ID   RXR_LYMST               Reviewed;         436 AA.
AC   Q5I7G2;
DT   25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Retinoic acid receptor RXR {ECO:0000250|UniProtKB:Q8T5C6};
DE   AltName: Full=Retinoid X receptor {ECO:0000312|EMBL:AAW34268.1};
DE            Short=LymRXR {ECO:0000303|PubMed:20381485};
GN   Name=RXR {ECO:0000312|EMBL:AAW34268.1};
OS   Lymnaea stagnalis (Great pond snail) (Helix stagnalis).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Heterobranchia; Euthyneura; Panpulmonata; Hygrophila; Lymnaeoidea;
OC   Lymnaeidae; Lymnaea.
OX   NCBI_TaxID=6523;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:AAW34268.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP   SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC   TISSUE=CNS {ECO:0000269|PubMed:20381485};
RX   PubMed=20381485; DOI=10.1016/j.ydbio.2010.03.023;
RA   Carter C.J., Farrar N., Carlone R.L., Spencer G.E.;
RT   "Developmental expression of a molluscan RXR and evidence for its novel,
RT   nongenomic role in growth cone guidance.";
RL   Dev. Biol. 343:124-137(2010).
CC   -!- FUNCTION: Ligand-dependent transcription factor probably involved in
CC       the retinoic acid response pathway. Binds 9-cis-retinoic acid (By
CC       similarity). Involved in embryo development, in particular eye and
CC       shell formation. May play a role in growth cone steering.
CC       {ECO:0000250|UniProtKB:Q8T5C6, ECO:0000269|PubMed:20381485,
CC       ECO:0000303|PubMed:20381485}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20381485}. Nucleus
CC       {ECO:0000255|PROSITE-ProRule:PRU00407, ECO:0000269|PubMed:20381485}.
CC       Membrane {ECO:0000269|PubMed:20381485}; Peripheral membrane protein
CC       {ECO:0000269|PubMed:20381485}. Cell projection, axon
CC       {ECO:0000269|PubMed:20381485}. Cell projection, growth cone
CC       {ECO:0000269|PubMed:20381485}. Note=Not present in nucleus of neurons
CC       in adult CNS. Detected in neurites and growth cones of cultured
CC       neurons. {ECO:0000269|PubMed:20381485}.
CC   -!- TISSUE SPECIFICITY: Expressed in the adult central nervous system where
CC       it is detected in neurons of all central ganglia, the neuropil and
CC       nerve bundles radiating from the brain (at protein level).
CC       {ECO:0000269|PubMed:20381485}.
CC   -!- DEVELOPMENTAL STAGE: Expressed from trochophore to hatchling stages
CC       with maximal expression at hatching and also expressed in the adult (at
CC       protein level). {ECO:0000269|PubMed:20381485}.
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:0000255}.
CC   -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR2
CC       subfamily. {ECO:0000255}.
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   EMBL; AY846875; AAW34268.1; -; mRNA.
DR   AlphaFoldDB; Q5I7G2; -.
DR   SMR; Q5I7G2; -.
DR   PRIDE; Q5I7G2; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0030426; C:growth cone; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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   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   Cell projection; Cytoplasm; Developmental protein; DNA-binding; Membrane;
KW   Metal-binding; Nucleus; Receptor; Transcription; Transcription regulation;
KW   Vitamin A; Zinc; Zinc-finger.
FT   CHAIN           1..436
FT                   /note="Retinoic acid receptor RXR"
FT                   /id="PRO_0000415395"
FT   DOMAIN          209..432
FT                   /note="NR LBD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
FT   DNA_BIND        114..189
FT                   /note="Nuclear receptor"
FT                   /evidence="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:0000255"
FT   REGION          1..108
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          183..206
FT                   /note="Hinge"
FT                   /evidence="ECO:0000255"
FT   REGION          188..209
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        57..92
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        188..202
FT                   /note="Basic and acidic 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:0000250|UniProtKB:Q8T5C6"
FT   BINDING         301
FT                   /ligand="9-cis-retinoate"
FT                   /ligand_id="ChEBI:CHEBI:78630"
FT                   /evidence="ECO:0000250|UniProtKB:Q8T5C6"
SQ   SEQUENCE   436 AA;  48239 MW;  35B5F1545F0534FB CRC64;
     MDRSEGMDTL ENSMSGGMSM GMSMGGHQGH PPDIKPDISS LTSPTSTHGG YYGFGPGSMS
     SMSSSTQPSP GPQQMHSPGM HSPTSSMGSP PMLCLSPTGP SPSPGLPHSS LHTKHICAIC
     GDRASGKHYG VYSCEGCKGF FKRTVRKDLT YACRDDKNCM IDKRQRNRCQ YCRYMKCLSM
     GMKREAVQEE RQRVKEKGDG EVESTSGANN DMPVEQILEA ELAVDPKIDT YIDAQKDPVT
     NICQAADKQL FTLVEWAKRI PHFTELPLED QVILLRAGWN ELLIAGFSHR SIMAKDGILL
     ATGLHVHRSS AHQAGVGTIF DRVLTELVAK MREMKMDKTE LGCLRAVVLF NPDAKGLTAV
     QEVEQLREKV YASLEEYTKT RYPEEPGRFA KLLLRLPALR SIGLKCLEHL FFFKLIGDQP
     IDTFLMEMLE NPSPTT