PGRC2_HUMAN
ID PGRC2_HUMAN Reviewed; 223 AA.
AC O15173; Q569H1;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Membrane-associated progesterone receptor component 2 {ECO:0000305};
DE AltName: Full=Progesterone membrane-binding protein;
DE AltName: Full=Steroid receptor protein DG6;
GN Name=PGRMC2 {ECO:0000312|HGNC:HGNC:16089};
GN Synonyms=DG6 {ECO:0000303|PubMed:9705155}, PMBP;
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=Tongue;
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 [GENOMIC DNA].
RG NIEHS SNPs program;
RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Kidney, and 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-90, 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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-90, AND IDENTIFICATION BY
RP 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-210 AND THR-211, 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 [8]
RP IDENTIFICATION BY 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 [9]
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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-90, 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-90, 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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-90 AND THR-211, 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 [13]
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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-211, AND IDENTIFICATION BY
RP 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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-90; SER-104; SER-208 AND
RP THR-211, AND 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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-90; SER-208 AND THR-211, AND
RP 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 [17]
RP TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
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 [18]
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 [19]
RP INTERACTION WITH AAAS, AND SUBCELLULAR LOCATION.
RX PubMed=27754849; DOI=10.1242/bio.021162;
RA Juehlen R., Landgraf D., Huebner A., Koehler K.;
RT "Identification of a novel putative interaction partner of the nucleoporin
RT ALADIN.";
RL Biol. Open 5:1697-1705(2016).
RN [20]
RP FUNCTION, SUBCELLULAR LOCATION, AND HEME-BINDING.
RX PubMed=28111073; DOI=10.1016/j.cell.2016.12.029;
RA Parker C.G., Galmozzi A., Wang Y., Correia B.E., Sasaki K., Joslyn C.M.,
RA Kim A.S., Cavallaro C.L., Lawrence R.M., Johnson S.R., Narvaiza I.,
RA Saez E., Cravatt B.F.;
RT "Ligand and Target Discovery by Fragment-Based Screening in Human Cells.";
RL Cell 168:527.E29-541.E29(2017).
RN [21]
RP REVIEW, FUNCTION, 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).
CC -!- FUNCTION: Required for the maintenance of uterine histoarchitecture and
CC normal female reproductive lifespan (By similarity). May serve as a
CC universal non-classical progesterone receptor in the uterus (Probable).
CC Intracellular heme chaperone required for delivery of labile, or
CC signaling heme, to the nucleus (By similarity). Plays a role in
CC adipocyte function and systemic glucose homeostasis (PubMed:28111073).
CC In brown fat, which has a high demand for heme, delivery of labile heme
CC in the nucleus regulates the activity of heme-responsive
CC transcriptional repressors such as NR1D1 and BACH1 (By similarity).
CC {ECO:0000250|UniProtKB:Q80UU9, ECO:0000269|PubMed:28111073,
CC ECO:0000305|PubMed:28396637}.
CC -!- SUBUNIT: Interacts with PGRMC1 (By similarity). Interacts with AAAS
CC (PubMed:27754849). {ECO:0000250|UniProtKB:Q80UU9,
CC ECO:0000269|PubMed:27754849}.
CC -!- INTERACTION:
CC O15173; Q96PS8: AQP10; NbExp=3; IntAct=EBI-1050125, EBI-12820279;
CC O15173; A0A024RCD1: ART5; NbExp=3; IntAct=EBI-1050125, EBI-18958976;
CC O15173; O95429: BAG4; NbExp=5; IntAct=EBI-1050125, EBI-2949658;
CC O15173; P01031: C5; NbExp=3; IntAct=EBI-1050125, EBI-8558308;
CC O15173; Q5RI15: COX20; NbExp=3; IntAct=EBI-1050125, EBI-2834035;
CC O15173; O14569: CYB561D2; NbExp=3; IntAct=EBI-1050125, EBI-717654;
CC O15173; P78329: CYP4F2; NbExp=3; IntAct=EBI-1050125, EBI-1752413;
CC O15173; Q6ZPD8: DGAT2L6; NbExp=3; IntAct=EBI-1050125, EBI-12831978;
CC O15173; Q8N5I4: DHRSX; NbExp=3; IntAct=EBI-1050125, EBI-3923585;
CC O15173; O14681: EI24; NbExp=3; IntAct=EBI-1050125, EBI-2339413;
CC O15173; Q7L5A8: FA2H; NbExp=3; IntAct=EBI-1050125, EBI-11337888;
CC O15173; Q96IV6: FAXDC2; NbExp=3; IntAct=EBI-1050125, EBI-12142299;
CC O15173; Q9H0Q3: FXYD6; NbExp=3; IntAct=EBI-1050125, EBI-713304;
CC O15173; O43681: GET3; NbExp=3; IntAct=EBI-1050125, EBI-2515857;
CC O15173; Q9H3K2: GHITM; NbExp=3; IntAct=EBI-1050125, EBI-2868909;
CC O15173; Q8TDV0: GPR151; NbExp=3; IntAct=EBI-1050125, EBI-11955647;
CC O15173; P11215: ITGAM; NbExp=3; IntAct=EBI-1050125, EBI-2568251;
CC O15173; Q8IWB1: ITPRIP; NbExp=3; IntAct=EBI-1050125, EBI-2556412;
CC O15173; Q9UBY5: LPAR3; NbExp=3; IntAct=EBI-1050125, EBI-12033434;
CC O15173; Q13021: MALL; NbExp=3; IntAct=EBI-1050125, EBI-750078;
CC O15173; Q6N075: MFSD5; NbExp=3; IntAct=EBI-1050125, EBI-3920969;
CC O15173; Q9P0S3: ORMDL1; NbExp=3; IntAct=EBI-1050125, EBI-1054848;
CC O15173; I3L0A0: PEDS1-UBE2V1; NbExp=3; IntAct=EBI-1050125, EBI-12213001;
CC O15173; Q9Y5Y5: PEX16; NbExp=3; IntAct=EBI-1050125, EBI-981985;
CC O15173; O00264: PGRMC1; NbExp=3; IntAct=EBI-1050125, EBI-1045534;
CC O15173; Q9Y342: PLLP; NbExp=3; IntAct=EBI-1050125, EBI-3919291;
CC O15173; Q01453: PMP22; NbExp=3; IntAct=EBI-1050125, EBI-2845982;
CC O15173; O76064: RNF8; NbExp=3; IntAct=EBI-1050125, EBI-373337;
CC O15173; Q96GQ5: RUSF1; NbExp=3; IntAct=EBI-1050125, EBI-8636004;
CC O15173; Q9H9B4: SFXN1; NbExp=3; IntAct=EBI-1050125, EBI-355861;
CC O15173; Q7RTY0: SLC16A13; NbExp=3; IntAct=EBI-1050125, EBI-12243266;
CC O15173; Q8IWU4: SLC30A8; NbExp=3; IntAct=EBI-1050125, EBI-10262251;
CC O15173; Q9H2H9: SLC38A1; NbExp=3; IntAct=EBI-1050125, EBI-9978441;
CC O15173; Q96H72: SLC39A13; NbExp=3; IntAct=EBI-1050125, EBI-10287091;
CC O15173; Q86UD5: SLC9B2; NbExp=3; IntAct=EBI-1050125, EBI-9916342;
CC O15173; O60906: SMPD2; NbExp=3; IntAct=EBI-1050125, EBI-12828299;
CC O15173; Q96JF0-2: ST6GAL2; NbExp=3; IntAct=EBI-1050125, EBI-12908338;
CC O15173; Q13277: STX3; NbExp=3; IntAct=EBI-1050125, EBI-1394295;
CC O15173; P59542: TAS2R19; NbExp=3; IntAct=EBI-1050125, EBI-12847034;
CC O15173; Q9NZ01: TECR; NbExp=3; IntAct=EBI-1050125, EBI-2877718;
CC O15173; P02787: TF; NbExp=3; IntAct=EBI-1050125, EBI-714319;
CC O15173; Q6UX40: TMEM107; NbExp=3; IntAct=EBI-1050125, EBI-12845616;
CC O15173; Q14656: TMEM187; NbExp=3; IntAct=EBI-1050125, EBI-13046724;
CC O15173; Q96HH6: TMEM19; NbExp=3; IntAct=EBI-1050125, EBI-741829;
CC O15173; Q9BTX3: TMEM208; NbExp=3; IntAct=EBI-1050125, EBI-12876824;
CC O15173; Q9H2L4: TMEM60; NbExp=3; IntAct=EBI-1050125, EBI-2852148;
CC O15173; Q8N2M4: TMEM86A; NbExp=3; IntAct=EBI-1050125, EBI-12015604;
CC O15173; Q8N661: TMEM86B; NbExp=3; IntAct=EBI-1050125, EBI-2548832;
CC O15173; O60636: TSPAN2; NbExp=3; IntAct=EBI-1050125, EBI-3914288;
CC O15173; O00124: UBXN8; NbExp=3; IntAct=EBI-1050125, EBI-1993850;
CC O15173; Q9P0L0: VAPA; NbExp=3; IntAct=EBI-1050125, EBI-1059156;
CC O15173; Q9BWQ6: YIPF2; NbExp=3; IntAct=EBI-1050125, EBI-751204;
CC O15173; Q8IVQ6: ZDHHC21; NbExp=3; IntAct=EBI-1050125, EBI-2849773;
CC O15173; O95159: ZFPL1; NbExp=3; IntAct=EBI-1050125, EBI-718439;
CC O15173; P22315: Fech; Xeno; NbExp=2; IntAct=EBI-1050125, EBI-7174007;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305|PubMed:23793472}; Single-
CC pass membrane protein {ECO:0000305}. Nucleus envelope
CC {ECO:0000269|PubMed:27754849, ECO:0000269|PubMed:28111073}. Endoplasmic
CC reticulum {ECO:0000269|PubMed:27754849}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O15173-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O15173-2; Sequence=VSP_053500;
CC -!- TISSUE SPECIFICITY: Expressed by endometrial glands and stroma (at
CC protein level). {ECO:0000269|PubMed:23793472}.
CC -!- DOMAIN: The cytochrome b5 heme-binding domain lacks the conserved iron-
CC binding His residues at positions 137 and 161. {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:28396637}.
CC -!- SIMILARITY: Belongs to the cytochrome b5 family. MAPR subfamily.
CC {ECO:0000305}.
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DR EMBL; AJ002030; CAA05152.1; -; mRNA.
DR EMBL; AK131272; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; DQ496105; ABF47094.1; -; Genomic_DNA.
DR EMBL; BC016692; AAH16692.1; -; mRNA.
DR EMBL; BC092478; AAH92478.1; -; mRNA.
DR CCDS; CCDS3739.2; -. [O15173-1]
DR RefSeq; NP_006311.2; NM_006320.4. [O15173-1]
DR AlphaFoldDB; O15173; -.
DR SMR; O15173; -.
DR BioGRID; 115693; 252.
DR IntAct; O15173; 140.
DR MINT; O15173; -.
DR STRING; 9606.ENSP00000429301; -.
DR TCDB; 9.B.433.1.1; the progesterone receptor membrane-associated component 2 (pgrmc2) family.
DR GlyGen; O15173; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O15173; -.
DR MetOSite; O15173; -.
DR PhosphoSitePlus; O15173; -.
DR SwissPalm; O15173; -.
DR BioMuta; PGRMC2; -.
DR EPD; O15173; -.
DR jPOST; O15173; -.
DR MassIVE; O15173; -.
DR MaxQB; O15173; -.
DR PaxDb; O15173; -.
DR PeptideAtlas; O15173; -.
DR PRIDE; O15173; -.
DR ProteomicsDB; 48495; -. [O15173-1]
DR TopDownProteomics; O15173-1; -. [O15173-1]
DR Antibodypedia; 27009; 277 antibodies from 32 providers.
DR DNASU; 10424; -.
DR Ensembl; ENST00000296425.10; ENSP00000296425.4; ENSG00000164040.18. [O15173-1]
DR Ensembl; ENST00000520121.6; ENSP00000429301.2; ENSG00000164040.18. [O15173-1]
DR Ensembl; ENST00000613358.4; ENSP00000481886.1; ENSG00000164040.18. [O15173-2]
DR GeneID; 10424; -.
DR KEGG; hsa:10424; -.
DR MANE-Select; ENST00000296425.10; ENSP00000296425.4; NM_006320.6; NP_006311.3.
DR UCSC; uc003igg.4; human. [O15173-1]
DR CTD; 10424; -.
DR DisGeNET; 10424; -.
DR GeneCards; PGRMC2; -.
DR HGNC; HGNC:16089; PGRMC2.
DR HPA; ENSG00000164040; Low tissue specificity.
DR MIM; 607735; gene.
DR neXtProt; NX_O15173; -.
DR OpenTargets; ENSG00000164040; -.
DR VEuPathDB; HostDB:ENSG00000164040; -.
DR eggNOG; KOG1110; Eukaryota.
DR GeneTree; ENSGT00940000159744; -.
DR HOGENOM; CLU_042860_1_0_1; -.
DR InParanoid; O15173; -.
DR OrthoDB; 1331617at2759; -.
DR PhylomeDB; O15173; -.
DR PathwayCommons; O15173; -.
DR Reactome; R-HSA-8980692; RHOA GTPase cycle.
DR Reactome; R-HSA-9013404; RAC2 GTPase cycle.
DR Reactome; R-HSA-9013405; RHOD GTPase cycle.
DR Reactome; R-HSA-9013408; RHOG GTPase cycle.
DR Reactome; R-HSA-9013423; RAC3 GTPase cycle.
DR SignaLink; O15173; -.
DR BioGRID-ORCS; 10424; 36 hits in 1079 CRISPR screens.
DR ChiTaRS; PGRMC2; human.
DR GenomeRNAi; 10424; -.
DR Pharos; O15173; Tbio.
DR PRO; PR:O15173; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; O15173; protein.
DR Bgee; ENSG00000164040; Expressed in jejunal mucosa and 208 other tissues.
DR ExpressionAtlas; O15173; baseline and differential.
DR Genevisible; O15173; HS.
DR GO; GO:0012505; C:endomembrane system; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; TAS:ProtInc.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005635; C:nuclear envelope; IDA:UniProtKB.
DR GO; GO:0020037; F:heme binding; IDA:UniProtKB.
DR GO; GO:0015232; F:heme transmembrane transporter activity; IEA:Ensembl.
DR GO; GO:0003707; F:nuclear steroid receptor activity; TAS:ProtInc.
DR GO; GO:0005496; F:steroid binding; TAS:ProtInc.
DR GO; GO:0060612; P:adipose tissue development; IMP: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 Alternative splicing; Endoplasmic reticulum; Lipid-binding; Membrane;
KW Nucleus; Phosphoprotein; Receptor; Reference proteome; Steroid-binding;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..223
FT /note="Membrane-associated progesterone receptor component
FT 2"
FT /id="PRO_0000121743"
FT TRANSMEM 42..66
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 102..201
FT /note="Cytochrome b5 heme-binding"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 202..223
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 90
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 104
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 208
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 210
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 211
FT /note="Phosphothreonine"
FT /evidence="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 1
FT /note="M -> MGGAGRGVGEGRGRGGGGRRWRAVM (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_053500"
SQ SEQUENCE 223 AA; 23818 MW; BE36229EDF0FF3AD CRC64;
MAAGDGDVKL GTLGSGSESS NDGGSESPGD AGAAAEGGGW AAAALALLTG GGEMLLNVAL
VALVLLGAYR LWVRWGRRGL GAGAGAGEES PATSLPRMKK RDFSLEQLRQ YDGSRNPRIL
LAVNGKVFDV TKGSKFYGPA GPYGIFAGRD ASRGLATFCL DKDALRDEYD DLSDLNAVQM
ESVREWEMQF KEKYDYVGRL LKPGEEPSEY TDEEDTKDHN KQD
