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NR5A2_RAT
ID   NR5A2_RAT               Reviewed;         560 AA.
AC   Q9QWM1; Q9QWM0;
DT   18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 148.
DE   RecName: Full=Nuclear receptor subfamily 5 group A member 2;
DE   AltName: Full=FTZ-F1 beta;
DE   AltName: Full=Liver receptor homolog 1;
DE            Short=LRH-1;
GN   Name=Nr5a2;
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] (ISOFORMS 1 AND 2).
RC   TISSUE=Liver;
RA   Yanase T., Ichino I., Oba K.;
RT   "Rat FTZ-F1beta1 (rat homologue 1 of mLRH-1).";
RL   Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Nuclear receptor that acts as a key metabolic sensor by
CC       regulating the expression of genes involved in bile acid synthesis,
CC       cholesterol homeostasis and triglyceride synthesis. Together with the
CC       oxysterol receptors NR1H3/LXR-alpha and NR1H2/LXR-beta, acts as an
CC       essential transcriptional regulator of lipid metabolism. Plays an anti-
CC       inflammatory role during the hepatic acute phase response by acting as
CC       a corepressor: inhibits the hepatic acute phase response by preventing
CC       dissociation of the N-Cor corepressor complex. Key regulator of
CC       cholesterol 7-alpha-hydroxylase gene (CYP7A) expression in liver. May
CC       also contribute to the regulation of pancreas-specific genes and play
CC       important roles in embryonic development (By similarity). Activates the
CC       transcription of CYP2C38 (By similarity).
CC       {ECO:0000250|UniProtKB:O00482, ECO:0000250|UniProtKB:P45448}.
CC   -!- SUBUNIT: Binds DNA as a monomer (By similarity). Interacts with GRIP1,
CC       NCOA2 and NR0B2. Interacts (when sumoylated) with GPS2; interaction
CC       with GPS2 onto hepatic acute phase protein promoters prevents N-Cor
CC       corepressor complex dissociation (By similarity). {ECO:0000250,
CC       ECO:0000250|UniProtKB:O00482}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1; Synonyms=FTZ-F1 beta1;
CC         IsoId=Q9QWM1-1; Sequence=Displayed;
CC       Name=2; Synonyms=FTZ-F1 beta2;
CC         IsoId=Q9QWM1-2; Sequence=VSP_017915;
CC   -!- PTM: Sumoylated by SUMO1 at Lys-289 during the hepatic acute phase
CC       response, leading to promote interaction with GPS2 and prevent N-Cor
CC       corepressor complex dissociation. {ECO:0000250|UniProtKB:O00482}.
CC   -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR5
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AB012960; BAA36339.1; -; mRNA.
DR   EMBL; AB012961; BAA36340.1; -; mRNA.
DR   RefSeq; NP_068510.1; NM_021742.1. [Q9QWM1-1]
DR   RefSeq; XP_006249990.1; XM_006249928.3. [Q9QWM1-2]
DR   AlphaFoldDB; Q9QWM1; -.
DR   SMR; Q9QWM1; -.
DR   STRING; 10116.ENSRNOP00000000812; -.
DR   PhosphoSitePlus; Q9QWM1; -.
DR   Ensembl; ENSRNOT00000000812; ENSRNOP00000000812; ENSRNOG00000000653. [Q9QWM1-1]
DR   Ensembl; ENSRNOT00000097279; ENSRNOP00000096873; ENSRNOG00000000653. [Q9QWM1-2]
DR   GeneID; 60349; -.
DR   KEGG; rno:60349; -.
DR   UCSC; RGD:68353; rat. [Q9QWM1-1]
DR   CTD; 2494; -.
DR   RGD; 68353; Nr5a2.
DR   eggNOG; KOG4218; Eukaryota.
DR   GeneTree; ENSGT00940000153391; -.
DR   HOGENOM; CLU_011437_0_0_1; -.
DR   InParanoid; Q9QWM1; -.
DR   OMA; FLMVEWA; -.
DR   OrthoDB; 619653at2759; -.
DR   PhylomeDB; Q9QWM1; -.
DR   TreeFam; TF350737; -.
DR   Reactome; R-RNO-383280; Nuclear Receptor transcription pathway.
DR   Reactome; R-RNO-4090294; SUMOylation of intracellular receptors.
DR   Reactome; R-RNO-9018519; Estrogen-dependent gene expression.
DR   PRO; PR:Q9QWM1; -.
DR   Proteomes; UP000002494; Chromosome 13.
DR   Bgee; ENSRNOG00000000653; Expressed in ovary and 10 other tissues.
DR   Genevisible; Q9QWM1; RN.
DR   GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR   GO; GO:0005634; C:nucleus; ISO:RGD.
DR   GO; GO:0090575; C:RNA polymerase II transcription regulator complex; ISO:RGD.
DR   GO; GO:0003682; F:chromatin binding; ISO:RGD.
DR   GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
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; ISS:UniProtKB.
DR   GO; GO:0003690; F:double-stranded DNA binding; IDA:RGD.
DR   GO; GO:0004879; F:nuclear receptor activity; IDA:RGD.
DR   GO; GO:0005543; F:phospholipid binding; ISO:RGD.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:RGD.
DR   GO; GO:0043565; F:sequence-specific DNA binding; ISO:RGD.
DR   GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:RGD.
DR   GO; GO:0000976; F:transcription cis-regulatory region binding; ISO:RGD.
DR   GO; GO:0001221; F:transcription coregulator binding; ISO:RGD.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0090425; P:acinar cell differentiation; IEA:Ensembl.
DR   GO; GO:0008206; P:bile acid metabolic process; ISO:RGD.
DR   GO; GO:0097720; P:calcineurin-mediated signaling; IMP:RGD.
DR   GO; GO:1990830; P:cellular response to leukemia inhibitory factor; ISO:RGD.
DR   GO; GO:0042632; P:cholesterol homeostasis; ISO:RGD.
DR   GO; GO:0030855; P:epithelial cell differentiation; ISO:RGD.
DR   GO; GO:0009755; P:hormone-mediated signaling pathway; IBA:GO_Central.
DR   GO; GO:0061113; P:pancreas morphogenesis; ISO:RGD.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:RGD.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR   GO; GO:0045070; P:positive regulation of viral genome replication; ISO:RGD.
DR   GO; GO:0042127; P:regulation of cell population proliferation; ISO: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; ISS:UniProtKB.
DR   GO; GO:0009888; P:tissue development; IBA:GO_Central.
DR   Gene3D; 1.10.565.10; -; 1.
DR   Gene3D; 3.30.50.10; -; 1.
DR   InterPro; IPR035500; NHR-like_dom_sf.
DR   InterPro; IPR016355; NR5_fam.
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   PANTHER; PTHR24086; PTHR24086; 1.
DR   Pfam; PF00104; Hormone_recep; 1.
DR   Pfam; PF00105; zf-C4; 1.
DR   PIRSF; PIRSF002530; Nuc_orph_FTZ-F1; 1.
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   2: Evidence at transcript level;
KW   Activator; Alternative splicing; DNA-binding; Isopeptide bond;
KW   Lipid-binding; Metal-binding; Nucleus; Receptor; Reference proteome;
KW   Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW   Zinc-finger.
FT   CHAIN           1..560
FT                   /note="Nuclear receptor subfamily 5 group A member 2"
FT                   /id="PRO_0000232606"
FT   DOMAIN          319..558
FT                   /note="NR LBD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
FT   DNA_BIND        104..179
FT                   /note="Nuclear receptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT   ZN_FING         107..127
FT                   /note="NR C4-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT   ZN_FING         143..162
FT                   /note="NR C4-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT   REGION          17..54
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           176..205
FT                   /note="FTZ-F1 box"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        31..54
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         535
FT                   /ligand="a phosphatidylglycerol phosphate"
FT                   /ligand_id="ChEBI:CHEBI:60522"
FT                   /evidence="ECO:0000250|UniProtKB:O00482"
FT   BINDING         539
FT                   /ligand="a phosphatidylglycerol phosphate"
FT                   /ligand_id="ChEBI:CHEBI:60522"
FT                   /evidence="ECO:0000250|UniProtKB:O00482"
FT   CROSSLNK        289
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO1)"
FT                   /evidence="ECO:0000250|UniProtKB:O00482"
FT   VAR_SEQ         22..43
FT                   /note="APAPGSETPHSPKLEEKHREKR -> G (in isoform 2)"
FT                   /evidence="ECO:0000303|Ref.1"
FT                   /id="VSP_017915"
SQ   SEQUENCE   560 AA;  63904 MW;  F738B943B443CCE2 CRC64;
     MSASSITGDF QDFLKHGLPA IAPAPGSETP HSPKLEEKHR EKRAGLPDRH RRPIPARSRL
     VMLPKVETEA SGLVRSHGEQ GQMPENMQVS QFKMVNYSYD EDLEELCPVC GDKVSGYHYG
     LLTCESCKGF FKRTVQNQKR YTCIENQNCQ IDKTQRKRCP YCRFKKCIDV GMKLEAVRAD
     RMRGGRNKFG PMYKRDRALK QQKKALIRAN GLKLEAMSQV IQAMPSDLTS AIQNIHSASK
     GLPLSHVALP PTDYDRSPFV TSPISMTMPP HGSLHGYQPY GHFPNRAIKS EYPDPYSSSP
     ESMMGYSYMD GYQTSSPASI PHLILELLKC EPDEPQVQAK IMAYLQQEQN NRNRQEKLSA
     FGLLCKMADQ TLFSIVEWAR SSIFFRELKV DDQMKLLQNC WSELLILDHI YRQVAHGKEG
     TIFLVTGEHV DYSSIISNTE VAFNNLLSLA QELVVRLRSL QFDQREFVCL KFLVLFSSDV
     KNLENFQLVE GVQEQVNAAL LDYTLCNYPQ QTEKFGQLLL RLPEIRAISK QAEDYLYYKH
     VNGDVPYNNL LIEMLHAKRA
 
 
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