Tag | Content |
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CPLM ID | CPLM-005057 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Mineralocorticoid receptor |
Protein Synonyms/Alias | MR; Nuclear receptor subfamily 3 group C member 2 |
Gene Name | Nr3c2 |
Gene Synonyms/Alias | Mlr |
Created Date | July 27, 2013 |
Organism | Rattus norvegicus (Rat) |
NCBI Taxa ID | 10116 |
Lysine Modification | Position | Peptide | Type | References |
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779 | KQMIQVVKWAKNLKT | ubiquitination | [1] |
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Reference | [1] Synaptic protein ubiquitination in rat brain revealed by antibody-based ubiquitome analysis. Na CH, Jones DR, Yang Y, Wang X, Xu Y, Peng J. J Proteome Res. 2012 Sep 7;11(9):4722-32. [ PMID: 22871113] |
Functional Description | Receptor for both mineralocorticoids (MC) such as aldosterone and glucocorticoids (GC) such as corticosterone or cortisol. Binds to mineralocorticoid response elements (MRE) and transactivates target genes. The effect of MC is to increase ion and water transport and thus raise extracellular fluid volume and blood pressure and lower potassium levels. |
Sequence Annotation | DNA_BIND 604 669 Nuclear receptor. ZN_FING 604 624 NR C4-type. ZN_FING 640 664 NR C4-type. REGION 1 603 Modulating. REGION 670 729 Hinge. REGION 730 981 Steroid-binding. REGION 779 782 Important for coactivator binding (By BINDING 767 767 Steroid (By similarity). BINDING 773 773 Steroid (By similarity). BINDING 814 814 Steroid (By similarity). BINDING 942 942 Steroid (By similarity). |
Keyword | Alternative splicing; Complete proteome; Cytoplasm; DNA-binding; Endoplasmic reticulum; Lipid-binding; Membrane; Metal-binding; Nucleus; Phosphoprotein; Receptor; Reference proteome; Steroid-binding; Transcription; Transcription regulation; Zinc; Zinc-finger. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 981 AA |
Protein Sequence | METKGYHSLP EGLDMERRWS QVSQTLERSS LGPAERTTEN NYMEIVNVSC VSGAIPNNST 60 QGSSKEKHEL LPYIQQDNSR SGILPSDIKT ELESKELSAT VAESMGLYMD SVRDAEYTYD 120 QQNQQGSLSP TKIYQNMEQL VKFYKENGHR SSTLSAMSRP LRSFMPDSAA SMNGGALRAI 180 VKSPIICHEK SSSVSSPLNM ASSVCSPVGI NSMSSSTTSF GSFPVHSPIT QGTSLTCSPS 240 VENRGSRSHS PTHASNVGSP LSSPLSSMKS PISSPPSHCS VKSPVSSPNN VPLRSSVSSP 300 ANLNNSRCSV SSPSNNTNNR STLSSPTAST VGSIGSPISN AFSYATSGAS AGAGAIQDVV 360 PSPDTHEKGA HDVPFPKTEE VEKAISNGVT GPLNIVQYIK SEPDGAFSSS CLGGNSKISP 420 SSPFSVPIKQ ESSKHSCSGA SFKGNPTVNP FPFMDGSYFS FMDDKDYYSL SGILGPPVPG 480 FDGSCEDSAF PVGIKQEPDD GSYYPEASIP SSAIVGVNSG GQSFHYRIGA QGTISLSRSP 540 RDQSFQHLSS FPPVNTLVES WKPHGDLSSR RSDGYPVLEY IPENVSSSTL RSVSTGSSRP 600 SKICLVCGDE ASGCHYGVVT CGSCKVFFKR AVEGQHNYLC AGRNDCIIDK IRRKNCPACR 660 LQKCLQAGMN LGARKSKKLG KLKGLHEEQP QQPPPPPPQS PEEGTTYIAP TKEPSVNSAL 720 VPQLTSITHA LTPSPAMILE NIEPETVYAG YDNSKPDTAE SLLSTLNRLA AKQMIQVVKW 780 AKNLKTCLSR TKSPSSSILG CVYHRSL 807 |
Gene Ontology | GO:0005737; C:cytoplasm; IDA:RGD. GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. GO:0005634; C:nucleus; IDA:RGD. GO:0003690; F:double-stranded DNA binding; IDA:RGD. GO:0042562; F:hormone binding; IDA:RGD. GO:0017082; F:mineralocorticoid receptor activity; IDA:RGD. GO:0046982; F:protein heterodimerization activity; IDA:RGD. GO:0042803; F:protein homodimerization activity; IDA:RGD. GO:0043565; F:sequence-specific DNA binding; IDA:RGD. GO:0005496; F:steroid binding; IDA:RGD. GO:0008270; F:zinc ion binding; IEA:InterPro. GO:0042127; P:regulation of cell proliferation; IDA:RGD. |
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