ARNT_ONCMY
ID ARNT_ONCMY Reviewed; 723 AA.
AC P79832; P79831;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 25-MAY-2022, entry version 111.
DE RecName: Full=Aryl hydrocarbon receptor nuclear translocator;
DE Short=rtARNT;
GN Name=arnt;
OS Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Oncorhynchus.
OX NCBI_TaxID=8022;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAC60052.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, INTERACTION WITH
RP AHR, AND SUBCELLULAR LOCATION.
RC TISSUE=Gonad {ECO:0000269|PubMed:8940073};
RX PubMed=8940073; DOI=10.1074/jbc.271.48.30886;
RA Pollenz R.S., Sullivan H.R., Holmes J., Necela B., Peterson R.E.;
RT "Isolation and expression of cDNAs from rainbow trout (Oncorhynchus mykiss)
RT that encode two novel basic helix-loop-helix/PER-ARNT-SIM (bHLH/PAS)
RT proteins with distinct functions in the presence of the aryl hydrocarbon
RT receptor. Evidence for alternative mRNA splicing and dominant negative
RT activity in the bHLH/PAS family.";
RL J. Biol. Chem. 271:30886-30896(1996).
RN [2] {ECO:0000305}
RP FUNCTION, AND DOMAIN.
RX PubMed=11230806; DOI=10.1016/s0006-2952(99)00036-2;
RA Necela B., Pollenz R.S.;
RT "Functional analysis of activation and repression domains of the rainbow
RT trout aryl hydrocarbon receptor nuclear translocator (rtARNT) protein
RT isoforms.";
RL Biochem. Pharmacol. 57:1177-1190(1999).
RN [3] {ECO:0000305}
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=14961334; DOI=10.1007/s1012601-0011-8;
RA Sojka K.M., Pollenz R.S.;
RT "Expression of aryl hydrocarbon receptor nuclear translocator (ARNT)
RT isoforms in juvenile and adult rainbow trout tissues.";
RL Mar. Biotechnol. 3:416-427(2001).
CC -!- FUNCTION: Isoform 1 specifically recognizes the xenobiotic response
CC element (XRE), functions positively in AHR-mediated signaling and
CC activates transcription. Isoform 2 has reduced affinity for the XRE and
CC functions negatively in AHR-mediated signaling by disrupting the
CC binding of dimers formed by isoform 1 and AHR to the XRE.
CC {ECO:0000269|PubMed:11230806, ECO:0000269|PubMed:8940073}.
CC -!- SUBUNIT: Efficient DNA-binding requires dimerization with another bHLH
CC protein. Heterodimer with the aryl hydrocarbon receptor (AHR).
CC -!- INTERACTION:
CC P79832; P30561: Ahr; Xeno; NbExp=2; IntAct=EBI-958635, EBI-78863;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981,
CC ECO:0000269|PubMed:14961334, ECO:0000269|PubMed:8940073}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1 {ECO:0000269|PubMed:8940073}; Synonyms=rtARNTb
CC {ECO:0000269|PubMed:8940073};
CC IsoId=P79832-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:8940073}; Synonyms=rtARNTa
CC {ECO:0000269|PubMed:8940073};
CC IsoId=P79832-2; Sequence=VSP_052086;
CC -!- TISSUE SPECIFICITY: In day 23 embryos, expressed at highest levels in
CC brain, spinal cord and epithelial cells of developing gill. Expressed
CC at higher levels throughout all tissues in day 27 and 35 sac fry,
CC predominantly in brain and spinal cord. In the adult, isoform 1 is
CC widely expressed (at protein level) and is detected in liver, gill,
CC gonad, brain, kidney, heart, spleen and muscle. Isoform 2 is expressed
CC (at protein level) only in gills with highest expression in the
CC epithelial cells sourrounding the gill lamellae.
CC {ECO:0000269|PubMed:14961334}.
CC -!- DEVELOPMENTAL STAGE: Isoform 1 is expressed both in juvenile and adult
CC with highest levels in day 42 sac fry. Isoform 2 is only expressed in
CC adult (at protein level). {ECO:0000269|PubMed:14961334}.
CC -!- DOMAIN: The C-terminal region of isoform 1 contains a transactivation
CC domain. The Pro/Ser/Thr-rich region in the C-terminus of isoform 2
CC inhibits DNA-binding of ARNT-AHR dimers. {ECO:0000269|PubMed:11230806}.
CC -!- MISCELLANEOUS: [Isoform 2]: Expressed at much lower levels than isoform
CC 1. {ECO:0000269|PubMed:14961334}.
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DR EMBL; U73840; AAC60051.1; -; mRNA.
DR EMBL; U73841; AAC60052.1; -; mRNA.
DR RefSeq; NP_001118182.1; NM_001124710.1. [P79832-1]
DR AlphaFoldDB; P79832; -.
DR SMR; P79832; -.
DR IntAct; P79832; 1.
DR PRIDE; P79832; -.
DR GeneID; 100136759; -.
DR KEGG; omy:100136759; -.
DR CTD; 405; -.
DR OrthoDB; 331262at2759; -.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005667; C:transcription regulator complex; IEA:InterPro.
DR GO; GO:0017162; F:aryl hydrocarbon receptor binding; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR GO; GO:0046982; F:protein heterodimerization activity; IPI:UniProtKB.
DR GO; GO:0003714; F:transcription corepressor activity; IDA:UniProtKB.
DR GO; GO:0009968; P:negative regulation of signal transduction; IDA:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0009967; P:positive regulation of signal transduction; IDA:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA: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 Activator; Alternative splicing; DNA-binding; Nucleus; Repeat; Repressor;
KW Transcription; Transcription regulation.
FT CHAIN 1..723
FT /note="Aryl hydrocarbon receptor nuclear translocator"
FT /id="PRO_0000245792"
FT DOMAIN 65..118
FT /note="bHLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT DOMAIN 137..208
FT /note="PAS 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT DOMAIN 325..395
FT /note="PAS 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT DOMAIN 400..443
FT /note="PAC"
FT /evidence="ECO:0000255"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 487..509
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 557..592
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 670..694
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 557..573
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 534..723
FT /note="RSVGMAPQMVQPSHSAGQVLAQMSRQNGAPPSNSSPLQGGAAVSWPGPAAGA
FT RPPFNNQQVVPQAGKALSPQFAMGSFVGGSSSSFGAMPTTAAPTPTMGANYPNINPRAT
FT LNTNGYDGLGSGQQFPSRAVEAVWPQWQGQQQAQNRAEQHPHTQNNQPDIFPDVLAMLD
FT QPANFNNDDFEIPIYPSFNE -> SSPPGQWRQCGPSGRASSKLRTGQSSTPTHRTTSL
FT TSSLMFSPCWTSQPTSTTMTLRFPSTPLSTSDLTYTLPLTSSVSQMSPSLSFGALCSLS
FT LPVVIQREHV (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:8940073"
FT /id="VSP_052086"
FT CONFLICT 521
FT /note="Missing (in Ref. 1; AAC60051)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 723 AA; 79047 MW; 83F6EBE711EDEB82 CRC64;
MDSSIPDIPD DSLGLGAGGA QASSSACCAK RVNKRRAAPD FDDDDDGSKL FRCDDDGGGG
DKERFARENH SEIERRRRNK MTAYITELSD MVPTCSALAR KPDKLTILRM AVSHMKSLRG
SGNTAADGTY KPSFLTDQEL KHLILEAADG FLFVVSCESG RVVYVSDSLT PVLNQSQSDW
LGSSLYDQLH PDDGDKLREQ LSTAESNNTG RMLDLKTGTV KKEGQQSSVR MCMGARRSFI
CRMRCGSCPV EPMSMNRLNF LRSRNRNGLG PPKDGEPQYV VVHCTGYIKS WPPTGVNLTD
EEADNILGSR YCLVAIGRLQ VTSCPSDTDM NSISVPVEFI SRHNCQGLFT FVDHRCMATV
GYQPQELLGK NILELAHPED QELLRDSFQQ VVKLKGQVLS VMFRFLSKTR DWLWIRTSSF
TFQNPFSEEI EYIICTNANV KQLQQQQAEL GGGGRDGLYE AGQVTLPQMP VQAVTAAGTD
HSKTMDKAEM HPSMYPNPDQ AKFLPSTSAP GVPIYPQDNN NYTTANRSND TYSRSVGMAP
QMVQPSHSAG QVLAQMSRQN GAPPSNSSPL QGGAAVSWPG PAAGARPPFN NQQVVPQAGK
ALSPQFAMGS FVGGSSSSFG AMPTTAAPTP TMGANYPNIN PRATLNTNGY DGLGSGQQFP
SRAVEAVWPQ WQGQQQAQNR AEQHPHTQNN QPDIFPDVLA MLDQPANFNN DDFEIPIYPS
FNE
