COT2_HUMAN
ID COT2_HUMAN Reviewed; 414 AA.
AC P24468; B4DQJ2; B6ZGU1; Q03754; Q3KQR7;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-1992, sequence version 1.
DT 03-AUG-2022, entry version 210.
DE RecName: Full=COUP transcription factor 2;
DE Short=COUP-TF2;
DE AltName: Full=Apolipoprotein A-I regulatory protein 1;
DE Short=ARP-1;
DE AltName: Full=COUP transcription factor II;
DE Short=COUP-TF II;
DE AltName: Full=Nuclear receptor subfamily 2 group F member 2;
GN Name=NR2F2; Synonyms=ARP1, TFCOUP2;
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), FUNCTION, AND SUBUNIT.
RX PubMed=1899293; DOI=10.1126/science.1899293;
RA Ladias J.A.A., Karathanasis S.K.;
RT "Regulation of the apolipoprotein AI gene by ARP-1, a novel member of the
RT steroid receptor superfamily.";
RL Science 251:561-565(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Speckmayer R.W.M., Paulweber B., Sandhofer F.;
RL Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND DNA-BINDING.
RX PubMed=18619963; DOI=10.1016/j.febslet.2008.07.003;
RA Kobayashi T., Kodani Y., Nozawa A., Endo Y., Sawasaki T.;
RT "DNA-binding profiling of human hormone nuclear receptors via fluorescence
RT correlation spectroscopy in a cell-free system.";
RL FEBS Lett. 582:2737-2744(2008).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Liver;
RA Schote A.B., Bechet T., Pirrotte P., Turner J.D., Muller C.P.;
RT "Characterisation of a new, DNA binding domain deficient chicken ovalbumin
RT upstream promoter- transcription factor IIdelta isoform in the human
RT brain.";
RL Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC TISSUE=Mammary gland;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC TISSUE=Kidney;
RA Kaighin V.A., Martin A.L., Aronstam R.S.;
RT "Isolation of cDNA coding for multiple human nuclear receptor clones.";
RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16572171; DOI=10.1038/nature04601;
RA Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J.,
RA Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E.,
RA Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B.,
RA Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R.,
RA O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B.,
RA Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S.,
RA Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.;
RT "Analysis of the DNA sequence and duplication history of human chromosome
RT 15.";
RL Nature 440:671-675(2006).
RN [8]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, Kidney, and Spleen;
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 [10]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-351 (ISOFORM 1).
RX PubMed=1820218;
RA Wang L.H., Ing N.H., Tsai S.Y., O'Malley B.W., Tsai M.J.;
RT "The COUP-TFs compose a family of functionally related transcription
RT factors.";
RL Gene Expr. 1:207-216(1991).
RN [11]
RP FUNCTION.
RX PubMed=9343308; DOI=10.1677/jme.0.0190163;
RA Chu K., Zingg H.H.;
RT "The nuclear orphan receptors COUP-TFII and Ear-2 act as silencers of the
RT human oxytocin gene promoter.";
RL J. Mol. Endocrinol. 19:163-172(1997).
RN [12]
RP SUBUNIT, AND INTERACTION WITH NR2F6.
RX PubMed=10318855; DOI=10.1074/jbc.274.20.14331;
RA Avram D., Ishmael J.E., Nevrivy D.J., Peterson V.J., Lee S.H., Dowell P.,
RA Leid M.;
RT "Heterodimeric interactions between chicken ovalbumin upstream promoter-
RT transcription factor family members ARP1 and ear2.";
RL J. Biol. Chem. 274:14331-14336(1999).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-51, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [15]
RP FUNCTION, TISSUE SPECIFICITY, AND INVOLVEMENT IN SRXX5.
RX PubMed=29478779; DOI=10.1016/j.ajhg.2018.01.021;
RA Bashamboo A., Eozenou C., Jorgensen A., Bignon-Topalovic J., Siffroi J.P.,
RA Hyon C., Tar A., Nagy P., Solyom J., Halasz Z., Paye-Jaouen A., Lambert S.,
RA Rodriguez-Buritica D., Bertalan R., Martinerie L., Rajpert-De Meyts E.,
RA Achermann J.C., McElreavey K.;
RT "Loss of function of the nuclear receptor NR2F2, encoding COUP-TF2, causes
RT testis development and cardiac defects in 46,XX children.";
RL Am. J. Hum. Genet. 102:487-493(2018).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (1.48 ANGSTROMS) OF 175-414, FUNCTION, SUBUNIT,
RP INTERACTION WITH NCOA1; NCOA2; NCOA3 AND PPARGC1A, AND MUTAGENESIS OF
RP ARG-228; TRP-249; SER-250; 253-PHE-VAL-254; 260-LEU-LEU-270;
RP 364-LEU-LEU-365 AND ASP-398.
RX PubMed=18798693; DOI=10.1371/journal.pbio.0060227;
RA Kruse S.W., Suino-Powell K., Zhou X.E., Kretschman J.E., Reynolds R.,
RA Vonrhein C., Xu Y., Wang L., Tsai S.Y., Tsai M.J., Xu H.E.;
RT "Identification of COUP-TFII orphan nuclear receptor as a retinoic acid-
RT activated receptor.";
RL PLoS Biol. 6:E227-E227(2008).
RN [17]
RP VARIANTS CHTD4 GLN-75 INS; VAL-170; ILE-205; ASP-251; TYR-341 AND SER-412,
RP AND CHARACTERIZATION OF VARIANTS CHTD4 GLN-75 INS; ILE-205 AND TYR-341.
RX PubMed=24702954; DOI=10.1016/j.ajhg.2014.03.007;
RG UK10K Consortium;
RA Al Turki S., Manickaraj A.K., Mercer C.L., Gerety S.S., Hitz M.P.,
RA Lindsay S., D'Alessandro L.C., Swaminathan G.J., Bentham J., Arndt A.K.,
RA Low J., Breckpot J., Gewillig M., Thienpont B., Abdul-Khaliq H.,
RA Harnack C., Hoff K., Kramer H.H., Schubert S., Siebert R., Toka O.,
RA Cosgrove C., Watkins H., Lucassen A.M., O'Kelly I.M., Salmon A.P.,
RA Bu'lock F.A., Granados-Riveron J., Setchfield K., Thornborough C.,
RA Brook J.D., Mulder B., Klaassen S., Bhattacharya S., Devriendt K.,
RA Fitzpatrick D.F., Wilson D.I., Mital S., Hurles M.E.;
RT "Rare variants in NR2F2 cause congenital heart defects in humans.";
RL Am. J. Hum. Genet. 94:574-585(2014).
CC -!- FUNCTION: Ligand-activated transcription factor. Activated by high
CC concentrations of 9-cis-retinoic acid and all-trans-retinoic acid, but
CC not by dexamethasone, cortisol or progesterone (in vitro). Regulation
CC of the apolipoprotein A-I gene transcription. Binds to DNA site A. May
CC be required to establish ovary identity during early gonad development
CC (PubMed:29478779). {ECO:0000269|PubMed:18798693,
CC ECO:0000269|PubMed:1899293, ECO:0000269|PubMed:29478779,
CC ECO:0000269|PubMed:9343308}.
CC -!- SUBUNIT: Interacts with SQSTM1 (By similarity). Binds DNA as a dimer;
CC homodimer or heterodimer with NR2F6. Interacts with NCOA1, NCOA2, NCOA3
CC and PPARGC1A. Interacts with ZFPM2 (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC P24468; Q13485: SMAD4; NbExp=4; IntAct=EBI-2795198, EBI-347263;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=P24468-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P24468-2; Sequence=VSP_042630;
CC Name=3;
CC IsoId=P24468-3; Sequence=VSP_043897;
CC -!- TISSUE SPECIFICITY: Ubiquitous. Expressed in the stromal cells of
CC developing fetal ovaries (PubMed:29478779).
CC {ECO:0000269|PubMed:29478779}.
CC -!- DISEASE: Congenital heart defects, multiple types, 4 (CHTD4)
CC [MIM:615779]: A disorder characterized by congenital developmental
CC abnormalities involving structures of the heart. Common defects include
CC transposition of the great arteries, aortic stenosis, atrial septal
CC defect, ventricular septal defect, pulmonic stenosis, and patent ductus
CC arteriosus. Some patients also have cardiac arrhythmias, which may be
CC due to the anatomic defect itself or to surgical interventions.
CC {ECO:0000269|PubMed:24702954}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: 46,XX sex reversal 5 (SRXX5) [MIM:618901]: A condition in
CC which male gonads develop in a genetic female (female to male sex
CC reversal). Additional features in SRXX5 patients are congenital heart
CC disease, congenital diaphragmatic hernia, and blepharophimosis-ptosis-
CC epicanthus inversus syndrome. SRXX5 inheritance is autosomal dominant.
CC {ECO:0000269|PubMed:29478779}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR2
CC subfamily. {ECO:0000305}.
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DR EMBL; M64497; AAA86429.1; -; mRNA.
DR EMBL; U60477; AAB09475.1; -; Genomic_DNA.
DR EMBL; AB307711; BAH02302.1; -; mRNA.
DR EMBL; FM208183; CAR63888.1; -; mRNA.
DR EMBL; AK298824; BAG60954.1; -; mRNA.
DR EMBL; AK301595; BAG63083.1; -; mRNA.
DR EMBL; AK316086; BAH14457.1; -; mRNA.
DR EMBL; HQ692849; ADZ17360.1; -; mRNA.
DR EMBL; HQ692850; ADZ17361.1; -; mRNA.
DR EMBL; AC016251; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471101; EAX02195.1; -; Genomic_DNA.
DR EMBL; CH471101; EAX02196.1; -; Genomic_DNA.
DR EMBL; CH471101; EAX02197.1; -; Genomic_DNA.
DR EMBL; BC014664; AAH14664.1; -; mRNA.
DR EMBL; BC042897; AAH42897.1; -; mRNA.
DR EMBL; BC106083; AAI06084.1; -; mRNA.
DR EMBL; M62760; AAA21479.1; -; mRNA.
DR CCDS; CCDS10375.1; -. [P24468-1]
DR CCDS; CCDS45358.1; -. [P24468-2]
DR CCDS; CCDS45359.1; -. [P24468-3]
DR PIR; A37133; A37133.
DR RefSeq; NP_001138627.1; NM_001145155.1. [P24468-2]
DR RefSeq; NP_001138628.1; NM_001145156.1. [P24468-3]
DR RefSeq; NP_001138629.1; NM_001145157.1. [P24468-3]
DR RefSeq; NP_066285.1; NM_021005.3. [P24468-1]
DR PDB; 3CJW; X-ray; 1.48 A; A=175-414.
DR PDBsum; 3CJW; -.
DR AlphaFoldDB; P24468; -.
DR SMR; P24468; -.
DR BioGRID; 112884; 121.
DR CORUM; P24468; -.
DR DIP; DIP-29713N; -.
DR IntAct; P24468; 53.
DR MINT; P24468; -.
DR STRING; 9606.ENSP00000377721; -.
DR BindingDB; P24468; -.
DR ChEMBL; CHEMBL1961790; -.
DR iPTMnet; P24468; -.
DR PhosphoSitePlus; P24468; -.
DR BioMuta; NR2F2; -.
DR DMDM; 114203; -.
DR EPD; P24468; -.
DR jPOST; P24468; -.
DR MassIVE; P24468; -.
DR MaxQB; P24468; -.
DR PaxDb; P24468; -.
DR PeptideAtlas; P24468; -.
DR PRIDE; P24468; -.
DR ProteomicsDB; 54206; -. [P24468-1]
DR ProteomicsDB; 54207; -. [P24468-2]
DR ProteomicsDB; 54208; -. [P24468-3]
DR Antibodypedia; 16260; 331 antibodies from 34 providers.
DR DNASU; 7026; -.
DR Ensembl; ENST00000394166.8; ENSP00000377721.3; ENSG00000185551.15. [P24468-1]
DR Ensembl; ENST00000394171.6; ENSP00000377726.2; ENSG00000185551.15. [P24468-3]
DR Ensembl; ENST00000421109.6; ENSP00000401674.2; ENSG00000185551.15. [P24468-2]
DR Ensembl; ENST00000453270.2; ENSP00000389853.2; ENSG00000185551.15. [P24468-3]
DR GeneID; 7026; -.
DR KEGG; hsa:7026; -.
DR MANE-Select; ENST00000394166.8; ENSP00000377721.3; NM_021005.4; NP_066285.1.
DR UCSC; uc002btp.4; human. [P24468-1]
DR CTD; 7026; -.
DR DisGeNET; 7026; -.
DR GeneCards; NR2F2; -.
DR HGNC; HGNC:7976; NR2F2.
DR HPA; ENSG00000185551; Tissue enhanced (ovary).
DR MalaCards; NR2F2; -.
DR MIM; 107773; gene.
DR MIM; 615779; phenotype.
DR MIM; 618901; phenotype.
DR neXtProt; NX_P24468; -.
DR OpenTargets; ENSG00000185551; -.
DR Orphanet; 99067; Complete atrioventricular septal defect with ventricular hypoplasia.
DR Orphanet; 99068; Complete atrioventricular septal defect-tetralogy of Fallot.
DR PharmGKB; PA31759; -.
DR VEuPathDB; HostDB:ENSG00000185551; -.
DR eggNOG; KOG3575; Eukaryota.
DR GeneTree; ENSGT00940000157540; -.
DR HOGENOM; CLU_007368_20_1_1; -.
DR InParanoid; P24468; -.
DR OMA; NWPYMST; -.
DR OrthoDB; 666130at2759; -.
DR PhylomeDB; P24468; -.
DR TreeFam; TF352097; -.
DR PathwayCommons; P24468; -.
DR Reactome; R-HSA-381340; Transcriptional regulation of white adipocyte differentiation.
DR SignaLink; P24468; -.
DR SIGNOR; P24468; -.
DR BioGRID-ORCS; 7026; 40 hits in 1105 CRISPR screens.
DR ChiTaRS; NR2F2; human.
DR EvolutionaryTrace; P24468; -.
DR GeneWiki; COUP-TFII; -.
DR GenomeRNAi; 7026; -.
DR Pharos; P24468; Tchem.
DR PRO; PR:P24468; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; P24468; protein.
DR Bgee; ENSG00000185551; Expressed in urethra and 214 other tissues.
DR ExpressionAtlas; P24468; baseline and differential.
DR Genevisible; P24468; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:UniProtKB.
DR GO; GO:0004879; F:nuclear receptor activity; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
DR GO; GO:0001972; F:retinoic acid binding; IDA:UniProtKB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0048856; P:anatomical structure development; IBA:GO_Central.
DR GO; GO:0009952; P:anterior/posterior pattern specification; IEA:Ensembl.
DR GO; GO:0048514; P:blood vessel morphogenesis; IEA:Ensembl.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0008585; P:female gonad development; IMP:UniProtKB.
DR GO; GO:0009566; P:fertilization; IEA:Ensembl.
DR GO; GO:0030900; P:forebrain development; IEA:Ensembl.
DR GO; GO:1904936; P:interneuron migration; IEA:Ensembl.
DR GO; GO:0060838; P:lymphatic endothelial cell fate commitment; IMP:BHF-UCL.
DR GO; GO:0001893; P:maternal placenta development; IEA:Ensembl.
DR GO; GO:0045736; P:negative regulation of cyclin-dependent protein serine/threonine kinase activity; IDA:BHF-UCL.
DR GO; GO:0010596; P:negative regulation of endothelial cell migration; IMP:BHF-UCL.
DR GO; GO:0001937; P:negative regulation of endothelial cell proliferation; IMP:BHF-UCL.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:BHF-UCL.
DR GO; GO:0060674; P:placenta blood vessel development; IEA:Ensembl.
DR GO; GO:0003084; P:positive regulation of systemic arterial blood pressure; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:BHF-UCL.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0009956; P:radial pattern formation; IEA:Ensembl.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0032355; P:response to estradiol; IEA:Ensembl.
DR GO; GO:0007519; P:skeletal muscle tissue development; IEA:Ensembl.
DR GO; GO:0060707; P:trophoblast giant cell differentiation; IEA:Ensembl.
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; IPR001628; Znf_hrmn_rcpt.
DR InterPro; IPR013088; Znf_NHR/GATA.
DR Pfam; PF00104; Hormone_recep; 1.
DR Pfam; PF00105; zf-C4; 1.
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; Activator; Alternative splicing; Disease variant;
KW DNA-binding; Metal-binding; Nucleus; Phosphoprotein; Receptor;
KW Reference proteome; Transcription; Transcription regulation; Zinc;
KW Zinc-finger.
FT CHAIN 1..414
FT /note="COUP transcription factor 2"
FT /id="PRO_0000053606"
FT DOMAIN 177..403
FT /note="NR LBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
FT DNA_BIND 76..151
FT /note="Nuclear receptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 79..99
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 115..139
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT REGION 1..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 117..414
FT /note="Interaction with ZFPM2"
FT /evidence="ECO:0000250"
FT REGION 337..414
FT /note="Important for dimerization"
FT COMPBIAS 26..41
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 43..57
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 51
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT VAR_SEQ 1..153
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039, ECO:0000303|Ref.6"
FT /id="VSP_043897"
FT VAR_SEQ 1..147
FT /note="MAMVVSTWRDPQDEVPGSQGSQASQAPPVPGPPPGAPHTPQTPGQGGPASTP
FT AQTAAGGQGGPGGPGSDKQQQQQHIECVVCGDKSSGKHYGQFTCEGCKSFFKRSVRRNL
FT SYTCRANRNCPIDQHHRNQCQYCRLKKCLKVGMRRE -> MQAVWDLEQGKYGF (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|Ref.4,
FT ECO:0000303|Ref.6"
FT /id="VSP_042630"
FT VARIANT 75
FT /note="Q -> QQ (in CHTD4; the mutation results in reduced
FT transcription activation of the EGR1 promoter; does not
FT affect transcription activation of the APOB FT promoter)"
FT /evidence="ECO:0000269|PubMed:24702954"
FT /id="VAR_071766"
FT VARIANT 170
FT /note="D -> V (in CHTD4)"
FT /evidence="ECO:0000269|PubMed:24702954"
FT /id="VAR_071767"
FT VARIANT 205
FT /note="N -> I (in CHTD4; the mutation results in increased
FT transcription activation of the EGR1 promoter;
FT transcription activation of the APOB promoter is decreased;
FT dbSNP:rs587777372)"
FT /evidence="ECO:0000269|PubMed:24702954"
FT /id="VAR_071768"
FT VARIANT 251
FT /note="E -> D (in CHTD4)"
FT /evidence="ECO:0000269|PubMed:24702954"
FT /id="VAR_071769"
FT VARIANT 341
FT /note="S -> Y (in CHTD4; the mutation results in reduced
FT transcriptional activity; dbSNP:rs587777371)"
FT /evidence="ECO:0000269|PubMed:24702954"
FT /id="VAR_071770"
FT VARIANT 412
FT /note="A -> S (in CHTD4; dbSNP:rs201527820)"
FT /evidence="ECO:0000269|PubMed:24702954"
FT /id="VAR_071771"
FT MUTAGEN 228
FT /note="R->E: Reduces transcription activation by 40%; when
FT associated with R-398."
FT /evidence="ECO:0000269|PubMed:18798693"
FT MUTAGEN 249
FT /note="W->A: Reduces transcription activation by 50%; when
FT associated with A-250."
FT /evidence="ECO:0000269|PubMed:18798693"
FT MUTAGEN 250
FT /note="S->A: Reduces transcription activation by 50%; when
FT associated with A-249."
FT /evidence="ECO:0000269|PubMed:18798693"
FT MUTAGEN 250
FT /note="S->W: Reduces transcription activation by 50%."
FT /evidence="ECO:0000269|PubMed:18798693"
FT MUTAGEN 253..254
FT /note="FV->AA: Reduces transcription activation by 50%."
FT /evidence="ECO:0000269|PubMed:18798693"
FT MUTAGEN 269..270
FT /note="LL->AA: Reduces transcription activation by 50%."
FT MUTAGEN 364..365
FT /note="LL->AA: Reduces transcription activation by 80%."
FT /evidence="ECO:0000269|PubMed:18798693"
FT MUTAGEN 398
FT /note="D->R: Reduces transcription activation by 40%; when
FT associated with E-228."
FT /evidence="ECO:0000269|PubMed:18798693"
FT HELIX 175..187
FT /evidence="ECO:0007829|PDB:3CJW"
FT HELIX 212..229
FT /evidence="ECO:0007829|PDB:3CJW"
FT STRAND 230..232
FT /evidence="ECO:0007829|PDB:3CJW"
FT HELIX 233..235
FT /evidence="ECO:0007829|PDB:3CJW"
FT HELIX 238..260
FT /evidence="ECO:0007829|PDB:3CJW"
FT HELIX 290..304
FT /evidence="ECO:0007829|PDB:3CJW"
FT HELIX 309..320
FT /evidence="ECO:0007829|PDB:3CJW"
FT HELIX 331..352
FT /evidence="ECO:0007829|PDB:3CJW"
FT HELIX 359..364
FT /evidence="ECO:0007829|PDB:3CJW"
FT HELIX 367..372
FT /evidence="ECO:0007829|PDB:3CJW"
FT HELIX 375..382
FT /evidence="ECO:0007829|PDB:3CJW"
FT HELIX 384..387
FT /evidence="ECO:0007829|PDB:3CJW"
FT HELIX 392..394
FT /evidence="ECO:0007829|PDB:3CJW"
FT HELIX 396..400
FT /evidence="ECO:0007829|PDB:3CJW"
SQ SEQUENCE 414 AA; 45571 MW; C24CB2E8C8A27E8C CRC64;
MAMVVSTWRD PQDEVPGSQG SQASQAPPVP GPPPGAPHTP QTPGQGGPAS TPAQTAAGGQ
GGPGGPGSDK QQQQQHIECV VCGDKSSGKH YGQFTCEGCK SFFKRSVRRN LSYTCRANRN
CPIDQHHRNQ CQYCRLKKCL KVGMRREAVQ RGRMPPTQPT HGQFALTNGD PLNCHSYLSG
YISLLLRAEP YPTSRFGSQC MQPNNIMGIE NICELAARML FSAVEWARNI PFFPDLQITD
QVALLRLTWS ELFVLNAAQC SMPLHVAPLL AAAGLHASPM SADRVVAFMD HIRIFQEQVE
KLKALHVDSA EYSCLKAIVL FTSDACGLSD VAHVESLQEK SQCALEEYVR SQYPNQPTRF
GKLLLRLPSL RTVSSSVIEQ LFFVRLVGKT PIETLIRDML LSGSSFNWPY MAIQ
