ID   SGMR1_MOUSE             Reviewed;         223 AA.
AC   O55242; Q9JKU9;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   24-JAN-2024, entry version 165.
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 [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   [5]
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   [6]
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   [7]
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   [8]
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   [9]
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   [10]
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   [11]
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   [12]
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   [13]
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   [14]
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   [15]
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   [16]
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   [17]
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   [18]
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   -!- 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=2;
CC       Name=1;
CC         IsoId=O55242-1; Sequence=Displayed;
CC       Name=2; Synonyms=Beta;
CC         IsoId=O55242-2; Sequence=VSP_021987;
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   -!- 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}.
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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; 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.
DR   RefSeq; NP_001273468.1; NM_001286539.1. [O55242-2]
DR   RefSeq; NP_001273469.1; NM_001286540.1.
DR   RefSeq; NP_001273470.1; NM_001286541.1.
DR   RefSeq; NP_001273480.1; NM_001286551.1.
DR   RefSeq; NP_035144.1; NM_011014.3. [O55242-1]
DR   RefSeq; XP_017175516.1; XM_017320027.1.
DR   AlphaFoldDB; O55242; -.
DR   SMR; O55242; -.
DR   BioGRID; 201973; 3.
DR   IntAct; O55242; 3.
DR   STRING; 10090.ENSMUSP00000056027; -.
DR   BindingDB; O55242; -.
DR   ChEMBL; CHEMBL3465; -.
DR   DrugCentral; O55242; -.
DR   GuidetoPHARMACOLOGY; 2552; -.
DR   PhosphoSitePlus; O55242; -.
DR   EPD; O55242; -.
DR   jPOST; O55242; -.
DR   MaxQB; O55242; -.
DR   PaxDb; 10090-ENSMUSP00000056027; -.
DR   PeptideAtlas; O55242; -.
DR   ProteomicsDB; 261337; -. [O55242-1]
DR   ProteomicsDB; 261338; -. [O55242-2]
DR   Pumba; O55242; -.
DR   Antibodypedia; 2756; 284 antibodies from 34 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; 168990at2759; -.
DR   PhylomeDB; O55242; -.
DR   TreeFam; TF300106; -.
DR   BioGRID-ORCS; 18391; 5 hits in 79 CRISPR screens.
DR   ChiTaRS; Sigmar1; mouse.
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; IEA:UniProtKB-SubCell.
DR   GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0030426; C:growth cone; IEA:UniProtKB-SubCell.
DR   GO; GO:0005811; C:lipid droplet; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; ISS:UniProtKB.
DR   GO; GO:0005635; C:nuclear envelope; ISO:MGI.
DR   GO; GO:0005637; C:nuclear inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005640; C:nuclear outer membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0014069; C:postsynaptic density; IDA:UniProtKB.
DR   GO; GO:0098839; C:postsynaptic density membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004985; F:G protein-coupled opioid receptor activity; IEA:Ensembl.
DR   GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR   GO; GO:0038023; F:signaling receptor activity; IDA:MGI.
DR   GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR   GO; GO:0007399; P:nervous system development; ISO:MGI.
DR   GO; GO:0070207; P:protein homotrimerization; ISO:MGI.
DR   GO; GO:0043523; P:regulation of neuron apoptotic process; ISS:UniProtKB.
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.
DR   Genevisible; O55242; MM.
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         118..148
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|Ref.3"
FT                   /id="VSP_021987"
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
//