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MCR_SHEEP
ID   MCR_SHEEP               Reviewed;         258 AA.
AC   Q9BDJ7;
DT   30-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 91.
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   Ovis aries (Sheep).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Caprinae; Ovis.
OX   NCBI_TaxID=9940;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Kidney;
RA   Hantzis V., Albiston A.L., Wintour E.M., Peers A., Funder J.W., Myles K.,
RA   Koukoulous I., Moritz K., Dodic M.;
RT   "Partial cloning of the ovine mineralocorticoid receptor and its
RT   programming by prenatal dexamethasone treatment.";
RL   Submitted (FEB-2001) 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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC       Note=Cytoplasmic and nuclear in the absence of ligand, nuclear after
CC       ligand-binding. {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; AF349768; AAK15580.1; -; mRNA.
DR   AlphaFoldDB; Q9BDJ7; -.
DR   SMR; Q9BDJ7; -.
DR   Proteomes; UP000002356; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0005496; F:steroid binding; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.565.10; -; 1.
DR   InterPro; IPR035500; NHR-like_dom_sf.
DR   InterPro; IPR000536; Nucl_hrmn_rcpt_lig-bd.
DR   InterPro; IPR001723; Nuclear_hrmn_rcpt.
DR   Pfam; PF00104; Hormone_recep; 1.
DR   PRINTS; PR00398; STRDHORMONER.
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; Lipid-binding; Nucleus; Phosphoprotein; Receptor;
KW   Reference proteome; Steroid-binding; Transcription;
KW   Transcription regulation.
FT   CHAIN           <1..258
FT                   /note="Mineralocorticoid receptor"
FT                   /id="PRO_0000053687"
FT   DOMAIN          <1..238
FT                   /note="NR LBD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
FT   REGION          <1..6
FT                   /note="Hinge"
FT   REGION          56..59
FT                   /note="Important for coactivator binding"
FT                   /evidence="ECO:0000250"
FT   BINDING         44
FT                   /ligand="21-hydroxyprogesterone"
FT                   /ligand_id="ChEBI:CHEBI:16973"
FT                   /evidence="ECO:0000250|UniProtKB:P08235"
FT   BINDING         44
FT                   /ligand="aldosterone"
FT                   /ligand_id="ChEBI:CHEBI:27584"
FT                   /evidence="ECO:0000250|UniProtKB:P08235"
FT   BINDING         44
FT                   /ligand="progesterone"
FT                   /ligand_id="ChEBI:CHEBI:17026"
FT                   /evidence="ECO:0000250|UniProtKB:P08235"
FT   BINDING         50
FT                   /ligand="21-hydroxyprogesterone"
FT                   /ligand_id="ChEBI:CHEBI:16973"
FT                   /evidence="ECO:0000250|UniProtKB:P08235"
FT   BINDING         50
FT                   /ligand="aldosterone"
FT                   /ligand_id="ChEBI:CHEBI:27584"
FT                   /evidence="ECO:0000250|UniProtKB:P08235"
FT   BINDING         50
FT                   /ligand="progesterone"
FT                   /ligand_id="ChEBI:CHEBI:17026"
FT                   /evidence="ECO:0000250|UniProtKB:P08235"
FT   BINDING         91
FT                   /ligand="21-hydroxyprogesterone"
FT                   /ligand_id="ChEBI:CHEBI:16973"
FT                   /evidence="ECO:0000250|UniProtKB:P08235"
FT   BINDING         91
FT                   /ligand="aldosterone"
FT                   /ligand_id="ChEBI:CHEBI:27584"
FT                   /evidence="ECO:0000250|UniProtKB:P08235"
FT   BINDING         91
FT                   /ligand="progesterone"
FT                   /ligand_id="ChEBI:CHEBI:17026"
FT                   /evidence="ECO:0000250|UniProtKB:P08235"
FT   BINDING         219
FT                   /ligand="21-hydroxyprogesterone"
FT                   /ligand_id="ChEBI:CHEBI:16973"
FT                   /evidence="ECO:0000250|UniProtKB:P08235"
FT   BINDING         219
FT                   /ligand="aldosterone"
FT                   /ligand_id="ChEBI:CHEBI:27584"
FT                   /evidence="ECO:0000250|UniProtKB:P08235"
FT   BINDING         219
FT                   /ligand="progesterone"
FT                   /ligand_id="ChEBI:CHEBI:17026"
FT                   /evidence="ECO:0000250|UniProtKB:P08235"
FT   NON_TER         1
SQ   SEQUENCE   258 AA;  29912 MW;  182C2C6EAD3F2A1A CRC64;
     LSTISQALTP SPSMILETIQ PEIVYAGYDS SKPNTADNLL STLNRLAGKQ MIQVVKWAKV
     LPGFKNLPLE DQITLIQYSW MCLSSFALSW RSYKHTYPQF LYFPPDLVFN EKKMHHSAMF
     ELCQGMHHIL LQFVRLHLTS EEYSIIKVLL LLSTIPKDGL KTQAVFEEMR TNNIKELRKM
     VTKCPNNFGQ SWQSFYQLTK LLDSMHELVS DLLEFCFYTF RESQALKVEF PAMLVEIISD
     QLPKVESGNA QTLYFHRK
 
 
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