ID BMAL1_MESAU STANDARD; PRT; 626 AA. AC O88529; DT 10-OCT-2003 (Rel. 42, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 01-MAY-2005 (Rel. 47, Last annotation update) DE Aryl hydrocarbon receptor nuclear translocator-like protein 1 (Brain DE and muscle ARNT-like 1). GN Name=ARNTL; Synonyms=BMAL1; OS Mesocricetus auratus (Golden hamster). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Cricetinae; OC Mesocricetus. OX NCBI_TaxID=10036; RN [1] RP NUCLEOTIDE SEQUENCE. RX MEDLINE=98279137; PubMed=9616112; DOI=10.1126/science.280.5369.1564; RA Gekakis N., Staknis D., Nguyen H.B., Davis F.C., Wilsbacher L.D., RA King D.P., Takahashi J.S., Weitz C.J.; RT "Role of the CLOCK protein in the mammalian circadian mechanism."; RL Science 280:1564-1569(1998). CC -!- FUNCTION: CLOCK-BMAL1 heterodimers bind to an E-box element (3'- CC CACGTG-5'), thereby activating transcription of PER1, and possibly CC of other circadian clock proteins (By similarity). CC -!- SUBUNIT: Efficient DNA binding requires dimerization with another CC bHLH protein. Forms an heterodimer with CLOCK. Interacts with CC HSP90; with AHR in vitro, but not in vivo (By similarity). CC -!- SUBCELLULAR LOCATION: Nuclear (Potential). CC -!- SIMILARITY: Contains 1 basic helix-loop-helix (bHLH) domain. CC -!- SIMILARITY: Contains 2 PAS (PER-ARNT-SIM) dimerization domains. CC -!- SIMILARITY: Contains 1 PAS-associated C-terminal (PAC) domain. 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; AF070917; AAC23606.1; -. DR HSSP; P36956; 1AM9. DR IntAct; O88529; -. DR InterPro; IPR001092; HLH_basic. DR InterPro; IPR001067; Nuc_translocat. DR InterPro; IPR000014; PAS. DR Pfam; PF00010; HLH; 1. DR Pfam; PF00989; PAS; 2. DR PRINTS; PR00785; NCTRNSLOCATR. DR PROSITE; PS50888; HLH; 1. DR PROSITE; PS50112; PAS; 2. KW DNA-binding; Nuclear protein; Repeat; Transcription; KW Transcription regulation. FT DNA_BIND 73 85 Basic motif. FT DOMAIN 86 126 Helix-loop-helix motif. FT DOMAIN 143 215 PAS 1. FT DOMAIN 326 396 PAS 2. FT DOMAIN 401 444 PAC. SQ SEQUENCE 626 AA; 68701 MW; 65FDD28B38F1E016 CRC64; MADQRMDISS TISDFMSPGP TDLLSSSLGT SGVDCNRKRK GSATDYQESM DTDKDDPHGR LEYAEHQGRI KNAREAHSQI EKRRRDKMNS FIDELASLVP TCNAMSRKLD KLTVLRMAVQ HMKTLRGATN PYTEANYKPT FLSDDELKHL ILRAADGFLF VVGCDRGKIL FVSESVFKIL NYSQNDLIGQ SLFDYLHPKD IAKVKEQLSS SDTAPRERLI DAKTGLPVKT DITPGPSRLC SGARRSFFCR MKCNRPSVKV EDKDFASTCS KKKADRKSFC TIHSTGYLKS WPPTKMGLDE DNEPDNEGCN LSCLVAIGRL HSHVVPQPVN GEIRVKSMEY VSRHAIDGKF VFVDQRATAI LAYLPQELLG TSCYEYFHQD DIGHLAECHR QVLQTREKIT TNCYKFKIKD GSFITLRSRW FSFMNPWTKE VEYIVSTNTV VLANVLEGGD PTFPQLTASP HSMDSMLPSG EGGPKRTHPT VPGIPGGTRA GAGKIGRMIA EEIMEIHRIR GSSPSSCGSS PLNITSTPPP DASSPGGKKI LNGGTPDIPS TGLLPGQAQE TPGYPYSDSS SILGENPHIG IDMIDNDQGS SSPSNDEAAM AVIMSLLEAD AGLGGPVDFS DLPWPL //