GCR_RAT
ID GCR_RAT Reviewed; 795 AA.
AC P06536; O08624; Q8R463; Q8R5J0;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 2.
DT 03-AUG-2022, entry version 235.
DE RecName: Full=Glucocorticoid receptor;
DE Short=GR;
DE AltName: Full=Nuclear receptor subfamily 3 group C member 1;
GN Name=Nr3c1; Synonyms=Grl;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Hepatoma;
RX PubMed=3755378; DOI=10.1016/0092-8674(86)90659-8;
RA Miesfeld R., Rusconi S., Godowski P.J., Maler B.A., Okret S.,
RA Wikstroem A.-C., Gustafsson J.-A., Yamamoto K.R.;
RT "Genetic complementation of a glucocorticoid receptor deficiency by
RT expression of cloned receptor cDNA.";
RL Cell 46:389-399(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Heeley R.P., Gill E., van Zutphen B.;
RT "CAG repeat variation in the gene for rat glucocorticoid receptor: a study
RT of allele frequencies in inbred and wild rat populations and of the
RT steroid-binding properties of their polypeptides in vitro.";
RL Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS GLY-226 AND ASP-260.
RC STRAIN=Brown Norway/Crl, and SHR/OlaIpcv;
RA Pravenec M., Zidek V., Kostka V., Mlejnek P., Musilova A., Kren V.,
RA Jansa P., Forejt J., Lezin E.S., Kurtz T.W.;
RT "Genetic isolation of a QTL on chromosome 18 associated with salt
RT sensitivity in spontaneously hypertensive rats.";
RL Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-515.
RC STRAIN=Sprague-Dawley; TISSUE=Prostate;
RX PubMed=3684608; DOI=10.1093/nar/15.22.9603;
RA Chang C., Kokontis J., Chang C.T., Liao S.;
RT "Cloning and sequence analysis of the rat ventral prostate glucocorticoid
RT receptor cDNA.";
RL Nucleic Acids Res. 15:9603-9603(1987).
RN [5]
RP MUTAGENESIS OF ZINC-FINGER.
RX PubMed=3191912; DOI=10.1002/j.1460-2075.1988.tb03097.x;
RA Severne Y., Wieland S., Schaffner W., Rusconi S.;
RT "Metal binding 'finger' structures in the glucocorticoid receptor defined
RT by site-directed mutagenesis.";
RL EMBO J. 7:2503-2508(1988).
RN [6]
RP GLUCOCORTICOID-MEDIATED DOWN-REGULATION.
RX PubMed=3216865; DOI=10.1210/mend-2-12-1256;
RA Dong Y., Poellinger L., Gustafsson J.-A., Okret S.;
RT "Regulation of glucocorticoid receptor expression: evidence for
RT transcriptional and posttranslational mechanisms.";
RL Mol. Endocrinol. 2:1256-1264(1988).
RN [7]
RP MUTAGENESIS OF CYS-656.
RX PubMed=1939229; DOI=10.1016/s0021-9258(18)54533-6;
RA Chakraborti P.K., Garabedian M.J., Yamamoto K.R., Simons S.S. Jr.;
RT "Creation of 'super' glucocorticoid receptors by point mutations in the
RT steroid binding domain.";
RL J. Biol. Chem. 266:22075-22078(1991).
RN [8]
RP MUTAGENESIS OF ZINC-FINGER.
RX PubMed=8450530; DOI=10.1006/jmbi.1993.1130;
RA Zandi E., Galli I., Doebbeling U., Rusconi S.;
RT "Zinc finger mutations that alter domain interactions in the glucocorticoid
RT receptor.";
RL J. Mol. Biol. 230:124-136(1993).
RN [9]
RP REVIEW ON MUTAGENESIS.
RX PubMed=8191545; DOI=10.1016/0039-128x(94)90093-0;
RA Lanz R.B., Hug M., Gola M., Tallone T., Wieland S., Rusconi S.;
RT "Active, interactive, and inactive steroid receptor mutants.";
RL Steroids 59:148-152(1994).
RN [10]
RP HOMODIMERIZATION, HETERODIMERIZATION WITH NR3C2, AND MUTAGENESIS OF
RP ASP-481.
RX PubMed=8618925; DOI=10.1073/pnas.92.26.12480;
RA Liu W., Wang J., Sauter N.K., Pearce D.;
RT "Steroid receptor heterodimerization demonstrated in vitro and in vivo.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:12480-12484(1995).
RN [11]
RP INTERACTION WITH NCOA2.
RX PubMed=9111344; DOI=10.1128/mcb.17.5.2735;
RA Hong H., Kohli K., Garabedian M.J., Stallcup M.R.;
RT "GRIP1, a transcriptional coactivator for the AF-2 transactivation domain
RT of steroid, thyroid, retinoid, and vitamin D receptors.";
RL Mol. Cell. Biol. 17:2735-2744(1997).
RN [12]
RP PHOSPHORYLATION AT THR-171; SER-224; SER-232 AND SER-246.
RX PubMed=9603939; DOI=10.1074/jbc.273.23.14315;
RA Rogatsky I., Waase C.L.M., Garabedian M.J.;
RT "Phosphorylation and inhibition of rat glucocorticoid receptor
RT transcriptional activation by glycogen synthase kinase-3 (GSK-3). Species-
RT specific differences between human and rat glucocorticoid receptor
RT signaling as revealed through GSK-3 phosphorylation.";
RL J. Biol. Chem. 273:14315-14321(1998).
RN [13]
RP INTERACTION WITH NRIP1.
RX PubMed=10364267; DOI=10.1074/jbc.274.25.18121;
RA Subramaniam N., Treuter E., Okret S.;
RT "Receptor interacting protein RIP140 inhibits both positive and negative
RT gene regulation by glucocorticoids.";
RL J. Biol. Chem. 274:18121-18127(1999).
RN [14]
RP INTERACTION WITH POU2F1 AND POU2F2, AND MUTAGENESIS OF CYS-500 AND LEU-501.
RX PubMed=10480874; DOI=10.1074/jbc.274.38.26713;
RA Prefontaine G.G., Walther R., Giffin W., Lemieux M.E., Pope L.,
RA Hache R.J.G.;
RT "Selective binding of steroid hormone receptors to octamer transcription
RT factors determines transcriptional synergism at the mouse mammary tumor
RT virus promoter.";
RL J. Biol. Chem. 274:26713-26719(1999).
RN [15]
RP INTERACTION WITH NCOA6.
RX PubMed=10866662; DOI=10.1128/mcb.20.14.5048-5063.2000;
RA Mahajan M.A., Samuels H.H.;
RT "A new family of nuclear receptor coregulators that integrates nuclear
RT receptor signaling through CBP.";
RL Mol. Cell. Biol. 20:5048-5063(2000).
RN [16]
RP HOMODIMERIZATION, HETERODIMERIZATION WITH NR3C2, AND MUTAGENESIS OF
RP LEU-501.
RX PubMed=11278286; DOI=10.1074/jbc.m005363200;
RA Ou X.-M., Storring J.M., Kushwaha N., Albert P.R.;
RT "Heterodimerization of mineralocorticoid and glucocorticoid receptors at a
RT novel negative response element of the 5-HT1A receptor gene.";
RL J. Biol. Chem. 276:14299-14307(2001).
RN [17]
RP ALTERNATIVE INITIATION, AND MUTAGENESIS OF MET-1 AND MET-28.
RX PubMed=11435610; DOI=10.1210/mend.15.7.0667;
RA Yudt M.R., Cidlowski J.A.;
RT "Molecular identification and characterization of A and B forms of the
RT glucocorticoid receptor.";
RL Mol. Endocrinol. 15:1093-1103(2001).
RN [18]
RP INTERACTION WITH NCOA1, AND MUTAGENESIS OF GLU-773.
RX PubMed=12118039; DOI=10.1074/jbc.m204013200;
RA Kucera T., Waltner-Law M., Scott D.K., Prasad R., Granner D.K.;
RT "A point mutation of the AF2 transactivation domain of the glucocorticoid
RT receptor disrupts its interaction with steroid receptor coactivator 1.";
RL J. Biol. Chem. 277:26098-26102(2002).
RN [19]
RP FUNCTION, INTERACTION WITH NCOA1; NCOA3; SMARCA4; SMARCC1; SMARCD1 AND
RP SMARCE1, AND MUTAGENESIS OF ARG-488.
RX PubMed=12917342; DOI=10.1128/mcb.23.17.6210-6220.2003;
RA Hsiao P.W., Fryer C.J., Trotter K.W., Wang W., Archer T.K.;
RT "BAF60a mediates critical interactions between nuclear receptors and the
RT BRG1 chromatin-remodeling complex for transactivation.";
RL Mol. Cell. Biol. 23:6210-6220(2003).
RN [20]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=16641100; DOI=10.1073/pnas.0600895103;
RA Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.;
RT "Quantitative phosphoproteomics of vasopressin-sensitive renal cells:
RT regulation of aquaporin-2 phosphorylation at two sites.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).
RN [21]
RP SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=21730050; DOI=10.1074/jbc.m111.256610;
RA Gallo L.I., Lagadari M., Piwien-Pilipuk G., Galigniana M.D.;
RT "The 90-kDa heat-shock protein (Hsp90)-binding immunophilin FKBP51 is a
RT mitochondrial protein that translocates to the nucleus to protect cells
RT against oxidative stress.";
RL J. Biol. Chem. 286:30152-30160(2011).
RN [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-224; SER-232 AND SER-287,
RP VARIANT [LARGE SCALE ANALYSIS] GLY-226, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [23]
RP SUMOYLATION AT LYS-297; LYS-313 AND LYS-721, INTERACTION WITH UBE2I/UBC9
RP AND RWDD3, AND MUTAGENESIS OF LYS-297; LYS-313 AND LYS-721.
RX PubMed=23508108; DOI=10.1128/mcb.01470-12;
RA Druker J., Liberman A.C., Antunica-Noguerol M., Gerez J., Paez-Pereda M.,
RA Rein T., Iniguez-Lluhi J.A., Holsboer F., Arzt E.;
RT "RSUME enhances glucocorticoid receptor SUMOylation and transcriptional
RT activity.";
RL Mol. Cell. Biol. 33:2116-2127(2013).
RN [24]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 434-525.
RX PubMed=1865905; DOI=10.1038/352497a0;
RA Luisi B.F., Xu W.X., Otwinowski Z., Freedman L.P., Yamamoto K.R.,
RA Sigler P.B.;
RT "Crystallographic analysis of the interaction of the glucocorticoid
RT receptor with DNA.";
RL Nature 352:497-505(1991).
RN [25]
RP STRUCTURE BY NMR OF 440-510.
RX PubMed=2115209; DOI=10.1126/science.2115209;
RA Haerd T., Kellenbach E., Boelens R., Maler B.A., Dahlman K., Freedman L.P.,
RA Carlstedt-Duke J., Yamamoto K.R., Gustafsson J.-A., Kaptein R.;
RT "Solution structure of the glucocorticoid receptor DNA-binding domain.";
RL Science 249:157-160(1990).
RN [26]
RP STRUCTURE BY NMR OF 440-525.
RX PubMed=1751485; DOI=10.1021/bi00114a003;
RA Remerowski M.L., Kellenbach E., Boelens R., van der Marel A.,
RA van Boom J.H., Maler B.A., Yamamoto K.R., Kaptein R.;
RT "1H NMR studies of DNA recognition by the glucocorticoid receptor: complex
RT of the DNA binding domain with a half-site response element.";
RL Biochemistry 30:11620-11624(1991).
RN [27]
RP STRUCTURE BY NMR OF 440-525.
RX PubMed=1936288; DOI=10.1016/0014-5793(91)81322-y;
RA Kellenbach E., Maler B.A., Yamamoto K.R., Boelens R., Kaptein R.;
RT "Identification of the metal coordinating residues in the DNA binding
RT domain of the glucocorticoid receptor by 113Cd-1H heteronuclear NMR
RT spectroscopy.";
RL FEBS Lett. 291:367-370(1991).
RN [28]
RP STRUCTURE BY NMR OF 439-510.
RX PubMed=8257681; DOI=10.1021/bi00212a011;
RA Baumann H., Paulsen K., Kovacs H., Berglund H., Wright A.P.H.,
RA Gustafsson J.-A., Haerd T.;
RT "Refined solution structure of the glucocorticoid receptor DNA-binding
RT domain.";
RL Biochemistry 32:13463-13471(1993).
RN [29]
RP POLYMORPHISM OF POLY-GLN REGION.
RX PubMed=8493115; DOI=10.1093/nar/21.8.2014;
RA Gearing K.L., Gustafsson J.-A., Okret S.;
RT "Heterogeneity in the polyglutamine tract of the glucocorticoid receptor
RT from different rat strains.";
RL Nucleic Acids Res. 21:2014-2014(1993).
CC -!- FUNCTION: Receptor for glucocorticoids (GC). Has a dual mode of action:
CC as a transcription factor that binds to glucocorticoid response
CC elements (GRE), both for nuclear and mitochondrial DNA, and as a
CC modulator of other transcription factors. Affects inflammatory
CC responses, cellular proliferation and differentiation in target
CC tissues. Involved in chromatin remodeling (PubMed:12917342). Plays a
CC role in rapid mRNA degradation by binding to the 5' UTR of target mRNAs
CC and interacting with PNRC2 in a ligand-dependent manner which recruits
CC the RNA helicase UPF1 and the mRNA-decapping enzyme DCP1A, leading to
CC RNA decay (By similarity). Could act as a coactivator for STAT5-
CC dependent transcription upon growth hormone (GH) stimulation and could
CC reveal an essential role of hepatic GR in the control of body growth
CC (By similarity). {ECO:0000250|UniProtKB:P04150,
CC ECO:0000250|UniProtKB:P06537, ECO:0000269|PubMed:12917342}.
CC -!- FUNCTION: [Isoform A]: Has transcriptional activation and repression
CC activity. Mediates glucocorticoid-induced apoptosis. Promotes accurate
CC chromosome segregation during mitosis. May act as a tumor suppressor.
CC May play a negative role in adipogenesis through the regulation of
CC lipolytic and antilipogenic gene expression.
CC {ECO:0000250|UniProtKB:P04150, ECO:0000250|UniProtKB:P06537}.
CC -!- SUBUNIT: Interacts with GRIP1 (By similarity). Heteromultimeric
CC cytoplasmic complex with HSP90AA1, HSPA1A/HSPA1B, and FKBP5 or another
CC immunophilin such as PPID, STIP1, or the immunophilin homolog PPP5C
CC (PubMed:21730050). Upon ligand binding FKBP5 dissociates from the
CC complex and FKBP4 takes its place, thereby linking the complex to
CC dynein and mediating transport to the nucleus, where the complex
CC dissociates (By similarity). Probably forms a complex composed of
CC chaperones HSP90 and HSP70, co-chaperones CDC37, PPP5C, TSC1 and client
CC protein TSC2, CDK4, AKT, RAF1 and NR3C1; this complex does not contain
CC co-chaperones STIP1/HOP and PTGES3/p23 (By similarity). Directly
CC interacts with UNC45A (By similarity). Binds to DNA as a homodimer, and
CC as heterodimer with NR3C2 or the retinoid X receptor (By similarity).
CC Binds STAT5A and STAT5B homodimers and heterodimers (By similarity).
CC Interacts with NRIP1, POU2F1, POU2F2 and TRIM28 (PubMed:10364267,
CC PubMed:10480874). Interacts with several coactivator complexes,
CC including the SMARCA4 complex, CREBBP/EP300, TADA2L (Ada complex) and
CC p160 coactivators such as NCOA2 and NCOA6 (PubMed:9111344,
CC PubMed:10866662). Interaction with BAG1 inhibits transactivation (By
CC similarity). Interacts with HEXIM1 and TGFB1I1 (By similarity).
CC Interacts with NCOA1 (PubMed:12917342). Interacts with NCOA3, SMARCA4,
CC SMARCC1, SMARCD1, and SMARCE1 (PubMed:12917342, PubMed:12118039).
CC Interacts with CLOCK, CRY1 and CRY2 in a ligand-dependent fashion (By
CC similarity). Interacts with CIART (By similarity). Interacts with RWDD3
CC (PubMed:23508108). Interacts with UBE2I/UBC9 and this interaction is
CC enhanced in the presence of RWDD3 (PubMed:23508108). Interacts with
CC NR4A3 (via nuclear receptor DNA-binding domain), represses
CC transcription activity of NR4A3 on the POMC promoter Nur response
CC element (NurRE) (By similarity). Directly interacts with PNRC2 to
CC attract and form a complex with UPF1 and DCP1A; the interaction leads
CC to rapid mRNA degradation (By similarity). Interacts with GSK3B (By
CC similarity). Interacts with FNIP1 and FNIP2 (By similarity). Interacts
CC (via C-terminus) with HNRNPU (via C-terminus) (By similarity).
CC Interacts with MCM3AP (By similarity). Interacts (via domain NR LBD)
CC with HSP90AA1 and HSP90AB1 (By similarity). In the absence of hormonal
CC ligand, interacts with TACC1 (By similarity).
CC {ECO:0000250|UniProtKB:P04150, ECO:0000250|UniProtKB:P06537,
CC ECO:0000269|PubMed:10364267, ECO:0000269|PubMed:10480874,
CC ECO:0000269|PubMed:10866662, ECO:0000269|PubMed:12118039,
CC ECO:0000269|PubMed:12917342, ECO:0000269|PubMed:21730050,
CC ECO:0000269|PubMed:23508108, ECO:0000269|PubMed:9111344}.
CC -!- INTERACTION:
CC P06536; Q62667: Mvp; NbExp=2; IntAct=EBI-1187143, EBI-918333;
CC P06536; Q63604: Ntrk2; NbExp=2; IntAct=EBI-1187143, EBI-7287667;
CC P06536; Q15788: NCOA1; Xeno; NbExp=2; IntAct=EBI-1187143, EBI-455189;
CC P06536; Q9BTK6: PAGR1; Xeno; NbExp=2; IntAct=EBI-1187143, EBI-2372223;
CC P06536; P51532: SMARCA4; Xeno; NbExp=3; IntAct=EBI-1187143, EBI-302489;
CC P06536; Q96GM5: SMARCD1; Xeno; NbExp=2; IntAct=EBI-1187143, EBI-358489;
CC -!- SUBCELLULAR LOCATION: [Isoform A]: Cytoplasm
CC {ECO:0000250|UniProtKB:P04150}. Nucleus {ECO:0000250|UniProtKB:P04150}.
CC Mitochondrion {ECO:0000269|PubMed:21730050}. Cytoplasm, cytoskeleton,
CC spindle {ECO:0000250|UniProtKB:P04150}. Cytoplasm, cytoskeleton,
CC microtubule organizing center, centrosome
CC {ECO:0000250|UniProtKB:P04150}. Note=After ligand activation,
CC translocates from the cytoplasm to the nucleus (By similarity). In the
CC presence of NR1D1 shows a time-dependent subcellular localization,
CC localizing to the cytoplasm at ZT8 and to the nucleus at ZT20 (By
CC similarity). Lacks this diurnal pattern of localization in the absence
CC of NR1D1, localizing to both nucleus and the cytoplasm at ZT8 and ZT20
CC (By similarity). {ECO:0000250|UniProtKB:P04150,
CC ECO:0000250|UniProtKB:P06537}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=A;
CC IsoId=P06536-1; Sequence=Displayed;
CC Name=B;
CC IsoId=P06536-2; Sequence=VSP_018969;
CC -!- DOMAIN: Composed of three domains: a modulating N-terminal domain, a
CC DNA-binding domain and a C-terminal ligand-binding domain. The ligand-
CC binding domain is required for correct chromosome segregation during
CC mitosis although ligand binding is not required.
CC {ECO:0000250|UniProtKB:P04150}.
CC -!- PTM: Acetylation by CLOCK reduces its binding to glucocorticoid
CC response elements and its transcriptional activity. {ECO:0000250}.
CC -!- PTM: Increased proteasome-mediated degradation in response to
CC glucocorticoids. {ECO:0000250|UniProtKB:P04150}.
CC -!- PTM: Phosphorylated in the absence of hormone; becomes
CC hyperphosphorylated in the presence of glucocorticoids. The Ser-224,
CC Ser-246 and Ser-424-phosphorylated forms are mainly cytoplasmic, and
CC the Ser-232-phosphorylated form is nuclear. Phosphorylation at Ser-232
CC increases transcriptional activity. Phosphorylation at Ser-224, Ser-246
CC and Ser-424 decreases signaling capacity. Phosphorylation at Ser-424
CC may protect from glucocorticoid-induced apoptosis. Phosphorylation at
CC Ser-224 and Ser-232 is not required in regulation of chromosome
CC segregation. May be dephosphorylated by PPP5C, attenuates NR3C1 action.
CC {ECO:0000250|UniProtKB:P04150, ECO:0000250|UniProtKB:P06537}.
CC -!- PTM: Sumoylation at Lys-297 and Lys-313 negatively regulates its
CC transcriptional activity. Sumoylation at Lys-721 positively regulates
CC its transcriptional activity in the presence of RWDD3. Sumoylation at
CC Lys-297 and Lys-313 is dispensable whereas sumoylation at Lys-721 is
CC critical for the stimulatory effect of RWDD3 on its transcriptional
CC activity. Heat shock increases sumoylation in a RWDD3-dependent manner.
CC {ECO:0000269|PubMed:23508108}.
CC -!- PTM: Ubiquitinated; restricts glucocorticoid-mediated transcriptional
CC signaling. {ECO:0000250|UniProtKB:P06537}.
CC -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR3
CC subfamily. {ECO:0000305}.
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DR EMBL; M14053; AAA41203.1; -; mRNA.
DR EMBL; Y12264; CAA72938.1; -; mRNA.
DR EMBL; AY066016; AAL66772.2; -; mRNA.
DR EMBL; AF455050; AAL78956.1; -; mRNA.
DR EMBL; Y00489; CAA68545.1; -; mRNA.
DR EMBL; X69666; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; X69667; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; X69668; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; X69669; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; X69670; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; A24194; QRRTG.
DR RefSeq; NP_036708.2; NM_012576.2.
DR PDB; 1GDC; NMR; -; A=439-510.
DR PDB; 1GLU; X-ray; 2.90 A; A/B=440-514.
DR PDB; 1LAT; X-ray; 1.90 A; A/B=440-515.
DR PDB; 1R4O; X-ray; 2.50 A; A/B=440-525.
DR PDB; 1R4R; X-ray; 3.00 A; A/B=440-525.
DR PDB; 1RGD; NMR; -; A=440-510.
DR PDB; 2GDA; NMR; -; A=439-510.
DR PDB; 3FYL; X-ray; 1.63 A; A/B=440-525.
DR PDB; 3G6P; X-ray; 1.99 A; A/B=440-525.
DR PDB; 3G6Q; X-ray; 2.26 A; A/B=440-525.
DR PDB; 3G6R; X-ray; 2.30 A; A/B=440-525.
DR PDB; 3G6T; X-ray; 1.90 A; A/B=440-525.
DR PDB; 3G6U; X-ray; 1.90 A; A/B=440-525.
DR PDB; 3G8U; X-ray; 1.90 A; A/B=440-525.
DR PDB; 3G8X; X-ray; 2.05 A; A/B=440-525.
DR PDB; 3G97; X-ray; 2.08 A; A/B=440-525.
DR PDB; 3G99; X-ray; 1.81 A; A/B=440-525.
DR PDB; 3G9I; X-ray; 1.85 A; A/B=440-525.
DR PDB; 3G9J; X-ray; 2.32 A; A/B=440-525.
DR PDB; 3G9M; X-ray; 1.61 A; A/B=440-525.
DR PDB; 3G9O; X-ray; 1.65 A; A/B=440-525.
DR PDB; 3G9P; X-ray; 1.65 A; A/B=440-525.
DR PDBsum; 1GDC; -.
DR PDBsum; 1GLU; -.
DR PDBsum; 1LAT; -.
DR PDBsum; 1R4O; -.
DR PDBsum; 1R4R; -.
DR PDBsum; 1RGD; -.
DR PDBsum; 2GDA; -.
DR PDBsum; 3FYL; -.
DR PDBsum; 3G6P; -.
DR PDBsum; 3G6Q; -.
DR PDBsum; 3G6R; -.
DR PDBsum; 3G6T; -.
DR PDBsum; 3G6U; -.
DR PDBsum; 3G8U; -.
DR PDBsum; 3G8X; -.
DR PDBsum; 3G97; -.
DR PDBsum; 3G99; -.
DR PDBsum; 3G9I; -.
DR PDBsum; 3G9J; -.
DR PDBsum; 3G9M; -.
DR PDBsum; 3G9O; -.
DR PDBsum; 3G9P; -.
DR AlphaFoldDB; P06536; -.
DR SMR; P06536; -.
DR BioGRID; 246578; 15.
DR CORUM; P06536; -.
DR DIP; DIP-38940N; -.
DR ELM; P06536; -.
DR IntAct; P06536; 34.
DR STRING; 10116.ENSRNOP00000019409; -.
DR BindingDB; P06536; -.
DR ChEMBL; CHEMBL3368; -.
DR DrugCentral; P06536; -.
DR iPTMnet; P06536; -.
DR PhosphoSitePlus; P06536; -.
DR PaxDb; P06536; -.
DR PeptideAtlas; P06536; -.
DR PRIDE; P06536; -.
DR GeneID; 24413; -.
DR KEGG; rno:24413; -.
DR UCSC; RGD:2741; rat. [P06536-1]
DR CTD; 2908; -.
DR RGD; 2741; Nr3c1.
DR eggNOG; KOG3575; Eukaryota.
DR InParanoid; P06536; -.
DR OrthoDB; 333292at2759; -.
DR PhylomeDB; P06536; -.
DR Reactome; R-RNO-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand.
DR Reactome; R-RNO-383280; Nuclear Receptor transcription pathway.
DR Reactome; R-RNO-4090294; SUMOylation of intracellular receptors.
DR EvolutionaryTrace; P06536; -.
DR PRO; PR:P06536; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005829; C:cytosol; ISO:RGD.
DR GO; GO:0043197; C:dendritic spine; IDA:RGD.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0043005; C:neuron projection; IDA:RGD.
DR GO; GO:0016607; C:nuclear speck; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0014069; C:postsynaptic density; IDA:RGD.
DR GO; GO:0099092; C:postsynaptic density, intracellular component; IDA:SynGO.
DR GO; GO:0032991; C:protein-containing complex; IDA:RGD.
DR GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR GO; GO:0003682; F:chromatin binding; IDA:RGD.
DR GO; GO:0001046; F:core promoter sequence-specific DNA binding; ISO:RGD.
DR GO; GO:0003677; F:DNA binding; ISO:RGD.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISO:RGD.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IMP:RGD.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; ISO:RGD.
DR GO; GO:0003690; F:double-stranded DNA binding; IDA:RGD.
DR GO; GO:0031072; F:heat shock protein binding; IDA:RGD.
DR GO; GO:0042562; F:hormone binding; IPI:RGD.
DR GO; GO:0030544; F:Hsp70 protein binding; IDA:RGD.
DR GO; GO:0051879; F:Hsp90 protein binding; IDA:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0004883; F:nuclear glucocorticoid receptor activity; ISO:RGD.
DR GO; GO:0004879; F:nuclear receptor activity; ISS:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; ISO:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:UniProtKB.
DR GO; GO:0030971; F:receptor tyrosine kinase binding; IPI:RGD.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:RGD.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IDA:RGD.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:RGD.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:RGD.
DR GO; GO:0005496; F:steroid binding; IPI:RGD.
DR GO; GO:1990239; F:steroid hormone binding; ISS:UniProtKB.
DR GO; GO:0003713; F:transcription coactivator activity; IDA:RGD.
DR GO; GO:0008270; F:zinc ion binding; TAS:RGD.
DR GO; GO:0030325; P:adrenal gland development; ISO:RGD.
DR GO; GO:0007568; P:aging; IEP:RGD.
DR GO; GO:0008209; P:androgen metabolic process; IEP:RGD.
DR GO; GO:0007420; P:brain development; IEP:RGD.
DR GO; GO:0071549; P:cellular response to dexamethasone stimulus; IMP:RGD.
DR GO; GO:0071385; P:cellular response to glucocorticoid stimulus; ISS:UniProtKB.
DR GO; GO:0071286; P:cellular response to magnesium ion; IEP:RGD.
DR GO; GO:0071383; P:cellular response to steroid hormone stimulus; ISS:UniProtKB.
DR GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; ISO:RGD.
DR GO; GO:0006338; P:chromatin remodeling; IMP:UniProtKB.
DR GO; GO:0007623; P:circadian rhythm; IEP:RGD.
DR GO; GO:0045815; P:epigenetic maintenance of chromatin in transcription-competent conformation; IMP:UniProtKB.
DR GO; GO:0007565; P:female pregnancy; IEP:RGD.
DR GO; GO:0008211; P:glucocorticoid metabolic process; ISO:RGD.
DR GO; GO:0042921; P:glucocorticoid receptor signaling pathway; ISO:RGD.
DR GO; GO:0030518; P:intracellular steroid hormone receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0030324; P:lung development; IEP:RGD.
DR GO; GO:0060603; P:mammary gland duct morphogenesis; ISO:RGD.
DR GO; GO:0042711; P:maternal behavior; ISO:RGD.
DR GO; GO:0014889; P:muscle atrophy; IEP:RGD.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:RGD.
DR GO; GO:0031914; P:negative regulation of synaptic plasticity; IMP:RGD.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:RGD.
DR GO; GO:0043116; P:negative regulation of vascular permeability; IMP:RGD.
DR GO; GO:0061051; P:positive regulation of cell growth involved in cardiac muscle cell development; IMP:RGD.
DR GO; GO:0060999; P:positive regulation of dendritic spine development; IMP:RGD.
DR GO; GO:2000324; P:positive regulation of glucocorticoid receptor signaling pathway; IDA:RGD.
DR GO; GO:0014049; P:positive regulation of glutamate secretion; IMP:RGD.
DR GO; GO:1902895; P:positive regulation of miRNA transcription; ISO:RGD.
DR GO; GO:0043525; P:positive regulation of neuron apoptotic process; ISO:RGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:RGD.
DR GO; GO:0065003; P:protein-containing complex assembly; TAS:RGD.
DR GO; GO:0042127; P:regulation of cell population proliferation; IDA:RGD.
DR GO; GO:0031946; P:regulation of glucocorticoid biosynthetic process; ISO:RGD.
DR GO; GO:0006111; P:regulation of gluconeogenesis; ISO:RGD.
DR GO; GO:0010906; P:regulation of glucose metabolic process; IMP:RGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISO:RGD.
DR GO; GO:0014823; P:response to activity; IEP:RGD.
DR GO; GO:0046685; P:response to arsenic-containing substance; IDA:RGD.
DR GO; GO:0051592; P:response to calcium ion; IEP:RGD.
DR GO; GO:0051412; P:response to corticosterone; IEP:RGD.
DR GO; GO:0071548; P:response to dexamethasone; IEP:RGD.
DR GO; GO:0051602; P:response to electrical stimulus; IEP:RGD.
DR GO; GO:0014854; P:response to inactivity; IEP:RGD.
DR GO; GO:0032868; P:response to insulin; IEP:RGD.
DR GO; GO:0046689; P:response to mercury ion; IEP:RGD.
DR GO; GO:0009314; P:response to radiation; IEP:RGD.
DR Gene3D; 1.10.565.10; -; 1.
DR Gene3D; 3.30.50.10; -; 1.
DR InterPro; IPR001409; Glcrtcd_rcpt.
DR InterPro; IPR035500; NHR-like_dom_sf.
DR InterPro; IPR000536; Nucl_hrmn_rcpt_lig-bd.
DR InterPro; IPR001723; Nuclear_hrmn_rcpt.
DR InterPro; IPR001628; Znf_hrmn_rcpt.
DR InterPro; IPR013088; Znf_NHR/GATA.
DR Pfam; PF02155; GCR; 2.
DR Pfam; PF00104; Hormone_recep; 1.
DR Pfam; PF00105; zf-C4; 1.
DR PRINTS; PR00528; GLCORTICOIDR.
DR PRINTS; PR00398; STRDHORMONER.
DR PRINTS; PR00047; STROIDFINGER.
DR SMART; SM00430; HOLI; 1.
DR SMART; SM00399; ZnF_C4; 1.
DR SUPFAM; SSF48508; SSF48508; 1.
DR PROSITE; PS51843; NR_LBD; 1.
DR PROSITE; PS00031; NUCLEAR_REC_DBD_1; 1.
DR PROSITE; PS51030; NUCLEAR_REC_DBD_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative initiation; Chromatin regulator;
KW Cytoplasm; Cytoskeleton; DNA-binding; Isopeptide bond; Lipid-binding;
KW Metal-binding; Methylation; Mitochondrion; Nucleus; Phosphoprotein;
KW Receptor; Reference proteome; Steroid-binding; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..795
FT /note="Glucocorticoid receptor"
FT /id="PRO_0000019941"
FT DOMAIN 542..776
FT /note="NR LBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
FT DNA_BIND 440..505
FT /note="Nuclear receptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 440..460
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 476..500
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT REGION 1..439
FT /note="Modulating"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 67..103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 151..206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 504..795
FT /note="Interaction with CLOCK"
FT /evidence="ECO:0000250"
FT REGION 506..541
FT /note="Hinge"
FT REGION 550..715
FT /note="Interaction with CRY1"
FT /evidence="ECO:0000250"
FT COMPBIAS 67..102
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 151..171
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 187..206
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 24
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P06537"
FT MOD_RES 46
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04150"
FT MOD_RES 134
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P06537"
FT MOD_RES 155
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04150"
FT MOD_RES 162
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P06537"
FT MOD_RES 171
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:9603939"
FT MOD_RES 224
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:9603939,
FT ECO:0007744|PubMed:22673903"
FT MOD_RES 232
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:9603939,
FT ECO:0007744|PubMed:22673903"
FT MOD_RES 246
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:9603939"
FT MOD_RES 287
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 327
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P06537"
FT MOD_RES 424
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04150"
FT MOD_RES 499
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P04150"
FT MOD_RES 511
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P04150"
FT MOD_RES 513
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P04150"
FT MOD_RES 514
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P04150"
FT CROSSLNK 278
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P04150"
FT CROSSLNK 297
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO); alternate"
FT /evidence="ECO:0000269|PubMed:23508108"
FT CROSSLNK 297
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P04150"
FT CROSSLNK 313
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO); alternate"
FT /evidence="ECO:0000269|PubMed:23508108"
FT CROSSLNK 313
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P04150"
FT CROSSLNK 438
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P06537"
FT CROSSLNK 721
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000269|PubMed:23508108"
FT VAR_SEQ 1..27
FT /note="Missing (in isoform B)"
FT /evidence="ECO:0000305"
FT /id="VSP_018969"
FT VARIANT 77
FT /note="Missing (in strain: Brown Norway/Crl)"
FT VARIANT 78..79
FT /note="Missing (in strain: SHR/OlaIpcv)"
FT VARIANT 83..96
FT /note="Missing (in strain: Sprague-Dawley)"
FT VARIANT 226
FT /note="S -> G (in strain: SHR/OlaIpcv and Brown Norway/
FT Crl)"
FT /evidence="ECO:0000269|Ref.3, ECO:0007744|PubMed:22673903"
FT VARIANT 260
FT /note="N -> D (in strain: SHR/OlaIpcv and Brown Norway/
FT Crl)"
FT /evidence="ECO:0000269|Ref.3"
FT MUTAGEN 1
FT /note="M->T: Abolishes expression of A-type isoforms."
FT /evidence="ECO:0000269|PubMed:11435610"
FT MUTAGEN 28
FT /note="M->T: Abolishes expression of B-type isoforms."
FT /evidence="ECO:0000269|PubMed:11435610"
FT MUTAGEN 297
FT /note="K->R: Enhances transcriptional activity; when
FT associated with R-313."
FT /evidence="ECO:0000269|PubMed:23508108"
FT MUTAGEN 313
FT /note="K->R: Enhances transcriptional activity; when
FT associated with R-297."
FT /evidence="ECO:0000269|PubMed:23508108"
FT MUTAGEN 481
FT /note="D->R: Disrupts dimerization and decreases
FT transcription transactivation."
FT /evidence="ECO:0000269|PubMed:8618925"
FT MUTAGEN 488
FT /note="R->Q: Loss of chromatin specific function and
FT reduces chromatin remodeling. Abolishes interaction with
FT SMARD1."
FT /evidence="ECO:0000269|PubMed:12917342"
FT MUTAGEN 500
FT /note="C->Y: Abolishes interaction with POU2F2."
FT /evidence="ECO:0000269|PubMed:10480874"
FT MUTAGEN 501
FT /note="L->P: Abrogates DNA-binding and transcription
FT transactivation. Abolishes interaction with POU2F1 and
FT POU2F2."
FT /evidence="ECO:0000269|PubMed:10480874,
FT ECO:0000269|PubMed:11278286"
FT MUTAGEN 656
FT /note="C->S: Strongly increases affinity for
FT dexamethasone."
FT /evidence="ECO:0000269|PubMed:1939229"
FT MUTAGEN 721
FT /note="K->R: Abolishes the stimulatory effect of RWDD3 on
FT its transcriptional activity. Diminishes NCOA2 coactivator
FT activity."
FT /evidence="ECO:0000269|PubMed:23508108"
FT MUTAGEN 773
FT /note="E->A: Abolishes interaction with NCOA1 and reduces
FT transcription transactivation; when associated with S-656."
FT /evidence="ECO:0000269|PubMed:12118039"
FT CONFLICT 95..96
FT /note="Missing (in Ref. 3; AAL78956)"
FT /evidence="ECO:0000305"
FT CONFLICT 98
FT /note="D -> G (in Ref. 1; AAA41203)"
FT /evidence="ECO:0000305"
FT CONFLICT 345
FT /note="S -> T (in Ref. 4; CAA68545)"
FT /evidence="ECO:0000305"
FT CONFLICT 600
FT /note="L -> P (in Ref. 2; CAA72938 and 3; AAL66772/
FT AAL78956)"
FT /evidence="ECO:0000305"
FT CONFLICT 602
FT /note="L -> F (in Ref. 3; AAL66772/AAL78956)"
FT /evidence="ECO:0000305"
FT TURN 441..443
FT /evidence="ECO:0007829|PDB:3G9M"
FT STRAND 444..446
FT /evidence="ECO:0007829|PDB:3G97"
FT STRAND 449..451
FT /evidence="ECO:0007829|PDB:3G9M"
FT STRAND 454..456
FT /evidence="ECO:0007829|PDB:3G9M"
FT HELIX 458..469
FT /evidence="ECO:0007829|PDB:3G9M"
FT STRAND 477..480
FT /evidence="ECO:0007829|PDB:3G9M"
FT HELIX 488..490
FT /evidence="ECO:0007829|PDB:3G9M"
FT HELIX 493..503
FT /evidence="ECO:0007829|PDB:3G9M"
FT HELIX 509..513
FT /evidence="ECO:0007829|PDB:3G9M"
SQ SEQUENCE 795 AA; 87556 MW; 9C9DE0B1D6724845 CRC64;
MDSKESLAPP GRDEVPGSLL GQGRGSVMDF YKSLRGGATV KVSASSPSVA AASQADSKQQ
RILLDFSKGS TSNVQQRQQQ QQQQQQQQQQ QQQQQQPDLS KAVSLSMGLY MGETETKVMG
NDLGYPQQGQ LGLSSGETDF RLLEESIANL NRSTSVPENP KSSTSATGCA TPTEKEFPKT
HSDASSEQQN RKSQTGTNGG SVKLYPTDQS TFDLLKDLEF SAGSPSKDTN ESPWRSDLLI
DENLLSPLAG EDDPFLLEGN TNEDCKPLIL PDTKPKIKDT GDTILSSPSS VALPQVKTEK
DDFIELCTPG VIKQEKLGPV YCQASFSGTN IIGNKMSAIS VHGVSTSGGQ MYHYDMNTAS
LSQQQDQKPV FNVIPPIPVG SENWNRCQGS GEDSLTSLGA LNFPGRSVFS NGYSSPGMRP
DVSSPPSSSS AATGPPPKLC LVCSDEASGC HYGVLTCGSC KVFFKRAVEG QHNYLCAGRN
DCIIDKIRRK NCPACRYRKC LQAGMNLEAR KTKKKIKGIQ QATAGVSQDT SENPNKTIVP
AALPQLTPTL VSLLEVIEPE VLYAGYDSSV PDSAWRIMTT LNMLGGRQVI AAVKWAKAIL
GLRNLHLDDQ MTLLQYSWMF LMAFALGWRS YRQSSGNLLC FAPDLIINEQ RMSLPCMYDQ
CKHMLFVSSE LQRLQVSYEE YLCMKTLLLL SSVPKEGLKS QELFDEIRMT YIKELGKAIV
KREGNSSQNW QRFYQLTKLL DSMHEVVENL LTYCFQTFLD KTMSIEFPEM LAEIITNQIP
KYSNGNIKKL LFHQK
