ID ARNT2_MOUSE Reviewed; 712 AA. AC Q61324; Q7TQG2; Q8CHG9; DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. DT 06-FEB-2007, sequence version 2. DT 24-JAN-2024, entry version 179. DE RecName: Full=Aryl hydrocarbon receptor nuclear translocator 2; DE Short=ARNT protein 2; GN Name=Arnt2; Synonyms=Kiaa0307; 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 1). RC STRAIN=C57BL/6J; TISSUE=Embryo; RX PubMed=8657146; DOI=10.1128/mcb.16.4.1706; RA Hirose K., Morita M., Ema M., Mimura J., Hamada H., Fujii H., Saijo Y., RA Gotoh O., Sogawa K., Fujii-Kuriyama Y.; RT "cDNA cloning and tissue-specific expression of a novel basic helix-loop- RT helix/PAS factor (Arnt2) with close sequence similarity to the aryl RT hydrocarbon receptor nuclear translocator (Arnt)."; RL Mol. Cell. Biol. 16:1706-1713(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Brain; RX PubMed=12465718; DOI=10.1093/dnares/9.5.179; RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Hara Y., Nagase T., Ohara O., RA Koga H.; RT "Prediction of the coding sequences of mouse homologues of KIAA gene: I. RT The complete nucleotide sequences of 100 mouse KIAA-homologous cDNAs RT identified by screening of terminal sequences of cDNA clones randomly RT sampled from size-fractionated libraries."; RL DNA Res. 9:179-188(2002). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC STRAIN=C57BL/6J; TISSUE=Brain; 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 [4] 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 [5] RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-42, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain; RX PubMed=24129315; DOI=10.1074/mcp.o113.027870; RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M., RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V., RA Bedford M.T., Comb M.J.; RT "Immunoaffinity enrichment and mass spectrometry analysis of protein RT methylation."; RL Mol. Cell. Proteomics 13:372-387(2014). RN [6] RP INTERACTION WITH SIM1 AND NPAS4, AND MUTAGENESIS OF LEU-86; LEU-106; RP LEU-141; ALA-145; ILE-238; VAL-279; ARG-340 AND ASN-422. 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). CC -!- FUNCTION: Transcription factor that plays a role in the development of CC the hypothalamo-pituitary axis, postnatal brain growth, and visual and CC renal function. Specifically recognizes the xenobiotic response element CC (XRE). {ECO:0000250|UniProtKB:Q9HBZ2}. CC -!- SUBUNIT: Efficient DNA binding requires dimerization with another bHLH CC protein (By similarity). Heterodimer with NPAS4 or SIM1 CC (PubMed:27782878). Heterodimer with the aryl hydrocarbon receptor (AHR) CC or the SIM1 protein (By similarity). Interacts with TACC3 CC (PubMed:11025203). {ECO:0000250|UniProtKB:Q9HBZ2, CC ECO:0000269|PubMed:11025203, ECO:0000269|PubMed:27782878}. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9HBZ2, CC ECO:0000255|PROSITE-ProRule:PRU00981}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q61324-1; Sequence=Displayed; CC Name=2; CC IsoId=Q61324-2; Sequence=VSP_022689; CC -!- TISSUE SPECIFICITY: Restricted to adult brain and kidney. CC -!- SEQUENCE CAUTION: CC Sequence=BAC41409.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; D63644; BAA09799.1; -; mRNA. DR EMBL; AB093225; BAC41409.1; ALT_INIT; mRNA. DR EMBL; BC054546; AAH54546.1; -; mRNA. DR CCDS; CCDS59733.1; -. [Q61324-1] DR RefSeq; NP_031514.3; NM_007488.3. [Q61324-1] DR RefSeq; XP_006507303.1; XM_006507240.2. DR RefSeq; XP_006507305.1; XM_006507242.2. DR RefSeq; XP_011239957.1; XM_011241655.2. DR PDB; 7XI3; X-ray; 4.27 A; A=50-439. DR PDBsum; 7XI3; -. DR AlphaFoldDB; Q61324; -. DR SMR; Q61324; -. DR BioGRID; 198206; 25. DR IntAct; Q61324; 2. DR STRING; 10090.ENSMUSP00000082154; -. DR iPTMnet; Q61324; -. DR PhosphoSitePlus; Q61324; -. DR MaxQB; Q61324; -. DR PaxDb; 10090-ENSMUSP00000082154; -. DR PeptideAtlas; Q61324; -. DR ProteomicsDB; 283273; -. [Q61324-1] DR ProteomicsDB; 283274; -. [Q61324-2] DR Pumba; Q61324; -. DR Antibodypedia; 3911; 313 antibodies from 32 providers. DR DNASU; 11864; -. DR Ensembl; ENSMUST00000085077.5; ENSMUSP00000082154.4; ENSMUSG00000015709.10. [Q61324-1] DR Ensembl; ENSMUST00000208232.2; ENSMUSP00000146413.2; ENSMUSG00000015709.10. [Q61324-2] DR Ensembl; ENSMUST00000209133.2; ENSMUSP00000147129.2; ENSMUSG00000015709.10. [Q61324-2] DR GeneID; 11864; -. DR KEGG; mmu:11864; -. DR UCSC; uc009ief.2; mouse. [Q61324-1] DR AGR; MGI:107188; -. DR CTD; 9915; -. DR MGI; MGI:107188; Arnt2. DR VEuPathDB; HostDB:ENSMUSG00000015709; -. DR eggNOG; KOG3561; Eukaryota. DR GeneTree; ENSGT00940000158198; -. DR HOGENOM; CLU_011864_1_1_1; -. DR InParanoid; Q61324; -. DR OMA; RVRKDCY; -. DR OrthoDB; 2872674at2759; -. DR PhylomeDB; Q61324; -. DR TreeFam; TF319983; -. 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 Reactome; R-MMU-9768919; NPAS4 regulates expression of target genes. DR BioGRID-ORCS; 11864; 2 hits in 76 CRISPR screens. DR ChiTaRS; Arnt2; mouse. DR PRO; PR:Q61324; -. DR Proteomes; UP000000589; Chromosome 7. DR RNAct; Q61324; Protein. DR Bgee; ENSMUSG00000015709; Expressed in retrosplenial region and 228 other cell types or tissues. DR ExpressionAtlas; Q61324; baseline and differential. DR GO; GO:0034751; C:aryl hydrocarbon receptor complex; IBA:GO_Central. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0005654; C:nucleoplasm; ISO:MGI. DR GO; GO:0005634; C:nucleus; ISS:UniProtKB. DR GO; GO:0005667; C:transcription regulator complex; IDA:MGI. DR GO; GO:0017162; F:aryl hydrocarbon receptor binding; IPI:UniProtKB. DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:NTNU_SB. 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:0046982; F:protein heterodimerization activity; IDA: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; IDA:NTNU_SB. DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI. DR GO; GO:0007420; P:brain development; ISS:UniProtKB. DR GO; GO:0007417; P:central nervous system development; IMP:UniProtKB. DR GO; GO:0001701; P:in utero embryonic development; IEP:UniProtKB. DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI. DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:MGI. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; IDA:UniProtKB. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:NTNU_SB. DR GO; GO:0006355; P:regulation of DNA-templated transcription; ISO:MGI. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central. DR GO; GO:0001666; P:response to hypoxia; ISO:MGI. DR GO; GO:0009636; P:response to toxic substance; TAS:UniProtKB. DR GO; GO:0009410; P:response to xenobiotic stimulus; TAS:UniProtKB. DR GO; GO:0007165; P:signal transduction; NAS:UniProtKB. DR CDD; cd18947; bHLH-PAS_ARNT; 1. DR CDD; cd00130; PAS; 2. DR Gene3D; 4.10.280.10; Helix-loop-helix DNA-binding domain; 1. DR Gene3D; 3.30.450.20; PAS domain; 2. 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 NCBIfam; TIGR00229; sensory_box; 1. DR PANTHER; PTHR23042:SF6; ARYL HYDROCARBON RECEPTOR NUCLEAR TRANSLOCATOR 2; 1. DR PANTHER; PTHR23042; CIRCADIAN PROTEIN CLOCK/ARNT/BMAL/PAS; 1. DR Pfam; PF00010; HLH; 1. DR Pfam; PF00989; PAS; 1. DR Pfam; PF14598; PAS_11; 1. DR PRINTS; PR00785; NCTRNSLOCATR. DR SMART; SM00353; HLH; 1. DR SMART; SM00086; PAC; 1. DR SMART; SM00091; PAS; 2. DR SUPFAM; SSF47459; HLH, helix-loop-helix DNA-binding domain; 1. DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 2. DR PROSITE; PS50888; BHLH; 1. DR PROSITE; PS50112; PAS; 2. DR Genevisible; Q61324; MM. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; DNA-binding; Methylation; Nucleus; KW Reference proteome; Repeat; Transcription; Transcription regulation. FT CHAIN 1..712 FT /note="Aryl hydrocarbon receptor nuclear translocator 2" FT /id="PRO_0000127123" FT DOMAIN 63..116 FT /note="bHLH" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981" FT DOMAIN 134..209 FT /note="PAS 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00140" FT DOMAIN 323..393 FT /note="PAS 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00140" FT DOMAIN 398..441 FT /note="PAC" FT REGION 36..73 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 573..712 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 46..73 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 573..678 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 42 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0007744|PubMed:24129315" FT VAR_SEQ 1..11 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:12465718" FT /id="VSP_022689" FT MUTAGEN 86 FT /note="L->E: Compromises SIM1:ARNT2 heterodimer stability. FT Compromises NPAS4:ARNT2 heterodimer stability." FT /evidence="ECO:0000269|PubMed:27782878" FT MUTAGEN 106 FT /note="L->E: Compromises SIM1:ARNT2 heterodimer stability. FT Compromises NPAS4:ARNT2 heterodimer stability." FT /evidence="ECO:0000269|PubMed:27782878" FT MUTAGEN 141 FT /note="L->E: Compromises SIM1:ARNT2 heterodimer stability. FT Does not compromise NPAS4:ARNT2 heterodimer stability." FT /evidence="ECO:0000269|PubMed:27782878" FT MUTAGEN 145 FT /note="A->D: Compromises SIM1:ARNT2 heterodimer stability. FT Does not compromise NPAS4:ARNT2 heterodimer stability." FT /evidence="ECO:0000269|PubMed:27782878" FT MUTAGEN 238 FT /note="I->D: Compromises SIM1:ARNT2 heterodimer stability. FT Does not compromise NPAS4:ARNT2 heterodimer stability." FT /evidence="ECO:0000269|PubMed:27782878" FT MUTAGEN 279 FT /note="V->D: Compromises SIM1:ARNT2 heterodimer stability. FT Does not compromise NPAS4:ARNT2 heterodimer stability." FT /evidence="ECO:0000269|PubMed:27782878" FT MUTAGEN 340 FT /note="R->A: Compromises SIM1:ARNT2 heterodimer stability. FT Does not compromise NPAS4:ARNT2 heterodimer stability." FT /evidence="ECO:0000269|PubMed:27782878" FT MUTAGEN 422 FT /note="N->A: Compromises SIM1:ARNT2 heterodimer stability. FT Does not compromise NPAS4:ARNT2 heterodimer stability." FT /evidence="ECO:0000269|PubMed:27782878" FT CONFLICT 206 FT /note="M -> I (in Ref. 1; BAA09799)" FT /evidence="ECO:0000305" FT CONFLICT 432 FT /note="I -> T (in Ref. 3; AAH54546)" FT /evidence="ECO:0000305" SQ SEQUENCE 712 AA; 77902 MW; FACD27033F7F18DE CRC64; MATPAAVNPP EMASDIPGSV ALPVAPMAAT GQVRMAGAMP ARGGKRRSGM DFDDEDGEGP SKFSRENHSE IERRRRNKMT QYITELSDMV PTCSALARKP DKLTILRMAV SHMKSMRGTG NKSTDGAYKP SFLTEQELKH LILEAADGFL FVVAAETGRV IYVSDSVTPV LNQPQSEWFG STLYEQVHPD DVEKLREQLC TSENSMTGRI LDLKTGTVKK EGQQSSMRMC MGSRRSFICR MRCGNAPLDH LPLNRITTMR KRFRNGLGPV KEGEAQYAVV HCTGYIKAWP PAGMTIPEED ADVGQGSKYC LVAIGRLQVT SSPVCMDMSG MSVPTEFLSR HNSDGIITFV DPRCISVIGY QPQDLLGKDI LEFCHPEDQS HLRESFQQVV KLKGQVLSVM YRFRTKNREW LLIRTSSFTF QNPYSDEIEY VICTNTNVKQ LQQQQAELEV HQRDGLSSYD LSQVPVPNLP AGVHEAGKSV EKADAIFSQE RDPRFAEMFA GISASEKKMM SSASASGSQQ IYSQGSPFPA GHSGKAFSSS VVHVPGVNDI QSSSSTGQNI SQISRQLNQG QVAWTGSRPP FPGQPSKTQS SAFGIGSSHP YPADPSSYSP LSSPAASSPS GNAYPSLANR TPGFAESGQS GGQFQGRPSE VWSQWQSQHH GQQSGEQHSH QQPGQTEVFQ DMLPMPGDPT QGTGNYNIED FADLGMFPPF SE //