ID A0A1S3KZK0_SALSA Unreviewed; 535 AA.
AC A0A1S3KZK0;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Retinoic acid receptor RXR {ECO:0000256|RuleBase:RU369010};
DE AltName: Full=Nuclear receptor subfamily 2 group B member {ECO:0000256|RuleBase:RU369010};
GN Name=LOC106563228 {ECO:0000313|RefSeq:XP_013984088.1};
OS Salmo salar (Atlantic salmon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8030 {ECO:0000313|Proteomes:UP000087266, ECO:0000313|RefSeq:XP_013984088.1};
RN [1] {ECO:0000313|RefSeq:XP_013984088.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_013984088.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Receptor for retinoic acid that acts as a transcription
CC factor. Forms homo- or heterodimers with retinoic acid receptors (rars)
CC and binds to target response elements in response to their ligands,
CC all-trans or 9-cis retinoic acid, to regulate gene expression in
CC various biological processes. {ECO:0000256|RuleBase:RU369010}.
CC -!- SUBUNIT: Homodimer. Heterodimer; with a rar molecule.
CC {ECO:0000256|RuleBase:RU369010}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU004334}.
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:0000256|RuleBase:RU369010}.
CC -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR2
CC subfamily. {ECO:0000256|ARBA:ARBA00006421}.
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DR RefSeq; XP_013984088.1; XM_014128613.1.
DR AlphaFoldDB; A0A1S3KZK0; -.
DR GeneID; 106563228; -.
DR CTD; 555578; -.
DR OrthoDB; 5400963at2759; -.
DR Proteomes; UP000087266; Chromosome ssa11.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR GO; GO:0003707; F:nuclear steroid receptor activity; IEA:UniProtKB-UniRule.
DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR CDD; cd06956; NR_DBD_RXR; 1.
DR CDD; cd06943; NR_LBD_RXR_like; 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; 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 PANTHER; PTHR24083; NUCLEAR HORMONE RECEPTOR; 1.
DR PANTHER; PTHR24083:SF39; RETINOIC ACID RECEPTOR RXR-ALPHA; 1.
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; 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 3: Inferred from homology;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU004334};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU004334};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU004334};
KW Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|RuleBase:RU004334};
KW Reference proteome {ECO:0000313|Proteomes:UP000087266};
KW Transcription {ECO:0000256|ARBA:ARBA00023163,
KW ECO:0000256|RuleBase:RU004334};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015,
KW ECO:0000256|RuleBase:RU004334};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU004334};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|RuleBase:RU004334}.
FT DOMAIN 200..275
FT /note="Nuclear receptor"
FT /evidence="ECO:0000259|PROSITE:PS51030"
FT DOMAIN 300..531
FT /note="NR LBD"
FT /evidence="ECO:0000259|PROSITE:PS51843"
FT REGION 49..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 78..120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..68
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 535 AA; 59080 MW; 6A072C9EDF0A1F35 CRC64;
METKPFMSLG FLKPQCSLAP PPQRGRSGEA CSCFTGMCHL HHPRISTGNT HRHLHIPSPS
SPSWQTPHLG RHLYQINSSG QVTSSPLSSP TSHRGMHPSL LNPSSMGPSG SLHSPISTLS
SPMNGLGSPF SVINSPMGPH SMSSPGMGYG PSVSPQMFQL NSQMNSVSSS EDIKPPLGLN
GVMKVPAQPS PGCMPLSLTK HICAICGDRS SGKHYGVYSC EGCKGFFKRT VRKDLTYTCR
DNKDCLIDKR QRNRCQYCRY QKCLACGMKR EVLLHTAVQE ERQRAKERSE NEVESTSSVN
EDMPVEKILE AELAVEPKTE TYIETNLGMP SNSPNDPVTN ICQAADKQLF TLVEWAKRIP
HFSELPLDDQ VILLRAGWNE LLIASFSHRS IAVKDGILLA TGLHVHRNSA HSAGVGAIFD
RVLTELVSKM RDMQMDKTEL GCLRAIVLFN PDSKGLSNPG EVEALREKVY ASLEAYCKQK
YPDQPGRFAK LLLRLPALRS IGLKCLEHLF FFKLIGDTPI DTFLMEMLEA PHQMT
//
