ID SGMR1_MOUSE Reviewed; 223 AA. AC O55242; A2AMS0; B7ZJH6; B7ZJH7; B7ZJH8; B7ZJH9; Q9JKU9; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1998, sequence version 1. DT 02-SEP-2026, entry version 174. DE RecName: Full=Sigma non-opioid intracellular receptor 1; DE AltName: Full=Sigma 1-type opioid receptor; DE Short=Sigma1-receptor; DE Short=Sigma1R; GN Name=Sigmar1; Synonyms=Oprs1; 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 [GENOMIC DNA / MRNA] (ISOFORM 1), AND FUNCTION. RC STRAIN=129/Sv, and C57BL/6J; TISSUE=Kidney; RX PubMed=9425306; DOI=10.1006/bbrc.1997.7840; RA Seth P., Leibach F.H., Ganapathy V.; RT "Cloning and structural analysis of the cDNA and the gene encoding the RT murine type 1 sigma receptor."; RL Biochem. Biophys. Res. Commun. 241:535-540(1997). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND TISSUE SPECIFICITY. RC STRAIN=C57BL/6J; TISSUE=Brain; RX PubMed=9603192; DOI=10.1046/j.1471-4159.1998.70062279.x; RA Pan Y.-X., Mei J., Xu J., Wan B.-L., Zuckerman A., Pasternak G.W.; RT "Cloning and characterization of a mouse sigma1 receptor."; RL J. Neurochem. 70:2279-2285(1998). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). RC STRAIN=C3H/HeJ; TISSUE=Mammary gland; RA Wang L.-M., Shelness G.S., Childers S.R., Mach R.H., Wheeler K.T.; RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3; 4; 5 AND 6), TISSUE SPECIFICITY, RP AND INTERACTION WITH OPRM1. RX PubMed=28350844; DOI=10.1371/journal.pone.0174694; RA Pan L., Pasternak D.A., Xu J., Xu M., Lu Z., Pasternak G.W., Pan Y.X.; RT "Isolation and characterization of alternatively spliced variants of the RT mouse sigma1 receptor gene, Sigmar1."; RL PLoS ONE 12:e0174694-e0174694(2017). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC STRAIN=C57BL/6J, and NOD; TISSUE=Dendritic cell, and Osteoclast; 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 [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC STRAIN=FVB/N; TISSUE=Liver, and 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 [7] RP TISSUE SPECIFICITY. RX PubMed=11207432; DOI=10.1016/s0891-0618(00)00106-x; RA Kitaichi K., Chabot J.-G., Moebius F.F., Flandorfer A., Glossmann H., RA Quirion R.; RT "Expression of the purported sigma(1) (sigma(1)) receptor in the mammalian RT brain and its possible relevance in deficits induced by antagonism of the RT NMDA receptor complex as revealed using an antisense strategy."; RL J. Chem. Neuroanat. 20:375-387(2000). RN [8] RP TISSUE SPECIFICITY. RX PubMed=11476895; DOI=10.1016/s0167-4889(01)00117-3; RA Seth P., Ganapathy M.E., Conway S.J., Bridges C.D., Smith S.B., RA Casellas P., Ganapathy V.; RT "Expression pattern of the type 1 sigma receptor in the brain and identity RT of critical anionic amino acid residues in the ligand-binding domain of the RT receptor."; RL Biochim. Biophys. Acta 1540:59-67(2001). RN [9] RP TISSUE SPECIFICITY. RX PubMed=11687279; DOI=10.1016/s0169-328x(01)00249-2; RA Ola M.S., Moore P., El-Sherbeny A., Roon P., Agarwal N., Sarthy V.P., RA Casellas P., Ganapathy V., Smith S.B.; RT "Expression pattern of sigma receptor 1 mRNA and protein in mammalian RT retina."; RL Brain Res. Mol. Brain Res. 95:86-95(2001). RN [10] RP FUNCTION, INTERACTION WITH ANK2 AND ITPR3, AND SUBCELLULAR LOCATION. RX PubMed=11149946; DOI=10.1073/pnas.98.2.491; RA Hayashi T., Su T.-P.; RT "Regulating ankyrin dynamics: roles of sigma-1 receptors."; RL Proc. Natl. Acad. Sci. U.S.A. 98:491-496(2001). RN [11] RP FUNCTION, AND DISRUPTION PHENOTYPE. RX PubMed=14622179; DOI=10.1046/j.1460-9568.2003.02950.x; RA Langa F., Codony X., Tovar V., Lavado A., Gimenez E., Cozar P., Cantero M., RA Dordal A., Hernandez E., Perez R., Monroy X., Zamanillo D., Guitart X., RA Montoliu L.; RT "Generation and phenotypic analysis of sigma receptor type I (sigma 1) RT knockout mice."; RL Eur. J. Neurosci. 18:2188-2196(2003). RN [12] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=12730355; DOI=10.1124/jpet.103.051284; RA Hayashi T., Su T.-P.; RT "Sigma-1 receptors (sigma(1) binding sites) form raft-like microdomains and RT target lipid droplets on the endoplasmic reticulum: roles in endoplasmic RT reticulum lipid compartmentalization and export."; RL J. Pharmacol. Exp. Ther. 306:718-725(2003). RN [13] RP FUNCTION. RX PubMed=15571673; DOI=10.1016/j.brainres.2004.10.020; RA Hiramatsu M., Hoshino T.; RT "Involvement of kappa-opioid receptors and sigma receptors in memory RT function demonstrated using an antisense strategy."; RL Brain Res. 1030:247-255(2004). RN [14] RP FUNCTION. RX PubMed=15777781; DOI=10.1016/j.ejphar.2005.01.036; RA Cendan C.M., Pujalte J.M., Portillo-Salido E., Montoliu L., Baeyens J.M.; RT "Formalin-induced pain is reduced in sigma(1) receptor knockout mice."; RL Eur. J. Pharmacol. 511:73-74(2005). RN [15] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, RC Pancreas, 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 [16] RP DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION. RX PubMed=20167253; DOI=10.1016/j.neuroscience.2010.02.022; RA Mavlyutov T.A., Epstein M.L., Andersen K.A., Ziskind-Conhaim L., RA Ruoho A.E.; RT "The sigma-1 receptor is enriched in postsynaptic sites of C-terminals in RT mouse motoneurons. An anatomical and behavioral study."; RL Neuroscience 167:247-255(2010). RN [17] RP INTERACTION WITH KCNA2, AND FUNCTION. RX PubMed=23332758; DOI=10.1016/j.cell.2012.12.004; RA Kourrich S., Hayashi T., Chuang J.Y., Tsai S.Y., Su T.P., Bonci A.; RT "Dynamic interaction between sigma-1 receptor and Kv1.2 shapes neuronal and RT behavioral responses to cocaine."; RL Cell 152:236-247(2013). RN [18] RP FUNCTION, AND DISRUPTION PHENOTYPE. RX PubMed=25678561; DOI=10.1093/brain/awv008; RA Bernard-Marissal N., Medard J.J., Azzedine H., Chrast R.; RT "Dysfunction in endoplasmic reticulum-mitochondria crosstalk underlies RT SIGMAR1 loss of function mediated motor neuron degeneration."; RL Brain 138:875-890(2015). RN [19] RP FUNCTION, AND INTERACTION WITH RNF112. RX PubMed=26792191; DOI=10.1016/j.neuropharm.2016.01.015; RA Su T.C., Lin S.H., Lee P.T., Yeh S.H., Hsieh T.H., Chou S.Y., Su T.P., RA Hung J.J., Chang W.C., Lee Y.C., Chuang J.Y.; RT "The sigma-1 receptor-zinc finger protein 179 pathway protects against RT hydrogen peroxide-induced cell injury."; RL Neuropharmacology 105:1-9(2016). CC -!- FUNCTION: Functions in lipid transport from the endoplasmic reticulum CC and is involved in a wide array of cellular functions probably through CC regulation of the biogenesis of lipid microdomains at the plasma CC membrane (PubMed:12730355). Involved in the regulation of different CC receptors it plays a role in BDNF signaling and EGF signaling. Also CC regulates ion channels like the potassium channel and could modulate CC neurotransmitter release. Plays a role in calcium signaling through CC modulation together with ANK2 of the ITP3R-dependent calcium efflux at CC the endoplasmic reticulum. Plays a role in several other cell functions CC including proliferation, survival and death. Originally identified for CC its ability to bind various psychoactive drugs it is involved in CC learning processes, memory and mood alteration (PubMed:11149946, CC PubMed:14622179, PubMed:15571673, PubMed:15777781, PubMed:23332758, CC PubMed:9425306, PubMed:9603192). Necessary for proper mitochondrial CC axonal transport in motor neurons, in particular the retrograde CC movement of mitochondria (PubMed:25678561). Plays a role in protecting CC cells against oxidative stress-induced cell death via its interaction CC with RNF112 (PubMed:26792191). {ECO:0000269|PubMed:11149946, CC ECO:0000269|PubMed:12730355, ECO:0000269|PubMed:14622179, CC ECO:0000269|PubMed:15571673, ECO:0000269|PubMed:15777781, CC ECO:0000269|PubMed:23332758, ECO:0000269|PubMed:25678561, CC ECO:0000269|PubMed:26792191, ECO:0000269|PubMed:9425306, CC ECO:0000269|PubMed:9603192}. CC -!- SUBUNIT: Homotrimer (By similarity). Interacts with KCNA4 (By CC similarity). Interacts with KCNA2; cocaine consumption leads to CC increased interaction (PubMed:23332758). Forms a ternary complex with CC ANK2 and ITPR3. The complex is disrupted by agonists (PubMed:11149946). CC Interacts with RNF112 in an oxidative stress-regulated manner CC (PubMed:26792191). {ECO:0000250|UniProtKB:Q99720, CC ECO:0000250|UniProtKB:Q9R0C9, ECO:0000269|PubMed:11149946, CC ECO:0000269|PubMed:23332758, ECO:0000269|PubMed:26792191}. CC -!- SUBUNIT: [Isoform 1]: Interacts with the mu-type opioid receptor OPRM1. CC {ECO:0000269|PubMed:28350844}. CC -!- SUBUNIT: [Isoform 2]: Interacts with the mu-type opioid receptor OPRM1. CC {ECO:0000269|PubMed:28350844}. CC -!- SUBUNIT: [Isoform 3]: Interacts with the mu-type opioid receptor OPRM1. CC {ECO:0000269|PubMed:28350844}. CC -!- SUBUNIT: [Isoform 4]: Interacts with the mu-type opioid receptor OPRM1. CC {ECO:0000269|PubMed:28350844}. CC -!- SUBUNIT: [Isoform 5]: Interacts with the mu-type opioid receptor OPRM1. CC {ECO:0000269|PubMed:28350844}. CC -!- SUBUNIT: [Isoform 6]: Interacts with the mu-type opioid receptor OPRM1. CC {ECO:0000269|PubMed:28350844}. CC -!- INTERACTION: CC O55242; P63141: Kcna2; NbExp=3; IntAct=EBI-1557700, EBI-644033; CC O55242; G3I8R9: HSPA5; Xeno; NbExp=3; IntAct=EBI-1557700, EBI-988311; CC -!- SUBCELLULAR LOCATION: Nucleus inner membrane CC {ECO:0000250|UniProtKB:Q99720}. Nucleus outer membrane CC {ECO:0000250|UniProtKB:Q99720}. Nucleus envelope CC {ECO:0000269|PubMed:12730355}. Cytoplasmic vesicle CC {ECO:0000250|UniProtKB:Q99720}. Endoplasmic reticulum membrane CC {ECO:0000269|PubMed:12730355}. Membrane {ECO:0000250|UniProtKB:Q99720}; CC Single-pass membrane protein {ECO:0000250|UniProtKB:Q99720}. Lipid CC droplet {ECO:0000269|PubMed:12730355}. Cell junction CC {ECO:0000250|UniProtKB:Q99720}. Cell membrane CC {ECO:0000250|UniProtKB:Q99720}. Cell projection, growth cone CC {ECO:0000250|UniProtKB:Q99720}. Postsynaptic density membrane CC {ECO:0000269|PubMed:20167253}. Note=During interphase, detected at the CC inner and outer nuclear membrane and the endoplasmic reticulum. CC Detected on cytoplasmic vesicles during mitosis (By similarity). CC Targeted to lipid droplets, cholesterol and galactosylceramide-enriched CC domains of the endoplasmic reticulum (PubMed:12730355). Enriched at CC cell-cell communication regions, growth cone and postsynaptic CC structures. Localization is modulated by ligand-binding. In motor CC neurons it is enriched at cholinergic postsynaptic densities CC (PubMed:20167253). {ECO:0000250|UniProtKB:Q99720, CC ECO:0000269|PubMed:12730355, ECO:0000269|PubMed:20167253}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=6; CC Name=1; Synonyms=SIG-1 {ECO:0000303|PubMed:28350844}, SIG-1R CC {ECO:0000303|PubMed:28350844}; CC IsoId=O55242-1; Sequence=Displayed; CC Name=2; Synonyms=Beta, SIG-1A {ECO:0000303|PubMed:28350844}, SR-1A CC {ECO:0000303|PubMed:28350844}; CC IsoId=O55242-2; Sequence=VSP_021987; CC Name=3; Synonyms=SIG-1B {ECO:0000303|PubMed:28350844}, SR-1B CC {ECO:0000303|PubMed:28350844}; CC IsoId=O55242-3; Sequence=VSP_062658; CC Name=4; Synonyms=SIG-1C {ECO:0000303|PubMed:28350844}, SR-1C CC {ECO:0000303|PubMed:28350844}; CC IsoId=O55242-4; Sequence=VSP_062659; CC Name=5; Synonyms=SIG-1D {ECO:0000303|PubMed:28350844}, SR-1D CC {ECO:0000303|PubMed:28350844}; CC IsoId=O55242-5; Sequence=VSP_062656; CC Name=6; Synonyms=SIG-1E {ECO:0000303|PubMed:28350844}, SR-1E CC {ECO:0000303|PubMed:28350844}; CC IsoId=O55242-6; Sequence=VSP_062657; CC -!- TISSUE SPECIFICITY: Widely expressed with higher expression in liver, CC brain, kidney and thymus. Expressed throughout the brain with higher CC expression within cerebral cortex, hippocampus and cerebellum. Within CC the hippocampus expressed in cornu ammonis pyramidal neurons, the CC granular cells of the dentate gyrus as well as interneurons. Within the CC cerebellum, expressed in Purkinje cell bodies (PubMed:11207432, CC PubMed:11476895, PubMed:11687279, PubMed:9603192). Highly expressed in CC the brainstem and motor neurons of the spinal cord (PubMed:20167253). CC Expressed by neural retina, retinal pigment epithelial cells and lens CC (PubMed:11207432, PubMed:11476895, PubMed:11687279, PubMed:9603192). CC {ECO:0000269|PubMed:11207432, ECO:0000269|PubMed:11476895, CC ECO:0000269|PubMed:11687279, ECO:0000269|PubMed:20167253, CC ECO:0000269|PubMed:9603192}. CC -!- TISSUE SPECIFICITY: [Isoform 1]: Widely expressed. Predominant CC alternative splicing isoform in all tissues examined. Highest CC expression in liver. Lowest expression in heart. CC {ECO:0000269|PubMed:28350844}. CC -!- TISSUE SPECIFICITY: [Isoform 2]: Widely expressed. Expressed at lower CC levels than isoforms 1 and 6 and at higher levels than isoforms 3, 4 CC and 5 in all tissues examined. Highest expression in brain, followed by CC liver. In the brain, highest expression in the brainstem with low CC levels in the cerebellum, striatum and thalamus. Lowest expression in CC heart. {ECO:0000269|PubMed:28350844}. CC -!- TISSUE SPECIFICITY: [Isoform 3]: Widely expressed. Expressed at lower CC levels than isoforms 1, 6 and 2 and at higher levels than isoforms 4 CC and 5 in all tissues examined. Highest expression in liver. Lowest CC expression in heart. {ECO:0000269|PubMed:28350844}. CC -!- TISSUE SPECIFICITY: [Isoform 4]: Widely expressed. Expressed at lower CC levels than isoforms 1, 6, 2, 3 and 5 in all tissues examined. Highest CC expression in liver. Lowest expression in heart. In the brain, high CC expression in the brainstem compared to the prefrontal cortex and CC cerebellum. {ECO:0000269|PubMed:28350844}. CC -!- TISSUE SPECIFICITY: [Isoform 5]: Widely expressed. Expressed at lower CC levels than isoforms 1, 6, 2 and 3 and at higher levels than isoform 4 CC in all tissues examined. Highest expression in liver. Lowest expression CC in heart. {ECO:0000269|PubMed:28350844}. CC -!- TISSUE SPECIFICITY: [Isoform 6]: Widely expressed. Expressed at lower CC levels than isoform 1 and at higher levels than isoforms 2, 3, 5 and 4 CC in all tissues examined. Highest expression in liver. Lowest expression CC in heart. {ECO:0000269|PubMed:28350844}. CC -!- DOMAIN: The C-terminal helices form a flat, hydrophobic surface that is CC probably tightly associated with the cytosolic surface of the CC endoplasmic reticulum membrane. {ECO:0000250|UniProtKB:Q99720}. CC -!- DISRUPTION PHENOTYPE: Mice display decreased hypermotility response CC induced by (+)SKF-10047 challenge and reduced formalin-induced pain CC (PubMed:14622179). Mice display motor coordination defects, muscle CC weakness, partial neuromuscular junction innervation, and motor neuron CC degeneration (PubMed:20167253, PubMed:25678561). CC {ECO:0000269|PubMed:14622179, ECO:0000269|PubMed:20167253, CC ECO:0000269|PubMed:25678561}. CC -!- MISCELLANEOUS: Depletion by RNAi enhances kappa-type opioid receptor- CC mediated analgesia and prevents the memory-improving effects of CC (-)- and (+)-pentazocine. CC -!- MISCELLANEOUS: Sigma receptors are classified into two subtypes (Sigma- CC 1 and Sigma-2) based on their different pharmacological profile. CC {ECO:0000250|UniProtKB:Q5BJF2}. CC -!- SIMILARITY: Belongs to the ERG2 family. {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; AF030198; AAC39951.1; -; mRNA. DR EMBL; AF030199; AAB97683.1; -; Genomic_DNA. DR EMBL; AF004927; AAC33306.1; -; mRNA. DR EMBL; AF226605; AAF64281.1; -; mRNA. DR EMBL; AY390764; AAR27306.1; -; mRNA. DR EMBL; AY390765; AAR27307.1; -; mRNA. DR EMBL; AY390766; AAR27308.1; -; mRNA. DR EMBL; AY390767; AAR27309.1; -; mRNA. DR EMBL; AY390768; AAR27310.1; -; mRNA. DR EMBL; AK154300; BAE32499.1; -; mRNA. DR EMBL; AK159886; BAE35455.1; -; mRNA. DR EMBL; BC002000; AAH02000.1; -; mRNA. DR EMBL; BC019930; AAH19930.1; -; mRNA. DR CCDS; CCDS18070.1; -. [O55242-1] DR CCDS; CCDS71362.1; -. [O55242-2] DR PIR; JC5815; JC5815. DR RefSeq; NP_001273467.1; NM_001286538.1. [O55242-3] DR RefSeq; NP_001273468.1; NM_001286539.1. [O55242-2] DR RefSeq; NP_001273469.1; NM_001286540.1. [O55242-4] DR RefSeq; NP_001273470.1; NM_001286541.1. [O55242-6] DR RefSeq; NP_001273471.1; NM_001286542.1. [O55242-5] DR RefSeq; NP_001273480.1; NM_001286551.1. DR RefSeq; NP_035144.1; NM_011014.3. [O55242-1] DR AlphaFoldDB; O55242; -. DR SMR; O55242; -. DR BioGRID; 201973; 6. DR FunCoup; O55242; 576. DR IntAct; O55242; 3. DR STRING; 10090.ENSMUSP00000056027; -. DR BindingDB; O55242; -. DR ChEMBL; CHEMBL3465; -. DR DrugCentral; O55242; -. DR GuidetoPHARMACOLOGY; 2552; -. DR PhosphoSitePlus; O55242; -. DR jPOST; O55242; -. DR PaxDb; 10090-ENSMUSP00000056027; -. DR PeptideAtlas; O55242; -. DR ProteomicsDB; 261337; -. [O55242-1] DR ProteomicsDB; 261338; -. [O55242-2] DR Pumba; O55242; -. DR Antibodypedia; 2756; 254 antibodies from 36 providers. DR DNASU; 18391; -. DR Ensembl; ENSMUST00000059354.15; ENSMUSP00000056027.8; ENSMUSG00000036078.17. [O55242-1] DR Ensembl; ENSMUST00000071561.7; ENSMUSP00000071492.7; ENSMUSG00000036078.17. [O55242-2] DR GeneID; 18391; -. DR KEGG; mmu:18391; -. DR UCSC; uc008sjk.2; mouse. [O55242-1] DR AGR; MGI:1195268; -. DR CTD; 10280; -. DR MGI; MGI:1195268; Sigmar1. DR VEuPathDB; HostDB:ENSMUSG00000036078; -. DR eggNOG; KOG4143; Eukaryota. DR GeneTree; ENSGT00390000012082; -. DR HOGENOM; CLU_085469_0_0_1; -. DR InParanoid; O55242; -. DR OMA; AMYVIHA; -. DR OrthoDB; 347124at2759; -. DR PhylomeDB; O55242; -. DR BioGRID-ORCS; 18391; 5 hits in 79 CRISPR screens. DR PRO; PR:O55242; -. DR Proteomes; UP000000589; Chromosome 4. DR RNAct; O55242; protein. DR Bgee; ENSMUSG00000036078; Expressed in left lobe of liver and 241 other cell types or tissues. DR ExpressionAtlas; O55242; baseline and differential. DR GO; GO:0070161; C:anchoring junction; ISS:UniProtKB. DR GO; GO:0030424; C:axon; ISO:GO_Central. DR GO; GO:0005737; C:cytoplasm; ISO:GO_Central. DR GO; GO:0031410; C:cytoplasmic vesicle; ISS:UniProtKB. DR GO; GO:0030425; C:dendrite; ISO:GO_Central. DR GO; GO:0005783; C:endoplasmic reticulum; ISO:GO_Central. DR GO; GO:0005789; C:endoplasmic reticulum membrane; EXP:UniProtKB. DR GO; GO:0098978; C:glutamatergic synapse; ISO:GO_Central. DR GO; GO:0030426; C:growth cone; IEA:UniProtKB-SubCell. DR GO; GO:0005811; C:lipid droplet; EXP:UniProtKB. DR GO; GO:0016020; C:membrane; ISS:UniProtKB. DR GO; GO:0043025; C:neuronal cell body; ISO:GO_Central. DR GO; GO:0005635; C:nuclear envelope; EXP:UniProtKB. DR GO; GO:0005637; C:nuclear inner membrane; ISS:UniProtKB. DR GO; GO:0005640; C:nuclear outer membrane; ISS:UniProtKB. DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB. DR GO; GO:0098794; C:postsynapse; IDA:SynGO. DR GO; GO:0014069; C:postsynaptic density; IDA:UniProtKB. DR GO; GO:0098839; C:postsynaptic density membrane; EXP:UniProtKB. DR GO; GO:0004985; F:G protein-coupled opioid receptor activity; IDA:MGI. DR GO; GO:0042802; F:identical protein binding; ISO:GO_Central. DR GO; GO:0031852; F:mu-type opioid receptor binding; IDA:MGI. DR GO; GO:0038023; F:signaling receptor activity; IDA:MGI. DR GO; GO:1990708; P:conditioned place preference; IEA:Ensembl. DR GO; GO:0019371; P:cyclooxygenase pathway; ISO:GO_Central. DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; ISO:GO_Central. DR GO; GO:0045019; P:negative regulation of nitric oxide biosynthetic process; ISO:GO_Central. DR GO; GO:1903573; P:negative regulation of response to endoplasmic reticulum stress; ISO:GO_Central. DR GO; GO:0007399; P:nervous system development; ISO:GO_Central. DR GO; GO:1904751; P:positive regulation of protein localization to nucleolus; ISO:GO_Central. DR GO; GO:0001516; P:prostaglandin biosynthetic process; ISO:GO_Central. DR GO; GO:0070207; P:protein homotrimerization; ISO:GO_Central. DR GO; GO:0043523; P:regulation of neuron apoptotic process; ISS:UniProtKB. DR GO; GO:0150052; P:regulation of postsynapse assembly; ISO:GO_Central. DR GO; GO:1905897; P:regulation of response to endoplasmic reticulum stress; IBA:GO_Central. DR GO; GO:0097305; P:response to alcohol; IEA:Ensembl. DR GO; GO:1904313; P:response to methamphetamine hydrochloride; IEA:Ensembl. DR InterPro; IPR006716; ERG2_sigma1_rcpt-like. DR PANTHER; PTHR10868; SIGMA 1-TYPE OPIOID RECEPTOR-RELATED; 1. DR PANTHER; PTHR10868:SF1; SIGMA NON-OPIOID INTRACELLULAR RECEPTOR 1; 1. DR Pfam; PF04622; ERG2_Sigma1R; 1. PE 1: Evidence at protein level; KW Alternative splicing; Cell junction; Cell membrane; Cell projection; KW Cytoplasmic vesicle; Endoplasmic reticulum; Lipid droplet; Lipid transport; KW Membrane; Nucleus; Postsynaptic cell membrane; Receptor; KW Reference proteome; Synapse; Transmembrane; Transmembrane helix; Transport. FT CHAIN 1..223 FT /note="Sigma non-opioid intracellular receptor 1" FT /id="PRO_0000268653" FT TOPO_DOM 1..9 FT /note="Lumenal" FT /evidence="ECO:0000250|UniProtKB:Q99720" FT TRANSMEM 10..30 FT /note="Helical" FT /evidence="ECO:0000250|UniProtKB:Q99720" FT TOPO_DOM 31..223 FT /note="Cytoplasmic" FT /evidence="ECO:0000250|UniProtKB:Q99720" FT REGION 2..8 FT /note="Targeting to endoplasmic reticulum-associated lipid FT droplets" FT /evidence="ECO:0000269|PubMed:12730355" FT REGION 99..106 FT /note="Important for ligand-binding" FT /evidence="ECO:0000250|UniProtKB:Q60492" FT REGION 177..223 FT /note="C-terminal hydrophobic region" FT /evidence="ECO:0000305" FT SITE 126 FT /note="Important for ligand binding" FT /evidence="ECO:0000250|UniProtKB:Q99720" FT SITE 172 FT /note="Important for ligand binding" FT /evidence="ECO:0000250|UniProtKB:Q99720" FT VAR_SEQ 38..146 FT /note="Missing (in isoform 5)" FT /evidence="ECO:0000303|PubMed:28350844" FT /id="VSP_062656" FT VAR_SEQ 52..118 FT /note="Missing (in isoform 6)" FT /evidence="ECO:0000303|PubMed:28350844" FT /id="VSP_062657" FT VAR_SEQ 118..148 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:28350844, ECO:0000303|Ref.3" FT /id="VSP_021987" FT VAR_SEQ 149..223 FT /note="GETVVHGPGEATALEWGPNTWMVEYGRGVIPSTLFFALADTFFSTQDYLTLF FT YTLRAYARGLRLELTTYLFGQDS -> APRTTSHSSIPFGPMPGASGLSLPPTSLAKTP FT DQPGLKEDLWMDRSAAGPHPSLYSLELIFRQQRIPCRY (in isoform 3)" FT /evidence="ECO:0000303|PubMed:28350844" FT /id="VSP_062658" FT VAR_SEQ 149..186 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:28350844" FT /id="VSP_062659" FT CONFLICT 192 FT /note="S -> G (in Ref. 3; AAF64281)" FT /evidence="ECO:0000305" SQ SEQUENCE 223 AA; 25250 MW; 54BB2F14472E3512 CRC64; MPWAAGRRWA WITLILTIIA VLIQAAWLWL GTQNFVFSRE EIAQLARQYA GLDHELAFSR LIVELRRLHP GHVLPDEELQ WVFVNAGGWM GAMCILHASL SEYVLLFGTA LGSHGHSGRY WAEISDTIIS GTFHQWKEGT TKSEVFYPGE TVVHGPGEAT ALEWGPNTWM VEYGRGVIPS TLFFALADTF FSTQDYLTLF YTLRAYARGL RLELTTYLFG QDS //