RXR_BIOGL
ID RXR_BIOGL Reviewed; 436 AA.
AC Q8T5C6;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Retinoic acid receptor RXR;
DE AltName: Full=RXR-like protein {ECO:0000312|EMBL:AAL86461.1};
DE AltName: Full=Retinoid X receptor {ECO:0000303|PubMed:15821117, ECO:0000303|PubMed:16274693};
DE Short=BgRXR {ECO:0000303|PubMed:15821117, ECO:0000303|PubMed:16274693};
GN Name=RXR {ECO:0000312|EMBL:AAL86461.1};
OS Biomphalaria glabrata (Bloodfluke planorb) (Freshwater snail).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Heterobranchia; Euthyneura; Panpulmonata; Hygrophila; Lymnaeoidea;
OC Planorbidae; Biomphalaria.
OX NCBI_TaxID=6526;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAL86461.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DIMERIZATION, AND SUBCELLULAR
RP LOCATION.
RC TISSUE=Embryo {ECO:0000269|PubMed:15821117};
RX PubMed=15821117; DOI=10.1677/jme.1.01766;
RA Bouton D., Escriva H., de Mendonca R.L., Glineur C., Bertin B., Noel C.,
RA Robinson-Rechavi M., de Groot A., Cornette J., Laudet V., Pierce R.J.;
RT "A conserved retinoid X receptor (RXR) from the mollusk Biomphalaria
RT glabrata transactivates transcription in the presence of retinoids.";
RL J. Mol. Endocrinol. 34:567-582(2005).
RN [2] {ECO:0000305}
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 207-436 IN COMPLEX WITH
RP 9-CIS-RETINOIC ACID AND NCOA1-DERIVED PEPTIDE, RETINOIC ACID-BINDING, AND
RP TETRAMERIZATION.
RX PubMed=16274693; DOI=10.1016/j.jmb.2005.09.090;
RA de Groot A., de Rosny E., Juillan-Binard C., Ferrer J.L., Laudet V.,
RA Pierce R.J., Pebay-Peyroula E., Fontecilla-Camps J.C., Borel F.;
RT "Crystal structure of a novel tetrameric complex of agonist-bound ligand-
RT binding domain of Biomphalaria glabrata retinoid X receptor.";
RL J. Mol. Biol. 354:841-853(2005).
CC -!- FUNCTION: Ligand-dependent transcription factor probably involved in
CC the retinoic acid response pathway. Binds 9-cis-retinoic acid (9C-RA)
CC and, to a lesser extent, docosahexaenoic acid (DHA), phytanic acid,
CC methoprene acid and oleic acid. Binds to double-stranded DNA sequences
CC containing direct repeats (DR) with the consensus sequence 5'-
CC [AG]GGTCA-3' and 1, 2, 3, 4 or 5 nucleotides in between (DR1, DR2, DR3.
CC DR4 and DR5, respectively). Binding to DR1 is strongest. Transactivates
CC gene expression when 9C-RA or DHA is bound.
CC {ECO:0000269|PubMed:15821117}.
CC -!- SUBUNIT: Homodimer (via ligand-binding domain). Heterodimer (Probable).
CC Homotetramer consisting of 2 canonical homodimers. Within the tetramer,
CC each monomer binds one molecule of 9C-RA and a NCOA1-derived peptide
CC containing an L-X(2)-L-L motif (Probable).
CC {ECO:0000269|PubMed:15821117, ECO:0000269|PubMed:16274693,
CC ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407,
CC ECO:0000269|PubMed:15821117}.
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:0000305}.
CC -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR2
CC subfamily. {ECO:0000255}.
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DR EMBL; AY048663; AAL86461.1; -; mRNA.
DR RefSeq; NP_001298239.1; NM_001311310.1.
DR PDB; 1XIU; X-ray; 2.50 A; A/B=207-436.
DR PDBsum; 1XIU; -.
DR AlphaFoldDB; Q8T5C6; -.
DR SMR; Q8T5C6; -.
DR STRING; 6526.Q8T5C6; -.
DR GeneID; 106073343; -.
DR VEuPathDB; VectorBase:BGLB010204; -.
DR EvolutionaryTrace; Q8T5C6; -.
DR Proteomes; UP000076420; Genome assembly.
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:InterPro.
DR GO; GO:0016918; F:retinal binding; IEA:UniProtKB-KW.
DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR Gene3D; 1.10.565.10; -; 1.
DR Gene3D; 3.30.50.10; -; 1.
DR IDEAL; IID50154; -.
DR InterPro; IPR035500; NHR-like_dom_sf.
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 Pfam; PF00104; Hormone_recep; 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; SSF48508; SSF48508; 1.
DR PROSITE; PS51843; NR_LBD; 1.
DR PROSITE; PS00031; NUCLEAR_REC_DBD_1; 1.
DR PROSITE; PS51030; NUCLEAR_REC_DBD_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA-binding; Lipid-binding; Metal-binding; Nucleus; Receptor;
KW Transcription; Transcription regulation; Vitamin A; Zinc; Zinc-finger.
FT CHAIN 1..436
FT /note="Retinoic acid receptor RXR"
FT /id="PRO_0000394456"
FT DOMAIN 209..432
FT /note="NR LBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01189,
FT ECO:0000269|PubMed:16274693"
FT DNA_BIND 117..182
FT /note="Nuclear receptor"
FT /evidence="ECO:0000250|UniProtKB:P19793,
FT ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 117..137
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 153..172
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT REGION 1..116
FT /note="Modulating"
FT /evidence="ECO:0000250|UniProtKB:P19793"
FT REGION 1..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 183..206
FT /note="Hinge"
FT /evidence="ECO:0000250|UniProtKB:P19793"
FT REGION 189..209
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 60..92
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 290
FT /ligand="9-cis-retinoate"
FT /ligand_id="ChEBI:CHEBI:78630"
FT /evidence="ECO:0000269|PubMed:16274693,
FT ECO:0007744|PDB:1XIU"
FT BINDING 301
FT /ligand="9-cis-retinoate"
FT /ligand_id="ChEBI:CHEBI:78630"
FT /evidence="ECO:0000269|PubMed:16274693,
FT ECO:0007744|PDB:1XIU"
FT HELIX 214..224
FT /evidence="ECO:0007829|PDB:1XIU"
FT STRAND 232..234
FT /evidence="ECO:0007829|PDB:1XIU"
FT HELIX 238..258
FT /evidence="ECO:0007829|PDB:1XIU"
FT HELIX 263..265
FT /evidence="ECO:0007829|PDB:1XIU"
FT HELIX 268..290
FT /evidence="ECO:0007829|PDB:1XIU"
FT HELIX 291..293
FT /evidence="ECO:0007829|PDB:1XIU"
FT STRAND 294..299
FT /evidence="ECO:0007829|PDB:1XIU"
FT STRAND 303..307
FT /evidence="ECO:0007829|PDB:1XIU"
FT HELIX 308..313
FT /evidence="ECO:0007829|PDB:1XIU"
FT HELIX 317..326
FT /evidence="ECO:0007829|PDB:1XIU"
FT HELIX 328..333
FT /evidence="ECO:0007829|PDB:1XIU"
FT HELIX 338..349
FT /evidence="ECO:0007829|PDB:1XIU"
FT HELIX 360..381
FT /evidence="ECO:0007829|PDB:1XIU"
FT HELIX 388..393
FT /evidence="ECO:0007829|PDB:1XIU"
FT HELIX 396..417
FT /evidence="ECO:0007829|PDB:1XIU"
FT HELIX 423..428
FT /evidence="ECO:0007829|PDB:1XIU"
SQ SEQUENCE 436 AA; 48225 MW; 94D6E84B5CEBD4F9 CRC64;
MDRSEGMDTL ENSMPSGMSM GMTMGGHQGH PPPDIKPDIS SLTSPTSTHG YYGFGPGGMP
SMASSTQPSP GPQQMHSPGM HSPTSSMGSP PMLCLSPSGP SPSPGLPHSS LHTKHICAIC
GDRASGKHYG VYSCEGCKGF FKRTVRKDLT YACRDDKNCM IDKRQRNRCQ YCRYMKCLSM
GMKREAVQEE RQRVKEKGDG EVESTSGANN DMPVEQILEA ELAVDPKIDT YIDAQKDPVT
NICQAADKQL FTLVEWAKRI PHFTELPLED QVILLRAGWN ELLIAGFSHR SIMAKDGILL
ATGLHVHRSS AHQAGVGTIF DRVLTELVAK MRDMKMDKTE LGCLRAVVLF NPDAKGLTAV
QEVEQLREKV YASLEEYTKS RYPEEPGRFA KLLLRLPALR SIGLKCLEHL FFFKLIGDQP
IDTFLMEMLE NPSPAT
