ID A0A3Q1AUJ8_AMPOC Unreviewed; 496 AA.
AC A0A3Q1AUJ8;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 25.
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};
OS Amphiprion ocellaris (Clown anemonefish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Amphiprion.
OX NCBI_TaxID=80972 {ECO:0000313|Ensembl:ENSAOCP00000005162.1, ECO:0000313|Proteomes:UP000257160};
RN [1] {ECO:0000313|Ensembl:ENSAOCP00000005162.1}
RP IDENTIFICATION.
RG Ensembl;
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 -!- 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; A0A3Q1AUJ8; -.
DR STRING; 80972.ENSAOCP00000005162; -.
DR Ensembl; ENSAOCT00000006782.1; ENSAOCP00000005162.1; ENSAOCG00000008638.1.
DR GeneTree; ENSGT00940000159789; -.
DR OMA; NAVSHIC; -.
DR Proteomes; UP000257160; Unplaced.
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:SF39; RETINOIC ACID RECEPTOR RXR-ALPHA; 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:UP000257160};
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 166..241
FT /note="Nuclear receptor"
FT /evidence="ECO:0000259|PROSITE:PS51030"
FT DOMAIN 261..492
FT /note="NR LBD"
FT /evidence="ECO:0000259|PROSITE:PS51843"
FT REGION 44..89
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 496 AA; 54450 MW; CCB212804777E456 CRC64;
METKPFLSLG FLKPQCSLAP PMQRGRSGEA CSCFSGVCPL HQRRLSSDSS GQVTSSPLGS
PTSHRGMHPS LLSPTSMGPS GSLHSPISTL SSPMNGLASP FSVISSPMGP HSMNSPGMGY
GPSVSPQLNS PMNSVSSTED IKPPLGLNGV MKVPAQPSGT ALSLTKHICA ICGDRSSGKH
YGVYSCEGCK GFFKRTVRKD LTYTCRDNKD CVIDKRQRNR CQYCRYQKCL AMGMKREAVQ
EERQRAKDRN ENEVESTSCA NEDMPVEKIL EAEQAVEPKT ETYIETNLGV PSNSPNDPVT
NICQAADKQL FTLVEWAKRI PHFSELPLDD QVILLRAGWN ELLIASFSHR SIAVKDGILL
ATGLHVHRNS AHSAGVGAIF DRVLTELVSK MRDMQMDKTE LGCLRAIVLF NPDSKGLSNP
GEVEALREKV YASLEAYCKQ KYPEQPGRFA KLLLRLPALR SIGLKCLEHL FFFKLIGDTP
IDTFLMEMLE APHQMT
//
