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SGMR2_BOVIN
ID   SGMR2_BOVIN             Reviewed;         176 AA.
AC   Q3MHW7; A1L510;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2005, sequence version 1.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=Sigma intracellular receptor 2 {ECO:0000303|PubMed:28559337};
DE            Short=Sigma-2 receptor {ECO:0000303|PubMed:28559337};
DE            Short=Sigma2 receptor {ECO:0000303|PubMed:28559337};
DE   AltName: Full=Transmembrane protein 97;
GN   Name=TMEM97; Synonyms=S2R {ECO:0000303|PubMed:28559337};
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA   Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA   Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT   "Characterization of 954 bovine full-CDS cDNA sequences.";
RL   BMC Genomics 6:166-166(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Uterus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   FUNCTION.
RX   PubMed=28559337; DOI=10.1073/pnas.1705154114;
RA   Alon A., Schmidt H.R., Wood M.D., Sahn J.J., Martin S.F., Kruse A.C.;
RT   "Identification of the gene that codes for the sigma2 receptor.";
RL   Proc. Natl. Acad. Sci. U.S.A. 114:7160-7165(2017).
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:0000269|PubMed:28559337}.
CC   -!- SUBUNIT: Interacts with NPC1. {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}.
CC   -!- CAUTION: The molecular identity of the sigma-2 receptor has been
CC       unclear for a long time. It is now identified as TMEM97
CC       (PubMed:28559337). Previously identified as PGRMC1 (AC O00264).
CC       {ECO:0000250|UniProtKB:Q5BJF2, ECO:0000269|PubMed:28559337}.
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DR   EMBL; BT029797; ABM06065.1; -; mRNA.
DR   EMBL; BC104594; AAI04595.1; -; mRNA.
DR   RefSeq; NP_001029575.1; NM_001034403.1.
DR   PDB; 7M93; X-ray; 2.94 A; A/B/C/D=1-168.
DR   PDB; 7M94; X-ray; 2.71 A; A/B/C/D=1-168.
DR   PDB; 7M95; X-ray; 2.41 A; A/B=1-168.
DR   PDB; 7M96; X-ray; 2.41 A; A/B/C/D=1-168.
DR   PDB; 7MFI; X-ray; 2.81 A; A/B/C/D=1-168.
DR   PDBsum; 7M93; -.
DR   PDBsum; 7M94; -.
DR   PDBsum; 7M95; -.
DR   PDBsum; 7M96; -.
DR   PDBsum; 7MFI; -.
DR   AlphaFoldDB; Q3MHW7; -.
DR   SMR; Q3MHW7; -.
DR   STRING; 9913.ENSBTAP00000010666; -.
DR   PaxDb; Q3MHW7; -.
DR   Ensembl; ENSBTAT00000010666; ENSBTAP00000010666; ENSBTAG00000008109.
DR   GeneID; 511378; -.
DR   KEGG; bta:511378; -.
DR   CTD; 27346; -.
DR   VEuPathDB; HostDB:ENSBTAG00000008109; -.
DR   VGNC; VGNC:36129; TMEM97.
DR   eggNOG; ENOG502RZRX; Eukaryota.
DR   GeneTree; ENSGT00390000007149; -.
DR   HOGENOM; CLU_086812_1_0_1; -.
DR   InParanoid; Q3MHW7; -.
DR   OMA; FYFASHI; -.
DR   OrthoDB; 1459246at2759; -.
DR   TreeFam; TF300241; -.
DR   Proteomes; UP000009136; Chromosome 19.
DR   Bgee; ENSBTAG00000008109; Expressed in diaphragm and 105 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   1: Evidence at protein level;
KW   3D-structure; Endoplasmic reticulum; Membrane; Nucleus; Reference proteome;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..176
FT                   /note="Sigma intracellular receptor 2"
FT                   /id="PRO_0000254566"
FT   TOPO_DOM        1..9
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        10..30
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        31..68
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        69..89
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        90..99
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        100..120
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        121..141
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        142..162
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        163..176
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          10..158
FT                   /note="EXPERA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01087"
FT   HELIX           6..27
FT                   /evidence="ECO:0007829|PDB:7M95"
FT   HELIX           29..31
FT                   /evidence="ECO:0007829|PDB:7M95"
FT   HELIX           36..38
FT                   /evidence="ECO:0007829|PDB:7M95"
FT   HELIX           41..54
FT                   /evidence="ECO:0007829|PDB:7M95"
FT   STRAND          57..61
FT                   /evidence="ECO:0007829|PDB:7M95"
FT   HELIX           64..75
FT                   /evidence="ECO:0007829|PDB:7M95"
FT   HELIX           77..90
FT                   /evidence="ECO:0007829|PDB:7M95"
FT   HELIX           94..96
FT                   /evidence="ECO:0007829|PDB:7M95"
FT   HELIX           97..120
FT                   /evidence="ECO:0007829|PDB:7M95"
FT   TURN            127..131
FT                   /evidence="ECO:0007829|PDB:7M95"
FT   HELIX           137..147
FT                   /evidence="ECO:0007829|PDB:7M95"
FT   HELIX           149..163
FT                   /evidence="ECO:0007829|PDB:7M95"
FT   HELIX           165..167
FT                   /evidence="ECO:0007829|PDB:7M96"
SQ   SEQUENCE   176 AA;  20784 MW;  320AEFE88377504A CRC64;
     MGTLGARRGL EWFLGFYFLS HIPITLLMDL QGVLPRDLYP VELRNLQQWY IEEFKDPLLQ
     TPPAWFKSFL FCELVFQLPF FPIAAYAFFK GGCKWIRTPA IIYSVHTMTT LIPILSTLLL
     DDFSKASHFR GQGPKTFQER LFLISVYIPY FLIPLILLLF MVRNPYYKSE EKRKKK
 
 
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