RARG_NOTVI
ID RARG_NOTVI Reviewed; 505 AA.
AC P18516; Q04643;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 2.
DT 25-MAY-2022, entry version 125.
DE RecName: Full=Retinoic acid receptor gamma;
DE Short=RAR-gamma;
DE AltName: Full=Nuclear receptor subfamily 1 group B member 3;
DE AltName: Full=Retinoic acid receptor delta;
DE Short=RAR-delta;
GN Name=RARG; Synonyms=NR1B3;
OS Notophthalmus viridescens (Eastern newt) (Triturus viridescens).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Caudata; Salamandroidea; Salamandridae; Pleurodelinae;
OC Notophthalmus.
OX NCBI_TaxID=8316;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS DELTA-1A; DELTA-1B AND DELTA-2),
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC TISSUE=Tail;
RX PubMed=8382939; DOI=10.1016/0925-4773(93)90091-b;
RA Ragsdale C.W. Jr., Gates P.B., Hill D.S., Brockes J.P.;
RT "Delta retinoic acid receptor isoform delta 1 is distinguished by its
RT exceptional N-terminal sequence and abundance in the limb regeneration
RT blastema.";
RL Mech. Dev. 40:99-112(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM DELTA-1B).
RX PubMed=2552324; DOI=10.1038/341654a0;
RA Ragsdale C.W. Jr., Petkovich M., Gates P.B., Chambon P., Brockes J.P.;
RT "Identification of a novel retinoic acid receptor in regenerative tissues
RT of the newt.";
RL Nature 341:654-657(1989).
RN [3]
RP PARTIAL NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2536901; DOI=10.1038/337566a0;
RA Giguere V., Ong E.S., Evans R.M., Tabin C.J.;
RT "Spatial and temporal expression of the retinoic acid receptor in the
RT regenerating amphibian limb.";
RL Nature 337:566-569(1989).
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). {ECO:0000250}.
CC -!- SUBUNIT: Heterodimer; with a RXR molecule. Binds DNA preferentially as
CC a RAR/RXR heterodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing, Alternative initiation; Named isoforms=3;
CC Name=Delta-1A;
CC IsoId=P18516-1; Sequence=Displayed;
CC Name=Delta-2;
CC IsoId=P18516-2; Sequence=VSP_003643;
CC Name=Delta-1B;
CC IsoId=P18516-3; Sequence=VSP_018770;
CC -!- TISSUE SPECIFICITY: Isoform Delta-1A and Isoform Delta-1B are most
CC abundant in regenerating limbs, tails, and the anterior half of the
CC lower jaw. Isoform Delta-2 is broadly and uniformly distributed.
CC {ECO:0000269|PubMed:8382939}.
CC -!- DOMAIN: Composed of three domains: a modulating N-terminal domain, a
CC DNA-binding domain and a C-terminal ligand-binding domain.
CC -!- MISCELLANEOUS: [Isoform Delta-1B]: Produced by alternative initiation
CC at Met-52 of isoform Delta-1A. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR1
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA49562.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; X69944; CAA49564.1; -; mRNA.
DR EMBL; X69944; CAA49565.1; -; mRNA.
DR EMBL; X69944; CAA49562.1; ALT_INIT; mRNA.
DR EMBL; X69945; CAA49566.1; -; mRNA.
DR EMBL; X17586; CAA35603.1; -; mRNA.
DR PIR; S06124; S06124.
DR PIR; S31516; S31516.
DR AlphaFoldDB; P18516; -.
DR SMR; P18516; -.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0004879; F:nuclear receptor activity; IEA:InterPro.
DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0048384; P:retinoic acid receptor signaling pathway; 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; IPR003078; Retinoic_acid_rcpt.
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; PR01292; RETNOICACIDR.
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 Alternative initiation; Alternative splicing; DNA-binding; Metal-binding;
KW Nucleus; Receptor; Transcription; Transcription regulation; Zinc;
KW Zinc-finger.
FT CHAIN 1..505
FT /note="Retinoic acid receptor gamma"
FT /id="PRO_0000019931"
FT DOMAIN 238..472
FT /note="NR LBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
FT DNA_BIND 143..208
FT /note="Nuclear receptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 143..163
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 179..203
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT REGION 1..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 52..142
FT /note="Modulating"
FT REGION 113..134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 209..237
FT /note="Hinge"
FT REGION 462..505
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..41
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 113..127
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 470..505
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..114
FT /note="MMKFSDTASCRDGGERPEEEGKGAGGRSKLRMGKEEFTGSVGKEEAAAVASM
FT SSSKDRICSTSTQLSQLHGFPPSMYPFAFSSNMRGSPPFDLTNGGAYFRSFPTDLPKEM
FT ASL -> MYDCMEAFMLAPHPLYDVTNPGACMLRKARLSPCFGGLDPFGWPQPASLQ
FT (in isoform Delta-2)"
FT /evidence="ECO:0000303|PubMed:8382939"
FT /id="VSP_003643"
FT VAR_SEQ 1..51
FT /note="Missing (in isoform Delta-1B)"
FT /evidence="ECO:0000303|PubMed:2552324,
FT ECO:0000303|PubMed:8382939"
FT /id="VSP_018770"
FT CONFLICT 281
FT /note="H -> D (in Ref. 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 303
FT /note="G -> S (in Ref. 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 497
FT /note="G -> A (in Ref. 3)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 505 AA; 56629 MW; 0466F549C962E262 CRC64;
MMKFSDTASC RDGGERPEEE GKGAGGRSKL RMGKEEFTGS VGKEEAAAVA SMSSSKDRIC
STSTQLSQLH GFPPSMYPFA FSSNMRGSPP FDLTNGGAYF RSFPTDLPKE MASLSVETQS
TSSEEMVPSS PSPPPPPRVY KPCFVCNDKS SGYHYGVSSC EGCKGFFRRS IQKNMVYTCH
RDKNCQINKV TRNRCQYCRL QKCFEVGMSK EAVRNDRNKK KKEIKEEVVT DSYEMPPEME
ALIQKVSKAH QETFPSLCQL GKYTTNSSAD HRVQLDLGLW HKFSELATKC IIKIVEFAKR
LPGFATLTIA DQITLLKAAC LDILMLRICT RYTPEQDTMT FSDGLTLNRT QMHNAGFGPL
TDLVFAFAEQ LLPLEMDDTE TGLLSAICLI CGDRMDLEEP EKVDKLQEPL LEALKIYARR
RRPNKPYMFP RMLMKITDLR GISTKGAERA ITLKMEIPGP MPPLIREMLE NPEAFEDDAS
PPPKSEQKPI KVEEKPGEKT STKDP
