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Nuclear receptor subfamily 4 group A member 3 (Mitogen-induced nuclear orphan receptor) (Neuron-derived orphan receptor 1) (Nuclear hormone receptor NOR-1)

 NR4A3_HUMAN             Reviewed;         626 AA.
Q92570; A2A3I7; Q12935; Q14979; Q16420; Q4VXA8; Q4VXA9; Q9UEK2;
Q9UEK3;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
21-MAR-2006, sequence version 3.
25-OCT-2017, entry version 175.
RecName: Full=Nuclear receptor subfamily 4 group A member 3;
AltName: Full=Mitogen-induced nuclear orphan receptor;
AltName: Full=Neuron-derived orphan receptor 1;
AltName: Full=Nuclear hormone receptor NOR-1;
Name=NR4A3; Synonyms=CHN, CSMF, MINOR, NOR1, TEC;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA).
TISSUE=Fetal brain;
PubMed=8809112; DOI=10.1016/0167-4781(96)00101-7;
Ohkura N., Ito M., Tsukada T., Sasaki K., Yamaguchi K., Miki K.;
"Structure, mapping and expression of a human NOR-1 gene, the third
member of the Nur77/NGFI-B family.";
Biochim. Biophys. Acta 1308:205-214(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA).
TISSUE=Peripheral blood;
PubMed=8614405; DOI=10.1210/mend.9.12.8614405;
Hedvat C.V., Irving S.G.;
"The isolation and characterization of MINOR, a novel mitogen-
inducible nuclear orphan receptor.";
Mol. Endocrinol. 9:1692-1700(1995).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA).
TISSUE=Fetal brain;
PubMed=8570200;
Clark J., Benjamin H., Gill S., Sidhar S., Goodwin G., Crew J.,
Gusterson B.A., Shipley J., Cooper C.S.;
"Fusion of the EWS gene to CHN, a member of the steroid/thyroid
receptor gene superfamily, in a human myxoid chondrosarcoma.";
Oncogene 12:229-235(1996).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BETA), AND CHROMOSOMAL
TRANSLOCATION WITH EWS.
TISSUE=Fetal heart;
PubMed=8634690; DOI=10.1093/hmg/4.12.2219;
Labelle Y., Zucman J., Stenman G., Kindblom L.-G., Knight J.,
Turc-Carel C., Dockhorn-Dworniczak B., Mandahl N., Desmaze C.,
Peter M., Aurias A., Delattre O., Thomas G.;
"Oncogenic conversion of a novel orphan nuclear receptor by chromosome
translocation.";
Hum. Mol. Genet. 4:2219-2226(1995).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164053; DOI=10.1038/nature02465;
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
Rogers J., Dunham I.;
"DNA sequence and analysis of human chromosome 9.";
Nature 429:369-374(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE
SPLICING (ISOFORM 3).
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-69 AND 301-443 (ISOFORM BETA), AND
ALTERNATIVE SPLICING.
TISSUE=Skeletal muscle;
PubMed=9573341; DOI=10.1016/S0378-1119(98)00095-X;
Ohkura N., Ito M., Tsukada T., Sasaki K., Yamaguchi K., Miki K.;
"Alternative splicing generates isoforms of human neuron-derived
orphan receptor-1 (NOR-1) mRNA.";
Gene 211:79-85(1998).
[8]
INTERACTION WITH SIX3.
PubMed=12543801;
Laflamme C., Filion C., Bridge J.A., Ladanyi M., Goldring M.B.,
Labelle Y.;
"The homeotic protein Six3 is a coactivator of the nuclear receptor
NOR-1 and a corepressor of the fusion protein EWS/NOR-1 in human
extraskeletal myxoid chondrosarcomas.";
Cancer Res. 63:449-454(2003).
[9]
FUNCTION, AND INDUCTION.
PubMed=20558821; DOI=10.1161/CIRCRESAHA.110.222083;
Zhao Y., Howatt D.A., Gizard F., Nomiyama T., Findeisen H.M.,
Heywood E.B., Jones K.L., Conneely O.M., Daugherty A., Bruemmer D.;
"Deficiency of the NR4A orphan nuclear receptor NOR1 decreases
monocyte adhesion and atherosclerosis.";
Circ. Res. 107:501-511(2010).
[10]
FUNCTION.
PubMed=24022864; DOI=10.1152/ajpendo.00169.2013;
Liu Q., Zhu X., Xu L., Fu Y., Garvey W.T.;
"6-Mercaptopurine augments glucose transport activity in skeletal
muscle cells in part via a mechanism dependent upon orphan nuclear
receptor NR4A3.";
Am. J. Physiol. 305:E1081-E1092(2013).
[11]
INTERACTION WITH PRKDC; XRCC6 AND XRCC5, AND PHOSPHORYLATION.
PubMed=25852083; DOI=10.1093/cvr/cvv126;
Medunjanin S., Daniel J.M., Weinert S., Dutzmann J., Burgbacher F.,
Brecht S., Bruemmer D., Kaehne T., Naumann M., Sedding D.G.,
Zuschratter W., Braun-Dullaeus R.C.;
"DNA-dependent protein kinase (DNA-PK) permits vascular smooth muscle
cell proliferation through phosphorylation of the orphan nuclear
receptor NOR1.";
Cardiovasc. Res. 106:488-497(2015).
-!- FUNCTION: Transcriptional activator that binds to regulatory
elements in promoter regions in a cell- and response element
(target)-specific manner. Induces gene expression by binding as
monomers to the NR4A1 response element (NBRE) 5'-AAAAGGTCA-3' site
and as homodimers to the Nur response element (NurRE) site in the
promoter of their regulated target genes (By similarity). Plays a
role in the regulation of proliferation, survival and
differentiation of many different cell types and also in
metabolism and inflammation. Mediates proliferation of vascular
smooth muscle, myeloid progenitor cell and type B pancreatic
cells; promotes mitogen-induced vascular smooth muscle cell
proliferation through transactivation of SKP2 promoter by binding
a NBRE site (By similarity). Upon PDGF stimulation, stimulates
vascular smooth muscle cell proliferation by regulating CCND1 and
CCND2 expression. In islets, induces type B pancreatic cell
proliferation through up-regulation of genes that activate cell
cycle, as well as genes that cause degradation of the CDKN1A (By
similarity). Negatively regulates myeloid progenitor cell
proliferation by repressing RUNX1 in a NBRE site-independent
manner. During inner ear, plays a role as a key mediator of the
proliferative growth phase of semicircular canal development (By
similarity). Mediates also survival of neuron and smooth muscle
cells; mediates CREB-induced neuronal survival, and during
hippocampus development, plays a critical role in pyramidal cell
survival and axonal guidance. Is required for S phase entry of the
cell cycle and survival of smooth muscle cells by inducing CCND1,
resulting in RB1 phosphorylation. Binds to NBRE motif in CCND1
promoter, resulting in the activation of the promoter and CCND1
transcription (By similarity). Plays also a role in inflammation;
upon TNF stimulation, mediates monocyte adhesion by inducing the
expression of VCAM1 and ICAM1 by binding to the NBRE consensus
site (By similarity) (PubMed:20558821). In mast cells activated by
Fc-epsilon receptor cross-linking, promotes the synthesis and
release of cytokines but impairs events leading to degranulation
(By similarity). Plays also a role in metabolism; by modulating
feeding behavior; and by playing a role in energy balance by
inhibiting the glucocorticoid-induced orexigenic neuropeptides
AGRP expression, at least in part by forming a complex with
activated NR3C1 on the AGRP- glucocorticoid response element
(GRE), and thus weakening the DNA binding activity of NR3C1. Upon
catecholamines stimulation, regulates gene expression that
controls oxidative metabolism in skeletal muscle (By similarity).
Plays a role in glucose transport by regulating translocation of
the SLC2A4 glucose transporter to the cell surface
(PubMed:24022864). Finally, during gastrulation plays a crucial
role in the formation of anterior mesoderm by controlling cell
migration. Inhibits adipogenesis (By similarity). Also
participates in cardiac hypertrophy by activating PARP1 (By
similarity). {ECO:0000250|UniProtKB:P51179,
ECO:0000250|UniProtKB:Q9QZB6, ECO:0000269|PubMed:20558821,
ECO:0000269|PubMed:24022864}.
-!- SUBUNIT: Interacts with SIX3 (via homeobox); differentially
regulates the transcriptional activities of NR4A3
(PubMed:12543801). Interacts with the constituents of DNA-PK
heterotrimer PRKDC, XRCC6 and XRCC5; phosphorylates and prevents
NR4A3 ubiquitinylation and degradation (PubMed:25852083).
Interacts with NCOA2; potentiates the activity of the NR4A3.
Interacts with NCOA1, NCOA3, MED1 and KAT2B. Interacts with EP300
and NCOA2; mediates the recruitment of MED1 in the coactivator
complex (By similarity). Interacts with NR3C1 (via nuclear
receptor DNA-binding domain); the interactions represses
transcription activity of NR4A3 on the POMC promoter Nur response
element (NurRE). Interacts with TRIM28; the interactions
potentiates NR4A3 activity on NurRE promoter. Binds DNA as a
monomer and homodimer. Interacts with PARP1; activates PARP1 by
improving acetylation of PARP1 and suppressing the interaction
between PARP1 and SIRT1 (By similarity).
{ECO:0000250|UniProtKB:P51179, ECO:0000250|UniProtKB:Q9QZB6,
ECO:0000269|PubMed:12543801, ECO:0000269|PubMed:25852083}.
-!- INTERACTION:
O95343:SIX3; NbExp=3; IntAct=EBI-13644623, EBI-13644574;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-
ProRule:PRU00407}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=Alpha;
IsoId=Q92570-1; Sequence=Displayed;
Name=Beta;
IsoId=Q92570-2; Sequence=VSP_003712, VSP_003713;
Name=3;
IsoId=Q92570-3; Sequence=VSP_037877;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Isoform alpha is highly expressed in skeletal
muscle. Isoform beta is highly expressed in skeletal muscle and
low expressed in fetal brain and placenta.
-!- INDUCTION: Induced by inflammatory stimuli in endothelial cells
through an NF-kappa-B-dependent transactivation of the NR4A3
Promoter. {ECO:0000269|PubMed:20558821}.
-!- DOMAIN: The AF-1 domain mediates transcription activation. The N-
terminal region (1-292) directly interacts with the C-terminal LBD
(380-627): the interaction is potentiated by AF-1-mediated
recruitment of NCOA2. {ECO:0000250|UniProtKB:Q9QZB6}.
-!- PTM: Phosphorylated by PRKDC. {ECO:0000269|PubMed:25852083}.
-!- DISEASE: Ewing sarcoma (ES) [MIM:612219]: A highly malignant,
metastatic, primitive small round cell tumor of bone and soft
tissue that affects children and adolescents. It belongs to the
Ewing sarcoma family of tumors, a group of morphologically
heterogeneous neoplasms that share the same cytogenetic features.
They are considered neural tumors derived from cells of the neural
crest. Ewing sarcoma represents the less differentiated form of
the tumors. Note=The gene represented in this entry is involved in
disease pathogenesis. A chromosomal aberration involving NR4A3 is
found in patients with Erwing sarcoma. Translocation t(9;22)(q22-
31;q11-12) with EWSR1.
-!- DISEASE: Note=A chromosomal aberration involving NR4A3 is a cause
of a form of extraskeletal myxoid chondrosarcomas (EMC).
Translocation t(9;17)(q22;q11) with TAF2N.
-!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR4
subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAB02581.1; Type=Frameshift; Positions=4, 20; Evidence={ECO:0000305};
Sequence=AAB36006.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/TECID75.html";
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EMBL; D78579; BAA11419.1; -; mRNA.
EMBL; U12767; AAB02581.1; ALT_FRAME; mRNA.
EMBL; S81243; AAB36006.1; ALT_INIT; mRNA.
EMBL; X89894; CAA61984.1; -; mRNA.
EMBL; AL359710; CAI95139.1; -; Genomic_DNA.
EMBL; AL359710; CAI95138.1; -; Genomic_DNA.
EMBL; AL358937; CAI95138.1; JOINED; Genomic_DNA.
EMBL; AL358937; CAI95320.1; -; Genomic_DNA.
EMBL; AL359710; CAI95320.1; JOINED; Genomic_DNA.
EMBL; AL359710; CAM16648.1; -; Genomic_DNA.
EMBL; AL358937; CAM16648.1; JOINED; Genomic_DNA.
EMBL; AL358937; CAM22558.1; -; Genomic_DNA.
EMBL; AL359710; CAM22558.1; JOINED; Genomic_DNA.
EMBL; CH471105; EAW58915.1; -; Genomic_DNA.
EMBL; D85241; BAA28608.1; -; mRNA.
EMBL; D85242; BAA31221.1; -; mRNA.
CCDS; CCDS6742.1; -. [Q92570-3]
CCDS; CCDS6743.1; -. [Q92570-1]
CCDS; CCDS6744.1; -. [Q92570-2]
PIR; S71930; S71930.
RefSeq; NP_008912.2; NM_006981.3. [Q92570-1]
RefSeq; NP_775291.1; NM_173199.2. [Q92570-2]
RefSeq; NP_775292.1; NM_173200.2. [Q92570-3]
RefSeq; XP_016870651.1; XM_017015162.1. [Q92570-1]
UniGene; Hs.279522; -.
ProteinModelPortal; Q92570; -.
SMR; Q92570; -.
BioGrid; 113713; 4.
IntAct; Q92570; 1.
STRING; 9606.ENSP00000333122; -.
ChEMBL; CHEMBL1961792; -.
iPTMnet; Q92570; -.
PhosphoSitePlus; Q92570; -.
BioMuta; NR4A3; -.
DMDM; 90110039; -.
MaxQB; Q92570; -.
PaxDb; Q92570; -.
PeptideAtlas; Q92570; -.
PRIDE; Q92570; -.
DNASU; 8013; -.
Ensembl; ENST00000330847; ENSP00000333122; ENSG00000119508. [Q92570-3]
Ensembl; ENST00000338488; ENSP00000340301; ENSG00000119508. [Q92570-2]
Ensembl; ENST00000395097; ENSP00000378531; ENSG00000119508. [Q92570-1]
Ensembl; ENST00000618101; ENSP00000482027; ENSG00000119508. [Q92570-3]
GeneID; 8013; -.
KEGG; hsa:8013; -.
UCSC; uc004bae.3; human. [Q92570-1]
CTD; 8013; -.
DisGeNET; 8013; -.
EuPathDB; HostDB:ENSG00000119508.17; -.
GeneCards; NR4A3; -.
HGNC; HGNC:7982; NR4A3.
HPA; HPA043360; -.
MalaCards; NR4A3; -.
MIM; 600542; gene+phenotype.
MIM; 612219; phenotype.
neXtProt; NX_Q92570; -.
OpenTargets; ENSG00000119508; -.
Orphanet; 209916; Extraskeletal myxoid chondrosarcoma.
PharmGKB; PA31763; -.
eggNOG; KOG4217; Eukaryota.
eggNOG; ENOG410YWNC; LUCA.
GeneTree; ENSGT00760000118887; -.
HOVERGEN; HBG052663; -.
InParanoid; Q92570; -.
KO; K08559; -.
OMA; SMYFKQS; -.
OrthoDB; EOG091G0GUM; -.
PhylomeDB; Q92570; -.
TreeFam; TF315430; -.
Reactome; R-HSA-383280; Nuclear Receptor transcription pathway.
Reactome; R-HSA-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function.
SignaLink; Q92570; -.
SIGNOR; Q92570; -.
ChiTaRS; NR4A3; human.
GeneWiki; Neuron-derived_orphan_receptor_1; -.
GenomeRNAi; 8013; -.
PRO; PR:Q92570; -.
Proteomes; UP000005640; Chromosome 9.
Bgee; ENSG00000119508; -.
CleanEx; HS_NR4A3; -.
CleanEx; HS_TEC; -.
ExpressionAtlas; Q92570; baseline and differential.
Genevisible; Q92570; HS.
GO; GO:0042629; C:mast cell granule; IEA:GOC.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; NAS:UniProtKB.
GO; GO:0005667; C:transcription factor complex; IEA:Ensembl.
GO; GO:0001046; F:core promoter sequence-specific DNA binding; ISS:UniProtKB.
GO; GO:0003677; F:DNA binding; NAS:UniProtKB.
GO; GO:0035259; F:glucocorticoid receptor binding; IEA:Ensembl.
GO; GO:0035035; F:histone acetyltransferase binding; IEA:Ensembl.
GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
GO; GO:0000978; F:RNA polymerase II core promoter proximal region sequence-specific DNA binding; IEA:Ensembl.
GO; GO:0003707; F:steroid hormone receptor activity; TAS:ProtInc.
GO; GO:0004887; F:thyroid hormone receptor activity; TAS:ProtInc.
GO; GO:0001223; F:transcription coactivator binding; IEA:Ensembl.
GO; GO:0001077; F:transcriptional activator activity, RNA polymerase II core promoter proximal region sequence-specific binding; IDA:UniProtKB.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0030534; P:adult behavior; IEA:Ensembl.
GO; GO:0031100; P:animal organ regeneration; IEA:Ensembl.
GO; GO:0007411; P:axon guidance; IEA:Ensembl.
GO; GO:0045333; P:cellular respiration; ISS:UniProtKB.
GO; GO:0071870; P:cellular response to catecholamine stimulus; ISS:UniProtKB.
GO; GO:0071376; P:cellular response to corticotropin-releasing hormone stimulus; ISS:UniProtKB.
GO; GO:0044320; P:cellular response to leptin stimulus; ISS:UniProtKB.
GO; GO:0035726; P:common myeloid progenitor cell proliferation; ISS:UniProtKB.
GO; GO:0097009; P:energy homeostasis; ISS:UniProtKB.
GO; GO:0045444; P:fat cell differentiation; ISS:UniProtKB.
GO; GO:0007369; P:gastrulation; ISS:UniProtKB.
GO; GO:0021766; P:hippocampus development; IEA:Ensembl.
GO; GO:0043303; P:mast cell degranulation; ISS:UniProtKB.
GO; GO:0001707; P:mesoderm formation; IEA:Ensembl.
GO; GO:1903208; P:negative regulation of hydrogen peroxide-induced neuron death; ISS:UniProtKB.
GO; GO:0043524; P:negative regulation of neuron apoptotic process; IEA:Ensembl.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; ISS:UniProtKB.
GO; GO:0050885; P:neuromuscular process controlling balance; IEA:Ensembl.
GO; GO:0010613; P:positive regulation of cardiac muscle hypertrophy; ISS:UniProtKB.
GO; GO:0045787; P:positive regulation of cell cycle; IEA:Ensembl.
GO; GO:0050679; P:positive regulation of epithelial cell proliferation; ISS:UniProtKB.
GO; GO:0046321; P:positive regulation of fatty acid oxidation; ISS:UniProtKB.
GO; GO:2000253; P:positive regulation of feeding behavior; ISS:UniProtKB.
GO; GO:0010828; P:positive regulation of glucose transport; IDA:UniProtKB.
GO; GO:2000108; P:positive regulation of leukocyte apoptotic process; IEA:Ensembl.
GO; GO:0038097; P:positive regulation of mast cell activation by Fc-epsilon receptor signaling pathway; ISS:UniProtKB.
GO; GO:0032765; P:positive regulation of mast cell cytokine production; ISS:UniProtKB.
GO; GO:1900625; P:positive regulation of monocyte aggregation; IMP:UniProtKB.
GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; ISS:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
GO; GO:0009444; P:pyruvate oxidation; ISS:UniProtKB.
GO; GO:2000505; P:regulation of energy homeostasis; ISS:UniProtKB.
GO; GO:0045652; P:regulation of megakaryocyte differentiation; TAS:Reactome.
GO; GO:0048660; P:regulation of smooth muscle cell proliferation; IDA:UniProtKB.
GO; GO:0061469; P:regulation of type B pancreatic cell proliferation; ISS:UniProtKB.
GO; GO:0042542; P:response to hydrogen peroxide; IEA:Ensembl.
GO; GO:0048752; P:semicircular canal morphogenesis; IEA:Ensembl.
GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; TAS:Reactome.
GO; GO:0060005; P:vestibular reflex; IEA:Ensembl.
Gene3D; 1.10.565.10; -; 2.
Gene3D; 3.30.50.10; -; 1.
InterPro; IPR035500; NHR_like_domain.
InterPro; IPR003072; NOR1_rcpt.
InterPro; IPR003070; Nuc_orph_rcpt.
InterPro; IPR000536; Nucl_hrmn_rcpt_lig-bd.
InterPro; IPR001723; Nuclear_hrmn_rcpt.
InterPro; IPR001628; Znf_hrmn_rcpt.
InterPro; IPR013088; Znf_NHR/GATA.
Pfam; PF00104; Hormone_recep; 1.
Pfam; PF00105; zf-C4; 1.
PRINTS; PR01286; NORNUCRECPTR.
PRINTS; PR01284; NUCLEARECPTR.
PRINTS; PR00398; STRDHORMONER.
PRINTS; PR00047; STROIDFINGER.
SMART; SM00430; HOLI; 1.
SMART; SM00399; ZnF_C4; 1.
SUPFAM; SSF48508; SSF48508; 1.
PROSITE; PS00031; NUCLEAR_REC_DBD_1; 1.
PROSITE; PS51030; NUCLEAR_REC_DBD_2; 1.
1: Evidence at protein level;
Alternative splicing; Chromosomal rearrangement; Complete proteome;
DNA-binding; Metal-binding; Nucleus; Proto-oncogene; Receptor;
Reference proteome; Transcription; Transcription regulation; Zinc;
Zinc-finger.
CHAIN 1 626 Nuclear receptor subfamily 4 group A
member 3.
/FTId=PRO_0000053722.
DNA_BIND 289 364 Nuclear receptor. {ECO:0000255|PROSITE-
ProRule:PRU00407}.
ZN_FING 292 312 NR C4-type. {ECO:0000255|PROSITE-
ProRule:PRU00407}.
ZN_FING 328 352 NR C4-type. {ECO:0000255|PROSITE-
ProRule:PRU00407}.
REGION 1 291 Interaction with NCOA1, NCOA2, NCOA3 and
KAT2B. {ECO:0000250|UniProtKB:Q9QZB6}.
REGION 1 138 Required for DNA-PK heterotrimer.
{ECO:0000269|PubMed:25852083}.
REGION 1 108 Activation function (AF)-1 domain.
{ECO:0000250|UniProtKB:Q9QZB6}.
REGION 379 626 Interaction with KAT2B.
{ECO:0000250|UniProtKB:Q9QZB6}.
REGION 440 490 Ligand-binding. {ECO:0000255}.
COMPBIAS 95 108 Poly-His.
COMPBIAS 282 287 Poly-Ser.
VAR_SEQ 1 1 M -> MHDSIRFGNVDM (in isoform 3).
{ECO:0000305}.
/FTId=VSP_037877.
VAR_SEQ 419 443 YCPTDQAAAGTDAEHVQQFYNLLTA -> VSFMISCFQMND
QGLYLWLLVIRVD (in isoform Beta).
{ECO:0000303|PubMed:8634690,
ECO:0000303|PubMed:9573341}.
/FTId=VSP_003712.
VAR_SEQ 444 626 Missing (in isoform Beta).
{ECO:0000303|PubMed:8634690,
ECO:0000303|PubMed:9573341}.
/FTId=VSP_003713.
CONFLICT 240 240 S -> G (in Ref. 1 and 2). {ECO:0000305}.
CONFLICT 454 454 K -> R (in Ref. 1; BAA11419).
{ECO:0000305}.
CONFLICT 579 579 T -> N (in Ref. 1; BAA11419).
{ECO:0000305}.
CONFLICT 585 585 G -> V (in Ref. 1; BAA11419).
{ECO:0000305}.
SEQUENCE 626 AA; 68230 MW; FB4A1AB7667D96F6 CRC64;
MPCVQAQYSP SPPGSSYAAQ TYSSEYTTEI MNPDYTKLTM DLGSTEITAT ATTSLPSIST
FVEGYSSNYE LKPSCVYQMQ RPLIKVEEGR APSYHHHHHH HHHHHHHHQQ QHQQPSIPPA
SSPEDEVLPS TSMYFKQSPP STPTTPAFPP QAGALWDEAL PSAPGCIAPG PLLDPPMKAV
PTVAGARFPL FHFKPSPPHP PAPSPAGGHH LGYDPTAAAA LSLPLGAAAA AGSQAAALES
HPYGLPLAKR AAPLAFPPLG LTPSPTASSL LGESPSLPSP PSRSSSSGEG TCAVCGDNAA
CQHYGVRTCE GCKGFFKRTV QKNAKYVCLA NKNCPVDKRR RNRCQYCRFQ KCLSVGMVKE
VVRTDSLKGR RGRLPSKPKS PLQQEPSQPS PPSPPICMMN ALVRALTDST PRDLDYSRYC
PTDQAAAGTD AEHVQQFYNL LTASIDVSRS WAEKIPGFTD LPKEDQTLLI ESAFLELFVL
RLSIRSNTAE DKFVFCNGLV LHRLQCLRGF GEWLDSIKDF SLNLQSLNLD IQALACLSAL
SMITERHGLK EPKRVEELCN KITSSLKDHQ SKGQALEPTE SKVLGALVEL RKICTLGLQR
IFYLKLEDLV SPPSIIDKLF LDTLPF


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