RXRG_CHICK
ID RXRG_CHICK Reviewed; 467 AA.
AC P28701; Q91380;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Retinoic acid receptor RXR-gamma;
DE AltName: Full=Nuclear receptor subfamily 2 group B member 3;
DE AltName: Full=Retinoid X receptor gamma;
GN Name=RXRG; Synonyms=NR2B3;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND DEVELOPMENTAL STAGE.
RX PubMed=1652422; DOI=10.1242/dev.111.3.771;
RA Rowe A., Eager N.S.C., Brickell P.M.;
RT "A member of the RXR nuclear receptor family is expressed in neural-crest-
RT derived cells of the developing chick peripheral nervous system.";
RL Development 111:771-778(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-17 (ISOFORM 2), AND TISSUE SPECIFICITY.
RC TISSUE=Liver;
RX PubMed=8037682; DOI=10.1042/bj3010283;
RA Seleiro E.A., Darling D., Brickell P.M.;
RT "The chicken retinoid-X-receptor-gamma gene gives rise to two distinct
RT species of mRNA with different patterns of expression.";
RL Biochem. J. 301:283-288(1994).
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 -!- SUBUNIT: Homodimer. Heterodimer; with a RAR molecule. Binds DNA
CC preferentially as a RAR/RXR heterodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P28701-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P28701-2; Sequence=VSP_011846;
CC -!- TISSUE SPECIFICITY: Isoform 1 is highly expressed inliver. Isoform 2 is
CC abundantly expressed in eye and dorsal root ganglia.
CC {ECO:0000269|PubMed:8037682}.
CC -!- DEVELOPMENTAL STAGE: At stage 16, in the posterior trunk region,
CC expressed in the neural crest and in neural crest cells migrating into
CC the sclerotome. From stages 24 to 27, expressed in the liver and in
CC elements of the developing peripheral nervous system derived from the
CC neural crest, including dorsal root ganglia, cranial ganglia, enteric
CC ganglia and peripheral nerve tracts. {ECO:0000269|PubMed:1652422}.
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; X58997; CAA41743.1; -; mRNA.
DR EMBL; S72435; AAB31348.2; -; mRNA.
DR PIR; A43781; A43781.
DR PIR; S46479; S46479.
DR RefSeq; NP_990625.1; NM_205294.1. [P28701-1]
DR AlphaFoldDB; P28701; -.
DR SMR; P28701; -.
DR STRING; 9031.ENSGALP00000005377; -.
DR PaxDb; P28701; -.
DR GeneID; 396231; -.
DR KEGG; gga:396231; -.
DR CTD; 6258; -.
DR VEuPathDB; HostDB:geneid_396231; -.
DR eggNOG; KOG3575; Eukaryota.
DR InParanoid; P28701; -.
DR OrthoDB; 912470at2759; -.
DR PhylomeDB; P28701; -.
DR PRO; PR:P28701; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IBA:GO_Central.
DR GO; GO:0005667; C:transcription regulator complex; IDA:AgBase.
DR GO; GO:0000987; F:cis-regulatory region sequence-specific DNA binding; IDA:AgBase.
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: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 Alternative splicing; DNA-binding; Metal-binding; Nucleus; Receptor;
KW Reference proteome; Transcription; Transcription regulation; Zinc;
KW Zinc-finger.
FT CHAIN 1..467
FT /note="Retinoic acid receptor RXR-gamma"
FT /id="PRO_0000053578"
FT DOMAIN 235..463
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..142
FT /note="Modulating"
FT /evidence="ECO:0000250"
FT REGION 209..232
FT /note="Hinge"
FT REGION 214..237
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 214..230
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..17
FT /note="MYGNYPHFIKFPAGFGN -> MQPGMQAPYSLEMGSFPHF (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:8037682"
FT /id="VSP_011846"
SQ SEQUENCE 467 AA; 51233 MW; CE340877BD66C8A2 CRC64;
MYGNYPHFIK FPAGFGNSPV HASSTSVSPS SSLSVGSTVD GHHNYLEAPT NASRALPSPM
NTIGSPVNAL GSPYRVIASS IGSHPVALSS SAPGMNFVTH SPQPNVLNNV SSSEDIKPLP
GLPGIGNMNY PSTSPGSLAK HICAICGDRS SGKHYGVYSC EGCKGFFKRT IRKDLIYTCR
DNKDCLIDKR QRNRCQYCRY QKCLAMGMKR EAVQEERQGS RERSENEAES TSGGSEDMPV
ERILEAELAV EPKTEAYSDV NTESSTNDPV TNICHAADKQ LFTLVEWAKR IPHFSDLTLE
DQVILLRAGW NELLIASFSH RSVSVQDGIL LATGLHVHRS SAHSAGVGSI FDRVLTELVS
KMKDMQMDKS ELGCLRAIVL FNPDAKGLSS PSEVESLREK VYATLEAYTK QKYPEQPGRF
AKLLLRLPAL RSIGLKCLEH LFFFKLIGDT PIDTFLMEML ETPLQVT
