ARNT_MOUSE
ID ARNT_MOUSE Reviewed; 791 AA.
AC P53762; Q60661; Q921F3;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=Aryl hydrocarbon receptor nuclear translocator;
DE Short=ARNT protein;
DE AltName: Full=Dioxin receptor, nuclear translocator;
DE AltName: Full=Hypoxia-inducible factor 1-beta;
DE Short=HIF-1-beta;
DE Short=HIF1-beta;
GN Name=Arnt;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
RC STRAIN=C57BL/6J; TISSUE=Liver;
RX PubMed=8065341; DOI=10.1128/mcb.14.9.6075-6086.1994;
RA Reisz-Porszasz S., Probst M.R., Fukunaga B.N., Hankinson O.;
RT "Identification of functional domains of the aryl hydrocarbon receptor
RT nuclear translocator protein (ARNT).";
RL Mol. Cell. Biol. 14:6075-6086(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT).
RC STRAIN=C57BL/6J;
RX PubMed=7961746; DOI=10.1016/s0021-9258(18)46900-1;
RA Li H., Dong L., Whitlock J.P. Jr.;
RT "Transcriptional activation function of the mouse Ah receptor nuclear
RT translocator.";
RL J. Biol. Chem. 269:28098-28105(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 [6]
RP INTERACTION WITH AHRR.
RX PubMed=9887096; DOI=10.1101/gad.13.1.20;
RA Mimura J., Ema M., Sogawa K., Fujii-Kuriyama Y.;
RT "Identification of a novel mechanism of regulation of Ah (dioxin) receptor
RT function.";
RL Genes Dev. 13:20-25(1999).
RN [7]
RP INTERACTION WITH TACC3.
RX PubMed=11025203; DOI=10.1016/s0925-4773(00)00415-9;
RA Sadek C.M., Jalaguier S., Feeney E.P., Aitola M., Damdimopoulos A.E.,
RA Pelto-Huikko M., Gustafsson J.-A.;
RT "Isolation and characterization of AINT: a novel ARNT interacting protein
RT expressed during murine embryonic development.";
RL Mech. Dev. 97:13-26(2000).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-77, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [9]
RP INTERACTION WITH AHR, MUTAGENESIS OF LEU-167; ILE-168 AND ALA-171, AND
RP REGION.
RX PubMed=24001774; DOI=10.1128/mcb.00698-13;
RA Wu D., Potluri N., Kim Y., Rastinejad F.;
RT "Structure and dimerization properties of the aryl hydrocarbon receptor
RT PAS-A domain.";
RL Mol. Cell. Biol. 33:4346-4356(2013).
RN [10] {ECO:0007744|PDB:4ZP4, ECO:0007744|PDB:4ZPH, ECO:0007744|PDB:4ZPK, ECO:0007744|PDB:4ZPR, ECO:0007744|PDB:4ZQD}
RP X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 81-464 IN COMPLEXES WITH EPAS1;
RP HIF1A; INHIBITOR AND DNA, MUTAGENESIS OF HIS-94; GLU-98; ARG-102; LEU-112;
RP LEU-132; VAL-136; LEU-167; ILE-168; ALA-171; ILE-264; ARG-266; VAL-305;
RP HIS-307; ARG-366; ASN-448 AND TYR-456, REGION, INTERACTION WITH EPAS1 AND
RP HIF1A, AND FUNCTION.
RX PubMed=26245371; DOI=10.1038/nature14883;
RA Wu D., Potluri N., Lu J., Kim Y., Rastinejad F.;
RT "Structural integration in hypoxia-inducible factors.";
RL Nature 524:303-308(2015).
RN [11] {ECO:0007744|PDB:5SY5, ECO:0007744|PDB:5SY7}
RP X-RAY CRYSTALLOGRAPHY (3.20 ANGSTROMS) OF 81-464 IN COMPLEXES WITH NPAS1;
RP NPAS3 AND DNA, MUTAGENESIS OF LEU-112; LEU-132; VAL-136; LEU-167; ILE-168;
RP ALA-171; ILE-264; ARG-266; VAL-305; HIS-307; ARG-366; ASN-448 AND TYR-456,
RP INTERACTION WITH NPAS1; NPAS3; SIM1; NPAS4 AND AHR, AND FUNCTION.
RX PubMed=27782878; DOI=10.7554/elife.18790;
RA Wu D., Su X., Potluri N., Kim Y., Rastinejad F.;
RT "NPAS1-ARNT and NPAS3-ARNT crystal structures implicate the bHLH-PAS family
RT as multi-ligand binding transcription factors.";
RL Elife 5:0-0(2016).
RN [12] {ECO:0007744|PDB:5NJ8}
RP X-RAY CRYSTALLOGRAPHY (3.30 ANGSTROMS) OF 84-345 IN COMPLEXES WITH AHR AND
RP DNA, SUBUNIT, INTERACTION WITH AHR, MUTAGENESIS OF ARG-102; LEU-112;
RP MET-139 AND LEU-164, FUNCTION, AND REGION.
RX PubMed=28602820; DOI=10.1016/j.str.2017.05.008;
RA Schulte K.W., Green E., Wilz A., Platten M., Daumke O.;
RT "Structural Basis for Aryl Hydrocarbon Receptor-Mediated Gene Activation.";
RL Structure 25:1025-1033(2017).
CC -!- FUNCTION: Required for activity of the Ah (dioxin) receptor. This
CC protein is required for the ligand-binding subunit to translocate from
CC the cytosol to the nucleus after ligand binding. The complex then
CC initiates transcription of genes involved in the activation of PAH
CC procarcinogens (By similarity). The heterodimer binds to core DNA
CC sequence 5'-TACGTG-3' within the hypoxia response element (HRE) of
CC target gene promoters and functions as a transcriptional regulator of
CC the adaptive response to hypoxia (PubMed:26245371, PubMed:27782878).
CC The heterodimer ARNT:AHR binds to core DNA sequence 5'-TGCGTG-3' within
CC the dioxin response element (DRE) of target gene promoters and
CC activates their transcription (PubMed:28602820). {ECO:0000250,
CC ECO:0000269|PubMed:26245371, ECO:0000269|PubMed:27782878,
CC ECO:0000269|PubMed:28602820}.
CC -!- SUBUNIT: Monomer (PubMed:28602820). Homodimer only upon binding to a
CC DNA (PubMed:26245371, PubMed:28602820). Efficient DNA binding requires
CC dimerization with another bHLH protein (By similarity). Interacts with
CC TACC3 (PubMed:11025203). Interacts with HIF1A, EPAS1, NPAS1 and NPAS3;
CC forms a heterodimer that binds core DNA sequence 5'-TACGTG-3' within
CC the hypoxia response element (HRE) of target gene promoters
CC (PubMed:26245371, PubMed:27782878). Forms a heterodimer with AHRR, as
CC well as with other bHLH proteins (PubMed:9887096). Interacts with NOCA7
CC (By similarity). Interacts with AHR; the heterodimer ARNT:AHR binds to
CC core DNA sequence 5'-TGCGTG-3' within the dioxin response element (DRE)
CC of target gene promoters and activates their transcription
CC (PubMed:28602820, PubMed:24001774, PubMed:27782878). Interacts with
CC SIM1 and NPAS4 (PubMed:27782878). {ECO:0000250,
CC ECO:0000250|UniProtKB:P27540, ECO:0000269|PubMed:11025203,
CC ECO:0000269|PubMed:24001774, ECO:0000269|PubMed:26245371,
CC ECO:0000269|PubMed:27782878, ECO:0000269|PubMed:28602820,
CC ECO:0000269|PubMed:9887096}.
CC -!- INTERACTION:
CC P53762; P97481: Epas1; NbExp=5; IntAct=EBI-78852, EBI-15704570;
CC P53762; Q61221-1: Hif1a; NbExp=5; IntAct=EBI-78852, EBI-8549331;
CC P53762; Q61045: Sim1; NbExp=4; IntAct=EBI-78852, EBI-78890;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Long;
CC IsoId=P53762-1; Sequence=Displayed;
CC Name=Short;
CC IsoId=P53762-2; Sequence=VSP_002093;
CC -!- TISSUE SPECIFICITY: Ubiquitous.
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DR EMBL; U10325; AAA56717.1; -; mRNA.
DR EMBL; U14333; AAA61732.1; -; mRNA.
DR EMBL; AK153355; BAE31928.1; -; mRNA.
DR EMBL; CH466620; EDL38816.1; -; Genomic_DNA.
DR EMBL; BC012870; AAH12870.1; -; mRNA.
DR CCDS; CCDS17614.1; -. [P53762-1]
DR PIR; A55448; A55448.
DR PIR; A56241; A56241.
DR RefSeq; NP_001032826.1; NM_001037737.2. [P53762-1]
DR PDB; 4ZP4; X-ray; 2.35 A; A/C=82-464.
DR PDB; 4ZPH; X-ray; 2.80 A; A/C=82-464.
DR PDB; 4ZPK; X-ray; 3.60 A; A=82-464.
DR PDB; 4ZPR; X-ray; 3.90 A; A=82-464.
DR PDB; 4ZQD; X-ray; 2.87 A; A/C=82-464.
DR PDB; 5NJ8; X-ray; 3.30 A; B/D=84-345.
DR PDB; 5SY5; X-ray; 3.20 A; A/C/E=82-464.
DR PDB; 5SY7; X-ray; 4.20 A; A=82-464.
DR PDB; 6E3S; X-ray; 3.00 A; A=81-464.
DR PDB; 6E3T; X-ray; 3.00 A; A=81-464.
DR PDB; 6E3U; X-ray; 2.85 A; A=81-464.
DR PDB; 7VNI; X-ray; 2.00 A; C/D=358-466.
DR PDBsum; 4ZP4; -.
DR PDBsum; 4ZPH; -.
DR PDBsum; 4ZPK; -.
DR PDBsum; 4ZPR; -.
DR PDBsum; 4ZQD; -.
DR PDBsum; 5NJ8; -.
DR PDBsum; 5SY5; -.
DR PDBsum; 5SY7; -.
DR PDBsum; 6E3S; -.
DR PDBsum; 6E3T; -.
DR PDBsum; 6E3U; -.
DR PDBsum; 7VNI; -.
DR AlphaFoldDB; P53762; -.
DR SMR; P53762; -.
DR BioGRID; 198205; 39.
DR CORUM; P53762; -.
DR DIP; DIP-280N; -.
DR IntAct; P53762; 10.
DR STRING; 10090.ENSMUSP00000099810; -.
DR iPTMnet; P53762; -.
DR PhosphoSitePlus; P53762; -.
DR EPD; P53762; -.
DR MaxQB; P53762; -.
DR PaxDb; P53762; -.
DR PRIDE; P53762; -.
DR ProteomicsDB; 281830; -. [P53762-1]
DR ProteomicsDB; 281831; -. [P53762-2]
DR Antibodypedia; 916; 703 antibodies from 43 providers.
DR DNASU; 11863; -.
DR Ensembl; ENSMUST00000102749; ENSMUSP00000099810; ENSMUSG00000015522. [P53762-1]
DR GeneID; 11863; -.
DR KEGG; mmu:11863; -.
DR UCSC; uc008qjr.2; mouse. [P53762-1]
DR CTD; 405; -.
DR MGI; MGI:88071; Arnt.
DR VEuPathDB; HostDB:ENSMUSG00000015522; -.
DR eggNOG; KOG3561; Eukaryota.
DR GeneTree; ENSGT00940000157585; -.
DR InParanoid; P53762; -.
DR OMA; VRRRFWG; -.
DR PhylomeDB; P53762; -.
DR TreeFam; TF319983; -.
DR Reactome; R-MMU-1234158; Regulation of gene expression by Hypoxia-inducible Factor.
DR Reactome; R-MMU-211945; Phase I - Functionalization of compounds.
DR Reactome; R-MMU-211976; Endogenous sterols.
DR Reactome; R-MMU-211981; Xenobiotics.
DR Reactome; R-MMU-8937144; Aryl hydrocarbon receptor signalling.
DR BioGRID-ORCS; 11863; 4 hits in 78 CRISPR screens.
DR ChiTaRS; Arnt; mouse.
DR PRO; PR:P53762; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; P53762; protein.
DR Bgee; ENSMUSG00000015522; Expressed in ascending aorta and 283 other tissues.
DR ExpressionAtlas; P53762; baseline and differential.
DR Genevisible; P53762; MM.
DR GO; GO:0034751; C:aryl hydrocarbon receptor complex; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0016604; C:nuclear body; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; ISO:MGI.
DR GO; GO:0005667; C:transcription regulator complex; IDA:MGI.
DR GO; GO:0017162; F:aryl hydrocarbon receptor binding; ISO:MGI.
DR GO; GO:0000987; F:cis-regulatory region sequence-specific DNA binding; ISO:MGI.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISO:MGI.
DR GO; GO:0004879; F:nuclear receptor activity; IMP:MGI.
DR GO; GO:0046982; F:protein heterodimerization activity; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IGI:MGI.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; ISO:MGI.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; IMP:MGI.
DR GO; GO:0001892; P:embryonic placenta development; IMP:MGI.
DR GO; GO:0046886; P:positive regulation of hormone biosynthetic process; ISO:MGI.
DR GO; GO:0033235; P:positive regulation of protein sumoylation; IDA:BHF-UCL.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IGI:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:MGI.
DR GO; GO:0010575; P:positive regulation of vascular endothelial growth factor production; ISO:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0043619; P:regulation of transcription from RNA polymerase II promoter in response to oxidative stress; ISO:MGI.
DR GO; GO:0001666; P:response to hypoxia; IDA:MGI.
DR GO; GO:0009636; P:response to toxic substance; TAS:MGI.
DR CDD; cd00130; PAS; 2.
DR Gene3D; 4.10.280.10; -; 1.
DR InterPro; IPR011598; bHLH_dom.
DR InterPro; IPR036638; HLH_DNA-bd_sf.
DR InterPro; IPR001067; Nuc_translocat.
DR InterPro; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013767; PAS_fold.
DR Pfam; PF00010; HLH; 1.
DR Pfam; PF00989; PAS; 1.
DR PRINTS; PR00785; NCTRNSLOCATR.
DR SMART; SM00353; HLH; 1.
DR SMART; SM00086; PAC; 1.
DR SMART; SM00091; PAS; 2.
DR SUPFAM; SSF47459; SSF47459; 1.
DR SUPFAM; SSF55785; SSF55785; 2.
DR TIGRFAMs; TIGR00229; sensory_box; 1.
DR PROSITE; PS50888; BHLH; 1.
DR PROSITE; PS50112; PAS; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Activator; Alternative splicing; DNA-binding;
KW Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Transcription; Transcription regulation; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P27540"
FT CHAIN 2..791
FT /note="Aryl hydrocarbon receptor nuclear translocator"
FT /id="PRO_0000127119"
FT DOMAIN 89..142
FT /note="bHLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT DOMAIN 161..235
FT /note="PAS 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT DOMAIN 349..419
FT /note="PAS 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT DOMAIN 424..467
FT /note="PAC"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 73..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 88..128
FT /note="DNA-binding"
FT /evidence="ECO:0000269|PubMed:26245371,
FT ECO:0000269|PubMed:28602820"
FT REGION 112..264
FT /note="Required for heterodimer formation with EPAS1"
FT /evidence="ECO:0000269|PubMed:26245371"
FT REGION 112..168
FT /note="Required for heterodimer formation with HIF1A"
FT /evidence="ECO:0000269|PubMed:26245371"
FT REGION 167..171
FT /note="Mediates the transcription activity and dimerization
FT of the AHR:ARNT complex"
FT /evidence="ECO:0000269|PubMed:24001774"
FT REGION 465..508
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 530..554
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 631..667
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 682..715
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 730..791
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 682..698
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 733..780
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P27540"
FT MOD_RES 77
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CROSSLNK 58
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P27540"
FT VAR_SEQ 77..100
FT /note="SDDEQSSADKERLARENHSEIERR -> TKFL (in isoform Short)"
FT /evidence="ECO:0000303|PubMed:7961746"
FT /id="VSP_002093"
FT MUTAGEN 94
FT /note="H->A: Reduces DNA binding."
FT /evidence="ECO:0000269|PubMed:26245371"
FT MUTAGEN 98
FT /note="E->A: Reduces DNA binding."
FT /evidence="ECO:0000269|PubMed:26245371"
FT MUTAGEN 102
FT /note="R->E: Reduces DNA binding. Decreases transcription
FT factor activity."
FT /evidence="ECO:0000269|PubMed:26245371,
FT ECO:0000269|PubMed:28602820"
FT MUTAGEN 112
FT /note="L->D: Interfers with transcription factor activity."
FT /evidence="ECO:0000269|PubMed:28602820"
FT MUTAGEN 112
FT /note="L->E: Impairs heterodimer formation with EPAS1.
FT Impairs heterodimer formation with HIF1A. Significantly
FT destabilizes ARNT?s heterodimeric interactions with both
FT NPAS1 and NPAS3. Compromises SIM1:ARNT heterodimer
FT stability. Compromise NPAS4:ARNT heterodimer stability.
FT Compromise AHR:ARNT heterodimer stability."
FT /evidence="ECO:0000269|PubMed:26245371,
FT ECO:0000269|PubMed:27782878"
FT MUTAGEN 132
FT /note="L->E: Impairs heterodimer formation with EPAS1.
FT Impairs heterodimer formation with HIF1A. Significantly
FT destabilizes ARNT?s heterodimeric interactions with both
FT NPAS1 and NPAS3. Compromises SIM1:ARNT heterodimer
FT stability. Compromise NPAS4:ARNT heterodimer stability.
FT Compromise AHR:ARNT heterodimer stability."
FT /evidence="ECO:0000269|PubMed:26245371,
FT ECO:0000269|PubMed:27782878"
FT MUTAGEN 136
FT /note="V->D: Impairs heterodimer formation with EPAS1.
FT Impairs heterodimer formation with HIF1A. Significantly
FT destabilizes ARNT?s heterodimeric interactions with both
FT NPAS1 and NPAS3. Compromises SIM1:ARNT heterodimer
FT stability. Compromise NPAS4:ARNT heterodimer stability.
FT Compromise AHR:ARNT heterodimer stability."
FT /evidence="ECO:0000269|PubMed:26245371,
FT ECO:0000269|PubMed:27782878"
FT MUTAGEN 139
FT /note="M->D: Interfers with transcription factor activity."
FT /evidence="ECO:0000269|PubMed:28602820"
FT MUTAGEN 164
FT /note="L->D: Does not affect transcription factor
FT activity."
FT /evidence="ECO:0000269|PubMed:28602820"
FT MUTAGEN 167
FT /note="L->E: Highly reduces transcription activity. Impairs
FT interaction with AHR. Impairs heterodimer formation with
FT EPAS1. Impairs heterodimer formation with HIF1A.
FT Significantly destabilizes ARNT?s heterodimeric
FT interactions with both NPAS1 and NPAS3. Compromises
FT SIM1:ARNT heterodimer stability. Compromise NPAS4:ARNT
FT heterodimer stability. Compromise AHR:ARNT heterodimer
FT stability."
FT /evidence="ECO:0000269|PubMed:24001774,
FT ECO:0000269|PubMed:26245371, ECO:0000269|PubMed:27782878"
FT MUTAGEN 168
FT /note="I->D: Highly reduces transcription activity. Impairs
FT interaction with AHR. Impairs heterodimer formation with
FT EPAS1. Impairs heterodimer formation with HIF1A.
FT Significantly destabilizes ARNT?s heterodimeric
FT interactions with both NPAS1 and NPAS3. Compromises
FT SIM1:ARNT heterodimer stability. Compromise NPAS4:ARNT
FT heterodimer stability. Compromise AHR:ARNT heterodimer
FT stability."
FT /evidence="ECO:0000269|PubMed:24001774,
FT ECO:0000269|PubMed:26245371, ECO:0000269|PubMed:27782878"
FT MUTAGEN 171
FT /note="A->D: Reduces transcription activity. Markedly
FT reduces interaction with AHR. Impairs heterodimer formation
FT with EPAS1. Markedly decreases heterodimer formation with
FT HIF1A. Significantly destabilizes ARNT?s heterodimeric
FT interactions with both NPAS1 and NPAS3. Compromises
FT SIM1:ARNT heterodimer stability. Compromise NPAS4:ARNT
FT heterodimer stability. Compromise AHR:ARNT heterodimer
FT stability."
FT /evidence="ECO:0000269|PubMed:24001774,
FT ECO:0000269|PubMed:26245371, ECO:0000269|PubMed:27782878"
FT MUTAGEN 264
FT /note="I->D: Impairs heterodimer formation with EPAS1.
FT Markedly decreases heterodimer formation with HIF1A.
FT Significantly destabilizes ARNT?s heterodimeric
FT interactions with both NPAS1 and NPAS3. Compromises
FT SIM1:ARNT heterodimer stability. Does not compromise
FT NPAS4:ARNT heterodimer stability. Does not compromise
FT AHR:ARNT heterodimer stability."
FT /evidence="ECO:0000269|PubMed:26245371,
FT ECO:0000269|PubMed:27782878"
FT MUTAGEN 266
FT /note="R->A: Markedly decreases heterodimer formation with
FT EPAS1. Decreases heterodimer formation with HIF1A.
FT Significantly destabilizes ARNT?s heterodimeric
FT interactions with both NPAS1 and NPAS3. Compromises
FT SIM1:ARNT heterodimer stability. Does not compromise
FT NPAS4:ARNT heterodimer stability. Does not compromise
FT AHR:ARNT heterodimer stability."
FT /evidence="ECO:0000269|PubMed:26245371,
FT ECO:0000269|PubMed:27782878"
FT MUTAGEN 305
FT /note="V->D: Markedly decreases heterodimer formation with
FT EPAS1. Markedly decreases heterodimer formation with HIF1A.
FT Significantly destabilizes ARNT?s heterodimeric
FT interactions with both NPAS1 and NPAS3. Compromises
FT SIM1:ARNT heterodimer stability. Does not compromise
FT NPAS4:ARNT heterodimer stability. Does not compromise
FT AHR:ARNT heterodimer stability."
FT /evidence="ECO:0000269|PubMed:26245371,
FT ECO:0000269|PubMed:27782878"
FT MUTAGEN 307
FT /note="H->A: Decreases heterodimer formation with EPAS1.
FT Decreases heterodimer formation with HIF1A. Significantly
FT destabilizes ARNT?s heterodimeric interactions with both
FT NPAS1 and NPAS3. Compromises SIM1:ARNT heterodimer
FT stability. Does not compromise NPAS4:ARNT heterodimer
FT stability. Does not compromise AHR:ARNT heterodimer
FT stability."
FT /evidence="ECO:0000269|PubMed:26245371,
FT ECO:0000269|PubMed:27782878"
FT MUTAGEN 366
FT /note="R->A: Markedly decreases heterodimer formation with
FT EPAS1. Markedly decreases heterodimer formation with HIF1A.
FT Impairs heterodimer formation with EPAS1; when associated
FT with N-448. Impairs heterodimer formation with HIF1A; when
FT associated with N-448. Significantly destabilizes ARNT?s
FT heterodimeric interactions with both NPAS1 and NPAS3.
FT Compromises SIM1:ARNT heterodimer stability. Does not
FT compromise NPAS4:ARNT heterodimer stability. Does not
FT compromise AHR:ARNT heterodimer stability."
FT /evidence="ECO:0000269|PubMed:26245371,
FT ECO:0000269|PubMed:27782878"
FT MUTAGEN 448
FT /note="N->A: Decreases heterodimer formation with EPAS1.
FT Decreases heterodimer formation with HIF1A. Impairs
FT heterodimer formation with EPAS1; when associated with A-
FT 366. Impairs heterodimer formation with HIF1A; when
FT associated with A-366. Significantly destabilizes ARNT?s
FT heterodimeric interactions with both NPAS1 and NPAS3.
FT Compromises SIM1:ARNT heterodimer stability. Does not
FT compromise NPAS4:ARNT heterodimer stability. Does not
FT compromise AHR:ARNT heterodimer stability."
FT /evidence="ECO:0000269|PubMed:26245371,
FT ECO:0000269|PubMed:27782878"
FT MUTAGEN 456
FT /note="Y->D: Decreases heterodimer formation with EPAS1.
FT Decreases heterodimer formation with HIF1A. Significantly
FT destabilizes ARNT?s heterodimeric interactions with both
FT NPAS1 and NPAS3. Compromises SIM1:ARNT heterodimer
FT stability. Does not compromise NPAS4:ARNT heterodimer
FT stability. Does not compromise AHR:ARNT heterodimer
FT stability."
FT /evidence="ECO:0000269|PubMed:26245371,
FT ECO:0000269|PubMed:27782878"
FT CONFLICT 411
FT /note="S -> T (in Ref. 2; AAA61732)"
FT /evidence="ECO:0000305"
FT CONFLICT 534
FT /note="A -> R (in Ref. 2; AAA61732)"
FT /evidence="ECO:0000305"
FT CONFLICT 644
FT /note="S -> T (in Ref. 1; AAA56717)"
FT /evidence="ECO:0000305"
FT CONFLICT 650
FT /note="A -> C (in Ref. 2; AAA61732)"
FT /evidence="ECO:0000305"
FT HELIX 99..115
FT /evidence="ECO:0007829|PDB:4ZP4"
FT HELIX 117..120
FT /evidence="ECO:0007829|PDB:4ZP4"
FT STRAND 122..124
FT /evidence="ECO:0007829|PDB:4ZP4"
FT HELIX 128..141
FT /evidence="ECO:0007829|PDB:4ZP4"
FT HELIX 161..172
FT /evidence="ECO:0007829|PDB:4ZP4"
FT STRAND 174..180
FT /evidence="ECO:0007829|PDB:4ZP4"
FT TURN 181..183
FT /evidence="ECO:0007829|PDB:4ZP4"
FT STRAND 185..189
FT /evidence="ECO:0007829|PDB:4ZP4"
FT HELIX 193..197
FT /evidence="ECO:0007829|PDB:4ZP4"
FT HELIX 201..204
FT /evidence="ECO:0007829|PDB:4ZP4"
FT STRAND 205..208
FT /evidence="ECO:0007829|PDB:6E3U"
FT HELIX 209..212
FT /evidence="ECO:0007829|PDB:4ZP4"
FT HELIX 215..217
FT /evidence="ECO:0007829|PDB:4ZP4"
FT HELIX 218..224
FT /evidence="ECO:0007829|PDB:4ZP4"
FT STRAND 260..268
FT /evidence="ECO:0007829|PDB:4ZP4"
FT STRAND 293..295
FT /evidence="ECO:0007829|PDB:5SY5"
FT STRAND 303..314
FT /evidence="ECO:0007829|PDB:4ZP4"
FT STRAND 335..342
FT /evidence="ECO:0007829|PDB:4ZP4"
FT STRAND 362..367
FT /evidence="ECO:0007829|PDB:4ZP4"
FT STRAND 371..376
FT /evidence="ECO:0007829|PDB:4ZP4"
FT HELIX 380..384
FT /evidence="ECO:0007829|PDB:4ZP4"
FT HELIX 388..391
FT /evidence="ECO:0007829|PDB:4ZP4"
FT HELIX 396..399
FT /evidence="ECO:0007829|PDB:4ZP4"
FT TURN 402..404
FT /evidence="ECO:0007829|PDB:4ZP4"
FT HELIX 405..417
FT /evidence="ECO:0007829|PDB:4ZP4"
FT TURN 418..420
FT /evidence="ECO:0007829|PDB:4ZP4"
FT STRAND 422..430
FT /evidence="ECO:0007829|PDB:4ZP4"
FT STRAND 436..447
FT /evidence="ECO:0007829|PDB:4ZP4"
FT TURN 449..451
FT /evidence="ECO:0007829|PDB:4ZP4"
FT STRAND 454..463
FT /evidence="ECO:0007829|PDB:4ZP4"
SQ SEQUENCE 791 AA; 86963 MW; BDEC0991CD57D402 CRC64;
MAATTANPEM TSDVPSLGPT IASGNPGPGI QGGGAVVQRA IKRRSGLDFD DEVEVNTKFL
RCDDDQMCND KERFARSDDE QSSADKERLA RENHSEIERR RRNKMTAYIT ELSDMVPTCS
ALARKPDKLT ILRMAVSHMK SLRGTGNTST DGSYKPSFLT DQELKHLILE AADGFLFIVS
CETGRVVYVS DSVTPVLNQP QSEWFGSTLY DQVHPDDVDK LREQLSTSEN ALTGRVLDLK
TGTVKKEGQQ SSMRMCMGSR RSFICRMRCG TSSVDPVSMN RLSFLRNRCR NGLGSVKEGE
PHFVVVHCTG YIKAWPPAGV SLPDDDPEAG QGSKFCLVAI GRLQVTSSPN CTDMSNICQP
TEFISRHNIE GIFTFVDHRC VATVGYQPQE LLGKNIVEFC HPEDQQLLRD SFQQVVKLKG
QVLSVMFRFR SKTREWLWMR TSSFTFQNPY SDEIEYIICT NTNVKNSSQE PRPTLSNTIP
RSQLGPTANL SLEMGTGQLP SRQQQQQHTE LDMVPGRDGL ASYNHSQVSV QPVASAGSEH
SKPLEKSEGL FAQDRDPRFP EIYPSITADQ SKGISSSTVP ATQQLFSQGS SFPPNPRPAE
NFRNSGLTPP VTIVQPSSSA GQILAQISRH SNPAQGSAPT WTSSSRPGFA AQQVPTQATA
KTRSSQFGVN NFQTSSSFSA MSLPGAPTAS SGTAAYPALP NRGSNFPPET GQTTGQFQAR
TAEGVGVWPQ WQGQQPHHRS SSSEQHVQQT QAQAPSQPEV FQEMLSMLGD QSNTYNNEEF
PDLTMFPPFS E
