RIC3_HUMAN
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 03-AUG-2022, entry version 135.
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};
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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; Q7Z5B4; -.
DR PeptideAtlas; Q7Z5B4; -.
DR PRIDE; Q7Z5B4; -.
DR ProteomicsDB; 69281; -. [Q7Z5B4-1]
DR ProteomicsDB; 69283; -. [Q7Z5B4-3]
DR ProteomicsDB; 69284; -. [Q7Z5B4-5]
DR ProteomicsDB; 69285; -. [Q7Z5B4-6]
DR Antibodypedia; 24077; 81 antibodies from 19 providers.
DR DNASU; 79608; -.
DR Ensembl; ENST00000309737.11; ENSP00000308820.6; ENSG00000166405.15. [Q7Z5B4-1]
DR Ensembl; ENST00000335425.7; ENSP00000333988.7; ENSG00000166405.15. [Q7Z5B4-3]
DR Ensembl; ENST00000343202.8; ENSP00000344904.4; ENSG00000166405.15. [Q7Z5B4-5]
DR Ensembl; ENST00000419822.2; ENSP00000404415.2; ENSG00000166405.15. [Q7Z5B4-2]
DR Ensembl; ENST00000425599.6; ENSP00000395320.2; ENSG00000166405.15. [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 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; YPVYDNS; -.
DR OrthoDB; 1096847at2759; -.
DR PhylomeDB; Q7Z5B4; -.
DR TreeFam; TF333291; -.
DR PathwayCommons; Q7Z5B4; -.
DR SignaLink; Q7Z5B4; -.
DR BioGRID-ORCS; 79608; 4 hits in 1068 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 101 other tissues.
DR ExpressionAtlas; Q7Z5B4; baseline and differential.
DR Genevisible; Q7Z5B4; HS.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; PTHR21723; 1.
DR Pfam; PF15361; RIC3; 1.
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
