ID   RARGB_DANRE             Reviewed;         489 AA.
AC   A2T928;
DT   21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 1.
DT   27-MAR-2024, entry version 87.
DE   RecName: Full=Retinoic acid receptor gamma-B;
DE            Short=RAR-gamma-B;
DE   AltName: Full=Nuclear receptor subfamily 1 group B member 3-B;
GN   Name=rargb {ECO:0000312|EMBL:ABM89228.1}; Synonyms=nr1b3b;
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:ABM89228.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
RC   TISSUE=Embryo {ECO:0000269|PubMed:17195188};
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).
RN   [2]
RP   DEVELOPMENTAL STAGE, INDUCTION, AND FUNCTION.
RX   PubMed=18929555; DOI=10.1016/j.ydbio.2008.09.022;
RA   Linville A., Radtke K., Waxman J.S., Yelon D., Schilling T.F.;
RT   "Combinatorial roles for zebrafish retinoic acid receptors in the
RT   hindbrain, limbs and pharyngeal arches.";
RL   Dev. Biol. 325:60-70(2009).
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 (By similarity). Required for hindbrain
CC       development. {ECO:0000250, ECO:0000269|PubMed:18929555}.
CC   -!- SUBUNIT: Heterodimer; with an rxr molecule. Binds DNA preferentially as
CC       a rar/rxr heterodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407}.
CC   -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC       Expressed ubiquitously throughout gastrulation. At the tailbud stage,
CC       expressed at higher levels in the anterior and tailbud. Also expressed
CC       in migrating cranial neural crest cells. {ECO:0000269|PubMed:17195188,
CC       ECO:0000269|PubMed:18929555}.
CC   -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR1
CC       subfamily. {ECO:0000255}.
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DR   EMBL; EF028131; ABM89228.1; -; mRNA.
DR   RefSeq; NP_001076779.1; NM_001083310.1.
DR   AlphaFoldDB; A2T928; -.
DR   SMR; A2T928; -.
DR   STRING; 7955.ENSDARP00000142165; -.
DR   PaxDb; 7955-ENSDARP00000052545; -.
DR   GeneID; 100034753; -.
DR   KEGG; dre:100034753; -.
DR   AGR; ZFIN:ZDB-GENE-070314-1; -.
DR   CTD; 100034753; -.
DR   ZFIN; ZDB-GENE-070314-1; rargb.
DR   eggNOG; KOG3575; Eukaryota.
DR   InParanoid; A2T928; -.
DR   OrthoDB; 5390715at2759; -.
DR   PhylomeDB; A2T928; -.
DR   PRO; PR:A2T928; -.
DR   Proteomes; UP000000437; Chromosome 11.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0004879; F:nuclear receptor activity; 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:0030154; P:cell differentiation; IBA:GO_Central.
DR   GO; GO:0071907; P:determination of digestive tract left/right asymmetry; IMP:ZFIN.
DR   GO; GO:0061371; P:determination of heart left/right asymmetry; IMP:ZFIN.
DR   GO; GO:0003140; P:determination of left/right asymmetry in lateral mesoderm; IMP:ZFIN.
DR   GO; GO:0071910; P:determination of liver left/right asymmetry; IMP:ZFIN.
DR   GO; GO:0035469; P:determination of pancreatic left/right asymmetry; IMP:ZFIN.
DR   GO; GO:0009755; P:hormone-mediated signaling pathway; IBA:GO_Central.
DR   GO; GO:0035622; P:intrahepatic bile duct development; IMP:ZFIN.
DR   GO; GO:0030514; P:negative regulation of BMP signaling pathway; IMP:ZFIN.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0048384; P:retinoic acid receptor signaling pathway; IBA:GO_Central.
DR   CDD; cd06964; NR_DBD_RAR; 1.
DR   CDD; cd06937; NR_LBD_RAR; 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; IPR047159; NR_DBD_RAR.
DR   InterPro; IPR047158; NR_LBD_RAR.
DR   InterPro; IPR000536; Nucl_hrmn_rcpt_lig-bd.
DR   InterPro; IPR001723; Nuclear_hrmn_rcpt.
DR   InterPro; IPR003078; Retinoic_acid_rcpt.
DR   InterPro; IPR001628; Znf_hrmn_rcpt.
DR   InterPro; IPR013088; Znf_NHR/GATA.
DR   PANTHER; PTHR24085; NUCLEAR HORMONE RECEPTOR; 1.
DR   PANTHER; PTHR24085:SF7; RETINOIC ACID RECEPTOR GAMMA; 1.
DR   Pfam; PF00104; Hormone_recep; 1.
DR   Pfam; PF00105; zf-C4; 1.
DR   PRINTS; PR01292; RETNOICACIDR.
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   2: Evidence at transcript level;
KW   DNA-binding; Metal-binding; Nucleus; Receptor; Reference proteome;
KW   Transcription; Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN           1..489
FT                   /note="Retinoic acid receptor gamma-B"
FT                   /id="PRO_0000299171"
FT   DOMAIN          161..395
FT                   /note="NR LBD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
FT   DNA_BIND        62..137
FT                   /note="Nuclear receptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT   ZN_FING         65..85
FT                   /note="NR C4-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT   ZN_FING         101..120
FT                   /note="NR C4-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT   REGION          37..57
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          398..489
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        454..489
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   489 AA;  55571 MW;  F181AE31C836F2C8 CRC64;
     MRDVFREATP MTCRSPLPDL RDMMEKLTVF EPTIDSTVET QSTSSEEMIP SSPSPPPPPR
     VYKPCFVCQD KSSGYHYGVS SCEGCKGFFR RSIQKNMVYT CHRDKNCQIN KVTRNRCQYC
     RLRKCFEVGM SKEAVRNDRN KKKKDVKEEV VLPESYELSG ELEELVNKVS KAHRETFPSL
     CQLGKYTTNS SADHRVQLDL GLWDKFSELS TKCIIKIVEF AKRLPGFTSL TIADQITLLK
     SACLDILMLR ICTRYTPEQD TMTFSDGLTL NRTQMHNAGF GPLTDLVFAF AGQLLPLEMD
     DTETGLLSAI CLICGDRMDL EEPHRVDQLQ EPLLEALKIY ARRRRPNKPH MFPRMLMKVT
     DLRGISTKGA ERAITLKMEI PGPMPPLIRE MLENPEIFED SSDSNDSGAA AVVPAPNIKR
     MGQRQAAWVK GERPEWVRGR RRGSKSRYKA GFKAGKARSR DSPDNNGEIR QGDERSEMSV
     RAEQDFALE
//