ID BMAL1_MESAU Reviewed; 626 AA. AC O88529; DT 15-AUG-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1998, sequence version 1. DT 29-MAY-2013, entry version 90. DE RecName: Full=Aryl hydrocarbon receptor nuclear translocator-like protein 1; DE AltName: Full=Brain 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; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Cricetidae; Cricetinae; Mesocricetus. OX NCBI_TaxID=10036; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX 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: ARNTL-CLOCK heterodimers activate E-box element (5'- CC CACGTG-3') transcription of a number of proteins of the circadian CC clock. This transcription is inhibited in a feedback loop by PER, CC and also by CRY proteins (By similarity). CC -!- SUBUNIT: Component of the circadian clock oscillator which CC includes the CRY proteins, CLOCK or NPAS2, ARNTL or ARNTL2, CSNK1D CC and/or CSNK1E, TIMELESS and the PER proteins. Efficient DNA CC binding requires dimerization with another bHLH protein. CC Heterodimerization with CLOCK is required for E-box-dependent CC transactivation, for CLOCK nuclear translocation and degradation, CC and, for phosphorylation of both CLOCK and ARNTL. Interaction with CC PER and CRY proteins requires translocation to the nucleus. CC Interaction of the CLOCK-ARNTL heterodimer with PER or CRY CC inhibits transcription activation. Interacts with HSP90; with AHR CC in vitro, but not in vivo. Part of a nuclear complex which also CC includes GNB2L1/RACK1 and PRKCA; GNB2L1 and PRKCA are recruited to CC the complex in a circadian manner. Interacts with CRY2 (By CC similarity). CC -!- SUBCELLULAR LOCATION: Nucleus (By similarity). CC -!- PTM: Acetylated on Lys-538 upon dimerization with CLOCK. CC Acetylation facilitates CRY1-mediated repression (By similarity). CC -!- PTM: Phosphorylated upon dimerization with CLOCK (By similarity). CC -!- PTM: Sumoylated on Lys-259 upon dimerization with CLOCK (By CC similarity). CC -!- SIMILARITY: Contains 1 bHLH (basic helix-loop-helix) domain. CC -!- SIMILARITY: Contains 1 PAC (PAS-associated C-terminal) domain. CC -!- SIMILARITY: Contains 2 PAS (PER-ARNT-SIM) domains. 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; -; mRNA. DR ProteinModelPortal; O88529; -. DR IntAct; O88529; 1. DR HOVERGEN; HBG107503; -. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0005667; C:transcription factor complex; ISS:UniProtKB. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0003700; F:sequence-specific DNA binding transcription factor activity; IEA:InterPro. DR GO; GO:0004871; F:signal transducer activity; IEA:InterPro. DR GO; GO:0032922; P:circadian regulation of gene expression; ISS:UniProtKB. DR GO; GO:0006355; P:regulation of transcription, DNA-dependent; ISS:UniProtKB. DR GO; GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. DR Gene3D; 4.10.280.10; -; 1. DR InterPro; IPR011598; bHLH_dom. DR InterPro; IPR001067; Nuc_translocat. DR InterPro; IPR001610; PAC. DR InterPro; IPR000014; PAS. DR InterPro; IPR013767; PAS_fold. DR InterPro; IPR013655; PAS_fold_3. DR Pfam; PF00010; HLH; 1. DR Pfam; PF00989; PAS; 1. DR Pfam; PF08447; PAS_3; 1. DR PRINTS; PR00785; NCTRNSLOCATR. DR SMART; SM00353; HLH; 1. DR SMART; SM00086; PAC; 1. DR SMART; SM00091; PAS; 2. DR SUPFAM; SSF47459; HLH_basic; 1. DR SUPFAM; SSF55785; SSF55785; 2. DR TIGRFAMs; TIGR00229; sensory_box; 1. DR PROSITE; PS50888; BHLH; 1. DR PROSITE; PS50113; PAC; FALSE_NEG. DR PROSITE; PS50112; PAS; 2. PE 2: Evidence at transcript level; KW Acetylation; Activator; Biological rhythms; DNA-binding; KW Isopeptide bond; Nucleus; Phosphoprotein; Repeat; Transcription; KW Transcription regulation; Ubl conjugation. FT CHAIN 1 626 Aryl hydrocarbon receptor nuclear FT translocator-like protein 1. FT /FTId=PRO_0000127157. FT DOMAIN 72 125 bHLH. FT DOMAIN 143 215 PAS 1. FT DOMAIN 326 396 PAS 2. FT DOMAIN 401 444 PAC. FT MOD_RES 538 538 N6-acetyllysine (By similarity). FT CROSSLNK 259 259 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in SUMO) (By FT similarity). 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 //