NR4A2_HUMAN
ID NR4A2_HUMAN Reviewed; 598 AA.
AC P43354; Q16311; Q53RZ2; Q6NXU0;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 220.
DE RecName: Full=Nuclear receptor subfamily 4 group A member 2;
DE AltName: Full=Immediate-early response protein NOT;
DE AltName: Full=Orphan nuclear receptor NURR1;
DE AltName: Full=Transcriptionally-inducible nuclear receptor;
GN Name=NR4A2; Synonyms=NOT, NURR1, TINUR;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Blood;
RX PubMed=7877627; DOI=10.1210/mend.8.11.7877627;
RA Mages H.W., Rilke O., Bravo R., Senger G., Kroczek R.A.;
RT "NOT, a human immediate-early response gene closely related to the
RT steroid/thyroid hormone receptor NAK1/TR3.";
RL Mol. Endocrinol. 8:1583-1591(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Fibroblast;
RX PubMed=10216262; DOI=10.1016/s0378-1119(99)00065-7;
RA Ichinose H., Ohye T., Suzuki T., Sumi-Ichinose C., Nomura T., Hagino Y.,
RA Nagatsu T.;
RT "Molecular cloning of the human Nurr1 gene: characterization of the human
RT gene and cDNAs.";
RL Gene 230:233-239(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10216261; DOI=10.1016/s0378-1119(99)00064-5;
RA Torii T., Kawarai T., Nakamura S., Kawakami H.;
RT "Organization of the human orphan nuclear receptor Nurr1 gene.";
RL Gene 230:225-232(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Skin, and Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 59-598 (ISOFORM 1).
RX PubMed=7706727;
RA Okabe T., Takayanagi R., Imasaki K., Haji M., Nawata H., Watanabe T.;
RT "cDNA cloning of a NGFI-B/nur77-related transcription factor from an
RT apoptotic human T cell line.";
RL J. Immunol. 154:3871-3879(1995).
RN [9]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=17184956; DOI=10.1016/j.ijdevneu.2006.11.003;
RA Messmer K., Remington M.P., Skidmore F., Fishman P.S.;
RT "Induction of tyrosine hydroxylase expression by the transcription factor
RT Pitx3.";
RL Int. J. Dev. Neurosci. 25:29-37(2007).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [11]
RP SUBCELLULAR LOCATION, NUCLEAR LOCALIZATION SIGNALS, AND NUCLEAR EXPORT
RP SEQUENCES.
RX PubMed=23283970; DOI=10.1074/jbc.m112.439190;
RA Garcia-Yague A.J., Rada P., Rojo A.I., Lastres-Becker I., Cuadrado A.;
RT "Nuclear import and export signals control the subcellular localization of
RT Nurr1 protein in response to oxidative stress.";
RL J. Biol. Chem. 288:5506-5517(2013).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 328-598.
RX PubMed=12774125; DOI=10.1038/nature01645;
RA Wang Z., Benoit G., Liu J., Prasad S., Aarnisalo P., Liu X., Xu H.,
RA Walker N.P., Perlmann T.;
RT "Structure and function of Nurr1 identifies a class of ligand-independent
RT nuclear receptors.";
RL Nature 423:555-560(2003).
CC -!- FUNCTION: Transcriptional regulator which is important for the
CC differentiation and maintenance of meso-diencephalic dopaminergic
CC (mdDA) neurons during development. It is crucial for expression of a
CC set of genes such as SLC6A3, SLC18A2, TH and DRD2 which are essential
CC for development of mdDA neurons (By similarity). {ECO:0000250,
CC ECO:0000269|PubMed:17184956}.
CC -!- SUBUNIT: Interacts with SFPQ, NCOR2, SIN3A and HADC1. The interaction
CC with NCOR2 increases in the absence of PITX3. Interacts with PER2 (By
CC similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC P43354; P05067: APP; NbExp=3; IntAct=EBI-2681738, EBI-77613;
CC P43354; P55273: CDKN2D; NbExp=4; IntAct=EBI-2681738, EBI-745859;
CC P43354; Q5T2S8: ODAD2; NbExp=3; IntAct=EBI-2681738, EBI-12200605;
CC P43354; Q5H9L2: TCEAL5; NbExp=2; IntAct=EBI-2681738, EBI-2681773;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Mostly nuclear;
CC oxidative stress promotes cytoplasmic localization.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P43354-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P43354-2; Sequence=VSP_056057;
CC -!- TISSUE SPECIFICITY: Expressed in a number of cell lines of T-cell, B-
CC cell and fibroblast origin. Strong expression in brain tissue.
CC -!- DEVELOPMENTAL STAGE: Rapidly and only very transiently expressed after
CC cell activation, during the G0-G1 transition of the cell cycle.
CC -!- DOMAIN: the ligand-binding domain (LBD) contains no cavity as a result
CC of the tight packing of side chains from several bulky hydrophobic
CC residues in the region normally occupied by ligands. NR4A2 lacks a
CC 'classical' binding site for coactivators (PubMed:12774125).
CC {ECO:0000269|PubMed:12774125}.
CC -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR4
CC subfamily. {ECO:0000305}.
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DR EMBL; X75918; CAA53518.1; -; mRNA.
DR EMBL; AB017586; BAA75666.1; -; Genomic_DNA.
DR EMBL; AB019433; BAA77328.1; -; Genomic_DNA.
DR EMBL; AK291456; BAF84145.1; -; mRNA.
DR EMBL; AC074099; AAY24203.1; -; Genomic_DNA.
DR EMBL; CH471058; EAX11454.1; -; Genomic_DNA.
DR EMBL; CH471058; EAX11455.1; -; Genomic_DNA.
DR EMBL; BC009288; AAH09288.1; -; mRNA.
DR EMBL; BC066890; AAH66890.1; -; mRNA.
DR EMBL; S77154; AAB33999.1; -; mRNA.
DR CCDS; CCDS2201.1; -. [P43354-1]
DR CCDS; CCDS86887.1; -. [P43354-2]
DR PIR; A57040; A57040.
DR RefSeq; NP_006177.1; NM_006186.3. [P43354-1]
DR RefSeq; XP_005246679.1; XM_005246622.3.
DR RefSeq; XP_016859708.1; XM_017004219.1. [P43354-1]
DR PDB; 1OVL; X-ray; 2.20 A; A/B/C/D/E/F=328-598.
DR PDB; 5Y41; X-ray; 2.05 A; A/B=328-598.
DR PDB; 5YD6; X-ray; 2.34 A; A/B/C/D=328-598.
DR PDB; 6DDA; X-ray; 3.20 A; A/B/C=328-598.
DR PDB; 6L6L; X-ray; 2.78 A; A/B=262-346.
DR PDB; 6L6Q; X-ray; 2.60 A; A/B=262-346.
DR PDBsum; 1OVL; -.
DR PDBsum; 5Y41; -.
DR PDBsum; 5YD6; -.
DR PDBsum; 6DDA; -.
DR PDBsum; 6L6L; -.
DR PDBsum; 6L6Q; -.
DR AlphaFoldDB; P43354; -.
DR BMRB; P43354; -.
DR SMR; P43354; -.
DR BioGRID; 110983; 20.
DR IntAct; P43354; 18.
DR STRING; 9606.ENSP00000344479; -.
DR BindingDB; P43354; -.
DR ChEMBL; CHEMBL5002; -.
DR iPTMnet; P43354; -.
DR PhosphoSitePlus; P43354; -.
DR SwissPalm; P43354; -.
DR BioMuta; NR4A2; -.
DR DMDM; 1171750; -.
DR jPOST; P43354; -.
DR MassIVE; P43354; -.
DR MaxQB; P43354; -.
DR PaxDb; P43354; -.
DR PeptideAtlas; P43354; -.
DR PRIDE; P43354; -.
DR ProteomicsDB; 55616; -. [P43354-1]
DR ProteomicsDB; 66777; -.
DR Antibodypedia; 621; 424 antibodies from 40 providers.
DR DNASU; 4929; -.
DR Ensembl; ENST00000339562.9; ENSP00000344479.4; ENSG00000153234.15. [P43354-1]
DR Ensembl; ENST00000409572.5; ENSP00000386747.1; ENSG00000153234.15. [P43354-1]
DR Ensembl; ENST00000426264.5; ENSP00000389986.1; ENSG00000153234.15. [P43354-2]
DR GeneID; 4929; -.
DR KEGG; hsa:4929; -.
DR MANE-Select; ENST00000339562.9; ENSP00000344479.4; NM_006186.4; NP_006177.1.
DR UCSC; uc002tyx.5; human. [P43354-1]
DR CTD; 4929; -.
DR DisGeNET; 4929; -.
DR GeneCards; NR4A2; -.
DR HGNC; HGNC:7981; NR4A2.
DR HPA; ENSG00000153234; Tissue enhanced (adrenal gland, bone marrow, ovary).
DR MalaCards; NR4A2; -.
DR MIM; 601828; gene.
DR neXtProt; NX_P43354; -.
DR OpenTargets; ENSG00000153234; -.
DR PharmGKB; PA31762; -.
DR VEuPathDB; HostDB:ENSG00000153234; -.
DR eggNOG; KOG4217; Eukaryota.
DR GeneTree; ENSGT00950000183038; -.
DR HOGENOM; CLU_007368_14_2_1; -.
DR InParanoid; P43354; -.
DR OMA; HAAGEYS; -.
DR OrthoDB; 454476at2759; -.
DR PhylomeDB; P43354; -.
DR TreeFam; TF315430; -.
DR PathwayCommons; P43354; -.
DR Reactome; R-HSA-383280; Nuclear Receptor transcription pathway.
DR Reactome; R-HSA-4090294; SUMOylation of intracellular receptors.
DR SignaLink; P43354; -.
DR SIGNOR; P43354; -.
DR BioGRID-ORCS; 4929; 16 hits in 1097 CRISPR screens.
DR ChiTaRS; NR4A2; human.
DR EvolutionaryTrace; P43354; -.
DR GeneWiki; Nuclear_receptor_related-1_protein; -.
DR GenomeRNAi; 4929; -.
DR Pharos; P43354; Tchem.
DR PRO; PR:P43354; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; P43354; protein.
DR Bgee; ENSG00000153234; Expressed in mucosa of paranasal sinus and 193 other tissues.
DR ExpressionAtlas; P43354; baseline and differential.
DR Genevisible; P43354; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016607; C:nuclear speck; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; TAS:ParkinsonsUK-UCL.
DR GO; GO:0005667; C:transcription regulator complex; IBA:GO_Central.
DR GO; GO:0008013; F:beta-catenin binding; TAS:ParkinsonsUK-UCL.
DR GO; GO:0003677; F:DNA binding; TAS:ParkinsonsUK-UCL.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISS:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR GO; GO:0035259; F:nuclear glucocorticoid receptor binding; IBA:GO_Central.
DR GO; GO:0004879; F:nuclear receptor activity; TAS:ParkinsonsUK-UCL.
DR GO; GO:0046965; F:nuclear retinoid X receptor binding; TAS:ParkinsonsUK-UCL.
DR GO; GO:0046982; F:protein heterodimerization activity; ISS:UniProtKB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0008344; P:adult locomotory behavior; IEA:Ensembl.
DR GO; GO:0060070; P:canonical Wnt signaling pathway; TAS:ParkinsonsUK-UCL.
DR GO; GO:0071376; P:cellular response to corticotropin-releasing hormone stimulus; ISS:UniProtKB.
DR GO; GO:0031668; P:cellular response to extracellular stimulus; IDA:MGI.
DR GO; GO:0034599; P:cellular response to oxidative stress; IEA:Ensembl.
DR GO; GO:0021953; P:central nervous system neuron differentiation; IBA:GO_Central.
DR GO; GO:0021952; P:central nervous system projection neuron axonogenesis; IEA:Ensembl.
DR GO; GO:0042416; P:dopamine biosynthetic process; IEA:Ensembl.
DR GO; GO:0071542; P:dopaminergic neuron differentiation; ISS:UniProtKB.
DR GO; GO:0045444; P:fat cell differentiation; ISS:UniProtKB.
DR GO; GO:0051866; P:general adaptation syndrome; IEA:Ensembl.
DR GO; GO:0021986; P:habenula development; IEA:Ensembl.
DR GO; GO:1904948; P:midbrain dopaminergic neuron differentiation; TAS:ParkinsonsUK-UCL.
DR GO; GO:2001234; P:negative regulation of apoptotic signaling pathway; IMP:ParkinsonsUK-UCL.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; IEA:Ensembl.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:ParkinsonsUK-UCL.
DR GO; GO:0051402; P:neuron apoptotic process; IEA:Ensembl.
DR GO; GO:0042551; P:neuron maturation; IEA:Ensembl.
DR GO; GO:0001764; P:neuron migration; TAS:ParkinsonsUK-UCL.
DR GO; GO:0043085; P:positive regulation of catalytic activity; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0009791; P:post-embryonic development; IEA:Ensembl.
DR GO; GO:0042053; P:regulation of dopamine metabolic process; IEA:Ensembl.
DR GO; GO:0043576; P:regulation of respiratory gaseous exchange; IEA:Ensembl.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0001975; P:response to amphetamine; IEA:Ensembl.
DR GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
DR GO; GO:0007165; P:signal transduction; NAS:ProtInc.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0006351; P:transcription, DNA-templated; IDA:UniProtKB.
DR Gene3D; 1.10.565.10; -; 1.
DR Gene3D; 3.30.50.10; -; 1.
DR InterPro; IPR035500; NHR-like_dom_sf.
DR InterPro; IPR003070; Nuc_orph_rcpt.
DR InterPro; IPR000536; Nucl_hrmn_rcpt_lig-bd.
DR InterPro; IPR001723; Nuclear_hrmn_rcpt.
DR InterPro; IPR003073; NURR_rcpt.
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; PR01284; NUCLEARECPTR.
DR PRINTS; PR01287; NURRNUCRCPTR.
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 3D-structure; Alternative splicing; Cytoplasm; DNA-binding; Metal-binding;
KW Nucleus; Receptor; Reference proteome; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..598
FT /note="Nuclear receptor subfamily 4 group A member 2"
FT /id="PRO_0000053718"
FT DOMAIN 360..595
FT /note="NR LBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
FT DNA_BIND 260..335
FT /note="Nuclear receptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 263..283
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 299..323
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 337..361
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 287..314
FT /note="Bipartite nuclear localization signal (NLS1)"
FT MOTIF 338..350
FT /note="Nuclear localization signal (NLS1)"
FT /evidence="ECO:0000269|PubMed:23283970"
FT MOTIF 443..452
FT /note="nuclear export sequence (NES1)"
FT MOTIF 568..577
FT /note="nuclear export sequence (NES2)"
FT VAR_SEQ 1..63
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_056057"
FT CONFLICT 465
FT /note="C -> W (in Ref. 8; AAB33999)"
FT /evidence="ECO:0000305"
FT CONFLICT 468
FT /note="V -> W (in Ref. 8; AAB33999)"
FT /evidence="ECO:0000305"
FT TURN 264..266
FT /evidence="ECO:0007829|PDB:6L6Q"
FT STRAND 271..274
FT /evidence="ECO:0007829|PDB:6L6Q"
FT HELIX 281..292
FT /evidence="ECO:0007829|PDB:6L6Q"
FT STRAND 300..303
FT /evidence="ECO:0007829|PDB:6L6Q"
FT TURN 310..313
FT /evidence="ECO:0007829|PDB:6L6Q"
FT HELIX 316..326
FT /evidence="ECO:0007829|PDB:6L6Q"
FT HELIX 330..332
FT /evidence="ECO:0007829|PDB:6L6Q"
FT HELIX 338..341
FT /evidence="ECO:0007829|PDB:1OVL"
FT HELIX 364..373
FT /evidence="ECO:0007829|PDB:5Y41"
FT HELIX 379..381
FT /evidence="ECO:0007829|PDB:5Y41"
FT HELIX 392..394
FT /evidence="ECO:0007829|PDB:1OVL"
FT HELIX 400..422
FT /evidence="ECO:0007829|PDB:5Y41"
FT TURN 425..429
FT /evidence="ECO:0007829|PDB:5Y41"
FT HELIX 432..454
FT /evidence="ECO:0007829|PDB:5Y41"
FT HELIX 457..459
FT /evidence="ECO:0007829|PDB:5Y41"
FT STRAND 461..463
FT /evidence="ECO:0007829|PDB:5Y41"
FT STRAND 467..471
FT /evidence="ECO:0007829|PDB:5Y41"
FT HELIX 472..479
FT /evidence="ECO:0007829|PDB:5Y41"
FT HELIX 482..494
FT /evidence="ECO:0007829|PDB:5Y41"
FT HELIX 500..511
FT /evidence="ECO:0007829|PDB:5Y41"
FT HELIX 521..542
FT /evidence="ECO:0007829|PDB:5Y41"
FT TURN 543..545
FT /evidence="ECO:0007829|PDB:5Y41"
FT HELIX 549..556
FT /evidence="ECO:0007829|PDB:5Y41"
FT HELIX 558..579
FT /evidence="ECO:0007829|PDB:5Y41"
FT HELIX 586..595
FT /evidence="ECO:0007829|PDB:5Y41"
SQ SEQUENCE 598 AA; 66591 MW; 28D8199AACE3E211 CRC64;
MPCVQAQYGS SPQGASPASQ SYSYHSSGEY SSDFLTPEFV KFSMDLTNTE ITATTSLPSF
STFMDNYSTG YDVKPPCLYQ MPLSGQQSSI KVEDIQMHNY QQHSHLPPQS EEMMPHSGSV
YYKPSSPPTP TTPGFQVQHS PMWDDPGSLH NFHQNYVATT HMIEQRKTPV SRLSLFSFKQ
SPPGTPVSSC QMRFDGPLHV PMNPEPAGSH HVVDGQTFAV PNPIRKPASM GFPGLQIGHA
SQLLDTQVPS PPSRGSPSNE GLCAVCGDNA ACQHYGVRTC EGCKGFFKRT VQKNAKYVCL
ANKNCPVDKR RRNRCQYCRF QKCLAVGMVK EVVRTDSLKG RRGRLPSKPK SPQEPSPPSP
PVSLISALVR AHVDSNPAMT SLDYSRFQAN PDYQMSGDDT QHIQQFYDLL TGSMEIIRGW
AEKIPGFADL PKADQDLLFE SAFLELFVLR LAYRSNPVEG KLIFCNGVVL HRLQCVRGFG
EWIDSIVEFS SNLQNMNIDI SAFSCIAALA MVTERHGLKE PKRVEELQNK IVNCLKDHVT
FNNGGLNRPN YLSKLLGKLP ELRTLCTQGL QRIFYLKLED LVPPPAIIDK LFLDTLPF
