Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

O55242 (SGMR1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 109. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Sigma non-opioid intracellular receptor 1
Alternative name(s):
Sigma 1-type opioid receptor
Short name=Sigma1-receptor
Short name=Sigma1R
Gene names
Name:Sigmar1
Synonyms:Oprs1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length223 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Functions in lipid transport from the endoplasmic reticulum and is involved in a wide array of cellular functions probably through regulation of the biogenesis of lipid microdomains at the plasma membrane. Involved in the regulation of different receptors it plays a role in BDNF signaling and EGF signaling. Also regulates ion channels like the potassium channel and could modulate neurotransmitter release. Plays a role in calcium signaling through modulation together with ANK2 of the ITP3R-dependent calcium efflux at the endoplasmic reticulum. Plays a role in several other cell functions including proliferation, survival and death. Originally identified for its ability to bind various psychoactive drugs it is involved in learning processes, memory and mood alteration. Ref.1 Ref.2 Ref.9 Ref.10 Ref.12 Ref.13

Subunit structure

Interacts with KCNA4 By similarity. Forms a ternary complex with ANK2 and ITPR3. The complex is disrupted by agonists. Ref.9

Subcellular location

Nucleus inner membrane. Nucleus outer membrane. Endoplasmic reticulum membrane. Lipid droplet. Cell junction. Cell membrane. Cell projectiongrowth cone. Note: Targeted to lipid droplets, cholesterol and galactosylceramide-enriched domains of the endoplasmic reticulum. Enriched at cell-cell communication regions, growth cone and postsynaptic structures. Localization is modulated by ligand-binding. Ref.9 Ref.11

Tissue specificity

Widely expressed with higher expression in liver, brain, kidney and thymus. Expressed throughout the brain with higher expression within cerebral cortex, hippocampus and cerebellum. Within the hippocampus expressed in cornu ammonis pyramidal neurons, the granular cells of the dentate gyrus as well as interneurons. Within the cerebellum, expressed in Purkinje cell bodies. Expressed by neural retina, retinal pigment epithelial cells and lens. Ref.2 Ref.6 Ref.7 Ref.8

Disruption phenotype

Mice display decreased hypermotility response induced by (+)SKF-10047 challenge and reduced formalin-induced pain. Ref.10

Miscellaneous

Depletion by RNAi enhances kappa-type opioid receptor-mediated analgesia and prevents the memory-improving effects of (-)- and (+)-pentazocine.

Sequence similarities

Belongs to the ERG2 family.

Ontologies

Keywords
   Biological processLipid transport
Transport
   Cellular componentCell junction
Cell membrane
Cell projection
Endoplasmic reticulum
Lipid droplet
Membrane
Nucleus
   Coding sequence diversityAlternative splicing
   DomainTransmembrane
Transmembrane helix
   Molecular functionReceptor
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processlipid transport

Inferred from electronic annotation. Source: UniProtKB-KW

nervous system development

Inferred from electronic annotation. Source: Ensembl

regulation of neuron apoptotic process

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentcell junction

Inferred from electronic annotation. Source: UniProtKB-SubCell

endoplasmic reticulum membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

growth cone

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

lipid particle

Inferred from electronic annotation. Source: UniProtKB-SubCell

nuclear inner membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

nuclear outer membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionopioid receptor activity

Inferred from electronic annotation. Source: Ensembl

protein binding

Inferred from physical interaction PubMed 17981125PubMed 23332758. Source: IntAct

receptor activity

Inferred from direct assay Ref.10. Source: MGI

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

I79_019946G3I8R93EBI-1557700,EBI-988311From a different organism.
Kcna2P631413EBI-1557700,EBI-644033

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O55242-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: O55242-2)

Also known as: Beta;

The sequence of this isoform differs from the canonical sequence as follows:
     118-148: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 223223Sigma non-opioid intracellular receptor 1
PRO_0000268653

Regions

Topological domain1 – 99Cytoplasmic Potential
Transmembrane10 – 3021Helical; Potential
Topological domain31 – 8050Extracellular Potential
Transmembrane81 – 10121Helical; Potential
Topological domain102 – 223122Cytoplasmic Potential
Region2 – 87Targeting to lipid droplets
Region118 – 14831Mediates ligand-binding By similarity

Natural variations

Alternative sequence118 – 14831Missing in isoform 2.
VSP_021987

Experimental info

Sequence conflict1921S → G in AAF64281. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified June 1, 1998. Version 1.
Checksum: 54BB2F14472E3512

FASTA22325,250
        10         20         30         40         50         60 
MPWAAGRRWA WITLILTIIA VLIQAAWLWL GTQNFVFSRE EIAQLARQYA GLDHELAFSR 

        70         80         90        100        110        120 
LIVELRRLHP GHVLPDEELQ WVFVNAGGWM GAMCILHASL SEYVLLFGTA LGSHGHSGRY 

       130        140        150        160        170        180 
WAEISDTIIS GTFHQWKEGT TKSEVFYPGE TVVHGPGEAT ALEWGPNTWM VEYGRGVIPS 

       190        200        210        220 
TLFFALADTF FSTQDYLTLF YTLRAYARGL RLELTTYLFG QDS 

« Hide

Isoform 2 (Beta) [UniParc].

Checksum: 6C75160BF446D3BC
Show »

FASTA19221,633

References

« Hide 'large scale' references
[1]"Cloning and structural analysis of the cDNA and the gene encoding the murine type 1 sigma receptor."
Seth P., Leibach F.H., Ganapathy V.
Biochem. Biophys. Res. Commun. 241:535-540(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), FUNCTION.
Strain: 129/Sv and C57BL/6.
Tissue: Kidney.
[2]"Cloning and characterization of a mouse sigma1 receptor."
Pan Y.-X., Mei J., Xu J., Wan B.-L., Zuckerman A., Pasternak G.W.
J. Neurochem. 70:2279-2285(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY.
Strain: C57BL/6.
Tissue: Brain.
[3]Wang L.-M., Shelness G.S., Childers S.R., Mach R.H., Wheeler K.T.
Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Strain: C3H/HeJ.
Tissue: Mammary gland.
[4]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Strain: C57BL/6J and NOD.
Tissue: Dendritic cell and Osteoclast.
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Strain: FVB/N.
Tissue: Liver and Mammary tumor.
[6]"Expression of the purported sigma(1) (sigma(1)) receptor in the mammalian brain and its possible relevance in deficits induced by antagonism of the NMDA receptor complex as revealed using an antisense strategy."
Kitaichi K., Chabot J.-G., Moebius F.F., Flandorfer A., Glossmann H., Quirion R.
J. Chem. Neuroanat. 20:375-387(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[7]"Expression pattern of the type 1 sigma receptor in the brain and identity of critical anionic amino acid residues in the ligand-binding domain of the receptor."
Seth P., Ganapathy M.E., Conway S.J., Bridges C.D., Smith S.B., Casellas P., Ganapathy V.
Biochim. Biophys. Acta 1540:59-67(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[8]"Expression pattern of sigma receptor 1 mRNA and protein in mammalian retina."
Ola M.S., Moore P., El-Sherbeny A., Roon P., Agarwal N., Sarthy V.P., Casellas P., Ganapathy V., Smith S.B.
Brain Res. Mol. Brain Res. 95:86-95(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[9]"Regulating ankyrin dynamics: roles of sigma-1 receptors."
Hayashi T., Su T.-P.
Proc. Natl. Acad. Sci. U.S.A. 98:491-496(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH ANK2 AND ITPR3, SUBCELLULAR LOCATION.
[10]"Generation and phenotypic analysis of sigma receptor type I (sigma 1) knockout mice."
Langa F., Codony X., Tovar V., Lavado A., Gimenez E., Cozar P., Cantero M., Dordal A., Hernandez E., Perez R., Monroy X., Zamanillo D., Guitart X., Montoliu L.
Eur. J. Neurosci. 18:2188-2196(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[11]"Sigma-1 receptors (sigma(1) binding sites) form raft-like microdomains and target lipid droplets on the endoplasmic reticulum: roles in endoplasmic reticulum lipid compartmentalization and export."
Hayashi T., Su T.-P.
J. Pharmacol. Exp. Ther. 306:718-725(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[12]"Involvement of kappa-opioid receptors and sigma receptors in memory function demonstrated using an antisense strategy."
Hiramatsu M., Hoshino T.
Brain Res. 1030:247-255(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[13]"Formalin-induced pain is reduced in sigma(1) receptor knockout mice."
Cendan C.M., Pujalte J.M., Portillo-Salido E., Montoliu L., Baeyens J.M.
Eur. J. Pharmacol. 511:73-74(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF030198 mRNA. Translation: AAC39951.1.
AF030199 Genomic DNA. Translation: AAB97683.1.
AF004927 mRNA. Translation: AAC33306.1.
AF226605 mRNA. Translation: AAF64281.1.
AK154300 mRNA. Translation: BAE32499.1.
AK159886 mRNA. Translation: BAE35455.1.
BC002000 mRNA. Translation: AAH02000.1.
BC019930 mRNA. Translation: AAH19930.1.
CCDSCCDS18070.1. [O55242-1]
CCDS71362.1. [O55242-2]
PIRJC5815.
RefSeqNP_001273467.1. NM_001286538.1.
NP_001273468.1. NM_001286539.1. [O55242-2]
NP_001273469.1. NM_001286540.1.
NP_001273470.1. NM_001286541.1.
NP_001273480.1. NM_001286551.1.
NP_035144.1. NM_011014.3. [O55242-1]
UniGeneMm.425181.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActO55242. 2 interactions.

Chemistry

BindingDBO55242.
ChEMBLCHEMBL3465.

PTM databases

PhosphoSiteO55242.

Proteomic databases

PaxDbO55242.
PRIDEO55242.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000059354; ENSMUSP00000056027; ENSMUSG00000036078. [O55242-1]
ENSMUST00000071561; ENSMUSP00000071492; ENSMUSG00000036078. [O55242-2]
GeneID18391.
KEGGmmu:18391.
UCSCuc008sjk.1. mouse. [O55242-1]

Organism-specific databases

CTD10280.
MGIMGI:1195268. Sigmar1.

Phylogenomic databases

eggNOGNOG296707.
GeneTreeENSGT00390000012082.
HOGENOMHOG000211245.
HOVERGENHBG058220.
InParanoidO55242.
OMAFYTLRAY.
OrthoDBEOG7GFB5Z.
PhylomeDBO55242.
TreeFamTF300106.

Gene expression databases

ArrayExpressO55242.
BgeeO55242.
CleanExMM_OPRS1.
GenevestigatorO55242.

Family and domain databases

InterProIPR006716. ERG2_sigma1_rcpt-like.
IPR028545. SIGMAR1.
[Graphical view]
PANTHERPTHR10868. PTHR10868. 1 hit.
PfamPF04622. ERG2_Sigma1R. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSIGMAR1. mouse.
NextBio293992.
PROO55242.
SOURCESearch...

Entry information

Entry nameSGMR1_MOUSE
AccessionPrimary (citable) accession number: O55242
Secondary accession number(s): Q9JKU9
Entry history
Integrated into UniProtKB/Swiss-Prot: December 12, 2006
Last sequence update: June 1, 1998
Last modified: July 9, 2014
This is version 109 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot