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MCR_PIG
ID   MCR_PIG                 Reviewed;         164 AA.
AC   P79404;
DT   30-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=Mineralocorticoid receptor;
DE            Short=MR;
DE   AltName: Full=Nuclear receptor subfamily 3 group C member 2;
DE   Flags: Fragment;
GN   Name=NR3C2; Synonyms=MLR;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Large white; TISSUE=Kidney;
RA   Perreau V., Moisan M.P.;
RT   "Sus scrofa mineralocorticoid receptor partial cDNA; hormone binding
RT   domain.";
RL   Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Receptor for both mineralocorticoids (MC) such as aldosterone
CC       and glucocorticoids (GC) such as corticosterone or cortisol. Binds to
CC       mineralocorticoid response elements (MRE) and transactivates target
CC       genes. The effect of MC is to increase ion and water transport and thus
CC       raise extracellular fluid volume and blood pressure and lower potassium
CC       levels (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Heteromultimeric cytoplasmic complex with HSP90, HSP70, and
CC       FKBP4, in the absence of ligand. After ligand binding, it translocates
CC       to the nucleus and binds to DNA as a homodimer and as a heterodimer
CC       with NR3C1. Binds the coactivator NCOA2. May interact with HSD11B2 in
CC       the absence of ligand. Binds the coactivators NCOA1, TIF1 and NRIP1 (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC       Endoplasmic reticulum membrane {ECO:0000250}; Peripheral membrane
CC       protein {ECO:0000250}. Note=Cytoplasmic and nuclear in the absence of
CC       ligand; nuclear after ligand-binding. When bound to HSD11B2, it is
CC       found associated with the endoplasmic reticulum membrane (By
CC       similarity). {ECO:0000250}.
CC   -!- DOMAIN: Composed of three domains: a modulating N-terminal domain, a
CC       DNA-binding domain and a C-terminal ligand-binding domain.
CC   -!- PTM: Phosphorylated. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR3
CC       subfamily. {ECO:0000305}.
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DR   EMBL; U88893; AAB53273.1; -; mRNA.
DR   AlphaFoldDB; P79404; -.
DR   SMR; P79404; -.
DR   STRING; 9823.ENSSSCP00000019392; -.
DR   PaxDb; P79404; -.
DR   PRIDE; P79404; -.
DR   eggNOG; KOG3575; Eukaryota.
DR   InParanoid; P79404; -.
DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; Unplaced.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0004879; F:nuclear receptor activity; IBA:GO_Central.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0005496; F:steroid binding; IEA:UniProtKB-KW.
DR   GO; GO:0030518; P:intracellular steroid hormone receptor signaling pathway; IBA:GO_Central.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   Gene3D; 1.10.565.10; -; 1.
DR   InterPro; IPR035500; NHR-like_dom_sf.
DR   InterPro; IPR000536; Nucl_hrmn_rcpt_lig-bd.
DR   Pfam; PF00104; Hormone_recep; 1.
DR   SMART; SM00430; HOLI; 1.
DR   SUPFAM; SSF48508; SSF48508; 1.
DR   PROSITE; PS51843; NR_LBD; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; DNA-binding; Endoplasmic reticulum; Lipid-binding; Membrane;
KW   Nucleus; Phosphoprotein; Receptor; Reference proteome; Steroid-binding;
KW   Transcription; Transcription regulation.
FT   CHAIN           <1..>164
FT                   /note="Mineralocorticoid receptor"
FT                   /id="PRO_0000053684"
FT   DOMAIN          <1..162
FT                   /note="NR LBD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
FT   BINDING         15
FT                   /ligand="21-hydroxyprogesterone"
FT                   /ligand_id="ChEBI:CHEBI:16973"
FT                   /evidence="ECO:0000250|UniProtKB:P08235"
FT   BINDING         15
FT                   /ligand="aldosterone"
FT                   /ligand_id="ChEBI:CHEBI:27584"
FT                   /evidence="ECO:0000250|UniProtKB:P08235"
FT   BINDING         15
FT                   /ligand="progesterone"
FT                   /ligand_id="ChEBI:CHEBI:17026"
FT                   /evidence="ECO:0000250|UniProtKB:P08235"
FT   BINDING         143
FT                   /ligand="21-hydroxyprogesterone"
FT                   /ligand_id="ChEBI:CHEBI:16973"
FT                   /evidence="ECO:0000250|UniProtKB:P08235"
FT   BINDING         143
FT                   /ligand="aldosterone"
FT                   /ligand_id="ChEBI:CHEBI:27584"
FT                   /evidence="ECO:0000250|UniProtKB:P08235"
FT   BINDING         143
FT                   /ligand="progesterone"
FT                   /ligand_id="ChEBI:CHEBI:17026"
FT                   /evidence="ECO:0000250|UniProtKB:P08235"
FT   NON_TER         1
FT   NON_TER         164
SQ   SEQUENCE   164 AA;  19695 MW;  AE97ADF1C32F8BBE CRC64;
     QYSWMCLSSF ALSWRSYKHT NSQFLYFAPD LVFNEEKMHQ SAMYELCQGM HQISLQFVRL
     QLTFEEYTIM KVLLLLSTIP KDGLKSQAAF EEMRTNYIKE LRKMVTRCPN NSGQSWQRFY
     QLTKLLDSMH DLVSDLLEFC FYTFRESQAL KVEFPRCWWR SSPT
 
 
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