SGMR1_MUSER
ID SGMR1_MUSER Reviewed; 223 AA.
AC Q5PXE3;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 03-AUG-2022, entry version 53.
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 Mustela erminea (Ermine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Mustelidae; Mustelinae;
OC Mustela.
OX NCBI_TaxID=36723;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Hopkins B., Ravindran S.;
RT "Full-length Mustela erminea sigma-1 receptor cDNA.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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. Involved in the regulation of different receptors it plays a
CC role in BDNF signaling and EGF signaling. Also regulates ion channels
CC like the potassium channel and could modulate neurotransmitter release.
CC Plays a role in calcium signaling through modulation together with ANK2
CC of the ITP3R-dependent calcium efflux at the endoplasmic reticulum.
CC Plays a role in several other cell functions including proliferation,
CC survival and death. Originally identified for its ability to bind
CC various psychoactive drugs it is involved in learning processes, memory
CC and mood alteration (By similarity). Necessary for proper mitochondrial
CC axonal transport in motor neurons, in particular the retrograde
CC movement of mitochondria. Plays a role in protecting cells against
CC oxidative stress-induced cell death via its interaction with RNF112 (By
CC similarity). {ECO:0000250|UniProtKB:O55242,
CC ECO:0000250|UniProtKB:Q99720}.
CC -!- SUBUNIT: Homotrimer. Forms a ternary complex with ANK2 and ITPR3. The
CC complex is disrupted by agonists. Interacts with KCNA4. Interacts with
CC KCNA2; cocaine consumption leads to increased interaction. Interacts
CC with RNF112 in an oxidative stress-regulated manner.
CC {ECO:0000250|UniProtKB:O55242, ECO:0000250|UniProtKB:Q99720,
CC ECO:0000250|UniProtKB:Q9R0C9}.
CC -!- SUBCELLULAR LOCATION: Nucleus inner membrane
CC {ECO:0000250|UniProtKB:Q99720}. Nucleus outer membrane
CC {ECO:0000250|UniProtKB:Q99720}. Nucleus envelope
CC {ECO:0000250|UniProtKB:Q99720}. Cytoplasmic vesicle
CC {ECO:0000250|UniProtKB:Q99720}. Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q99720}. Membrane
CC {ECO:0000250|UniProtKB:Q99720}; Single-pass membrane protein
CC {ECO:0000250|UniProtKB:Q99720}. Lipid droplet
CC {ECO:0000250|UniProtKB:O55242}. 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:0000250|UniProtKB:Q99720}. Note=During interphase, detected at the
CC inner and outer nuclear membrane and the endoplasmic reticulum.
CC Detected on cytoplasmic vesicles during mitosis. Targeted to lipid
CC droplets, cholesterol and galactosylceramide-enriched domains of the
CC endoplasmic reticulum (By similarity). Enriched at cell-cell
CC communication regions, growth cone and postsynaptic structures.
CC Localization is modulated by ligand-binding. In motor neurons it is
CC enriched at cholinergic postsynaptic densities (By similarity).
CC {ECO:0000250|UniProtKB:O55242, ECO:0000250|UniProtKB:Q99720}.
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 -!- 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; AY823410; AAV71153.1; -; mRNA.
DR AlphaFoldDB; Q5PXE3; -.
DR SMR; Q5PXE3; -.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-SubCell.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030426; C:growth cone; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB.
DR GO; GO:0005811; C:lipid droplet; IEA:UniProtKB-SubCell.
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; ISS:UniProtKB.
DR GO; GO:0098839; C:postsynaptic density membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0036474; P:cell death in response to hydrogen peroxide; ISS:UniProtKB.
DR GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR GO; GO:0043523; P:regulation of neuron apoptotic process; ISS:UniProtKB.
DR InterPro; IPR006716; ERG2_sigma1_rcpt-like.
DR PANTHER; PTHR10868; PTHR10868; 1.
DR Pfam; PF04622; ERG2_Sigma1R; 1.
PE 2: Evidence at transcript level;
KW Cell junction; Cell membrane; Cell projection; Cytoplasmic vesicle;
KW Endoplasmic reticulum; Lipid droplet; Lipid transport; Membrane; Nucleus;
KW Postsynaptic cell membrane; Receptor; Synapse; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..223
FT /note="Sigma non-opioid intracellular receptor 1"
FT /id="PRO_0000268654"
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:0000250|UniProtKB:O55242"
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"
SQ SEQUENCE 223 AA; 25145 MW; 1C3C1DDFB7D942A8 CRC64;
MQWALGRRWV WAALLLAAAA VLTQVVWLWL GTQSFVFQHE EIAQLARQYA GLDHELAFSR
LIVELRRLHP GHVLPDEELQ WVFVNAGGWM GAMCLLHASL SEYVLLFGTA LGSRGHSGRY
WAEISDTIIS GTFHQWREGT TKSEVFYPGE TVVHGPGEAT AVEWGPNTWM VEYGRGVIPS
TLAFALADTI FSTQDFLTLF YTLRAYARGL RLEFTTYLFG QDS
