase 3;
DE Flags: Precursor;
GN Name=Ric3;
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 [LARGE SCALE MRNA] (ISOFORM 3).
RC STRAIN=C57BL/6J; TISSUE=Cerebellum, Eye, and Retina;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [3]
RP TISSUE SPECIFICITY.
RX PubMed=12821669; DOI=10.1074/jbc.m300170200;
RA Halevi S., Yassin L., Eshel M., Sala F., Sala S., Criado M., Treinin M.;
RT "Conservation within the RIC-3 gene family. Effectors of mammalian
RT nicotinic acetylcholine receptor expression.";
RL J. Biol. Chem. 278:34411-34417(2003).
RN [4]
RP SUBCELLULAR LOCATION, TOPOLOGY, FUNCTION, COILED-COIL REGION, AND SIGNAL
RP SEQUENCE CLEAVAGE SITE.
RX PubMed=19812337; DOI=10.1523/jneurosci.1776-09.2009;
RA Wang Y., Yao Y., Tang X.Q., Wang Z.Z.;
RT "Mouse RIC-3, an endoplasmic reticulum chaperone, promotes assembly of the
RT alpha7 acetylcholine receptor through a cytoplasmic coiled-coil domain.";
RL J. Neurosci. 29:12625-12635(2009).
RN [5]
RP FUNCTION.
RX PubMed=32204458; DOI=10.3390/biom10030470;
RA Deshpande A., Vinayakamoorthy R.M., Garg B.K., Thummapudi J.P., Oza G.,
RA Adhikari K., Agarwal A., Dalvi P., Iyer S., Thulasi Raman S., Ramesh V.,
RA Rameshbabu A., Rezvaya A., Sukumaran S., Swaminathan S., Tilak B., Wang Z.,
RA Tran P.V., Loring R.H.;
RT "Why Does Knocking Out NACHO, But Not RIC3, Completely Block Expression of
RT alpha7 Nicotinic Receptors in Mouse Brain?";
RL Biomolecules 10:0-0(2020).
CC -!- FUNCTION: Molecular chaperone which promotes the proper subunit
CC assembly and surface trafficking of alpha-7 (CHRNA7) nicotinic
CC acetylcholine receptor (PubMed:19812337, PubMed:32204458). Promotes the
CC proper subunit assembly and cell surface expression of alpha-8 (CHRNA8)
CC nicotinic acetylcholine receptor (By similarity). May also promote
CC functional expression of homomeric serotoninergic 5-HT3 receptors, and
CC of heteromeric acetylcholine receptors alpha-3/beta-2, alpha-3/beta-4,
CC alpha-4/beta-2 and alpha-4/beta-4 (By similarity).
CC {ECO:0000250|UniProtKB:Q7Z5B4, ECO:0000269|PubMed:19812337,
CC ECO:0000269|PubMed:32204458}.
CC -!- SUBUNIT: Monomer and homodimer. Interacts with CHRNA7, CHRNA3, CHRNA4,
CC CHRNB2, CHRNB4 and HTR3A (By similarity).
CC {ECO:0000250|UniProtKB:Q7Z5B4}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:19812337}; Single-pass membrane protein
CC {ECO:0000269|PubMed:19812337}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8BPM6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BPM6-2; Sequence=VSP_027944;
CC Name=3;
CC IsoId=Q8BPM6-3; Sequence=VSP_027945, VSP_027946;
CC -!- TISSUE SPECIFICITY: Expressed in brain, with highest levels in
CC hippocampus, cerebellum and superior colliculus.
CC {ECO:0000269|PubMed:12821669}.
CC -!- DOMAIN: The coiled-coil domain mediates transient homodimerization with
CC other acetylcholine receptor-bound RIC3 molecules, promoting stepwise
CC ACHR homomeric assembly at the membrane.
CC -!- SIMILARITY: Belongs to the ric-3 family. {ECO:0000305}.
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DR EMBL; AK053760; BAC35510.1; -; mRNA.
DR EMBL; AK082275; BAC38452.1; -; mRNA.
DR EMBL; AK149334; BAE28817.1; -; mRNA.
DR EMBL; BC059258; AAH59258.1; -; mRNA.
DR CCDS; CCDS21733.1; -. [Q8BPM6-1]
DR RefSeq; NP_001033713.1; NM_001038624.1. [Q8BPM6-1]
DR RefSeq; NP_001298090.1; NM_001311161.1.
DR RefSeq; NP_848895.2; NM_178780.3. [Q8BPM6-3]
DR RefSeq; XP_006508005.1; XM_006507942.2. [Q8BPM6-2]
DR RefSeq; XP_006508006.1; XM_006507943.3. [Q8BPM6-2]
DR AlphaFoldDB; Q8BPM6; -.
DR SMR; Q8BPM6; -.
DR STRING; 10090.ENSMUSP00000056990; -.
DR PhosphoSitePlus; Q8BPM6; -.
DR MaxQB; Q8BPM6; -.
DR PaxDb; Q8BPM6; -.
DR PRIDE; Q8BPM6; -.
DR ProteomicsDB; 253129; -. [Q8BPM6-1]
DR ProteomicsDB; 253130; -. [Q8BPM6-2]
DR ProteomicsDB; 253131; -. [Q8BPM6-3]
DR Antibodypedia; 24077; 81 antibodies from 19 providers.
DR DNASU; 320360; -.
DR Ensembl; ENSMUST00000055993; ENSMUSP00000056990; ENSMUSG00000048330. [Q8BPM6-1]
DR GeneID; 320360; -.
DR KEGG; mmu:320360; -.
DR UCSC; uc009jdg.1; mouse. [Q8BPM6-1]
DR UCSC; uc009jdi.1; mouse. [Q8BPM6-3]
DR CTD; 79608; -.
DR MGI; MGI:2443887; Ric3.
DR VEuPathDB; HostDB:ENSMUSG00000048330; -.
DR eggNOG; ENOG502RZG3; Eukaryota.
DR GeneTree; ENSGT00440000034107; -.
DR HOGENOM; CLU_062635_1_0_1; -.
DR InParanoid; Q8BPM6; -.
DR OMA; YPVYDNS; -.
DR OrthoDB; 1096847at2759; -.
DR PhylomeDB; Q8BPM6; -.
DR TreeFam; TF333291; -.
DR BioGRID-ORCS; 320360; 2 hits in 72 CRISPR screens.
DR PRO; PR:Q8BPM6; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q8BPM6; protein.
DR Bgee; ENSMUSG00000048330; Expressed in rostral migratory stream and 128 other tissues.
DR ExpressionAtlas; Q8BPM6; baseline and differential.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IDA:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0043025; C:neuronal cell body; IBA:GO_Central.
DR GO; GO:0045202; C:synapse; IEA:GOC.
DR GO; GO:0033130; F:acetylcholine receptor binding; ISO:MGI.
DR GO; GO:0044183; F:protein folding chaperone; IDA:MGI.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; ISO:MGI.
DR GO; GO:2000010; P:positive regulation of protein localization to cell surface; ISO:MGI.
DR GO; GO:0034394; P:protein localization to cell surface; IBA:GO_Central.
DR GO; GO:0065003; P:protein-containing complex assembly; IDA:MGI.
DR GO; GO:0007271; P:synaptic transmission, cholinergic; ISO:MGI.
DR InterPro; IPR026160; Ric3.
DR InterPro; IPR032763; RIC3_N.
DR PANTHER; PTHR21723; PTHR21723; 1.
DR Pfam; PF15361; RIC3; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Chaperone; Coiled coil;
KW Endoplasmic reticulum; Isopeptide bond; Membrane; Reference proteome;
KW Signal; Transmembrane; Transmembrane helix; Ubl conjugation.
FT SIGNAL 1..31
FT /evidence="ECO:0000269|PubMed:19812337"
FT CHAIN 32..367
FT /note="Protein RIC-3"
FT /id="PRO_0000302732"
FT TOPO_DOM 32..95
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 96..116
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 117..367
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 30..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 262..301
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 322..367
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 138..169
FT /evidence="ECO:0000269|PubMed:19812337"
FT COMPBIAS 36..52
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 201
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q7Z5B4"
FT CROSSLNK 201
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q7Z5B4"
FT VAR_SEQ 1..159
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_027944"
FT VAR_SEQ 223..228
FT /note="YPEETY -> KMPLPC (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_027945"
FT VAR_SEQ 229..367
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_027946"
FT CONFLICT 46
FT /note="R -> Q (in Ref. 1; BAC38452)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 367 AA; 40283 MW; 688D772716BDE892 CRC64;
MAYSTVQRVA LASGLVLAVS LLLPKAFLSR GKRPEPPPGP EGKLDRFPPM MHHHSAPSDG
QTPGARFQRS HLAEAFAKAK GAGGGAGGGG SGRGLMGQII PIYGFGIFLY ILYILFKLSK
GKTAEDRNCS TAPPGNAHRK ITNFELVQLQ EKLKETEEAM EKLINRVGPN GESRAQAVTS
DQEKRLLHQL REITRVMKEG KFIDTSPEKE AEEAPYMEDW EGYPEETYPI YDLSDGIKRR
QETILVDYPD LKEPSAEEIA EQMGEIEEEG SERLSWDHLP TDPGAQKDNS VAPCDPKPES
CSCCVHEEED PAVLAENAGF SADGYSEQEE ATKENLPQDF TNEGLGVSTD NAHVGGMLRK
RNPQGFE
