RXRBB_DANRE
ID RXRBB_DANRE Reviewed; 422 AA.
AC Q90417;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Retinoic acid receptor RXR-beta-B;
DE AltName: Full=Nuclear receptor subfamily 2 group B member 2-B;
DE AltName: Full=Retinoic acid receptor RXR-delta;
DE AltName: Full=Retinoid X receptor beta-B;
DE AltName: Full=Retinoid X receptor delta;
GN Name=rxrbb; Synonyms=nr2b2b, rxrd;
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] {ECO:0000305, ECO:0000312|EMBL:AAC59721.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, HETERODIMERIZATION WITH RARGA, AND
RP 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 TISSUE SPECIFICITY, AND 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).
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: Shows uniform expression from the blastula to mid-
CC gastrula stages. At 12 hours post-fertilization (hpf), expressed
CC ubiquitously but more weakly. At 24 hpf, restricted to the ventral
CC diencephalon, pharangeal endoderm and trunk and tail mesoderm; mesoderm
CC expression is in medial cells of each somite along the dorsoventral
CC axis, forming stripes. At 48 hpf, expressed in forebrain, eye, midbrain
CC and anterior hindbrain. {ECO:0000269|PubMed:16448862}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC {ECO:0000269|PubMed:16448862, 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:0000255}.
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DR EMBL; U29941; AAC59721.1; -; mRNA.
DR PIR; I50516; I50516.
DR RefSeq; NP_571313.1; NM_131238.1.
DR AlphaFoldDB; Q90417; -.
DR SMR; Q90417; -.
DR STRING; 7955.ENSDARP00000104696; -.
DR PaxDb; Q90417; -.
DR PRIDE; Q90417; -.
DR GeneID; 30486; -.
DR KEGG; dre:30486; -.
DR CTD; 30486; -.
DR ZFIN; ZDB-GENE-990415-242; rxrbb.
DR eggNOG; KOG3575; Eukaryota.
DR InParanoid; Q90417; -.
DR OrthoDB; 912470at2759; -.
DR PhylomeDB; Q90417; -.
DR PRO; PR:Q90417; -.
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:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IDA:ZFIN.
DR GO; GO:0004879; F:nuclear receptor activity; IBA:GO_Central.
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:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
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 DNA-binding; Metal-binding; Nucleus; Receptor; Reference proteome;
KW Repressor; Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..422
FT /note="Retinoic acid receptor RXR-beta-B"
FT /id="PRO_0000053581"
FT DOMAIN 181..421
FT /note="NR LBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
FT DNA_BIND 90..155
FT /note="Nuclear receptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 90..110
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 126..150
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT REGION 1..89
FT /note="Modulating"
FT /evidence="ECO:0000250"
FT REGION 156..178
FT /note="Hinge"
FT /evidence="ECO:0000250"
FT REGION 161..182
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 161..177
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 422 AA; 46732 MW; 6CCDBA3CE29C7238 CRC64;
MNSLPPSTSA VSSPVSSVDS PLSAVSSSIG SPGVPGTPSI GYGPISNSQI NSSMSVSRLH
AVSSSDDVKP PFGLKSVSGS GPMLSQKRMC AICGDRSSGK HYGVYSCEGC KGFFKRTVRK
DLSYTCRDNK ECLVDKRQRN RCQYCRYQKC LAMGMKREAV QEERQKNKER DGDYECSSSA
NEEMPVEKIL EAETAVEHRT DLHSDATGSP NDPVTNICQA ADKQLFTLVE WAKRVPHFSD
VPLDDQVILL RAGWNELLIA AFSHRSISVK DEILLATGLH VPKESTHNLG VEAFFDRESS
HSAEVGALFD RVLTELVCKM RDMQMDKTEL GCLRAIVLFN PDAKGLTSSS EVELLREKVY
ASLESYCKQK YPDQQGRFAK LLLRLPALRS IGLKCLEHLF FFKLIGNTPI DTFLMEMLES
PH
