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Q9R0C9 (SGMR1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 79. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

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.7 Ref.10 Ref.11 Ref.12

Subunit structure

Forms a ternary complex with ANK2 and ITPR3. The complex is disrupted by agonists. Interacts with KCNA4. Ref.6 Ref.7

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.4 Ref.6 Ref.7 Ref.10

Tissue specificity

Expressed in ependymocytes and neurons throughout the CNS from the olfactory bulb to the spinal cord. Expressed by progenitor, mature and satellite oligodendrocytes and by Schwann cells (at protein level). Expressed in liver, intestine, kidney, brain, lung and heart. Expressed by retinal cells. Ref.1 Ref.4 Ref.5 Ref.8 Ref.9

Miscellaneous

Depletion by RNAi alters oligodendrocyte differentiation and enhances opioid analgesia.

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 direct assay PubMed 12438547. Source: RGD

opioid receptor signaling pathway

Inferred from direct assay PubMed 12438547. Source: GOC

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

Traceable author statement PubMed 12438547. Source: RGD

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 direct assay PubMed 12438547. Source: RGD

protein binding

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

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Hspa5P067613EBI-1557826,EBI-916036
Kcna2P631413EBI-1557826,EBI-644033From a different organism.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9R0C9-1)

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: Q9R0C9-2)

The sequence of this isoform differs from the canonical sequence as follows:
     103-106: YVLL → TILG
     107-223: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 223223Sigma non-opioid intracellular receptor 1
PRO_0000268655

Regions

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

Natural variations

Alternative sequence103 – 1064YVLL → TILG in isoform 2.
VSP_021988
Alternative sequence107 – 223117Missing in isoform 2.
VSP_021989

Experimental info

Sequence conflict1611A → D in AAD01198. Ref.1

Sequences

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

Last modified May 1, 2000. Version 1.
Checksum: B125A0388F1FFC6E

FASTA22325,270
        10         20         30         40         50         60 
MPWAVGRRWA WITLFLTIVA VLIQAVWLWL GTQSFVFQRE EIAQLARQYA GLDHELAFSR 

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

       130        140        150        160        170        180 
WAEISDTIIS GTFHQWREGT TKSEVYYPGE TVVHGPGEAT AVEWGPNTWM VEYGRGVIPS 

       190        200        210        220 
TLAFALSDTI FSTQDFLTLF YTLRAYARGL RLELTTYLFG QDP 

« Hide

Isoform 2 [UniParc].

Checksum: 8BA4159B6A9E2A0F
Show »

FASTA10612,153

References

« Hide 'large scale' references
[1]"Cloning and functional characterization of a sigma receptor from rat brain."
Seth P., Fei Y.-J., Li H.W., Huang W., Leibach F.H., Ganapathy V.
J. Neurochem. 70:922-931(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY.
Strain: Sprague-Dawley.
Tissue: Brain.
[2]"Sigma1 receptor modulation of opioid analgesia in the mouse."
Mei J., Pasternak G.W.
J. Pharmacol. Exp. Ther. 300:1070-1074(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION.
Tissue: Brain.
[3]"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).
Tissue: Prostate.
[4]"Immunocytochemical localization of the sigma(1) receptor in the adult rat central nervous system."
Alonso G., Phan V.-L., Guillemain I., Saunier M., Legrand A., Anoal M., Maurice T.
Neuroscience 97:155-170(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
[5]"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.
[6]"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: INTERACTION WITH ANK2 AND ITPR3, SUBCELLULAR LOCATION.
[7]"The sigma receptor as a ligand-regulated auxiliary potassium channel subunit."
Aydar E., Palmer C.P., Klyachko V.A., Jackson M.B.
Neuron 34:399-410(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TOPOLOGY, SUBCELLULAR LOCATION, INTERACTION WITH KCNA4.
[8]"Immunohistochemical localization of the sigma1-receptor in oligodendrocytes in the rat central nervous system."
Palacios G., Muro A., Vela J.M., Molina-Holgado E., Guitart X., Ovalle S., Zamanillo D.
Brain Res. 961:92-99(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[9]"Immunohistochemical localization of the sigma1 receptor in Schwann cells of rat sciatic nerve."
Palacios G., Muro A., Verdu E., Pumarola M., Vela J.M.
Brain Res. 1007:65-70(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[10]"Sigma-1 receptors at galactosylceramide-enriched lipid microdomains regulate oligodendrocyte differentiation."
Hayashi T., Su T.-P.
Proc. Natl. Acad. Sci. U.S.A. 101:14949-14954(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[11]"Sigma-1 receptors potentiate epidermal growth factor signaling towards neuritogenesis in PC12 cells: potential relation to lipid raft reconstitution."
Takebayashi M., Hayashi T., Su T.-P.
Synapse 53:90-103(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[12]"Chronic antidepressants potentiate via sigma-1 receptors the brain-derived neurotrophic factor-induced signaling for glutamate release."
Yagasaki Y., Numakawa T., Kumamaru E., Hayashi T., Su T.-P., Kunugi H.
J. Biol. Chem. 281:12941-12949(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF004218 mRNA. Translation: AAD01198.1.
AF067769 mRNA. Translation: AAF08342.1.
AF087827 mRNA. Translation: AAD49439.1.
BC061978 mRNA. Translation: AAH61978.1.
RefSeqNP_112258.1. NM_030996.1.
UniGeneRn.1129.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ9R0C9. 3 interactions.

Chemistry

BindingDBQ9R0C9.
ChEMBLCHEMBL3602.

Proteomic databases

PaxDbQ9R0C9.
PRIDEQ9R0C9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000019795; ENSRNOP00000019795; ENSRNOG00000014604. [Q9R0C9-1]
GeneID29336.
KEGGrno:29336.
UCSCRGD:68364. rat. [Q9R0C9-1]

Organism-specific databases

CTD10280.
RGD68364. Sigmar1.

Phylogenomic databases

eggNOGNOG296707.
GeneTreeENSGT00390000012082.
HOVERGENHBG058220.
InParanoidQ9R0C9.
OMAFYTLRAY.
OrthoDBEOG7GFB5Z.
PhylomeDBQ9R0C9.
TreeFamTF300106.

Gene expression databases

GenevestigatorQ9R0C9.

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

NextBio608816.
PROQ9R0C9.

Entry information

Entry nameSGMR1_RAT
AccessionPrimary (citable) accession number: Q9R0C9
Secondary accession number(s): Q9R1J7, Q9Z2W2
Entry history
Integrated into UniProtKB/Swiss-Prot: December 12, 2006
Last sequence update: May 1, 2000
Last modified: June 11, 2014
This is version 79 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