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COUP transcription factor 2 (COUP-TF2) (Apolipoprotein A-I regulatory protein 1) (ARP-1) (COUP transcription factor II) (COUP-TF II) (Nuclear receptor subfamily 2 group F member 2)

 COT2_HUMAN              Reviewed;         414 AA.
P24468; B4DQJ2; B6ZGU1; Q03754; Q3KQR7;
01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
01-MAR-1992, sequence version 1.
22-NOV-2017, entry version 182.
RecName: Full=COUP transcription factor 2;
Short=COUP-TF2;
AltName: Full=Apolipoprotein A-I regulatory protein 1;
Short=ARP-1;
AltName: Full=COUP transcription factor II;
Short=COUP-TF II;
AltName: Full=Nuclear receptor subfamily 2 group F member 2;
Name=NR2F2; Synonyms=ARP1, TFCOUP2;
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 1), FUNCTION, AND SUBUNIT.
PubMed=1899293; DOI=10.1126/science.1899293;
Ladias J.A.A., Karathanasis S.K.;
"Regulation of the apolipoprotein AI gene by ARP-1, a novel member of
the steroid receptor superfamily.";
Science 251:561-565(1991).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Speckmayer R.W.M., Paulweber B., Sandhofer F.;
Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND DNA-BINDING.
PubMed=18619963; DOI=10.1016/j.febslet.2008.07.003;
Kobayashi T., Kodani Y., Nozawa A., Endo Y., Sawasaki T.;
"DNA-binding profiling of human hormone nuclear receptors via
fluorescence correlation spectroscopy in a cell-free system.";
FEBS Lett. 582:2737-2744(2008).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
TISSUE=Liver;
Schote A.B., Bechet T., Pirrotte P., Turner J.D., Muller C.P.;
"Characterisation of a new, DNA binding domain deficient chicken
ovalbumin upstream promoter- transcription factor IIdelta isoform in
the human brain.";
Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
TISSUE=Mammary gland;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
TISSUE=Kidney;
Kaighin V.A., Martin A.L., Aronstam R.S.;
"Isolation of cDNA coding for multiple human nuclear receptor
clones.";
Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16572171; DOI=10.1038/nature04601;
Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R.,
Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G.,
Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A.,
Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W.,
Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X.,
Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K.,
Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S.,
Nusbaum C.;
"Analysis of the DNA sequence and duplication history of human
chromosome 15.";
Nature 440:671-675(2006).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Brain, Kidney, and Spleen;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[10]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-351 (ISOFORM 1).
PubMed=1820218;
Wang L.H., Ing N.H., Tsai S.Y., O'Malley B.W., Tsai M.J.;
"The COUP-TFs compose a family of functionally related transcription
factors.";
Gene Expr. 1:207-216(1991).
[11]
FUNCTION.
PubMed=9343308; DOI=10.1677/jme.0.0190163;
Chu K., Zingg H.H.;
"The nuclear orphan receptors COUP-TFII and Ear-2 act as silencers of
the human oxytocin gene promoter.";
J. Mol. Endocrinol. 19:163-172(1997).
[12]
SUBUNIT, AND INTERACTION WITH NR2F6.
PubMed=10318855; DOI=10.1074/jbc.274.20.14331;
Avram D., Ishmael J.E., Nevrivy D.J., Peterson V.J., Lee S.H.,
Dowell P., Leid M.;
"Heterodimeric interactions between chicken ovalbumin upstream
promoter-transcription factor family members ARP1 and ear2.";
J. Biol. Chem. 274:14331-14336(1999).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-51, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[15]
X-RAY CRYSTALLOGRAPHY (1.48 ANGSTROMS) OF 175-414, FUNCTION, SUBUNIT,
INTERACTION WITH NCOA1; NCOA2; NCOA3 AND PPARGC1A, AND MUTAGENESIS OF
ARG-228; TRP-249; SER-250; 253-PHE-VAL-254; 260-LEU-LEU-270;
364-LEU-LEU-365 AND ASP-398.
PubMed=18798693; DOI=10.1371/journal.pbio.0060227;
Kruse S.W., Suino-Powell K., Zhou X.E., Kretschman J.E., Reynolds R.,
Vonrhein C., Xu Y., Wang L., Tsai S.Y., Tsai M.J., Xu H.E.;
"Identification of COUP-TFII orphan nuclear receptor as a retinoic
acid-activated receptor.";
PLoS Biol. 6:E227-E227(2008).
[16]
VARIANTS CHTD4 GLN-75 INS; VAL-170; ILE-205; ASP-251; TYR-341 AND
SER-412, AND CHARACTERIZATION OF VARIANTS CHTD4 GLN-75 INS; ILE-205
AND TYR-341.
PubMed=24702954; DOI=10.1016/j.ajhg.2014.03.007;
UK10K Consortium;
Al Turki S., Manickaraj A.K., Mercer C.L., Gerety S.S., Hitz M.P.,
Lindsay S., D'Alessandro L.C., Swaminathan G.J., Bentham J.,
Arndt A.K., Low J., Breckpot J., Gewillig M., Thienpont B.,
Abdul-Khaliq H., Harnack C., Hoff K., Kramer H.H., Schubert S.,
Siebert R., Toka O., Cosgrove C., Watkins H., Lucassen A.M.,
O'Kelly I.M., Salmon A.P., Bu'lock F.A., Granados-Riveron J.,
Setchfield K., Thornborough C., Brook J.D., Mulder B., Klaassen S.,
Bhattacharya S., Devriendt K., Fitzpatrick D.F., Wilson D.I.,
Mital S., Hurles M.E.;
"Rare variants in NR2F2 cause congenital heart defects in humans.";
Am. J. Hum. Genet. 94:574-585(2014).
-!- FUNCTION: Ligand-activated transcription factor. Activated by high
concentrations of 9-cis-retinoic acid and all-trans-retinoic acid,
but not by dexamethasone, cortisol or progesterone (in vitro).
Regulation of the apolipoprotein A-I gene transcription. Binds to
DNA site A. {ECO:0000269|PubMed:18798693,
ECO:0000269|PubMed:1899293, ECO:0000269|PubMed:9343308}.
-!- SUBUNIT: Interacts with SQSTM1 (By similarity). Binds DNA as a
dimer; homodimer or heterodimer with NR2F6. Interacts with NCOA1,
NCOA2, NCOA3 and PPARGC1A. Interacts with ZFPM2 (By similarity).
{ECO:0000250}.
-!- INTERACTION:
Q13485:SMAD4; NbExp=4; IntAct=EBI-2795198, EBI-347263;
-!- SUBCELLULAR LOCATION: Nucleus.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=P24468-1; Sequence=Displayed;
Name=2;
IsoId=P24468-2; Sequence=VSP_042630;
Name=3;
IsoId=P24468-3; Sequence=VSP_043897;
-!- TISSUE SPECIFICITY: Ubiquitous.
-!- DISEASE: Congenital heart defects, multiple types, 4 (CHTD4)
[MIM:615779]: A disorder characterized by congenital developmental
abnormalities involving structures of the heart. Common defects
include transposition of the great arteries, aortic stenosis,
atrial septal defect, ventricular septal defect, pulmonic
stenosis, and patent ductus arteriosus. Some patients also have
cardiac arrhythmias, which may be due to the anatomic defect
itself or to surgical interventions.
{ECO:0000269|PubMed:24702954}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR2
subfamily. {ECO:0000305}.
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EMBL; M64497; AAA86429.1; -; mRNA.
EMBL; U60477; AAB09475.1; -; Genomic_DNA.
EMBL; AB307711; BAH02302.1; -; mRNA.
EMBL; FM208183; CAR63888.1; -; mRNA.
EMBL; AK298824; BAG60954.1; -; mRNA.
EMBL; AK301595; BAG63083.1; -; mRNA.
EMBL; AK316086; BAH14457.1; -; mRNA.
EMBL; HQ692849; ADZ17360.1; -; mRNA.
EMBL; HQ692850; ADZ17361.1; -; mRNA.
EMBL; AC016251; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471101; EAX02195.1; -; Genomic_DNA.
EMBL; CH471101; EAX02196.1; -; Genomic_DNA.
EMBL; CH471101; EAX02197.1; -; Genomic_DNA.
EMBL; BC014664; AAH14664.1; -; mRNA.
EMBL; BC042897; AAH42897.1; -; mRNA.
EMBL; BC106083; AAI06084.1; -; mRNA.
EMBL; M62760; AAA21479.1; -; mRNA.
CCDS; CCDS10375.1; -. [P24468-1]
CCDS; CCDS45358.1; -. [P24468-2]
CCDS; CCDS45359.1; -. [P24468-3]
PIR; A37133; A37133.
RefSeq; NP_001138627.1; NM_001145155.1. [P24468-2]
RefSeq; NP_001138628.1; NM_001145156.1. [P24468-3]
RefSeq; NP_001138629.1; NM_001145157.1. [P24468-3]
RefSeq; NP_066285.1; NM_021005.3. [P24468-1]
UniGene; Hs.347991; -.
PDB; 3CJW; X-ray; 1.48 A; A=175-414.
PDBsum; 3CJW; -.
ProteinModelPortal; P24468; -.
SMR; P24468; -.
BioGrid; 112884; 70.
CORUM; P24468; -.
DIP; DIP-29713N; -.
IntAct; P24468; 15.
MINT; MINT-1183332; -.
STRING; 9606.ENSP00000377721; -.
BindingDB; P24468; -.
ChEMBL; CHEMBL1961790; -.
iPTMnet; P24468; -.
PhosphoSitePlus; P24468; -.
BioMuta; NR2F2; -.
DMDM; 114203; -.
EPD; P24468; -.
MaxQB; P24468; -.
PaxDb; P24468; -.
PeptideAtlas; P24468; -.
PRIDE; P24468; -.
Ensembl; ENST00000394166; ENSP00000377721; ENSG00000185551. [P24468-1]
Ensembl; ENST00000394171; ENSP00000377726; ENSG00000185551. [P24468-3]
Ensembl; ENST00000421109; ENSP00000401674; ENSG00000185551. [P24468-2]
Ensembl; ENST00000453270; ENSP00000389853; ENSG00000185551. [P24468-3]
GeneID; 7026; -.
KEGG; hsa:7026; -.
UCSC; uc002btp.4; human. [P24468-1]
CTD; 7026; -.
DisGeNET; 7026; -.
EuPathDB; HostDB:ENSG00000185551.12; -.
GeneCards; NR2F2; -.
HGNC; HGNC:7976; NR2F2.
MalaCards; NR2F2; -.
MIM; 107773; gene.
MIM; 615779; phenotype.
neXtProt; NX_P24468; -.
OpenTargets; ENSG00000185551; -.
Orphanet; 1329; Complete atrioventricular canal.
Orphanet; 1330; Partial atrioventricular canal.
PharmGKB; PA31759; -.
eggNOG; KOG3575; Eukaryota.
eggNOG; ENOG410XRZC; LUCA.
GeneTree; ENSGT00760000118948; -.
HOGENOM; HOG000260820; -.
HOVERGEN; HBG005606; -.
InParanoid; P24468; -.
KO; K08548; -.
OMA; GNQGTQP; -.
OrthoDB; EOG091G0YX6; -.
PhylomeDB; P24468; -.
TreeFam; TF352097; -.
Reactome; R-HSA-381340; Transcriptional regulation of white adipocyte differentiation.
SignaLink; P24468; -.
SIGNOR; P24468; -.
ChiTaRS; NR2F2; human.
EvolutionaryTrace; P24468; -.
GeneWiki; COUP-TFII; -.
GenomeRNAi; 7026; -.
PRO; PR:P24468; -.
Proteomes; UP000005640; Chromosome 15.
Bgee; ENSG00000185551; -.
CleanEx; HS_NR2F2; -.
ExpressionAtlas; P24468; baseline and differential.
Genevisible; P24468; HS.
GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
GO; GO:0004879; F:nuclear receptor activity; IDA:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
GO; GO:0001972; F:retinoic acid binding; IDA:UniProtKB.
GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
GO; GO:0003707; F:steroid hormone receptor activity; IEA:InterPro.
GO; GO:0003714; F:transcription corepressor activity; TAS:ProtInc.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IDA:UniProtKB.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0009952; P:anterior/posterior pattern specification; IEA:Ensembl.
GO; GO:0048514; P:blood vessel morphogenesis; IEA:Ensembl.
GO; GO:0009566; P:fertilization; IEA:Ensembl.
GO; GO:0030900; P:forebrain development; IEA:Ensembl.
GO; GO:0060173; P:limb development; IEA:Ensembl.
GO; GO:0006629; P:lipid metabolic process; TAS:ProtInc.
GO; GO:0001893; P:maternal placenta development; IEA:Ensembl.
GO; GO:0045736; P:negative regulation of cyclin-dependent protein serine/threonine kinase activity; IDA:BHF-UCL.
GO; GO:0010596; P:negative regulation of endothelial cell migration; IMP:BHF-UCL.
GO; GO:0001937; P:negative regulation of endothelial cell proliferation; IMP:BHF-UCL.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:BHF-UCL.
GO; GO:0001764; P:neuron migration; IEA:Ensembl.
GO; GO:0060674; P:placenta blood vessel development; IEA:Ensembl.
GO; GO:0003084; P:positive regulation of systemic arterial blood pressure; IEA:Ensembl.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0009956; P:radial pattern formation; IEA:Ensembl.
GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; TAS:ProtInc.
GO; GO:0060849; P:regulation of transcription involved in lymphatic endothelial cell fate commitment; IMP:BHF-UCL.
GO; GO:0032355; P:response to estradiol; IEA:Ensembl.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
GO; GO:0007519; P:skeletal muscle tissue development; IEA:Ensembl.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0060707; P:trophoblast giant cell differentiation; IEA:Ensembl.
Gene3D; 1.10.565.10; -; 1.
Gene3D; 3.30.50.10; -; 1.
InterPro; IPR003068; COUP_TF.
InterPro; IPR035500; NHR_like_dom_sf.
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; PR01282; COUPTNFACTOR.
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;
3D-structure; Activator; Alternative splicing; Complete proteome;
Disease mutation; DNA-binding; Metal-binding; Nucleus; Phosphoprotein;
Receptor; Reference proteome; Transcription; Transcription regulation;
Zinc; Zinc-finger.
CHAIN 1 414 COUP transcription factor 2.
/FTId=PRO_0000053606.
DNA_BIND 76 151 Nuclear receptor. {ECO:0000255|PROSITE-
ProRule:PRU00407}.
ZN_FING 79 99 NR C4-type. {ECO:0000255|PROSITE-
ProRule:PRU00407}.
ZN_FING 115 139 NR C4-type. {ECO:0000255|PROSITE-
ProRule:PRU00407}.
REGION 117 414 Interaction with ZFPM2. {ECO:0000250}.
REGION 183 414 Ligand-binding. {ECO:0000250}.
REGION 337 414 Important for dimerization.
COMPBIAS 71 75 Poly-Gln.
MOD_RES 51 51 Phosphothreonine.
{ECO:0000244|PubMed:24275569}.
VAR_SEQ 1 153 Missing (in isoform 3).
{ECO:0000303|PubMed:14702039,
ECO:0000303|Ref.6}.
/FTId=VSP_043897.
VAR_SEQ 1 147 MAMVVSTWRDPQDEVPGSQGSQASQAPPVPGPPPGAPHTPQ
TPGQGGPASTPAQTAAGGQGGPGGPGSDKQQQQQHIECVVC
GDKSSGKHYGQFTCEGCKSFFKRSVRRNLSYTCRANRNCPI
DQHHRNQCQYCRLKKCLKVGMRRE -> MQAVWDLEQGKYG
F (in isoform 2).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334,
ECO:0000303|Ref.4, ECO:0000303|Ref.6}.
/FTId=VSP_042630.
VARIANT 75 75 Q -> QQ (in CHTD4; the mutation results
in reduced transcription activation of
the EGR1 promoter; does not affect
transcription activation of the APOB FT
promoter). {ECO:0000269|PubMed:24702954}.
/FTId=VAR_071766.
VARIANT 170 170 D -> V (in CHTD4).
{ECO:0000269|PubMed:24702954}.
/FTId=VAR_071767.
VARIANT 205 205 N -> I (in CHTD4; the mutation results in
increased transcription activation of the
EGR1 promoter; transcription activation
of the APOB promoter is decreased;
dbSNP:rs587777372).
{ECO:0000269|PubMed:24702954}.
/FTId=VAR_071768.
VARIANT 251 251 E -> D (in CHTD4).
{ECO:0000269|PubMed:24702954}.
/FTId=VAR_071769.
VARIANT 341 341 S -> Y (in CHTD4; the mutation results in
reduced transcriptional activity;
dbSNP:rs587777371).
{ECO:0000269|PubMed:24702954}.
/FTId=VAR_071770.
VARIANT 412 412 A -> S (in CHTD4; dbSNP:rs201527820).
{ECO:0000269|PubMed:24702954}.
/FTId=VAR_071771.
MUTAGEN 228 228 R->E: Reduces transcription activation by
40%; when associated with R-398.
{ECO:0000269|PubMed:18798693}.
MUTAGEN 249 249 W->A: Reduces transcription activation by
50%; when associated with A-250.
{ECO:0000269|PubMed:18798693}.
MUTAGEN 250 250 S->A: Reduces transcription activation by
50%; when associated with A-249.
{ECO:0000269|PubMed:18798693}.
MUTAGEN 250 250 S->W: Reduces transcription activation by
50%. {ECO:0000269|PubMed:18798693}.
MUTAGEN 253 254 FV->AA: Reduces transcription activation
by 50%. {ECO:0000269|PubMed:18798693}.
MUTAGEN 269 270 LL->AA: Reduces transcription activation
by 50%.
MUTAGEN 364 365 LL->AA: Reduces transcription activation
by 80%. {ECO:0000269|PubMed:18798693}.
MUTAGEN 398 398 D->R: Reduces transcription activation by
40%; when associated with E-228.
{ECO:0000269|PubMed:18798693}.
HELIX 175 187 {ECO:0000244|PDB:3CJW}.
HELIX 212 229 {ECO:0000244|PDB:3CJW}.
STRAND 230 232 {ECO:0000244|PDB:3CJW}.
HELIX 233 235 {ECO:0000244|PDB:3CJW}.
HELIX 238 260 {ECO:0000244|PDB:3CJW}.
HELIX 290 304 {ECO:0000244|PDB:3CJW}.
HELIX 309 320 {ECO:0000244|PDB:3CJW}.
HELIX 331 352 {ECO:0000244|PDB:3CJW}.
HELIX 359 364 {ECO:0000244|PDB:3CJW}.
HELIX 367 372 {ECO:0000244|PDB:3CJW}.
HELIX 375 382 {ECO:0000244|PDB:3CJW}.
HELIX 384 387 {ECO:0000244|PDB:3CJW}.
HELIX 392 394 {ECO:0000244|PDB:3CJW}.
HELIX 396 400 {ECO:0000244|PDB:3CJW}.
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


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