SGMR2_XENTR
ID SGMR2_XENTR Reviewed; 171 AA.
AC Q6DFQ5;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Sigma intracellular receptor 2 {ECO:0000250|UniProtKB:Q5BJF2};
DE Short=Sigma-2 receptor {ECO:0000250|UniProtKB:Q5BJF2};
DE Short=Sigma2 receptor {ECO:0000250|UniProtKB:Q5BJF2};
DE AltName: Full=Transmembrane protein 97;
GN Name=tmem97; Synonyms=s2r {ECO:0000250|UniProtKB:Q5BJF2};
GN ORFNames=TEgg113g04.1;
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].
RC TISSUE=Egg;
RG Sanger Xenopus tropicalis EST/cDNA project;
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Intracellular orphan receptor that binds numerous drugs and
CC which is highly expressed in various proliferating cells. Corresponds
CC to the sigma-2 receptor, which is thought to play important role in
CC regulating cell survival, morphology and differentiation. May play a
CC role as a regulator of cellular cholesterol homeostasis. May function
CC as sterol isomerase. May alter the activity of some cytochrome P450
CC proteins. {ECO:0000250|UniProtKB:Q5BJF2}.
CC -!- SUBCELLULAR LOCATION: Nucleus membrane {ECO:0000250|UniProtKB:Q5BJF2};
CC Multi-pass membrane protein {ECO:0000255}. Rough endoplasmic reticulum
CC membrane {ECO:0000250|UniProtKB:Q5BJF2}; Multi-pass membrane protein
CC {ECO:0000255}. Note=Localized at cell membrane and in lysosomes in
CC sterol-depleted cells when expression of endogenous TMEM97 is
CC stimulated. {ECO:0000250|UniProtKB:Q5BJF2}.
CC -!- MISCELLANEOUS: Sigma receptors are classified into two subtypes (Sigma-
CC 1 and Sigma-2) based on their different pharmacological profile. Sigma-
CC 2 receptors are identified by radioligand-binding studies as a binding
CC site with high affinity for di-o-tolylguanidine (DTG) and haloperidol.
CC {ECO:0000250|UniProtKB:Q5BJF2}.
CC -!- SIMILARITY: Belongs to the TMEM97/sigma-2 receptor family.
CC {ECO:0000305}.
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DR EMBL; CR848476; CAJ81433.1; -; mRNA.
DR EMBL; BC076679; AAH76679.1; -; mRNA.
DR RefSeq; NP_001005014.1; NM_001005014.2.
DR AlphaFoldDB; Q6DFQ5; -.
DR SMR; Q6DFQ5; -.
DR STRING; 8364.ENSXETP00000011270; -.
DR PaxDb; Q6DFQ5; -.
DR DNASU; 448515; -.
DR Ensembl; ENSXETT00000011270; ENSXETP00000011270; ENSXETG00000002126.
DR GeneID; 448515; -.
DR KEGG; xtr:448515; -.
DR CTD; 27346; -.
DR Xenbase; XB-GENE-5905052; tmem97.
DR eggNOG; ENOG502RZRX; Eukaryota.
DR HOGENOM; CLU_086812_1_0_1; -.
DR InParanoid; Q6DFQ5; -.
DR OrthoDB; 1459246at2759; -.
DR PhylomeDB; Q6DFQ5; -.
DR Proteomes; UP000008143; Chromosome 2.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000002126; Expressed in liver and 22 other tissues.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005764; C:lysosome; ISS:UniProtKB.
DR GO; GO:0031965; C:nuclear membrane; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0005791; C:rough endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0030867; C:rough endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0042632; P:cholesterol homeostasis; ISS:UniProtKB.
DR InterPro; IPR033118; EXPERA.
DR InterPro; IPR016964; Sigma2_recept.
DR PIRSF; PIRSF031032; TMP_97_prd; 1.
DR PROSITE; PS51751; EXPERA; 1.
PE 2: Evidence at transcript level;
KW Endoplasmic reticulum; Membrane; Nucleus; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..171
FT /note="Sigma intracellular receptor 2"
FT /id="PRO_0000254571"
FT TOPO_DOM 1..6
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 7..27
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 28..66
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 67..87
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 88..97
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 98..118
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 119..137
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 138..158
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 159..171
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 8..153
FT /note="EXPERA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01087"
SQ SEQUENCE 171 AA; 19846 MW; 25F8F77AFCB5974C CRC64;
MAVCARLLEW IFFFYFFSHI PITLLVDLQA VLPPSLYPQE LLDLMKWYTV AFKDHLMANP
PPWFKSFVYC EAILQLPFFP VAAYAFFKGG CKWIRIPAIV YSAHVATTVI AIIGHILFGE
FPKSDVIAPL TQKDRLTLVS IYAPYLLVPV LLLLTMLFSP RYRQEEKRKR K