ID A0A2U9D2Y6_SCOMX Unreviewed; 462 AA.
AC A0A2U9D2Y6;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 24-JAN-2024, entry version 22.
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 ORFNames=SMAX5B_015810 {ECO:0000313|EMBL:AWP21232.1};
OS Scophthalmus maximus (Turbot) (Psetta maxima).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Pleuronectiformes; Pleuronectoidei; Scophthalmidae;
OC Scophthalmus.
OX NCBI_TaxID=52904 {ECO:0000313|EMBL:AWP21232.1, ECO:0000313|Proteomes:UP000246464};
RN [1] {ECO:0000313|EMBL:AWP21232.1, ECO:0000313|Proteomes:UP000246464}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Martinez P.;
RT "Integrating genomic resources of turbot (Scophthalmus maximus) in depth
RT evaluation of genetic and physical mapping variation across individuals.";
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
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 -!- SUBUNIT: Homodimer. Heterodimer; with a rar molecule.
CC {ECO:0000256|RuleBase:RU369010}.
CC -!- SUBCELLULAR LOCATION: 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 EMBL; CP026264; AWP21232.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U9D2Y6; -.
DR Proteomes; UP000246464; Chromosome 22.
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:SF90; RETINOIC ACID RECEPTOR RXR-BETA; 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:UP000246464};
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 123..198
FT /note="Nuclear receptor"
FT /evidence="ECO:0000259|PROSITE:PS51030"
FT DOMAIN 217..458
FT /note="NR LBD"
FT /evidence="ECO:0000259|PROSITE:PS51843"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 197..218
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..39
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 197..213
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 462 AA; 50545 MW; 0F8C2650D886565D CRC64;
MGDSRDSHSP DSSSVSSPAS GQRSPPLVPS AASMTSLPPI TTTGVNSPIS SIGSPFSVIS
SSLGSPCLPG TPSVGYGPIS SPQINSTVSM SGLHAVSSSD DVKPPLGLKQ LSPHSPGPML
SQKRLCSICG DRSSGKHYGV YSCEGCKGFF KRTVRKDLTY TCRDSKDCMV DKRQRNRCQY
CRYQKCLAMG MKREAVQEER QRNKEREGEV ESTSAVNEEM PVEKILEAEV AVEQKTELHT
DGSSGGSSPN DPVTNICQAA DKQLFTLVEW AKRIPHFSEL ALDDQVILLR AGWNELLIAS
FSHRSISVKD GILLATGLHV HRNSAHSAGV GAIFDRAHNA EVGAIFDRVL TELVSKMRDM
QMDKTELGCL RAIILFNPDA KGLSNPSEVE LLRERVYASL ESYCKQKYPD QQGRFAKLLL
RLPALRSIGL KCLEHLFFFK LIGDTPIDTF LMEMLEAPHQ LT
//
