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Database: UniProt
Entry: A0A3Q1AMB0_AMPOC
LinkDB: A0A3Q1AMB0_AMPOC
Original site: A0A3Q1AMB0_AMPOC 
ID   A0A3Q1AMB0_AMPOC        Unreviewed;       470 AA.
AC   A0A3Q1AMB0;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 26.
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:ENSAOCP00000001929.1, ECO:0000313|Proteomes:UP000257160};
RN   [1] {ECO:0000313|Ensembl:ENSAOCP00000001929.1}
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}.
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DR   AlphaFoldDB; A0A3Q1AMB0; -.
DR   STRING; 80972.ENSAOCP00000001929; -.
DR   Ensembl; ENSAOCT00000012379.1; ENSAOCP00000001929.1; ENSAOCG00000005008.1.
DR   GeneTree; ENSGT00940000159208; -.
DR   OMA; DEHCRQE; -.
DR   OrthoDB; 5400963at2759; -.
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: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: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          124..199
FT                   /note="Nuclear receptor"
FT                   /evidence="ECO:0000259|PROSITE:PS51030"
FT   DOMAIN          225..466
FT                   /note="NR LBD"
FT                   /evidence="ECO:0000259|PROSITE:PS51843"
FT   REGION          1..40
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          198..225
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        7..40
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        198..221
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   470 AA;  51521 MW;  94F398198DC4A6D9 CRC64;
     MGDSRDSRSP DSSSVSSPPS GQRSPPLVPS AAASMTSLPP ITTTGVNSPI SSIGSPFSVI
     SSSLGSPCLP GTPSVGYGPI SSPQINSTVS MSGLHAVSSS DDVKPPLGLK QLSSHSPGPM
     LSQKRLCSIC GDRSSGKHYG VYSCEGCKGF FKRTVRKDLT YTCRDNKDCM VDKRQRNRCQ
     YCRYQKCLAM GMKREVAKMN DRSVQEERQR NKDREGEVES TSAVNEEMPV EKILEAEMAV
     EQKTELHADG TSGGSSPNDP VTNICQAADK QLFTLVEWAK RIPHFSELPL DDQVILLRAG
     WNELLIASFS HRSISVKDGI LLATGLHVHR NSAHSAGVGA IFDRAHNAEV GAIFDRVLTE
     LVSKMRDMQM DKTELGCLRA IILFNPDAKG LSNPSEVELL RERVYASLEA YCKQKYPDQQ
     GRFAKLLLRL PALRSIGLKC LEHLFFFKLI GDTPIDTFLM EMLEAPHQLT
//
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