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ARNT2_MOUSE
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   03-AUG-2022, entry version 171.
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};
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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. [Q61324-2]
DR   RefSeq; XP_006507305.1; XM_006507242.2. [Q61324-2]
DR   RefSeq; XP_011239957.1; XM_011241655.2. [Q61324-2]
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; Q61324; -.
DR   PeptideAtlas; Q61324; -.
DR   PRIDE; Q61324; -.
DR   ProteomicsDB; 283273; -. [Q61324-1]
DR   ProteomicsDB; 283274; -. [Q61324-2]
DR   Antibodypedia; 3911; 297 antibodies from 32 providers.
DR   DNASU; 11864; -.
DR   Ensembl; ENSMUST00000085077; ENSMUSP00000082154; ENSMUSG00000015709. [Q61324-1]
DR   Ensembl; ENSMUST00000208232; ENSMUSP00000146413; ENSMUSG00000015709. [Q61324-2]
DR   Ensembl; ENSMUST00000209133; ENSMUSP00000147129; ENSMUSG00000015709. [Q61324-2]
DR   GeneID; 11864; -.
DR   KEGG; mmu:11864; -.
DR   UCSC; uc009ief.2; mouse. [Q61324-1]
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; MRPFSAN; -.
DR   OrthoDB; 331262at2759; -.
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   BioGRID-ORCS; 11864; 1 hit in 71 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 227 other tissues.
DR   ExpressionAtlas; Q61324; baseline and differential.
DR   Genevisible; Q61324; MM.
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:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; ISO:MGI.
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; 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   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 compromises 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 compromises 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 compromises 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 compromises 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 compromises 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 compromises 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
 
 
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