RXRGA_DANRE
ID RXRGA_DANRE Reviewed; 441 AA.
AC Q90416; Q6PBU9;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2004, sequence version 2.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Retinoic acid receptor RXR-gamma-A;
DE AltName: Full=Nuclear receptor subfamily 2 group B member 3-A;
DE AltName: Full=Retinoic acid receptor RXR-alpha;
DE AltName: Full=Retinoid X receptor alpha;
DE AltName: Full=Retinoid X receptor gamma-A;
GN Name=rxrga; Synonyms=nr2b1, nr2b3a, rxr, rxra, rxrg;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, HETERODIMERIZATION WITH RARGA, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=7565671; DOI=10.1128/mcb.15.10.5226;
RA Jones B.B., Ohno C.K., Allenby G., Boffa M.B., Levin A.A., Grippo J.F.,
RA Petkovich M.;
RT "New retinoid X receptor subtypes in zebra fish (Danio rerio)
RT differentially modulate transcription and do not bind 9-cis retinoic
RT acid.";
RL Mol. Cell. Biol. 15:5226-5234(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Retina;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP DEVELOPMENTAL STAGE.
RX PubMed=16448862; DOI=10.1016/j.modgep.2005.10.005;
RA Tallafuss A., Hale L.A., Yan Y.-L., Dudley L., Eisen J.S.,
RA Postlethwait J.H.;
RT "Characterization of retinoid-X receptor genes rxra, rxrba, rxrbb and rxrg
RT during zebrafish development.";
RL Gene Expr. Patterns 6:556-565(2006).
RN [4]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=17195188; DOI=10.1002/dvdy.21049;
RA Waxman J.S., Yelon D.;
RT "Comparison of the expression patterns of newly identified zebrafish
RT retinoic acid and retinoid X receptors.";
RL Dev. Dyn. 236:587-595(2007).
CC -!- FUNCTION: Receptor for retinoic acid. Retinoic acid receptors bind as
CC heterodimers to their target response elements in response to their
CC ligands, all-trans or 9-cis retinoic acid, and regulate gene expression
CC in various biological processes. The rar/rxr heterodimers bind to the
CC retinoic acid response elements (RARE) composed of tandem 5'-AGGTCA-3'
CC sites known as DR1-DR5. The high affinity ligand for rxrs is 9-cis
CC retinoic acid (By similarity). {ECO:0000250,
CC ECO:0000269|PubMed:7565671}.
CC -!- SUBUNIT: Homodimer (By similarity). Heterodimer; with a rar molecule
CC (By similarity). Binds DNA preferentially as a rar/rxr heterodimer (By
CC similarity). Heterodimerizes with rarga. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407}.
CC -!- TISSUE SPECIFICITY: Uniformly expressed from the blastula to mid-
CC gastrula stages. In late gastrula stages, there is specific expression
CC in the presumptive hindbrain and spinal cord. At 16 hours post-
CC fertilization (hpf), expressed in the hindbrain from rhombomere 7/8 to
CC the anterior spinal cord; this expression continues until 42 hpf. At 24
CC hpf, also expressed in the lateral plate mesoderm flanking rhombomere 6
CC and in the cranial neural crest, but not in the migrating crest. At 26
CC hpf, also expressed in retina. At 48 hpf, strong retinal expression.
CC {ECO:0000269|PubMed:17195188, ECO:0000269|PubMed:7565671}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC {ECO:0000269|PubMed:16448862, ECO:0000269|PubMed:17195188,
CC ECO:0000269|PubMed:7565671}.
CC -!- DOMAIN: Composed of three domains: a modulating N-terminal domain, a
CC DNA-binding domain and a C-terminal ligand-binding domain.
CC -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR2
CC subfamily. {ECO:0000305}.
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DR EMBL; U29940; AAC59720.1; -; mRNA.
DR EMBL; BC059576; AAH59576.1; -; mRNA.
DR PIR; I50515; I50515.
DR AlphaFoldDB; Q90416; -.
DR SMR; Q90416; -.
DR PaxDb; Q90416; -.
DR PRIDE; Q90416; -.
DR ZFIN; ZDB-GENE-980526-36; rxrga.
DR InParanoid; Q90416; -.
DR PhylomeDB; Q90416; -.
DR SignaLink; Q90416; -.
DR PRO; PR:Q90416; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IBA:GO_Central.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:UniProtKB.
DR GO; GO:0004879; F:nuclear receptor activity; IDA:UniProtKB.
DR GO; GO:0003707; F:nuclear steroid receptor activity; IEA:InterPro.
DR GO; GO:0044323; F:retinoic acid-responsive element binding; IBA:GO_Central.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0048856; P:anatomical structure development; IBA:GO_Central.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0032526; P:response to retinoic acid; IBA:GO_Central.
DR GO; GO:0048384; P:retinoic acid receptor signaling pathway; IBA:GO_Central.
DR Gene3D; 1.10.565.10; -; 1.
DR Gene3D; 3.30.50.10; -; 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 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; 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 2: Evidence at transcript level;
KW Activator; DNA-binding; Metal-binding; Nucleus; Receptor;
KW Reference proteome; Transcription; Transcription regulation; Zinc;
KW Zinc-finger.
FT CHAIN 1..441
FT /note="Retinoic acid receptor RXR-gamma-A"
FT /id="PRO_0000053570"
FT DOMAIN 209..437
FT /note="NR LBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
FT DNA_BIND 117..182
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..177
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT REGION 1..116
FT /note="Modulating"
FT /evidence="ECO:0000250"
FT REGION 16..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 56..94
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 183..206
FT /note="Hinge"
FT REGION 188..210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 56..91
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 188..204
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 31
FT /note="S -> G (in Ref. 1; AAC59720)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 441 AA; 48720 MW; F169ADE221F2F13C CRC64;
MDNNDTYLHL SSSLQVAHGH LSSPPSQPPL SSMVSHHHPS IINGLGSPYS VITSSSLGSP
SASMPTTSNM GYGALNSPQM NSLNSVSSSE DIKPPPGLAG LGSYPCGSPG SLSKHICAIC
GDRSSGKHYG VYSCEGCKGF FKRTIRKDLT YTCRDNKDCQ IDKRQRNRCQ YCRYQKCLAM
GMKREAVQEE RQRGRERSDN EVDSSSSFNE EMPVEKILDA ELAVEPKTEA YMESSMSNST
NDPVTNICQA ADKQLFTLVE WAKRIPHFSD LPLDDQVILL RAGWNELLIA SFSHRSVTVK
DGILLATGLH VHRSSAHSAG VGSIFDRVLT ELVSKMRDMQ MDKTELGCLR AIVLFNPDAK
GLSNPSEVEA LREKVYASLE GYTKHNYPDQ PGRFAKLLLR LPALRSIGLK CLEHLFFFKL
IGDTPIDTFL MEMLEAPHQI T
