| Tag | Content |
|---|
| 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 |
|---|
| 779 | KQMIQVVKWAKNLKT | ubiquitination | [1] |
|
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. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |