PGRC1_HUMAN
ID PGRC1_HUMAN Reviewed; 195 AA.
AC O00264; B7Z1L3; Q9UGJ9;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 197.
DE RecName: Full=Membrane-associated progesterone receptor component 1;
DE Short=mPR;
DE AltName: Full=Dap1 {ECO:0000303|PubMed:28396637};
DE AltName: Full=IZA {ECO:0000303|PubMed:28396637};
GN Name=PGRMC1 {ECO:0000312|HGNC:HGNC:16090};
GN Synonyms=HPR6.6 {ECO:0000303|PubMed:9705155}, PGRMC;
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] (ISOFORM 1).
RC TISSUE=Liver;
RX PubMed=9705155; DOI=10.1515/bchm.1998.379.7.907;
RA Gerdes D., Wehling M., Leube B., Falkenstein E.;
RT "Cloning and tissue expression of two putative steroid membrane
RT receptors.";
RL Biol. Chem. 379:907-911(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Cerebellum;
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=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Ovary;
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 [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-109 (ISOFORM 1).
RX PubMed=11697142; DOI=10.3109/10425170109042047;
RA Bernauer S., Wehling M., Gerdes D., Falkenstein E.;
RT "The human membrane progesterone receptor gene: genomic structure and
RT promoter analysis.";
RL DNA Seq. 12:13-25(2001).
RN [7]
RP PROTEIN SEQUENCE OF 48-67; 81-88; 105-119; 124-132 AND 173-192,
RP PHOSPHORYLATION AT SER-181, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryonic kidney;
RA Bienvenut W.V., Waridel P., Quadroni M.;
RL Submitted (MAR-2009) to UniProtKB.
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-57, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Prostate cancer;
RX PubMed=17487921; DOI=10.1002/elps.200600782;
RA Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.;
RT "Toward a global characterization of the phosphoproteome in prostate cancer
RT cells: identification of phosphoproteins in the LNCaP cell line.";
RL Electrophoresis 28:2027-2034(2007).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17924679; DOI=10.1021/pr070152u;
RA Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
RT "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells
RT and high confident phosphopeptide identification by cross-validation of
RT MS/MS and MS/MS/MS spectra.";
RL J. Proteome Res. 6:4150-4162(2007).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-57, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=T-cell;
RX PubMed=19367720; DOI=10.1021/pr800500r;
RA Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
RT "Phosphorylation analysis of primary human T lymphocytes using sequential
RT IMAC and titanium oxide enrichment.";
RL J. Proteome Res. 7:5167-5176(2008).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-54 AND SER-57, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-57 AND SER-181, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-57, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18318008; DOI=10.1002/pmic.200700884;
RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
RA Zou H., Gu J.;
RT "Large-scale phosphoproteome analysis of human liver tissue by enrichment
RT and fractionation of phosphopeptides with strong anion exchange
RT chromatography.";
RL Proteomics 8:1346-1361(2008).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-57, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-57, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-57 AND SER-181, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [20]
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 [21]
RP CAUTION.
RX PubMed=21730960; DOI=10.1038/ncomms1386;
RA Xu J., Zeng C., Chu W., Pan F., Rothfuss J.M., Zhang F., Tu Z., Zhou D.,
RA Zeng D., Vangveravong S., Johnston F., Spitzer D., Chang K.C.,
RA Hotchkiss R.S., Hawkins W.G., Wheeler K.T., Mach R.H.;
RT "Identification of the PGRMC1 protein complex as the putative sigma-2
RT receptor binding site.";
RL Nat. Commun. 2:380-380(2011).
RN [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-57 AND SER-181, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [23]
RP CAUTION.
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 [24]
RP MISCELLANEOUS, REVIEW, AND SUBUNIT.
RX PubMed=23763432; DOI=10.1111/jne.12060;
RA Petersen S.L., Intlekofer K.A., Moura-Conlon P.J., Brewer D.N.,
RA Del Pino Sans J., Lopez J.A.;
RT "Nonclassical progesterone signalling molecules in the nervous system.";
RL J. Neuroendocrinol. 25:991-1001(2013).
RN [25]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-57 AND SER-181, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [26]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-54; SER-57; THR-74 AND
RP SER-181, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [27]
RP TISSUE SPECIFICITY.
RX PubMed=23793472; DOI=10.1177/1933719113492208;
RA Bunch K., Tinnemore D., Huff S., Hoffer Z.S., Burney R.O., Stallings J.D.;
RT "Expression patterns of progesterone receptor membrane components 1 and 2
RT in endometria from women with and without endometriosis.";
RL Reprod. Sci. 21:190-197(2014).
RN [28]
RP FUNCTION.
RX PubMed=25675345; DOI=10.1021/bi501177e;
RA Kaluka D., Batabyal D., Chiang B.Y., Poulos T.L., Yeh S.R.;
RT "Spectroscopic and mutagenesis studies of human PGRMC1.";
RL Biochemistry 54:1638-1647(2015).
RN [29]
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 [30]
RP FUNCTION, INTERACTION WITH FECH, AND HEME-BINDING.
RX PubMed=27599036; DOI=10.1021/acs.biochem.6b00756;
RA Piel R.B. III, Shiferaw M.T., Vashisht A.A., Marcero J.R., Praissman J.L.,
RA Phillips J.D., Wohlschlegel J.A., Medlock A.E.;
RT "A Novel Role for Progesterone Receptor Membrane Component 1 (PGRMC1): A
RT Partner and Regulator of Ferrochelatase.";
RL Biochemistry 55:5204-5217(2016).
RN [31]
RP REVIEW, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND MISCELLANEOUS.
RX PubMed=28396637; DOI=10.3389/fphar.2017.00159;
RA Ryu C.S., Klein K., Zanger U.M.;
RT "Membrane associated progesterone receptors: promiscuous proteins with
RT pleiotropic functions - focus on interactions with cytochromes P450.";
RL Front. Pharmacol. 8:159-159(2017).
RN [32]
RP CAUTION.
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 [33]
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).
RN [34] {ECO:0007744|PDB:4X8Y}
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 72-195 IN COMPLEX WITH HEME,
RP INTERACTION WITH CYP1A1; CYP3A4 AND EGFR, SUBUNIT, HEME-BINDING, FUNCTION,
RP AND MUTAGENESIS OF TYR-113.
RX PubMed=26988023; DOI=10.1038/ncomms11030;
RA Kabe Y., Nakane T., Koike I., Yamamoto T., Sugiura Y., Harada E.,
RA Sugase K., Shimamura T., Ohmura M., Muraoka K., Yamamoto A., Uchida T.,
RA Iwata S., Yamaguchi Y., Krayukhina E., Noda M., Handa H., Ishimori K.,
RA Uchiyama S., Kobayashi T., Suematsu M.;
RT "Haem-dependent dimerization of PGRMC1/Sigma-2 receptor facilitates cancer
RT proliferation and chemoresistance.";
RL Nat. Commun. 7:11030-11030(2016).
CC -!- FUNCTION: Component of a progesterone-binding protein complex
CC (PubMed:28396637). Binds progesterone (PubMed:25675345). Has many
CC reported cellular functions (heme homeostasis, interaction with CYPs).
CC Required for the maintenance of uterine histoarchitecture and normal
CC female reproductive lifespan (By similarity). Intracellular heme
CC chaperone. Regulates heme synthesis via interactions with FECH and acts
CC as a heme donor for at least some hemoproteins (PubMed:27599036).
CC {ECO:0000250|UniProtKB:O55022, ECO:0000269|PubMed:25675345,
CC ECO:0000269|PubMed:27599036, ECO:0000303|PubMed:28396637}.
CC -!- SUBUNIT: Homodimer. Forms stable homodimer through hydrophobic heme-
CC heme stacking interactions (PubMed:26988023, PubMed:28396637).
CC Interacts with FECH; the interaction results in decreased FECH activity
CC (PubMed:27599036). Interacts with EGFR, CYP1A1 and CYP3A4; the
CC interactions require PGRMC1 homodimerization (PubMed:28396637).
CC {ECO:0000269|PubMed:26988023, ECO:0000269|PubMed:27599036,
CC ECO:0000269|PubMed:28396637, ECO:0000303|PubMed:28396637}.
CC -!- INTERACTION:
CC O00264; Q13323: BIK; NbExp=3; IntAct=EBI-1045534, EBI-700794;
CC O00264; P49069: CAMLG; NbExp=3; IntAct=EBI-1045534, EBI-1748958;
CC O00264; Q9H6E4: CCDC134; NbExp=3; IntAct=EBI-1045534, EBI-953766;
CC O00264; O76071: CIAO1; NbExp=5; IntAct=EBI-1045534, EBI-725145;
CC O00264; Q8NES8: DEFB124; NbExp=3; IntAct=EBI-1045534, EBI-12843376;
CC O00264; P34910-2: EVI2B; NbExp=3; IntAct=EBI-1045534, EBI-17640610;
CC O00264; P22830: FECH; NbExp=3; IntAct=EBI-1045534, EBI-1390356;
CC O00264; O43681: GET3; NbExp=3; IntAct=EBI-1045534, EBI-2515857;
CC O00264; Q8NBJ4: GOLM1; NbExp=3; IntAct=EBI-1045534, EBI-712073;
CC O00264; Q8N6L0: KASH5; NbExp=3; IntAct=EBI-1045534, EBI-749265;
CC O00264; Q9UJ90: KCNE5; NbExp=3; IntAct=EBI-1045534, EBI-11981259;
CC O00264; O15173: PGRMC2; NbExp=3; IntAct=EBI-1045534, EBI-1050125;
CC O00264; P16435: POR; NbExp=5; IntAct=EBI-1045534, EBI-726554;
CC O00264; Q96EQ0: SGTB; NbExp=3; IntAct=EBI-1045534, EBI-744081;
CC O00264; Q9NQZ8: ZNF71; NbExp=5; IntAct=EBI-1045534, EBI-7138235;
CC O00264; P00181: CYP2C2; Xeno; NbExp=6; IntAct=EBI-1045534, EBI-4320576;
CC -!- SUBCELLULAR LOCATION: Microsome membrane
CC {ECO:0000250|UniProtKB:Q95250}; Single-pass membrane protein
CC {ECO:0000255}. Smooth endoplasmic reticulum membrane
CC {ECO:0000303|PubMed:28396637}; Single-pass membrane protein
CC {ECO:0000255}. Mitochondrion outer membrane
CC {ECO:0000250|UniProtKB:O55022}; Single-pass membrane protein
CC {ECO:0000305}; Extracellular side {ECO:0000250|UniProtKB:O55022}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O00264-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O00264-2; Sequence=VSP_054710;
CC -!- TISSUE SPECIFICITY: Widely expressed, with highest expression in liver
CC and kidney. Expressed by endometrial glands and stroma (at protein
CC level) (PubMed:23793472). {ECO:0000269|PubMed:23793472}.
CC -!- DOMAIN: The cytochrome b5 heme-binding domain lacks the conserved iron-
CC binding His residues at positions 107 and 131. {ECO:0000250}.
CC -!- MISCELLANEOUS: Non-classical progesterone receptors involved in
CC extranuclear signaling are classified in 2 groups: the class II
CC progestin and adipoQ receptor (PAQR) family (also called mPRs) (PAQR5,
CC PAQR6, PAQR7, PAQR8 and PAQR9) and the b5-like heme/steroid-binding
CC protein family (also called MAPRs) (PGRMC1, PGRMC2, NENF and CYB5D2).
CC {ECO:0000303|PubMed:23763432, ECO:0000303|PubMed:28396637}.
CC -!- SIMILARITY: Belongs to the cytochrome b5 family. MAPR subfamily.
CC {ECO:0000305}.
CC -!- CAUTION: Was initially identified as sigma-2 receptor, which is thought
CC to play important role in regulating cell survival, morphology and
CC differentiation (PubMed:21730960, PubMed:22292588, PubMed:28007569).
CC However, it was later shown that it is not the case (PubMed:28007569).
CC The sigma-2 receptor has been identified as TMEM97 (AC Q5BJF2)
CC (PubMed:28559337). {ECO:0000269|PubMed:21730960,
CC ECO:0000269|PubMed:22292588, ECO:0000269|PubMed:28007569,
CC ECO:0000269|PubMed:28559337}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; Y12711; CAA73248.1; -; mRNA.
DR EMBL; AK293618; BAH11549.1; -; mRNA.
DR EMBL; AC004835; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471161; EAW89881.1; -; Genomic_DNA.
DR EMBL; BC034238; AAH34238.1; -; mRNA.
DR EMBL; AJ249131; CAB65109.1; -; Genomic_DNA.
DR CCDS; CCDS14576.1; -. [O00264-1]
DR CCDS; CCDS65313.1; -. [O00264-2]
DR RefSeq; NP_001269550.1; NM_001282621.1. [O00264-2]
DR RefSeq; NP_006658.1; NM_006667.4. [O00264-1]
DR PDB; 4X8Y; X-ray; 1.95 A; A/B=72-195.
DR PDBsum; 4X8Y; -.
DR AlphaFoldDB; O00264; -.
DR SMR; O00264; -.
DR BioGRID; 116068; 282.
DR CORUM; O00264; -.
DR IntAct; O00264; 113.
DR MINT; O00264; -.
DR STRING; 9606.ENSP00000217971; -.
DR ChEMBL; CHEMBL4105706; -.
DR DrugBank; DB00514; Dextromethorphan.
DR DrugBank; DB00540; Nortriptyline.
DR DrugBank; DB01104; Sertraline.
DR GlyGen; O00264; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O00264; -.
DR PhosphoSitePlus; O00264; -.
DR SwissPalm; O00264; -.
DR BioMuta; PGRMC1; -.
DR OGP; O00264; -.
DR EPD; O00264; -.
DR jPOST; O00264; -.
DR MassIVE; O00264; -.
DR MaxQB; O00264; -.
DR PaxDb; O00264; -.
DR PeptideAtlas; O00264; -.
DR PRIDE; O00264; -.
DR ProteomicsDB; 47815; -. [O00264-1]
DR ProteomicsDB; 6345; -.
DR TopDownProteomics; O00264-1; -. [O00264-1]
DR Antibodypedia; 497; 214 antibodies from 38 providers.
DR DNASU; 10857; -.
DR Ensembl; ENST00000217971.8; ENSP00000217971.7; ENSG00000101856.10. [O00264-1]
DR Ensembl; ENST00000535419.2; ENSP00000442821.1; ENSG00000101856.10. [O00264-2]
DR GeneID; 10857; -.
DR KEGG; hsa:10857; -.
DR MANE-Select; ENST00000217971.8; ENSP00000217971.7; NM_006667.5; NP_006658.1.
DR UCSC; uc011mts.4; human. [O00264-1]
DR CTD; 10857; -.
DR DisGeNET; 10857; -.
DR GeneCards; PGRMC1; -.
DR HGNC; HGNC:16090; PGRMC1.
DR HPA; ENSG00000101856; Tissue enhanced (liver).
DR MIM; 300435; gene.
DR neXtProt; NX_O00264; -.
DR OpenTargets; ENSG00000101856; -.
DR Orphanet; 619; NON RARE IN EUROPE: Primary ovarian failure.
DR Orphanet; 98994; Total early-onset cataract.
DR PharmGKB; PA33248; -.
DR VEuPathDB; HostDB:ENSG00000101856; -.
DR eggNOG; KOG1110; Eukaryota.
DR GeneTree; ENSGT00940000160619; -.
DR HOGENOM; CLU_042860_5_0_1; -.
DR InParanoid; O00264; -.
DR OMA; ANEWETQ; -.
DR PhylomeDB; O00264; -.
DR TreeFam; TF314562; -.
DR PathwayCommons; O00264; -.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR SignaLink; O00264; -.
DR BioGRID-ORCS; 10857; 17 hits in 707 CRISPR screens.
DR ChiTaRS; PGRMC1; human.
DR GeneWiki; PGRMC1; -.
DR GenomeRNAi; 10857; -.
DR Pharos; O00264; Tchem.
DR PRO; PR:O00264; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; O00264; protein.
DR Bgee; ENSG00000101856; Expressed in seminal vesicle and 213 other tissues.
DR ExpressionAtlas; O00264; baseline and differential.
DR Genevisible; O00264; HS.
DR GO; GO:0044297; C:cell body; ISS:ARUK-UCL.
DR GO; GO:0012505; C:endomembrane system; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; TAS:ARUK-UCL.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ARUK-UCL.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005741; C:mitochondrial outer membrane; ISS:UniProtKB.
DR GO; GO:0043005; C:neuron projection; ISS:ARUK-UCL.
DR GO; GO:0043025; C:neuronal cell body; ISS:ARUK-UCL.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0030868; C:smooth endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0035579; C:specific granule membrane; TAS:Reactome.
DR GO; GO:0045202; C:synapse; ISS:ARUK-UCL.
DR GO; GO:0001540; F:amyloid-beta binding; TAS:ARUK-UCL.
DR GO; GO:0020037; F:heme binding; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0005496; F:steroid binding; TAS:ProtInc.
DR GO; GO:0006783; P:heme biosynthetic process; IDA:UniProtKB.
DR Gene3D; 3.10.120.10; -; 1.
DR InterPro; IPR001199; Cyt_B5-like_heme/steroid-bd.
DR InterPro; IPR036400; Cyt_B5-like_heme/steroid_sf.
DR Pfam; PF00173; Cyt-b5; 1.
DR SMART; SM01117; Cyt-b5; 1.
DR SUPFAM; SSF55856; SSF55856; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Direct protein sequencing;
KW Endoplasmic reticulum; Iron; Lipid-binding; Membrane; Metal-binding;
KW Microsome; Mitochondrion; Mitochondrion outer membrane; Phosphoprotein;
KW Receptor; Reference proteome; Steroid-binding; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..195
FT /note="Membrane-associated progesterone receptor component
FT 1"
FT /id="PRO_0000121739"
FT TOPO_DOM 1..24
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 25..43
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 44..195
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 72..171
FT /note="Cytochrome b5 heme-binding"
FT REGION 51..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 173..195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 113
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000269|PubMed:26988023,
FT ECO:0007744|PDB:4X8Y"
FT MOD_RES 54
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 57
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19367720,
FT ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 74
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 181
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|Ref.7, ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT VAR_SEQ 110..162
FT /note="EGPYGVFAGRDASRGLATFCLDKEALKDEYDDLSDLTAAQQETLSDWESQFT
FT F -> V (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054710"
FT MUTAGEN 113
FT /note="Y->F: Abolishes interaction with CYP1A1 and CYP3A4."
FT /evidence="ECO:0000269|PubMed:26988023"
FT HELIX 75..78
FT /evidence="ECO:0007829|PDB:4X8Y"
FT STRAND 82..87
FT /evidence="ECO:0007829|PDB:4X8Y"
FT STRAND 89..93
FT /evidence="ECO:0007829|PDB:4X8Y"
FT STRAND 96..99
FT /evidence="ECO:0007829|PDB:4X8Y"
FT HELIX 101..103
FT /evidence="ECO:0007829|PDB:4X8Y"
FT HELIX 104..107
FT /evidence="ECO:0007829|PDB:4X8Y"
FT HELIX 114..116
FT /evidence="ECO:0007829|PDB:4X8Y"
FT HELIX 122..127
FT /evidence="ECO:0007829|PDB:4X8Y"
FT HELIX 132..134
FT /evidence="ECO:0007829|PDB:4X8Y"
FT HELIX 142..144
FT /evidence="ECO:0007829|PDB:4X8Y"
FT HELIX 147..163
FT /evidence="ECO:0007829|PDB:4X8Y"
FT STRAND 164..170
FT /evidence="ECO:0007829|PDB:4X8Y"
SQ SEQUENCE 195 AA; 21671 MW; CCD5E802E1C9E604 CRC64;
MAAEDVVATG ADPSDLESGG LLHEIFTSPL NLLLLGLCIF LLYKIVRGDQ PAASGDSDDD
EPPPLPRLKR RDFTPAELRR FDGVQDPRIL MAINGKVFDV TKGRKFYGPE GPYGVFAGRD
ASRGLATFCL DKEALKDEYD DLSDLTAAQQ ETLSDWESQF TFKYHHVGKL LKEGEEPTVY
SDEEEPKDES ARKND
