SGMR2_HUMAN
ID SGMR2_HUMAN Reviewed; 176 AA.
AC Q5BJF2; B4DS02; Q07823;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Sigma intracellular receptor 2 {ECO:0000305};
DE Short=Sigma-2 receptor {ECO:0000303|PubMed:28559337};
DE Short=Sigma2 receptor {ECO:0000303|PubMed:28559337};
DE AltName: Full=Meningioma-associated protein 30 {ECO:0000303|PubMed:7694637};
DE AltName: Full=Transmembrane protein 97 {ECO:0000312|HGNC:HGNC:28106};
GN Name=TMEM97 {ECO:0000312|HGNC:HGNC:28106};
GN Synonyms=MAC30 {ECO:0000303|PubMed:7694637},
GN S2R {ECO:0000303|PubMed:28559337};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=7694637;
RA Murphy M., Pykett M.J., Harnish P., Zang K.D., George D.L.;
RT "Identification and characterization of genes differentially expressed in
RT meningiomas.";
RL Cell Growth Differ. 4:715-722(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP TISSUE SPECIFICITY.
RX PubMed=15375745; DOI=10.14670/hh-19.1021;
RA Kayed H., Kleeff J., Ding J., Hammer J., Giese T., Zentgraf H.,
RA Buchler M.W., Friess H.;
RT "Expression analysis of MAC30 in human pancreatic cancer and tumors of the
RT gastrointestinal tract.";
RL Histol. Histopathol. 19:1021-1031(2004).
RN [6]
RP INDUCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=18070364; DOI=10.1186/1471-2407-7-223;
RA Wilcox C.B., Feddes G.O., Willett-Brozick J.E., Hsu L.C., DeLoia J.A.,
RA Baysal B.E.;
RT "Coordinate up-regulation of TMEM97 and cholesterol biosynthesis genes in
RT normal ovarian surface epithelial cells treated with progesterone:
RT implications for pathogenesis of ovarian cancer.";
RL BMC Cancer 7:223-223(2007).
RN [7]
RP FUNCTION, INTERACTION WITH NPC1, AND SUBCELLULAR LOCATION.
RX PubMed=19583955; DOI=10.1016/j.cmet.2009.05.009;
RA Bartz F., Kern L., Erz D., Zhu M., Gilbert D., Meinhof T., Wirkner U.,
RA Erfle H., Muckenthaler M., Pepperkok R., Runz H.;
RT "Identification of cholesterol-regulating genes by targeted RNAi
RT screening.";
RL Cell Metab. 10:63-75(2009).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [9]
RP FUNCTION, AND REVIEW.
RX PubMed=22292588; DOI=10.1517/17425255.2012.658367;
RA Ahmed I.S., Chamberlain C., Craven R.J.;
RT "S2R(Pgrmc1): the cytochrome-related sigma-2 receptor that regulates lipid
RT and drug metabolism and hormone signaling.";
RL Expert Opin. Drug Metab. Toxicol. 8:361-370(2012).
RN [10]
RP POSSIBLE FUNCTION AS STEROL ISOMERASE, AND IDENTIFICATION OF EXPERA DOMAIN.
RX PubMed=25566323; DOI=10.3389/fgene.2014.00439;
RA Sanchez-Pulido L., Ponting C.P.;
RT "TM6SF2 and MAC30, new enzyme homologs in sterol metabolism and common
RT metabolic disease.";
RL Front. Genet. 5:439-439(2014).
RN [11]
RP REVIEW, FUNCTION, TISSUE SPECIFICITY, AND MISCELLANEOUS.
RX PubMed=23922215; DOI=10.1002/med.21297;
RA Huang Y.S., Lu H.L., Zhang L.J., Wu Z.;
RT "Sigma-2 receptor ligands and their perspectives in cancer diagnosis and
RT therapy.";
RL Med. Res. Rev. 34:532-566(2014).
RN [12]
RP REVIEW, FUNCTION, AND MISCELLANEOUS.
RX PubMed=25620095; DOI=10.2174/0929867322666150114163607;
RA Guo L., Zhen X.;
RT "Sigma-2 receptor ligands: neurobiological effects.";
RL Curr. Med. Chem. 22:989-1003(2015).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [14]
RP IDENTIFICATION AS SIGMA-2 RECEPTOR, AND MUTAGENESIS OF GLU-11; ASP-29;
RP GLU-37; GLU-42; GLU-53; ASP-56; GLU-61; GLU-73; GLU-121; ASP-122; GLU-135;
RP GLU-139; GLU-170 AND GLU-171.
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).
RN [15]
RP CAUTION.
RX PubMed=28007569; DOI=10.1016/j.phrs.2016.12.023;
RA Pati M.L., Groza D., Riganti C., Kopecka J., Niso M., Berardi F., Hager S.,
RA Heffeter P., Hirai M., Tsugawa H., Kabe Y., Suematsu M., Abate C.;
RT "Sigma-2 receptor and progesterone receptor membrane component 1 (PGRMC1)
RT are two different proteins: Proofs by fluorescent labeling and binding of
RT sigma-2 receptor ligands to PGRMC1.";
RL Pharmacol. Res. 117:67-74(2017).
CC -!- FUNCTION: Intracellular orphan receptor that binds numerous drugs and
CC which is highly expressed in various proliferating cancer cells
CC (PubMed:28559337). Corresponds to the sigma-2 receptor, which is
CC thought to play important role in regulating cell survival, morphology
CC and differentiation (PubMed:23922215, PubMed:25620095). Under
CC investigation for its potential diagnostic and therapeutic uses
CC (PubMed:23922215, PubMed:25620095). May play a role as a regulator of
CC cellular cholesterol homeostasis (PubMed:19583955). May function as
CC sterol isomerase (PubMed:25566323). May alter the activity of some
CC cytochrome P450 proteins (PubMed:22292588).
CC {ECO:0000269|PubMed:19583955, ECO:0000269|PubMed:28559337,
CC ECO:0000303|PubMed:22292588, ECO:0000303|PubMed:23922215,
CC ECO:0000303|PubMed:25620095, ECO:0000305|PubMed:25566323}.
CC -!- SUBUNIT: Interacts with NPC1. {ECO:0000269|PubMed:19583955}.
CC -!- INTERACTION:
CC Q5BJF2; A6NM10-2: AQP12B; NbExp=3; IntAct=EBI-12111910, EBI-17265552;
CC Q5BJF2; P41181: AQP2; NbExp=3; IntAct=EBI-12111910, EBI-12701138;
CC Q5BJF2; Q13520: AQP6; NbExp=3; IntAct=EBI-12111910, EBI-13059134;
CC Q5BJF2; Q3SXY8: ARL13B; NbExp=3; IntAct=EBI-12111910, EBI-11343438;
CC Q5BJF2; Q8WWH4: ASZ1; NbExp=3; IntAct=EBI-12111910, EBI-12239061;
CC Q5BJF2; O75787: ATP6AP2; NbExp=3; IntAct=EBI-12111910, EBI-2512037;
CC Q5BJF2; Q9BXK5: BCL2L13; NbExp=3; IntAct=EBI-12111910, EBI-747430;
CC Q5BJF2; Q13323: BIK; NbExp=3; IntAct=EBI-12111910, EBI-700794;
CC Q5BJF2; P19397: CD53; NbExp=3; IntAct=EBI-12111910, EBI-6657396;
CC Q5BJF2; P04233-2: CD74; NbExp=3; IntAct=EBI-12111910, EBI-12222807;
CC Q5BJF2; Q99675: CGRRF1; NbExp=3; IntAct=EBI-12111910, EBI-2130213;
CC Q5BJF2; O95471: CLDN7; NbExp=3; IntAct=EBI-12111910, EBI-740744;
CC Q5BJF2; Q9BQT9: CLSTN3; NbExp=3; IntAct=EBI-12111910, EBI-11291074;
CC Q5BJF2; Q7Z7G2: CPLX4; NbExp=3; IntAct=EBI-12111910, EBI-18013275;
CC Q5BJF2; Q15125: EBP; NbExp=3; IntAct=EBI-12111910, EBI-3915253;
CC Q5BJF2; Q9Y282: ERGIC3; NbExp=3; IntAct=EBI-12111910, EBI-781551;
CC Q5BJF2; Q5JX71: FAM209A; NbExp=3; IntAct=EBI-12111910, EBI-18304435;
CC Q5BJF2; O15552: FFAR2; NbExp=3; IntAct=EBI-12111910, EBI-2833872;
CC Q5BJF2; Q9Y680: FKBP7; NbExp=3; IntAct=EBI-12111910, EBI-3918971;
CC Q5BJF2; A2A2Y4: FRMD3; NbExp=3; IntAct=EBI-12111910, EBI-6911547;
CC Q5BJF2; Q14802-3: FXYD3; NbExp=3; IntAct=EBI-12111910, EBI-12175685;
CC Q5BJF2; O75712: GJB3; NbExp=3; IntAct=EBI-12111910, EBI-3908586;
CC Q5BJF2; O95377: GJB5; NbExp=3; IntAct=EBI-12111910, EBI-3909454;
CC Q5BJF2; Q8TDT2: GPR152; NbExp=3; IntAct=EBI-12111910, EBI-13345167;
CC Q5BJF2; O60883: GPR37L1; NbExp=3; IntAct=EBI-12111910, EBI-2927498;
CC Q5BJF2; Q8TED1: GPX8; NbExp=3; IntAct=EBI-12111910, EBI-11721746;
CC Q5BJF2; Q7Z5P4: HSD17B13; NbExp=3; IntAct=EBI-12111910, EBI-18053395;
CC Q5BJF2; P38484: IFNGR2; NbExp=3; IntAct=EBI-12111910, EBI-3905457;
CC Q5BJF2; P43628: KIR2DL3; NbExp=3; IntAct=EBI-12111910, EBI-8632435;
CC Q5BJF2; A8MZ59: LEUTX; NbExp=3; IntAct=EBI-12111910, EBI-17490413;
CC Q5BJF2; Q8TAF8: LHFPL5; NbExp=3; IntAct=EBI-12111910, EBI-2820517;
CC Q5BJF2; Q9H400: LIME1; NbExp=3; IntAct=EBI-12111910, EBI-2830566;
CC Q5BJF2; Q96AG4: LRRC59; NbExp=3; IntAct=EBI-12111910, EBI-358888;
CC Q5BJF2; Q9GZY8-5: MFF; NbExp=3; IntAct=EBI-12111910, EBI-11956541;
CC Q5BJF2; Q6IN84: MRM1; NbExp=3; IntAct=EBI-12111910, EBI-5454865;
CC Q5BJF2; Q9H2K0: MTIF3; NbExp=3; IntAct=EBI-12111910, EBI-3923617;
CC Q5BJF2; P15941-11: MUC1; NbExp=3; IntAct=EBI-12111910, EBI-17263240;
CC Q5BJF2; Q9Y375: NDUFAF1; NbExp=3; IntAct=EBI-12111910, EBI-741874;
CC Q5BJF2; Q8N183: NDUFAF2; NbExp=3; IntAct=EBI-12111910, EBI-2682365;
CC Q5BJF2; O14524-2: NEMP1; NbExp=3; IntAct=EBI-12111910, EBI-10969203;
CC Q5BJF2; Q9BQ51: PDCD1LG2; NbExp=3; IntAct=EBI-12111910, EBI-16427978;
CC Q5BJF2; Q13113: PDZK1IP1; NbExp=3; IntAct=EBI-12111910, EBI-716063;
CC Q5BJF2; P60201-2: PLP1; NbExp=3; IntAct=EBI-12111910, EBI-12188331;
CC Q5BJF2; Q9H902: REEP1; NbExp=3; IntAct=EBI-12111910, EBI-1644241;
CC Q5BJF2; Q9UBD6: RHCG; NbExp=3; IntAct=EBI-12111910, EBI-15853497;
CC Q5BJF2; Q96K19-5: RNF170; NbExp=3; IntAct=EBI-12111910, EBI-12055631;
CC Q5BJF2; Q9NR31: SAR1A; NbExp=3; IntAct=EBI-12111910, EBI-3920694;
CC Q5BJF2; O95470: SGPL1; NbExp=3; IntAct=EBI-12111910, EBI-1046170;
CC Q5BJF2; Q13336-2: SLC14A1; NbExp=3; IntAct=EBI-12111910, EBI-19141793;
CC Q5BJF2; Q15849: SLC14A2; NbExp=4; IntAct=EBI-12111910, EBI-1573290;
CC Q5BJF2; O43278-2: SPINT1; NbExp=3; IntAct=EBI-12111910, EBI-12078338;
CC Q5BJF2; Q8WWF3: SSMEM1; NbExp=3; IntAct=EBI-12111910, EBI-17280858;
CC Q5BJF2; Q9BVX2: TMEM106C; NbExp=3; IntAct=EBI-12111910, EBI-2821497;
CC Q5BJF2; Q9NUH8: TMEM14B; NbExp=3; IntAct=EBI-12111910, EBI-8638294;
CC Q5BJF2; Q96B21: TMEM45B; NbExp=3; IntAct=EBI-12111910, EBI-3923061;
CC Q5BJF2; Q4KMG9: TMEM52B; NbExp=3; IntAct=EBI-12111910, EBI-18178701;
CC Q5BJF2; Q9BSE2: TMEM79; NbExp=3; IntAct=EBI-12111910, EBI-8649725;
CC Q5BJF2; Q9Y320: TMX2; NbExp=3; IntAct=EBI-12111910, EBI-6447886;
CC Q5BJF2; Q9H7M9: VSIR; NbExp=3; IntAct=EBI-12111910, EBI-744988;
CC -!- SUBCELLULAR LOCATION: Nucleus membrane {ECO:0000269|PubMed:19583955};
CC Multi-pass membrane protein {ECO:0000255}. Rough endoplasmic reticulum
CC membrane {ECO:0000269|PubMed:19583955}; 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:0000269|PubMed:19583955}.
CC -!- TISSUE SPECIFICITY: Widely expressed in normal tissues. Expressed in
CC pancreatic, renal, breast, colon, ovarian surface epithelial (OSE)
CC cells. Highly expressed in various proliferating cancer cells
CC (PubMed:23922215). {ECO:0000269|PubMed:15375745,
CC ECO:0000269|PubMed:18070364, ECO:0000269|PubMed:7694637,
CC ECO:0000303|PubMed:23922215}.
CC -!- INDUCTION: Up-regulated in ovarian surface epithelial (OSE) cells with
CC progesterone. {ECO:0000269|PubMed:18070364}.
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:0000303|PubMed:28559337}.
CC -!- MISCELLANEOUS: Potentially useful for cancer diagnostics or as target
CC for anticancer therapeutics or adjuvant anticancer treatment agents
CC (PubMed:23922215). Some exogenous ligands display a neuroprotective
CC effect (PubMed:25620095). {ECO:0000303|PubMed:23922215,
CC ECO:0000303|PubMed:25620095}.
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 (PubMed:22292588, PubMed:28007569). {ECO:0000269|PubMed:28007569,
CC ECO:0000269|PubMed:28559337, ECO:0000303|PubMed:22292588}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA16188.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; L19183; AAA16188.1; ALT_FRAME; mRNA.
DR EMBL; AK299511; BAG61464.1; -; mRNA.
DR EMBL; AC002094; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC091504; AAH91504.1; -; mRNA.
DR CCDS; CCDS11226.2; -.
DR PIR; I65744; I65744.
DR RefSeq; NP_055388.2; NM_014573.2.
DR AlphaFoldDB; Q5BJF2; -.
DR SMR; Q5BJF2; -.
DR BioGRID; 118158; 94.
DR IntAct; Q5BJF2; 74.
DR MINT; Q5BJF2; -.
DR STRING; 9606.ENSP00000226230; -.
DR BindingDB; Q5BJF2; -.
DR ChEMBL; CHEMBL4105907; -.
DR GuidetoPHARMACOLOGY; 2553; -.
DR TCDB; 8.A.93.1.1; the sigma2 receptor or tmem97 (s2r) family.
DR iPTMnet; Q5BJF2; -.
DR MetOSite; Q5BJF2; -.
DR PhosphoSitePlus; Q5BJF2; -.
DR SwissPalm; Q5BJF2; -.
DR BioMuta; TMEM97; -.
DR DMDM; 74736009; -.
DR EPD; Q5BJF2; -.
DR jPOST; Q5BJF2; -.
DR MassIVE; Q5BJF2; -.
DR MaxQB; Q5BJF2; -.
DR PaxDb; Q5BJF2; -.
DR PeptideAtlas; Q5BJF2; -.
DR PRIDE; Q5BJF2; -.
DR ProteomicsDB; 62679; -.
DR TopDownProteomics; Q5BJF2; -.
DR Antibodypedia; 50911; 103 antibodies from 11 providers.
DR DNASU; 27346; -.
DR Ensembl; ENST00000226230.8; ENSP00000226230.6; ENSG00000109084.14.
DR GeneID; 27346; -.
DR KEGG; hsa:27346; -.
DR MANE-Select; ENST00000226230.8; ENSP00000226230.6; NM_014573.3; NP_055388.2.
DR UCSC; uc002hat.3; human.
DR CTD; 27346; -.
DR DisGeNET; 27346; -.
DR GeneCards; TMEM97; -.
DR HGNC; HGNC:28106; TMEM97.
DR HPA; ENSG00000109084; Tissue enhanced (liver, pancreas).
DR MIM; 612912; gene.
DR neXtProt; NX_Q5BJF2; -.
DR OpenTargets; ENSG00000109084; -.
DR PharmGKB; PA143485635; -.
DR VEuPathDB; HostDB:ENSG00000109084; -.
DR eggNOG; ENOG502S64S; Eukaryota.
DR GeneTree; ENSGT00390000007149; -.
DR HOGENOM; CLU_086812_1_0_1; -.
DR InParanoid; Q5BJF2; -.
DR OMA; FYFASHI; -.
DR OrthoDB; 1514706at2759; -.
DR PhylomeDB; Q5BJF2; -.
DR TreeFam; TF300241; -.
DR PathwayCommons; Q5BJF2; -.
DR SignaLink; Q5BJF2; -.
DR SIGNOR; Q5BJF2; -.
DR BioGRID-ORCS; 27346; 48 hits in 1086 CRISPR screens.
DR ChiTaRS; TMEM97; human.
DR GenomeRNAi; 27346; -.
DR Pharos; Q5BJF2; Tchem.
DR PRO; PR:Q5BJF2; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q5BJF2; protein.
DR Bgee; ENSG00000109084; Expressed in adrenal tissue and 202 other tissues.
DR ExpressionAtlas; Q5BJF2; baseline and differential.
DR Genevisible; Q5BJF2; HS.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:HPA.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005764; C:lysosome; IDA:UniProtKB.
DR GO; GO:0031965; C:nuclear membrane; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0005791; C:rough endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0030867; C:rough endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0042632; P:cholesterol homeostasis; IDA:UniProtKB.
DR GO; GO:0001558; P:regulation of cell growth; NAS: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 Endoplasmic reticulum; Membrane; Nucleus; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..176
FT /note="Sigma intracellular receptor 2"
FT /id="PRO_0000254567"
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..140
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 141..161
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 162..176
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 10..158
FT /note="EXPERA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01087"
FT MUTAGEN 11
FT /note="E->Q: Decreases DTG binding."
FT /evidence="ECO:0000269|PubMed:28559337"
FT MUTAGEN 29
FT /note="D->N: Abolishes DTG binding."
FT /evidence="ECO:0000269|PubMed:28559337"
FT MUTAGEN 37
FT /note="E->Q: No effect on DTG binding."
FT /evidence="ECO:0000269|PubMed:28559337"
FT MUTAGEN 42
FT /note="E->Q: No effect on DTG binding."
FT /evidence="ECO:0000269|PubMed:28559337"
FT MUTAGEN 53
FT /note="E->Q: No effect on DTG binding."
FT /evidence="ECO:0000269|PubMed:28559337"
FT MUTAGEN 56
FT /note="D->N: Abolishes DTG binding."
FT /evidence="ECO:0000269|PubMed:28559337"
FT MUTAGEN 61
FT /note="E->Q: No effect on DTG binding."
FT /evidence="ECO:0000269|PubMed:28559337"
FT MUTAGEN 73
FT /note="E->Q: No effect on DTG binding."
FT /evidence="ECO:0000269|PubMed:28559337"
FT MUTAGEN 121
FT /note="E->Q: No effect on DTG binding."
FT /evidence="ECO:0000269|PubMed:28559337"
FT MUTAGEN 122
FT /note="D->N: Decreases DTG binding."
FT /evidence="ECO:0000269|PubMed:28559337"
FT MUTAGEN 135
FT /note="E->Q: Decreases DTG binding."
FT /evidence="ECO:0000269|PubMed:28559337"
FT MUTAGEN 139
FT /note="E->Q: Decreases DTG binding."
FT /evidence="ECO:0000269|PubMed:28559337"
FT MUTAGEN 170
FT /note="E->Q: Decreases DTG binding."
FT /evidence="ECO:0000269|PubMed:28559337"
FT MUTAGEN 171
FT /note="E->Q: Decreases DTG binding."
FT /evidence="ECO:0000269|PubMed:28559337"
FT CONFLICT 5
FT /note="A -> S (in Ref. 1; AAA16188)"
FT /evidence="ECO:0000305"
FT CONFLICT 34
FT /note="L -> V (in Ref. 1; AAA16188)"
FT /evidence="ECO:0000305"
FT CONFLICT 113
FT /note="P -> L (in Ref. 1; AAA16188)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 176 AA; 20848 MW; 685248D421877F84 CRC64;
MGAPATRRCV EWLLGLYFLS HIPITLFMDL QAVLPRELYP VEFRNLLKWY AKEFKDPLLQ
EPPAWFKSFL FCELVFQLPF FPIATYAFLK GSCKWIRTPA IIYSVHTMTT LIPILSTFLF
EDFSKASGFK GQRPETLHER LTLVSVYAPY LLIPFILLIF MLRSPYYKYE EKRKKK
