ARNT2_DANRE
ID ARNT2_DANRE Reviewed; 737 AA.
AC Q9DG12; Q9DG11; Q9DG13; Q9IAS2;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2006, sequence version 2.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Aryl hydrocarbon receptor nuclear translocator 2;
DE Short=ARNT protein 2;
DE Short=zfARNT2;
GN Name=arnt2 {ECO:0000312|ZFIN:ZDB-GENE-001207-3};
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAG25920.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), FUNCTION, INTERACTION
RP WITH AHR AND HIF2A, AND TISSUE SPECIFICITY.
RC TISSUE=Liver {ECO:0000269|PubMed:11072074};
RX PubMed=11072074; DOI=10.1016/s0167-4781(00)00225-6;
RA Tanguay R.L., Andreasen E., Heideman W., Peterson R.E.;
RT "Identification and expression of alternatively spliced aryl hydrocarbon
RT nuclear translocator 2 (ARNT2) cDNAs from zebrafish with distinct
RT functions.";
RL Biochim. Biophys. Acta 1494:117-128(2000).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAF73280.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Embryo {ECO:0000269|PubMed:10960127};
RX PubMed=10960127; DOI=10.1007/s101260000001;
RA Wang W.-D., Wu J.-C., Hsu H.-J., Kong Z.-L., Hu C.-H.;
RT "Overexpression of a zebrafish ARNT2-like factor represses CYP1A
RT transcription in ZLE cells.";
RL Mar. Biotechnol. 2:376-386(2000).
CC -!- FUNCTION: Transcription factor that plays a role in the development of
CC the hypothalamo-pituitary axis. Specifically recognizes the xenobiotic
CC response element (XRE) (By similarity). Isoform 1 acts as a
CC transcriptional activator (PubMed:11072074). Isoform 3 acts as a
CC transcriptional repressor (PubMed:10960127, PubMed:11072074).
CC {ECO:0000250|UniProtKB:Q9HBZ2, ECO:0000269|PubMed:10960127,
CC ECO:0000269|PubMed:11072074}.
CC -!- SUBUNIT: Efficient DNA binding requires dimerization with another bHLH
CC protein. Heterodimer with the aryl hydrocarbon receptor (AHR), SIM1 or
CC HIF2A/EPAS-1. {ECO:0000250|UniProtKB:Q9HBZ2,
CC ECO:0000269|PubMed:11072074}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1 {ECO:0000269|PubMed:11072074}; Synonyms=2b
CC {ECO:0000269|PubMed:11072074};
CC IsoId=Q9DG12-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:11072074}; Synonyms=2c
CC {ECO:0000269|PubMed:11072074};
CC IsoId=Q9DG12-2; Sequence=VSP_052058;
CC Name=3 {ECO:0000269|PubMed:10960127, ECO:0000269|PubMed:11072074};
CC Synonyms=2a {ECO:0000269|PubMed:10960127, ECO:0000269|PubMed:11072074};
CC IsoId=Q9DG12-3; Sequence=VSP_052059, VSP_052060;
CC -!- TISSUE SPECIFICITY: Isoform 1 and isoform 2 are most highly expressed
CC in the brain, eye and skeletal muscle and to a lower degree in liver,
CC heart, kidney and swim bladder. Isoform 3 is most highly expressed in
CC the eye, forebrain, midbrain, hindbrain, skeletal muscle, gills and
CC brain but is barely detectable in liver, heart, kidney and swim
CC bladder. Before the pharyngula period isoform 3 is expressed throughout
CC the entire embryo and during this period extensively in the brain and
CC eye. {ECO:0000269|PubMed:10960127, ECO:0000269|PubMed:11072074}.
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DR EMBL; AF219987; AAG25919.1; -; mRNA.
DR EMBL; AF219988; AAG25920.1; -; mRNA.
DR EMBL; AF219989; AAG25921.1; -; mRNA.
DR EMBL; AF155066; AAF73280.1; -; mRNA.
DR RefSeq; NP_571749.1; NM_131674.1.
DR AlphaFoldDB; Q9DG12; -.
DR SMR; Q9DG12; -.
DR STRING; 7955.ENSDARP00000110276; -.
DR PaxDb; Q9DG12; -.
DR PRIDE; Q9DG12; -.
DR GeneID; 64277; -.
DR KEGG; dre:64277; -.
DR CTD; 9915; -.
DR ZFIN; ZDB-GENE-001207-3; arnt2.
DR eggNOG; KOG3561; Eukaryota.
DR InParanoid; Q9DG12; -.
DR PhylomeDB; Q9DG12; -.
DR Reactome; R-DRE-211945; Phase I - Functionalization of compounds.
DR Reactome; R-DRE-211976; Endogenous sterols.
DR Reactome; R-DRE-211981; Xenobiotics.
DR Reactome; R-DRE-8937144; Aryl hydrocarbon receptor signalling.
DR PRO; PR:Q9DG12; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0034751; C:aryl hydrocarbon receptor complex; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005667; C:transcription regulator complex; IEA:InterPro.
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; IBA:GO_Central.
DR GO; GO:0046982; F:protein heterodimerization activity; NAS:UniProtKB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0007411; P:axon guidance; IMP:ZFIN.
DR GO; GO:0007420; P:brain development; ISS:UniProtKB.
DR GO; GO:0003208; P:cardiac ventricle morphogenesis; IMP:ZFIN.
DR GO; GO:0098609; P:cell-cell adhesion; IMP:ZFIN.
DR GO; GO:0021536; P:diencephalon development; IMP:ZFIN.
DR GO; GO:0071542; P:dopaminergic neuron differentiation; IMP:ZFIN.
DR GO; GO:0021979; P:hypothalamus cell differentiation; IMP:ZFIN.
DR GO; GO:0072576; P:liver morphogenesis; IMP:ZFIN.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IPI:ZFIN.
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; IDA:UniProtKB.
DR GO; GO:0001666; P:response to hypoxia; IDA:UniProtKB.
DR GO; GO:0007165; P:signal transduction; IDA:UniProtKB.
DR GO; GO:0048798; P:swim bladder inflation; IMP:ZFIN.
DR GO; GO:0021591; P:ventricular system development; IMP:ZFIN.
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 Activator; Alternative splicing; DNA-binding; Nucleus; Reference proteome;
KW Repeat; Repressor; Transcription; Transcription regulation.
FT CHAIN 1..737
FT /note="Aryl hydrocarbon receptor nuclear translocator 2"
FT /id="PRO_0000239938"
FT DOMAIN 78..131
FT /note="bHLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT DOMAIN 149..221
FT /note="PAS 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT DOMAIN 340..406
FT /note="PAS 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT DOMAIN 413..456
FT /note="PAC"
FT /evidence="ECO:0000255"
FT REGION 1..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 525..556
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 588..721
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 588..704
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 66..80
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11072074"
FT /id="VSP_052058"
FT VAR_SEQ 405..425
FT /note="VKLKGQVLSVMYRFRMKNREW -> RQNQIKPVSQHQSHISHMMFF (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:10960127,
FT ECO:0000303|PubMed:11072074"
FT /id="VSP_052059"
FT VAR_SEQ 426..737
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:10960127,
FT ECO:0000303|PubMed:11072074"
FT /id="VSP_052060"
FT CONFLICT 137
FT /note="T -> A (in Ref. 1; AAG25920)"
FT /evidence="ECO:0000305"
FT CONFLICT 370
FT /note="I -> T (in Ref. 1; AAG25920)"
FT /evidence="ECO:0000305"
FT CONFLICT 379
FT /note="D -> V (in Ref. 2; AAF73280)"
FT /evidence="ECO:0000305"
FT CONFLICT 438
FT /note="P -> S (in Ref. 1; AAG25921)"
FT /evidence="ECO:0000305"
FT CONFLICT 495
FT /note="T -> S (in Ref. 1; AAG25921)"
FT /evidence="ECO:0000305"
FT CONFLICT 625
FT /note="A -> V (in Ref. 1; AAG25921)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 737 AA; 80972 MW; 96CB457F52B12F09 CRC64;
MATPAAVNPS EMGTDLPGPV SMPGAVVGAG QVRMTGAMPG RGGKRRSAGM DFDDEDGEGP
SKFSRYDDDQ IPGDKERYAR ENHSEIERRR RNKMTQYITE LSDMVPTCSA LARKPDKLTI
LRMAVSHMKS MRGTGNTSTD GAYKPSFLTE QELKHLILEA ADGFLFVVAA ETGRVIYVSD
SVTPVLNHPQ SEWFGSTLFE QVHPDDVDKL REQLSTSENS MTGRILDLKT GTVKKEGQQS
SMRMCMGSRR SFICRMRCGS APLDHISLNR LSSMRKRYRN GLGPSKEGEA QYSVVHCTGY
IKAWPPAGMT IPDEDTEAGQ TSKYCLVAIG RLQVTSSPVS MDMNGLSVPT EFLSRHNSDG
IITFVDPRCI NVIGYQPQDL LGKDILEFCH PEDQSHLRES FQQVVKLKGQ VLSVMYRFRM
KNREWMLIRT SSFTFQNPYS DEIEYIICTN TNVKQLQQQQ QAELEVHQRD GLTAYDLSQV
PVSGVSAGVH ESGKTIDKTE SLFSQERDPR FSDIYTGIST SEKKMMVPSS TSGGQQLYSQ
GSPFQPGHSG KSFSSSVIHV PGVNDIQSTA GSAGQNLSQI SRQINTGQVS WSGNRPPFSG
QQIPAQSNKA QSSPFGIGSS HSYQADPSSY SPLSSPATSS PSGNAYSNLA NRNTAFDVSG
ESSQSGGQFQ GRPSEVWSQW QSQHHSQQAG DPHPHTQASQ TEVFQDMLPM PGDPTQGTTN
YNIEDFADLG MFPPFSE
