ID RIC3_HUMAN Reviewed; 369 AA. AC Q7Z5B4; B0B1U0; B2RD25; D3DQU5; Q6UX78; Q7Z5B3; Q86T94; Q8TBJ9; Q9HAH8; DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2003, sequence version 1. DT 24-JAN-2024, entry version 142. DE RecName: Full=Protein RIC-3; DE AltName: Full=Resistant to inhibitor of cholinesterase 3; DE Flags: Precursor; GN Name=RIC3; ORFNames=UNQ720/PRO1385; 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 [MRNA] (ISOFORMS 1 AND 2), ALTERNATIVE SPLICING RP (ISOFORMS 1; 2; 3 AND 4), TISSUE SPECIFICITY, AND FUNCTION. 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 [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), ALTERNATIVE SPLICING, FUNCTION, AND RP TISSUE SPECIFICITY. RC TISSUE=Hippocampus; RX PubMed=18691158; DOI=10.1042/bsr20080055; RA Seredenina T., Ferraro T., Terstappen G.C., Caricasole A., Roncarati R.; RT "Molecular cloning and characterization of a novel human variant of RIC-3, RT a putative chaperone of nicotinic acetylcholine receptors."; RL Biosci. Rep. 28:299-306(2008). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RX PubMed=12975309; DOI=10.1101/gr.1293003; RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A., RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.; RT "The secreted protein discovery initiative (SPDI), a large-scale effort to RT identify novel human secreted and transmembrane proteins: a bioinformatics RT assessment."; RL Genome Res. 13:2265-2270(2003). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4). RC TISSUE=Brain, and Embryo; 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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). RC TISSUE=Spinal cord; 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 [6] 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 [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), AND VARIANT HIS-57. RC 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 [9] RP FUNCTION, AND INTERACTION WITH CHRNA7. RX PubMed=15504725; DOI=10.1074/jbc.m410039200; RA Williams M.E., Burton B., Urrutia A., Shcherbatko A., Chavez-Noriega L.E., RA Cohen C.J., Aiyar J.; RT "Ric-3 promotes functional expression of the nicotinic acetylcholine RT receptor alpha7 subunit in mammalian cells."; RL J. Biol. Chem. 280:1257-1263(2005). RN [10] RP FUNCTION, INTERACTION WITH HTR3A, AND SUBCELLULAR LOCATION. RX PubMed=15809299; DOI=10.1074/jbc.m414341200; RA Cheng A., McDonald N.A., Connolly C.N.; RT "Cell surface expression of 5-hydroxytryptamine type 3 receptors is RT promoted by RIC-3."; RL J. Biol. Chem. 280:22502-22507(2005). RN [11] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=15927954; DOI=10.1074/jbc.m503746200; RA Castillo M., Mulet J., Gutierrez L.M., Ortiz J.A., Castelan F., Gerber S., RA Sala S., Sala F., Criado M.; RT "Dual role of the RIC-3 protein in trafficking of serotonin and nicotinic RT acetylcholine receptors."; RL J. Biol. Chem. 280:27062-27068(2005). RN [12] RP FUNCTION, AND INTERACTION WITH CHRNA7; CHRNA3; CHRNA4; CHRNB2 AND CHRNB4. RX PubMed=16120769; DOI=10.1124/mol.105.017459; RA Lansdell S.J., Gee V.J., Harkness P.C., Doward A.I., Baker E.R., Gibb A.J., RA Millar N.S.; RT "RIC-3 enhances functional expression of multiple nicotinic acetylcholine RT receptor subtypes in mammalian cells."; RL Mol. Pharmacol. 68:1431-1438(2005). RN [13] RP SUBCELLULAR LOCATION, TOPOLOGY, AND FUNCTION. RX PubMed=17609200; DOI=10.1074/jbc.m703899200; RA Cheng A., Bollan K.A., Greenwood S.M., Irving A.J., Connolly C.N.; RT "Differential subcellular localization of RIC-3 isoforms and their role in RT determining 5-HT3 receptor composition."; RL J. Biol. Chem. 282:26158-26166(2007). RN [14] RP TISSUE SPECIFICITY. RX PubMed=17640815; DOI=10.1016/j.neuroscience.2007.06.008; RA Severance E.G., Yolken R.H.; RT "Lack of RIC-3 congruence with beta2 subunit-containing nicotinic RT acetylcholine receptors in bipolar disorder."; RL Neuroscience 148:454-460(2007). RN [15] RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-202, AND IDENTIFICATION BY RP MASS SPECTROMETRY. RC TISSUE=Mammary cancer; RX PubMed=17370265; DOI=10.1002/pmic.200600410; RA Denis N.J., Vasilescu J., Lambert J.-P., Smith J.C., Figeys D.; RT "Tryptic digestion of ubiquitin standards reveals an improved strategy for RT identifying ubiquitinated proteins by mass spectrometry."; RL Proteomics 7:868-874(2007). RN [16] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-202, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., RA Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [17] 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). RN [18] RP VARIANT [LARGE SCALE ANALYSIS] VAL-346. RX PubMed=16959974; DOI=10.1126/science.1133427; RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., RA Velculescu V.E.; RT "The consensus coding sequences of human breast and colorectal cancers."; RL Science 314:268-274(2006). CC -!- FUNCTION: Molecular chaperone which facilitates proper subunit assembly CC and surface trafficking of alpha-7 (CHRNA7) and alpha-8 (CHRNA8) CC nicotinic acetylcholine receptors (PubMed:12821669, PubMed:15504725, CC PubMed:16120769, PubMed:18691158, PubMed:32204458). 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. {ECO:0000269|PubMed:12821669, CC ECO:0000269|PubMed:15504725, ECO:0000269|PubMed:15809299, CC ECO:0000269|PubMed:15927954, ECO:0000269|PubMed:16120769, CC ECO:0000269|PubMed:17609200, ECO:0000269|PubMed:18691158, CC ECO:0000269|PubMed:32204458}. CC -!- SUBUNIT: Monomer and homodimer. Interacts with CHRNA7, CHRNA3, CHRNA4, CC CHRNB2, CHRNB4 and HTR3A. {ECO:0000269|PubMed:15504725, CC ECO:0000269|PubMed:15809299, ECO:0000269|PubMed:16120769}. CC -!- INTERACTION: CC Q7Z5B4-5; Q07817: BCL2L1; NbExp=3; IntAct=EBI-12375429, EBI-78035; CC Q7Z5B4-5; Q9NWW5: CLN6; NbExp=3; IntAct=EBI-12375429, EBI-6165897; CC Q7Z5B4-5; Q7L5A8: FA2H; NbExp=3; IntAct=EBI-12375429, EBI-11337888; CC Q7Z5B4-5; Q969F0: FATE1; NbExp=3; IntAct=EBI-12375429, EBI-743099; CC Q7Z5B4-5; O14653: GOSR2; NbExp=3; IntAct=EBI-12375429, EBI-4401517; CC Q7Z5B4-5; Q9NZG7: NINJ2; NbExp=3; IntAct=EBI-12375429, EBI-10317425; CC Q7Z5B4-5; A5D903: PRB1; NbExp=3; IntAct=EBI-12375429, EBI-10173935; CC Q7Z5B4-5; Q86Y82: STX12; NbExp=3; IntAct=EBI-12375429, EBI-2691717; CC Q7Z5B4-5; O15400: STX7; NbExp=3; IntAct=EBI-12375429, EBI-3221827; CC Q7Z5B4-5; Q969X1: TMBIM1; NbExp=3; IntAct=EBI-12375429, EBI-2820569; CC Q7Z5B4-5; Q9UIK5: TMEFF2; NbExp=3; IntAct=EBI-12375429, EBI-11423693; CC Q7Z5B4-5; P17152: TMEM11; NbExp=3; IntAct=EBI-12375429, EBI-723946; CC Q7Z5B4-5; Q8N2M4: TMEM86A; NbExp=3; IntAct=EBI-12375429, EBI-12015604; CC Q7Z5B4-5; Q9Y228: TRAF3IP3; NbExp=3; IntAct=EBI-12375429, EBI-765817; CC Q7Z5B4-5; O95070: YIF1A; NbExp=3; IntAct=EBI-12375429, EBI-2799703; CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Endoplasmic reticulum membrane; CC Single-pass membrane protein. CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Endoplasmic reticulum membrane; CC Single-pass membrane protein. Golgi apparatus membrane; Single-pass CC membrane protein. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=5; CC Name=1; Synonyms=a; CC IsoId=Q7Z5B4-1; Sequence=Displayed; CC Name=2; Synonyms=d; CC IsoId=Q7Z5B4-2; Sequence=VSP_027940, VSP_027941; CC Name=3; Synonyms=c; CC IsoId=Q7Z5B4-3; Sequence=VSP_027939; CC Name=4; Synonyms=b; CC IsoId=Q7Z5B4-5; Sequence=VSP_027943; CC Name=5; Synonyms=e; CC IsoId=Q7Z5B4-6; Sequence=VSP_043786; CC -!- TISSUE SPECIFICITY: Broadly expressed, with high levels in muscle, CC brain, heart, pancreas and testis. In the central nervous system, CC highest levels are detected in the cerebellum and pituitary gland. CC Over-expressed in brains from patients with bipolar disease or CC schizophrenia. Isoform 5 is predominantly expressed in the brain. CC {ECO:0000269|PubMed:12821669, ECO:0000269|PubMed:17640815, CC ECO:0000269|PubMed:18691158}. 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. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the ric-3 family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAB13871.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; 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; AY326435; AAP92162.1; -; mRNA. DR EMBL; AY326436; AAP92163.1; -; mRNA. DR EMBL; AM422214; CAM12309.1; -; mRNA. DR EMBL; AY358475; AAQ88839.1; -; mRNA. DR EMBL; AK021670; BAB13871.1; ALT_SEQ; mRNA. DR EMBL; AK315379; BAG37772.1; -; mRNA. DR EMBL; AL832601; CAD89943.1; -; mRNA. DR EMBL; AC091013; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC116456; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC129895; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471064; EAW68628.1; -; Genomic_DNA. DR EMBL; CH471064; EAW68630.1; -; Genomic_DNA. DR EMBL; BC022455; AAH22455.1; -; mRNA. DR CCDS; CCDS44533.1; -. [Q7Z5B4-3] DR CCDS; CCDS55741.1; -. [Q7Z5B4-6] DR CCDS; CCDS55742.1; -. [Q7Z5B4-1] DR CCDS; CCDS7788.1; -. [Q7Z5B4-5] DR RefSeq; NP_001128581.1; NM_001135109.3. [Q7Z5B4-3] DR RefSeq; NP_001193600.1; NM_001206671.3. [Q7Z5B4-1] DR RefSeq; NP_001193601.1; NM_001206672.3. [Q7Z5B4-6] DR RefSeq; NP_001333619.1; NM_001346690.1. DR RefSeq; NP_078833.3; NM_024557.5. [Q7Z5B4-5] DR RefSeq; XP_006718381.1; XM_006718318.3. [Q7Z5B4-5] DR AlphaFoldDB; Q7Z5B4; -. DR SMR; Q7Z5B4; -. DR BioGRID; 122743; 70. DR IntAct; Q7Z5B4; 32. DR MINT; Q7Z5B4; -. DR STRING; 9606.ENSP00000308820; -. DR DrugBank; DB00277; Theophylline. DR TCDB; 8.A.71.1.1; the ric3 protein (ric3) family. DR iPTMnet; Q7Z5B4; -. DR PhosphoSitePlus; Q7Z5B4; -. DR BioMuta; RIC3; -. DR DMDM; 74713638; -. DR jPOST; Q7Z5B4; -. DR MassIVE; Q7Z5B4; -. DR MaxQB; Q7Z5B4; -. DR PaxDb; 9606-ENSP00000308820; -. DR PeptideAtlas; Q7Z5B4; -. DR ProteomicsDB; 69281; -. [Q7Z5B4-1] DR ProteomicsDB; 69283; -. [Q7Z5B4-3] DR ProteomicsDB; 69284; -. [Q7Z5B4-5] DR ProteomicsDB; 69285; -. [Q7Z5B4-6] DR Antibodypedia; 24077; 92 antibodies from 19 providers. DR DNASU; 79608; -. DR Ensembl; ENST00000309737.11; ENSP00000308820.6; ENSG00000166405.16. [Q7Z5B4-1] DR Ensembl; ENST00000335425.7; ENSP00000333988.7; ENSG00000166405.16. [Q7Z5B4-3] DR Ensembl; ENST00000343202.8; ENSP00000344904.4; ENSG00000166405.16. [Q7Z5B4-5] DR Ensembl; ENST00000419822.2; ENSP00000404415.2; ENSG00000166405.16. [Q7Z5B4-2] DR Ensembl; ENST00000425599.6; ENSP00000395320.2; ENSG00000166405.16. [Q7Z5B4-6] DR GeneID; 79608; -. DR KEGG; hsa:79608; -. DR MANE-Select; ENST00000309737.11; ENSP00000308820.6; NM_001206671.4; NP_001193600.1. DR UCSC; uc001mgc.3; human. [Q7Z5B4-1] DR AGR; HGNC:30338; -. DR CTD; 79608; -. DR DisGeNET; 79608; -. DR GeneCards; RIC3; -. DR HGNC; HGNC:30338; RIC3. DR HPA; ENSG00000166405; Low tissue specificity. DR MalaCards; RIC3; -. DR MIM; 610509; gene. DR neXtProt; NX_Q7Z5B4; -. DR OpenTargets; ENSG00000166405; -. DR PharmGKB; PA142671066; -. DR VEuPathDB; HostDB:ENSG00000166405; -. DR eggNOG; ENOG502RZG3; Eukaryota. DR GeneTree; ENSGT00440000034107; -. DR HOGENOM; CLU_1447194_0_0_1; -. DR InParanoid; Q7Z5B4; -. DR OMA; THFPRSH; -. DR OrthoDB; 5355665at2759; -. DR PhylomeDB; Q7Z5B4; -. DR TreeFam; TF333291; -. DR PathwayCommons; Q7Z5B4; -. DR SignaLink; Q7Z5B4; -. DR BioGRID-ORCS; 79608; 4 hits in 1146 CRISPR screens. DR ChiTaRS; RIC3; human. DR GeneWiki; RIC3; -. DR GenomeRNAi; 79608; -. DR Pharos; Q7Z5B4; Tbio. DR PRO; PR:Q7Z5B4; -. DR Proteomes; UP000005640; Chromosome 11. DR RNAct; Q7Z5B4; Protein. DR Bgee; ENSG00000166405; Expressed in adenohypophysis and 103 other cell types or tissues. DR ExpressionAtlas; Q7Z5B4; baseline and differential. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell. 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; IEA:Ensembl. DR GO; GO:0044183; F:protein folding chaperone; IEA:Ensembl. DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IEA:Ensembl. DR GO; GO:2000010; P:positive regulation of protein localization to cell surface; IDA:UniProtKB. DR GO; GO:0034394; P:protein localization to cell surface; IBA:GO_Central. DR GO; GO:0065003; P:protein-containing complex assembly; IEA:Ensembl. DR GO; GO:0007271; P:synaptic transmission, cholinergic; IBA:GO_Central. DR InterPro; IPR026160; Ric3. DR InterPro; IPR032763; RIC3_N. DR PANTHER; PTHR21723:SF1; PROTEIN RIC-3; 1. DR PANTHER; PTHR21723; RESISTANCE TO INHIBITORS OF CHOLINESTERASE PROTEIN 3 RIC3; 1. DR Pfam; PF15361; RIC3; 1. DR Genevisible; Q7Z5B4; HS. PE 1: Evidence at protein level; KW Acetylation; Alternative splicing; Chaperone; Coiled coil; KW Endoplasmic reticulum; Golgi apparatus; Isopeptide bond; Membrane; KW Reference proteome; Signal; Transmembrane; Transmembrane helix; KW Ubl conjugation. FT SIGNAL 1..28 FT /evidence="ECO:0000250" FT CHAIN 29..369 FT /note="Protein RIC-3" FT /id="PRO_0000302731" FT TOPO_DOM 29..95 FT /note="Lumenal" FT /evidence="ECO:0000255" FT TRANSMEM 96..116 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 117..369 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT REGION 30..67 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 272..295 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 316..369 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 140..169 FT /evidence="ECO:0000250" FT COMPBIAS 329..348 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 202 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:19608861" FT CROSSLNK 202 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin); alternate" FT /evidence="ECO:0000269|PubMed:17370265" FT VAR_SEQ 41..222 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:17974005" FT /id="VSP_027939" FT VAR_SEQ 118..128 FT /note="LSKGKTTAEDG -> VSRIILIILHQ (in isoform 2)" FT /evidence="ECO:0000303|PubMed:12821669, FT ECO:0000303|PubMed:12975309" FT /id="VSP_027940" FT VAR_SEQ 129..369 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:12821669, FT ECO:0000303|PubMed:12975309" FT /id="VSP_027941" FT VAR_SEQ 143..224 FT /note="TSFELAQLQEKLKETEAAMEKLINRVGPNGESRAQTVTSDQEKRLLHQLREI FT TRVMKEGKFIDRFSPEKEAEEAPYMEDWEG -> S (in isoform 5)" FT /evidence="ECO:0000303|PubMed:18691158" FT /id="VSP_043786" FT VAR_SEQ 174 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:15489334" FT /id="VSP_027943" FT VARIANT 57 FT /note="P -> H (in dbSNP:rs17855498)" FT /evidence="ECO:0000269|PubMed:15489334" FT /id="VAR_034943" FT VARIANT 130 FT /note="C -> Y (in dbSNP:rs55990541)" FT /id="VAR_062208" FT VARIANT 346 FT /note="G -> V (in a colorectal cancer sample; somatic FT mutation)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_036391" FT CONFLICT 23 FT /note="Missing (in Ref. 1; AAP92163)" FT /evidence="ECO:0000305" FT CONFLICT 165 FT /note="I -> F (in Ref. 8; AAH22455)" FT /evidence="ECO:0000305" FT CONFLICT Q7Z5B4-2:124 FT /note="I -> T (in Ref. 1; AAP92163)" FT /evidence="ECO:0000305" SQ SEQUENCE 369 AA; 41092 MW; 15FD70384070345D CRC64; MAYSTVQRVA LASGLVLALS LLLPKAFLSR GKRQEPPPTP EGKLGRFPPM MHHHQAPSDG QTPGARFQRS HLAEAFAKAK GSGGGAGGGG SGRGLMGQII PIYGFGIFLY ILYILFKLSK GKTTAEDGKC YTAMPGNTHR KITSFELAQL QEKLKETEAA MEKLINRVGP NGESRAQTVT SDQEKRLLHQ LREITRVMKE GKFIDRFSPE KEAEEAPYME DWEGYPEETY PIYDLSDCIK RRQETILVDY PDPKELSAEE IAERMGMIEE EESDHLGWES LPTDPRAQED NSVTSCDPKP ETCSCCFHED EDPAVLAENA GFSADSYPEQ EETTKEEWSQ DFKDEGLGIS TDKAYTGSML RKRNPQGLE //