ID A0A1S3LWH2_SALSA Unreviewed; 501 AA.
AC A0A1S3LWH2;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Retinoic acid receptor RXR {ECO:0000256|RuleBase:RU369010};
DE AltName: Full=Nuclear receptor subfamily 2 group B member {ECO:0000256|RuleBase:RU369010};
GN Name=LOC106568909 {ECO:0000313|RefSeq:XP_013995191.1};
OS Salmo salar (Atlantic salmon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8030 {ECO:0000313|Proteomes:UP000087266, ECO:0000313|RefSeq:XP_013995191.1};
RN [1] {ECO:0000313|RefSeq:XP_013995191.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_013995191.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Receptor for retinoic acid that acts as a transcription
CC factor. Forms homo- or heterodimers with retinoic acid receptors (rars)
CC and binds to target response elements in response to their ligands,
CC all-trans or 9-cis retinoic acid, to regulate gene expression in
CC various biological processes. {ECO:0000256|RuleBase:RU369010}.
CC -!- FUNCTION: Receptor for retinoic acid. Retinoic acid receptors bind as
CC heterodimers to their target response elements in response to their
CC ligands, all-trans or 9-cis retinoic acid, and regulate gene expression
CC in various biological processes. The RAR/RXR heterodimers bind to the
CC retinoic acid response elements (RARE) composed of tandem 5'-AGGTCA-3'
CC sites known as DR1-DR5. The high affinity ligand for RXRs is 9-cis
CC retinoic acid. {ECO:0000256|ARBA:ARBA00037559}.
CC -!- SUBUNIT: Homodimer. Heterodimer; with a rar molecule.
CC {ECO:0000256|RuleBase:RU369010}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Nucleus {ECO:0000256|RuleBase:RU004334}.
CC -!- DOMAIN: Composed of three domains: a modulating N-terminal domain, a
CC DNA-binding domain and a C-terminal ligand-binding domain.
CC {ECO:0000256|RuleBase:RU369010}.
CC -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR2
CC subfamily. {ECO:0000256|ARBA:ARBA00006421}.
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DR RefSeq; XP_013995191.1; XM_014139716.1.
DR AlphaFoldDB; A0A1S3LWH2; -.
DR STRING; 8030.ENSSSAP00000039957; -.
DR PaxDb; 8030-ENSSSAP00000039957; -.
DR Ensembl; ENSSSAT00000066153; ENSSSAP00000039957; ENSSSAG00000041320.
DR GeneID; 106568909; -.
DR KEGG; sasa:106568909; -.
DR CTD; 30464; -.
DR OrthoDB; 5400963at2759; -.
DR Proteomes; UP000087266; Chromosome ssa14.
DR Bgee; ENSSSAG00000041320; Expressed in muscle tissue and 14 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR GO; GO:0003707; F:nuclear steroid receptor activity; IEA:UniProtKB-UniRule.
DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR CDD; cd06956; NR_DBD_RXR; 1.
DR CDD; cd06943; NR_LBD_RXR_like; 1.
DR Gene3D; 3.30.50.10; Erythroid Transcription Factor GATA-1, subunit A; 1.
DR Gene3D; 1.10.565.10; Retinoid X Receptor; 1.
DR InterPro; IPR035500; NHR-like_dom_sf.
DR InterPro; IPR021780; Nuc_recep-AF1.
DR InterPro; IPR000536; Nucl_hrmn_rcpt_lig-bd.
DR InterPro; IPR001723; Nuclear_hrmn_rcpt.
DR InterPro; IPR000003; Retinoid-X_rcpt/HNF4.
DR InterPro; IPR001628; Znf_hrmn_rcpt.
DR InterPro; IPR013088; Znf_NHR/GATA.
DR PANTHER; PTHR24083; NUCLEAR HORMONE RECEPTOR; 1.
DR PANTHER; PTHR24083:SF100; RETINOIC ACID RECEPTOR RXR-GAMMA; 1.
DR Pfam; PF00104; Hormone_recep; 1.
DR Pfam; PF11825; Nuc_recep-AF1; 1.
DR Pfam; PF00105; zf-C4; 1.
DR PRINTS; PR00545; RETINOIDXR.
DR PRINTS; PR00398; STRDHORMONER.
DR PRINTS; PR00047; STROIDFINGER.
DR SMART; SM00430; HOLI; 1.
DR SMART; SM00399; ZnF_C4; 1.
DR SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 1.
DR SUPFAM; SSF48508; Nuclear receptor ligand-binding domain; 1.
DR PROSITE; PS51843; NR_LBD; 1.
DR PROSITE; PS00031; NUCLEAR_REC_DBD_1; 1.
DR PROSITE; PS51030; NUCLEAR_REC_DBD_2; 1.
PE 3: Inferred from homology;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU004334};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU004334};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU004334};
KW Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|RuleBase:RU004334};
KW Reference proteome {ECO:0000313|Proteomes:UP000087266};
KW Transcription {ECO:0000256|ARBA:ARBA00023163,
KW ECO:0000256|RuleBase:RU004334};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015,
KW ECO:0000256|RuleBase:RU004334};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU004334};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|RuleBase:RU004334}.
FT DOMAIN 174..249
FT /note="Nuclear receptor"
FT /evidence="ECO:0000259|PROSITE:PS51030"
FT DOMAIN 269..497
FT /note="NR LBD"
FT /evidence="ECO:0000259|PROSITE:PS51843"
FT REGION 64..85
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 248..270
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 248..262
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 501 AA; 55247 MW; 065F092023C8DC81 CRC64;
MRIITGVEDS RGKMESDLID VSQSELEMYG NYQSLMLLPG FDNASVQVSH LSSTPSQPLS
IMVGPPHPHH HHHPSVISTT VNPGRPRPSP ISTLGSPFNG LGGSPYSVIT SSSLGSPGVS
MPHTPTIGFS TLSSPQMNSL NSVSSSEDIK PPPGLAGLGH MNSYGCMSPG SMSKHICAIC
GDRSSGKHYA VYSCEGCKGF FKRTIRKDLT YTCRDSKECL IDKRQRNRCQ YCRYQKCLAM
GMKREAVQEE RQRGRDKSDN EVESTSSFNG DMPVEKILDA ELAIEPKTEA YMEASTGNST
NDPVTNICQA ADKQLFTLVE WAKRIPHFSE LPLDDQVILL RAGWNELLIA SFSHRSVTVK
DGILLATGLH VHRSSAHSAG VGSIFDRVLT ELVSKMKDMQ MDKTELGCLR AIVLFNPDAK
GLSNPTEVEA LREKVYASLE SYTKHRYPEQ PGRFAKLLLR LPALRSIGLK CLEHLFFFKL
IGDTPIDTFL MEMLEAPHQI T
//
