ID   SGMR1_XENTR             Reviewed;         221 AA.
AC   Q66IM1;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 85.
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   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: May function in lipid transport from the endoplasmic
CC       reticulum and be involved in a wide array of cellular functions
CC       probably through regulation of the biogenesis of lipid microdomains at
CC       the plasma membrane. May regulate calcium efflux at the endoplasmic
CC       reticulum (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Homotrimer (By similarity). {ECO:0000250|UniProtKB:Q99720}.
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}. 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 (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; BC081292; AAH81292.1; -; mRNA.
DR   RefSeq; NP_001008207.1; NM_001008206.1.
DR   AlphaFoldDB; Q66IM1; -.
DR   SMR; Q66IM1; -.
DR   STRING; 8364.ENSXETP00000034034; -.
DR   PaxDb; Q66IM1; -.
DR   DNASU; 493569; -.
DR   GeneID; 493569; -.
DR   KEGG; xtr:493569; -.
DR   CTD; 10280; -.
DR   Xenbase; XB-GENE-5786075; sigmar1.
DR   eggNOG; KOG4143; Eukaryota.
DR   HOGENOM; CLU_085469_0_0_1; -.
DR   InParanoid; Q66IM1; -.
DR   OrthoDB; 1285317at2759; -.
DR   PhylomeDB; Q66IM1; -.
DR   Proteomes; UP000008143; Chromosome 1.
DR   Proteomes; UP000790000; Unplaced.
DR   GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR   GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB.
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:0006869; P:lipid transport; IEA:UniProtKB-KW.
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   Cytoplasmic vesicle; Endoplasmic reticulum; Lipid transport; Membrane;
KW   Nucleus; Receptor; Reference proteome; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN           1..221
FT                   /note="Sigma non-opioid intracellular receptor 1"
FT                   /id="PRO_0000268661"
FT   TOPO_DOM        1..4
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000250|UniProtKB:Q99720"
FT   TRANSMEM        5..27
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:Q99720"
FT   TOPO_DOM        28..221
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q99720"
FT   REGION          96..103
FT                   /note="Important for ligand-binding"
FT                   /evidence="ECO:0000250|UniProtKB:Q60492"
FT   REGION          174..221
FT                   /note="C-terminal hydrophobic region"
FT                   /evidence="ECO:0000305"
FT   SITE            123
FT                   /note="Important for ligand binding"
FT                   /evidence="ECO:0000250|UniProtKB:Q99720"
FT   SITE            169
FT                   /note="Important for ligand binding"
FT                   /evidence="ECO:0000250|UniProtKB:Q99720"
SQ   SEQUENCE   221 AA;  24601 MW;  21E5CD2C3CD73F6F CRC64;
     MALWRGLRAV LAVAGLAVAV QLLRGWLGSK SYVFNREEIA RLAKEHSGLD YEVAFSKIIT
     ELRKKHPGRI LPDEDLQWVF VNAGGWMGSM CLLHASLTEY VLLFGTAVDT SGHSGRYWAE
     ISDTILSGTF RQWKEGSTKS EIFYPGDTIV HEVGEATSVQ WSAGTWMVEY GRGFIPSTLG
     FALADTIFST QDFLTLFYTV KVYGKALLLE TSTHLSELGF F