ID A0A6I9YDD0_9SAUR Unreviewed; 480 AA.
AC A0A6I9YDD0;
DT 07-OCT-2020, integrated into UniProtKB/TrEMBL.
DT 07-OCT-2020, sequence version 1.
DT 18-JUN-2025, 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 Name=RXRA {ECO:0000313|RefSeq:XP_013922176.1};
OS Thamnophis sirtalis.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Colubridae; Natricinae; Thamnophis.
OX NCBI_TaxID=35019 {ECO:0000313|Proteomes:UP000504617, ECO:0000313|RefSeq:XP_013922176.1};
RN [1] {ECO:0000313|RefSeq:XP_013922176.1}
RP IDENTIFICATION.
RC TISSUE=Skeletal muscle {ECO:0000313|RefSeq:XP_013922176.1};
RG RefSeq;
RL Submitted (MAR-2025) 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 RefSeq; XP_013922176.1; XM_014066701.1.
DR AlphaFoldDB; A0A6I9YDD0; -.
DR GeneID; 106549135; -.
DR KEGG; tsr:106549135; -.
DR CTD; 6256; -.
DR OrthoDB; 5873264at2759; -.
DR Proteomes; UP000504617; Unplaced.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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 FunFam; 1.10.565.10:FF:000002; Retinoic acid receptor RXR-alpha; 1.
DR FunFam; 3.30.50.10:FF:000005; Retinoic acid receptor RXR-alpha; 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; IPR050274; Nuclear_hormone_rcpt_NR2.
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 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:UP000504617};
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 131..206
FT /note="Nuclear receptor"
FT /evidence="ECO:0000259|PROSITE:PS51030"
FT DOMAIN 245..476
FT /note="NR LBD"
FT /evidence="ECO:0000259|PROSITE:PS51843"
FT REGION 16..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 202..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..25
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 91..101
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 224..236
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 480 AA; 52799 MW; AA3CB1F3C7D5B247 CRC64;
MDTKHFLPLD FSAQVNSTSL SSPTGRGSHM GTPALHPSMG PSLGGSLGSP SQLHSPINGM
GPPFSVISSP MGPHAMSGPS TPGLGYGAGS PQLNSPLNPV SSTEDIKPPL GINGVLKVPM
HPSSAMPAFT KHICAICGDR SSGKHYGVYS CEGCKGFFKR TVRKDLSYTC RDNKDCLIDK
RQRNRCQYCR YQKCLAMGMK REGMEHHPSR PTRLPGRQEQ PAVQEERQRG KDRNENEVES
TSNANEDMPV EKILEAELAV EPKTETYIEA NMGLAPNSPN DPVTNICQAA DKQLFTLVEW
AKRIPHFSEL PLDDQVILLR AGWNELLIAS FSHRSIAVKD GILLATGLHV HRNSAHSAGV
GAIFDRVLTE LVSKMRDMQM DKTELGCLRA IVLFNPDSKG LSNPAEVEAL REKVYASLEA
YCKQKYPEQP GRFAKLLLRL PALRSIGLKC LEHLFFFKLI GDTPIDTFLM EMLEAPHQMT
//
