RXRB_CANLF
ID RXRB_CANLF Reviewed; 533 AA.
AC Q5TJF7;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Retinoic acid receptor RXR-beta;
DE AltName: Full=Nuclear receptor subfamily 2 group B member 2;
DE AltName: Full=Retinoid X receptor beta;
GN Name=RXRB; Synonyms=NR2B2;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Doberman pinscher;
RX PubMed=15607421; DOI=10.1016/j.ygeno.2004.09.009;
RA Debenham S.L., Hart E.A., Ashurst J.L., Howe K.L., Quail M.A.,
RA Ollier W.E.R., Binns M.M.;
RT "Genomic sequence of the class II region of the canine MHC: comparison with
RT the MHC of other mammalian species.";
RL Genomics 85:48-59(2005).
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). {ECO:0000250|UniProtKB:P28704}.
CC -!- SUBUNIT: Homodimer (in vitro). Heterodimer with other retinoic acid
CC receptor family members. Binds DNA preferentially as a RAR/RXR
CC heterodimer. Interacts with NR1H3 (By similarity). Interacts with
CC AKAP13 (By similarity). {ECO:0000250|UniProtKB:P28702,
CC ECO:0000250|UniProtKB:P28704}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407}.
CC Cytoplasm {ECO:0000250|UniProtKB:P28702}.
CC -!- DOMAIN: Composed of three domains: a modulating N-terminal domain, a
CC DNA-binding domain and a C-terminal ligand-binding domain.
CC {ECO:0000250|UniProtKB:P28704}.
CC -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR2
CC subfamily. {ECO:0000305}.
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DR EMBL; AJ630366; CAI11431.1; -; Genomic_DNA.
DR AlphaFoldDB; Q5TJF7; -.
DR SMR; Q5TJF7; -.
DR STRING; 9612.ENSCAFP00000001304; -.
DR PaxDb; Q5TJF7; -.
DR eggNOG; KOG3575; Eukaryota.
DR InParanoid; Q5TJF7; -.
DR Proteomes; UP000002254; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IBA:GO_Central.
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; 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; 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 3: Inferred from homology;
KW Cytoplasm; DNA-binding; Metal-binding; Methylation; Nucleus; Receptor;
KW Reference proteome; Transcription; Transcription regulation; Zinc;
KW Zinc-finger.
FT CHAIN 1..533
FT /note="Retinoic acid receptor RXR-beta"
FT /id="PRO_0000053571"
FT DOMAIN 296..529
FT /note="NR LBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
FT DNA_BIND 205..270
FT /note="Nuclear receptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 205..225
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 241..265
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT REGION 1..204
FT /note="Modulating"
FT /evidence="ECO:0000250"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 37..183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 271..295
FT /note="Hinge"
FT REGION 276..299
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 313..336
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 90..132
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 141..155
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 156..170
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 276..292
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 25
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P28702"
SQ SEQUENCE 533 AA; 56917 MW; 01E923B8FA2CA5CF CRC64;
MSWAARPPFL PQRHAAGQCG PVGVRKEMHC GVASRWRRRR PWLDPAAAAA AAAAAGEQQT
PEPEPGEAGR DGMGDSGRDS RSPDSSSPNP LSQGAPPPSP PGLPLPPSSA PTLGGSGAPP
PPPMPPPQLG SPFPVISSSM GSPGLPPPAP PGFSGPVSSP QINSTVSLPG GGSGPPEDVK
PPVLGVRGLH CPPPPGGPGA GKRLCAICGD RSSGKHYGVY SCEGCKGFFK RTIRKDLTYS
CRDNKDCTVD KRQRNRCQYC RYQKCLATGM KREAVQEERQ RGKDKDGDGE GAGGAPEEMP
VDRILEAELA VEQKSDQGVE GPGGTGGSGS SPNDPVTNIC QAADKQLFTL VEWAKRIPHF
SSLPLDDQVI LLRAGWNELL IASFSHRSID VRDGILLATG LHVHRNSAHS AGVGAIFDRV
LTELVSKMRD MRMDKTELGC LRAIILFNPD AKGLSNPSEV EVLREKVYAS LETYCKQKYP
EQQGRFAKLL LRLPALRSIG LKCLEHLFFF KLIGDTPIDT FLMEMLEAPH QLA
