RXRA_RAT
ID RXRA_RAT Reviewed; 467 AA.
AC Q05343;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Retinoic acid receptor RXR-alpha;
DE AltName: Full=Nuclear receptor subfamily 2 group B member 1;
DE AltName: Full=Retinoid X receptor alpha;
GN Name=Rxra; Synonyms=Nr2b1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND HETERODIMERIZATION WITH PPARA.
RC TISSUE=Liver;
RX PubMed=8381967; DOI=10.1073/pnas.90.4.1440;
RA Gearing K.L., Gottlicher M., Teboul M., Widmark E., Gustafsson J.-A.;
RT "Interaction of the peroxisome-proliferator-activated receptor and retinoid
RT X receptor.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:1440-1444(1993).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [3]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=28267642; DOI=10.1016/j.jsbmb.2017.03.002;
RA Cheng B., Al-Shammari F.H., Ghader I.A., Sequeira F., Thakkar J.,
RA Mathew T.C.;
RT "Fundamental studies of adrenal retinoid-X-receptor: Protein isoform,
RT tissue expression, subcellular distribution, and ligand availability.";
RL J. Steroid Biochem. Mol. Biol. 171:110-120(2017).
RN [4]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=28167758; DOI=10.1073/pnas.1621425114;
RA Lee D.Y., Lin T.E., Lee C.I., Zhou J., Huang Y.H., Lee P.L., Shih Y.T.,
RA Chien S., Chiu J.J.;
RT "MicroRNA-10a is crucial for endothelial response to different flow
RT patterns via interaction of retinoid acid receptors and histone
RT deacetylases.";
RL Proc. Natl. Acad. Sci. U.S.A. 114:2072-2077(2017).
CC -!- FUNCTION: Receptor for retinoic acid that acts as a transcription
CC factor (By similarity). Forms homo- or heterodimers with retinoic acid
CC receptors (RARs) and binds to target response elements in response to
CC their ligands, all-trans or 9-cis retinoic acid, to regulate gene
CC expression in various biological processes (By similarity). The RAR/RXR
CC heterodimers bind to the retinoic acid response elements (RARE)
CC composed of tandem 5'-AGGTCA-3' sites known as DR1-DR5 to regulate
CC transcription (By similarity). The high affinity ligand for retinoid X
CC receptors (RXRs) is 9-cis retinoic acid (By similarity). In the absence
CC of ligand, the RXR-RAR heterodimers associate with a multiprotein
CC complex containing transcription corepressors that induce histone
CC deacetylation, chromatin condensation and transcriptional suppression
CC (By similarity). On ligand binding, the corepressors dissociate from
CC the receptors and coactivators are recruited leading to transcriptional
CC activation (By similarity). Serves as a common heterodimeric partner
CC for a number of nuclear receptors, such as RARA, RARB and PPARA (By
CC similarity). The RXRA/RARB heterodimer can act as a transcriptional
CC repressor or transcriptional activator, depending on the RARE DNA
CC element context (By similarity). The RXRA/PPARA heterodimer is required
CC for PPARA transcriptional activity on fatty acid oxidation genes such
CC as ACOX1 and the P450 system genes (PubMed:8381967). Together with
CC RARA, positively regulates microRNA-10a expression, thereby inhibiting
CC the GATA6/VCAM1 signaling response to pulsatile shear stress in
CC vascular endothelial cells (By similarity). Acts as an enhancer of RARA
CC binding to RARE DNA element (By similarity). May facilitate the nuclear
CC import of heterodimerization partners such as VDR and NR4A1 (By
CC similarity). Promotes myelin debris phagocytosis and remyelination by
CC macrophages (By similarity). Plays a role in the attenuation of the
CC innate immune system in response to viral infections, possibly by
CC negatively regulating the transcription of antiviral genes such as type
CC I IFN genes (By similarity). Involved in the regulation of calcium
CC signaling by repressing ITPR2 gene expression, thereby controlling
CC cellular senescence (By similarity). {ECO:0000250|UniProtKB:P19793,
CC ECO:0000269|PubMed:8381967}.
CC -!- SUBUNIT: Homodimer (By similarity). Heterodimer (via C-terminus) with
CC RARA; required for ligand-dependent retinoic acid receptor
CC transcriptional activity; association with RARA is enhanced by
CC pulsatile shear stress (By similarity). Heterodimer with PPARA (via the
CC leucine-like zipper in the LBD); the interaction is required for PPARA
CC transcriptional activity (By similarity). Heterodimerizes with PPARG
CC (By similarity). Heterodimerizes (via NR LBD) with RARB (By
CC similarity). Heterodimerizes with NR1H4; the heterodimerization
CC enhances the binding affinity for LXXLL motifs from coactivators (By
CC similarity). Interacts with NCOA3 and NCOA6 coactivators (By
CC similarity). Interacts with FAM120B (By similarity). Interacts with
CC coactivator PELP1, SENP6, SFPQ, DNTTIP2 and RNF8 (By similarity).
CC Interacts with PRMT2 (By similarity). Interacts with ASXL1 (By
CC similarity). Interacts with BHLHE40/DEC1, BHLHE41/DEC2, MED1, NCOR1 and
CC NCOR2 (By similarity). Interacts in a ligand-dependent fashion with
CC MED1 and NCOA1 (By similarity). Interacts with VDR (By similarity).
CC Interacts with EP300; the interaction is decreased by 9-cis retinoic
CC acid (By similarity). Heterodimer (via C-terminus) with NR4A1 (DNA-
CC binding domain); the interaction is enhanced by 9-cis retinoic acid (By
CC similarity). NR4A1 competes with EP300 for interaction with RXRA and
CC thereby attenuates EP300 mediated acetylation of RXRA (By similarity).
CC In the absence of hormonal ligand, interacts with TACC1 (By
CC similarity). {ECO:0000250|UniProtKB:P19793,
CC ECO:0000250|UniProtKB:P28700}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407,
CC ECO:0000269|PubMed:28167758, ECO:0000269|PubMed:28267642}. Cytoplasm
CC {ECO:0000250|UniProtKB:P19793}. Mitochondrion
CC {ECO:0000250|UniProtKB:P19793}. Note=Localization to the nucleus is
CC enhanced by vitamin D3 (By similarity). Nuclear localization may be
CC enhanced by the interaction with heterodimerization partner VDR (By
CC similarity). Translocation to the mitochondrion upon interaction with
CC NR4A1 (By similarity). Increased nuclear localization upon pulsatile
CC shear stress (By similarity). {ECO:0000250|UniProtKB:P19793}.
CC -!- TISSUE SPECIFICITY: Expressed in the adrenal gland with main expression
CC in the zona fasciculata and medulla (at protein level)
CC (PubMed:28267642). Expressed in aortic endothelial cells, with high
CC expression in the descending thoracic aorta and the outer curvature of
CC the aortic arch, where pulsatory shear stress exists, but very low in
CC the inner curvature of the aortic arch, where oscillatory shear stress
CC prevails (at protein level) (PubMed:28167758).
CC {ECO:0000269|PubMed:28167758, ECO:0000269|PubMed:28267642}.
CC -!- DOMAIN: Composed of three domains: a modulating N-terminal or AF1
CC domain, a DNA-binding domain and a C-terminal ligand-binding or AF2
CC domain.
CC -!- PTM: Phosphorylated on serine and threonine residues mainly in the N-
CC terminal modulating domain (By similarity). Constitutively
CC phosphorylated on Ser-22 in the presence or absence of ligand (By
CC similarity). Under stress conditions, hyperphosphorylated by activated
CC JNK on Ser-61, Ser-75, Thr-87 and Ser-265 (By similarity).
CC Phosphorylated on Ser-28, in vitro, by PKA (By similarity). This
CC phosphorylation is required for repression of cAMP-mediated
CC transcriptional activity of RARA (By similarity).
CC {ECO:0000250|UniProtKB:P19793, ECO:0000250|UniProtKB:P28700}.
CC -!- PTM: Sumoylation negatively regulates transcriptional activity.
CC Desumoylated specifically by SENP6. {ECO:0000250|UniProtKB:P19793}.
CC -!- PTM: Acetylated by EP300; acetylation enhances DNA binding and
CC transcriptional activity. {ECO:0000250|UniProtKB:P19793}.
CC -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR2
CC subfamily. {ECO:0000305}.
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DR EMBL; L06482; AAA42093.1; -; mRNA.
DR PIR; A47278; A47278.
DR PIR; I67427; I67427.
DR AlphaFoldDB; Q05343; -.
DR BMRB; Q05343; -.
DR SMR; Q05343; -.
DR STRING; 10116.ENSRNOP00000012892; -.
DR BindingDB; Q05343; -.
DR ChEMBL; CHEMBL4431; -.
DR DrugCentral; Q05343; -.
DR iPTMnet; Q05343; -.
DR PhosphoSitePlus; Q05343; -.
DR PaxDb; Q05343; -.
DR UCSC; RGD:3610; rat.
DR RGD; 3610; Rxra.
DR eggNOG; KOG3575; Eukaryota.
DR InParanoid; Q05343; -.
DR PhylomeDB; Q05343; -.
DR Reactome; R-RNO-159418; Recycling of bile acids and salts.
DR Reactome; R-RNO-192105; Synthesis of bile acids and bile salts.
DR Reactome; R-RNO-193368; Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
DR Reactome; R-RNO-193807; Synthesis of bile acids and bile salts via 27-hydroxycholesterol.
DR Reactome; R-RNO-200425; Carnitine metabolism.
DR Reactome; R-RNO-204174; Regulation of pyruvate dehydrogenase (PDH) complex.
DR Reactome; R-RNO-211976; Endogenous sterols.
DR Reactome; R-RNO-381340; Transcriptional regulation of white adipocyte differentiation.
DR Reactome; R-RNO-383280; Nuclear Receptor transcription pathway.
DR Reactome; R-RNO-400206; Regulation of lipid metabolism by PPARalpha.
DR Reactome; R-RNO-4090294; SUMOylation of intracellular receptors.
DR Reactome; R-RNO-5362517; Signaling by Retinoic Acid.
DR Reactome; R-RNO-9029569; NR1H3 & NR1H2 regulate gene expression linked to cholesterol transport and efflux.
DR Reactome; R-RNO-9616222; Transcriptional regulation of granulopoiesis.
DR Reactome; R-RNO-9623433; NR1H2 & NR1H3 regulate gene expression to control bile acid homeostasis.
DR Reactome; R-RNO-9707564; Cytoprotection by HMOX1.
DR PRO; PR:Q05343; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0030424; C:axon; IDA:RGD.
DR GO; GO:0000785; C:chromatin; ISO:RGD.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0043235; C:receptor complex; ISO:RGD.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; ISO:RGD.
DR GO; GO:0005667; C:transcription regulator complex; ISO:RGD.
DR GO; GO:0031490; F:chromatin DNA binding; ISO:RGD.
DR GO; GO:0003677; F:DNA binding; ISO:RGD.
DR GO; GO:0050692; F:DNA binding domain binding; ISO:RGD.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISO:RGD.
DR GO; GO:0003690; F:double-stranded DNA binding; ISO:RGD.
DR GO; GO:0019899; F:enzyme binding; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0050693; F:LBD domain binding; ISO:RGD.
DR GO; GO:0004879; F:nuclear receptor activity; ISO:RGD.
DR GO; GO:0016922; F:nuclear receptor binding; ISO:RGD.
DR GO; GO:0042974; F:nuclear retinoic acid receptor binding; IPI:RGD.
DR GO; GO:0003707; F:nuclear steroid receptor activity; TAS:RGD.
DR GO; GO:0042809; F:nuclear vitamin D receptor binding; ISO:RGD.
DR GO; GO:0042277; F:peptide binding; ISO:RGD.
DR GO; GO:0019904; F:protein domain specific binding; IPI:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; IPI:RGD.
DR GO; GO:0001972; F:retinoic acid binding; ISO:RGD.
DR GO; GO:0044323; F:retinoic acid-responsive element binding; ISO:RGD.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:RGD.
DR GO; GO:0001162; F:RNA polymerase II intronic transcription regulatory region sequence-specific DNA binding; ISO:RGD.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; ISO:RGD.
DR GO; GO:0043565; F:sequence-specific DNA binding; ISO:RGD.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:RGD.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; ISO:RGD.
DR GO; GO:0001223; F:transcription coactivator binding; ISO:RGD.
DR GO; GO:0001221; F:transcription coregulator binding; ISO:RGD.
DR GO; GO:0008270; F:zinc ion binding; ISO:RGD.
DR GO; GO:0007568; P:aging; IEP:RGD.
DR GO; GO:0048856; P:anatomical structure development; IBA:GO_Central.
DR GO; GO:0031103; P:axon regeneration; IEP:RGD.
DR GO; GO:0043010; P:camera-type eye development; ISO:RGD.
DR GO; GO:0060038; P:cardiac muscle cell proliferation; ISO:RGD.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0032869; P:cellular response to insulin stimulus; IEP:RGD.
DR GO; GO:0007566; P:embryo implantation; ISO:RGD.
DR GO; GO:0007565; P:female pregnancy; IEP:RGD.
DR GO; GO:0010467; P:gene expression; ISO:RGD.
DR GO; GO:0007507; P:heart development; ISO:RGD.
DR GO; GO:0009755; P:hormone-mediated signaling pathway; ISO:RGD.
DR GO; GO:0001701; P:in utero embryonic development; ISO:RGD.
DR GO; GO:0006954; P:inflammatory response; IEP:RGD.
DR GO; GO:0001889; P:liver development; IEP:RGD.
DR GO; GO:0001893; P:maternal placenta development; ISO:RGD.
DR GO; GO:0007494; P:midgut development; IEP:RGD.
DR GO; GO:0042789; P:mRNA transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IMP:RGD.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0035357; P:peroxisome proliferator activated receptor signaling pathway; ISO:RGD.
DR GO; GO:0001890; P:placenta development; IEP:RGD.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IMP:RGD.
DR GO; GO:0002157; P:positive regulation of thyroid hormone mediated signaling pathway; ISO:RGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:1901522; P:positive regulation of transcription from RNA polymerase II promoter involved in cellular response to chemical stimulus; ISO:RGD.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:RGD.
DR GO; GO:0045994; P:positive regulation of translational initiation by iron; ISO:RGD.
DR GO; GO:0070564; P:positive regulation of vitamin D receptor signaling pathway; ISO:RGD.
DR GO; GO:0060687; P:regulation of branching involved in prostate gland morphogenesis; ISO:RGD.
DR GO; GO:0031641; P:regulation of myelination; IDA:RGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:RGD.
DR GO; GO:0045471; P:response to ethanol; IEP:RGD.
DR GO; GO:0051384; P:response to glucocorticoid; IMP:RGD.
DR GO; GO:0007584; P:response to nutrient; IEP:RGD.
DR GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
DR GO; GO:0032526; P:response to retinoic acid; IEP:RGD.
DR GO; GO:0010269; P:response to selenium ion; IEP:RGD.
DR GO; GO:0033189; P:response to vitamin A; IEP:RGD.
DR GO; GO:0033280; P:response to vitamin D; IEP:RGD.
DR GO; GO:0048384; P:retinoic acid receptor signaling pathway; ISO:RGD.
DR GO; GO:0060528; P:secretory columnal luminar epithelial cell differentiation involved in prostate glandular acinus development; ISO:RGD.
DR GO; GO:0055012; P:ventricular cardiac muscle cell differentiation; ISO:RGD.
DR GO; GO:0055010; P:ventricular cardiac muscle tissue morphogenesis; ISO:RGD.
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 1: Evidence at protein level;
KW Acetylation; Cytoplasm; DNA-binding; Isopeptide bond; Metal-binding;
KW Mitochondrion; Nucleus; Phosphoprotein; Receptor; Reference proteome;
KW Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..467
FT /note="Retinoic acid receptor RXR-alpha"
FT /id="PRO_0000053568"
FT DOMAIN 232..463
FT /note="NR LBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
FT DNA_BIND 140..205
FT /note="Nuclear receptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 140..160
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 176..200
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT REGION 1..139
FT /note="Modulating"
FT /evidence="ECO:0000250"
FT REGION 1..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 79..109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 165..170
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250|UniProtKB:P19793"
FT REGION 206..229
FT /note="Hinge"
FT /evidence="ECO:0000250"
FT REGION 211..233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 353..373
FT /note="Required for nuclear export"
FT /evidence="ECO:0000250|UniProtKB:P19793"
FT COMPBIAS 9..28
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 79..108
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 211..227
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 140
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P19793"
FT BINDING 143
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P19793"
FT BINDING 157
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P19793"
FT BINDING 160
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P19793"
FT BINDING 176
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P19793"
FT BINDING 182
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P19793"
FT BINDING 192
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P19793"
FT BINDING 195
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P19793"
FT BINDING 321
FT /ligand="9-cis-retinoate"
FT /ligand_id="ChEBI:CHEBI:78630"
FT /evidence="ECO:0000250|UniProtKB:P19793"
FT BINDING 321
FT /ligand="all-trans-retinoate"
FT /ligand_id="ChEBI:CHEBI:35291"
FT /evidence="ECO:0000250|UniProtKB:P19793"
FT BINDING 332
FT /ligand="9-cis-retinoate"
FT /ligand_id="ChEBI:CHEBI:78630"
FT /evidence="ECO:0000250|UniProtKB:P19793"
FT BINDING 332
FT /ligand="all-trans-retinoate"
FT /ligand_id="ChEBI:CHEBI:35291"
FT /evidence="ECO:0000250|UniProtKB:P19793"
FT MOD_RES 22
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P28700"
FT MOD_RES 28
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19793"
FT MOD_RES 61
FT /note="Phosphoserine; by MAPK8 and MAPK9"
FT /evidence="ECO:0000250|UniProtKB:P28700"
FT MOD_RES 75
FT /note="Phosphoserine; by MAPK8 and MAPK9"
FT /evidence="ECO:0000250|UniProtKB:P28700"
FT MOD_RES 87
FT /note="Phosphothreonine; by MAPK8 and MAPK9"
FT /evidence="ECO:0000250|UniProtKB:P28700"
FT MOD_RES 134
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19793"
FT MOD_RES 150
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P19793"
FT MOD_RES 264
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19793"
FT MOD_RES 265
FT /note="Phosphoserine; by MAPK8 and MAPK9"
FT /evidence="ECO:0000250|UniProtKB:P28700"
FT CROSSLNK 4
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P19793"
FT CROSSLNK 113
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250"
SQ SEQUENCE 467 AA; 51266 MW; AF86A74FD05BD470 CRC64;
MDTKHFLPLD FSTQVNSSSL SSPTGRGSMA APSLHPSLGP GLGSPLGSPG QLHSPISTLS
SPINGMGPPF SVISSPMGPH SMSVPTTPTL GFETGSPQLN SPMNPVSSSE DIKPPLGLNG
VLKVPAHPSG NMSSFTKHIC AICGDRSSGK HYGVYSCEGC KGFFKRTVRK DLTYTCRDNK
DCLIDKRQRN RCQYCRYQKC LAMGMKREAV QEERQRGKDR NENEVESTSS ANEDMPVEKI
LEAELAVEPK TETYVEANMG LNPSSPNDPV TNICQAADKQ LFTLVEWAKR IPHFSELPLD
DQVILLRAGW NELLIASFSH RSIAVKDGIL LATGLHVHRN SAHSAGVGAI FDRVLTELVS
KMRDMQMDKT ELGCLRAIVL FNPDSKGLSN PAEVEALREK VYASLEAYCK HKYPEQPGRF
AKLLLRLPAL RSIGLKCLEH LFFFKLIGDT PIDTFLMEML EAPHQTT
