Detail Information for IndEnz0002019155
IED ID IndEnz0002019155
Enzyme Type ID protease019155
Protein Name Cyclic AMP-dependent transcription factor ATF-6 alpha
cAMP-dependent transcription factor ATF-6 alpha
Activating transcription factor 6 alpha
ATF6-alpha

Cleaved into: Processed cyclic AMP-dependent transcription factor ATF-6 alpha
Gene Name ATF6
Organism Homo sapiens (Human)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human)
Enzyme Sequence MGEPAGVAGTMESPFSPGLFHRLDEDWDSALFAELGYFTDTDELQLEAANETYENNFDNLDFDLDLMPWESDIWDINNQICTVKDIKAEPQPLSPASSSYSVSSPRSVDSYSSTQHVPEELDLSSSSQMSPLSLYGENSNSLSSAEPLKEDKPVTGPRNKTENGLTPKKKIQVNSKPSIQPKPLLLPAAPKTQTNSSVPAKTIIIQTVPTLMPLAKQQPIISLQPAPTKGQTVLLSQPTVVQLQAPGVLPSAQPVLAVAGGVTQLPNHVVNVVPAPSANSPVNGKLSVTKPVLQSTMRNVGSDIAVLRRQQRMIKNRESACQSRKKKKEYMLGLEARLKAALSENEQLKKENGTLKRQLDEVVSENQRLKVPSPKRRVVCVMIVLAFIILNYGPMSMLEQDSRRMNPSVSPANQRRHLLGFSAKEAQDTSDGIIQKNSYRYDHSVSNDKALMVLTEEPLLYIPPPPCQPLINTTESLRLNHELRGWVHRHEVERTKSRRMTNNQQKTRILQGALEQGSNSQLMAVQYTETTSSISRNSGSELQVYYASPRSYQDFFEAIRRRGDTFYVVSFRRDHLLLPATTHNKTTRPKMSIVLPAININENVINGQDYEVMMQIDCQVMDTRILHIKSSSVPPYLRDQQRNQTNTFFGSPPAATEATHVVSTIPESLQ
Enzyme Length 670
Uniprot Accession Number P18850
Absorption
Active Site
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number
Enzyme Function FUNCTION: [Cyclic AMP-dependent transcription factor ATF-6 alpha]: Precursor of the transcription factor form (Processed cyclic AMP-dependent transcription factor ATF-6 alpha), which is embedded in the endoplasmic reticulum membrane (PubMed:10564271, PubMed:11158310, PubMed:11779464). Endoplasmic reticulum stress promotes processing of this form, releasing the transcription factor form that translocates into the nucleus, where it activates transcription of genes involved in the unfolded protein response (UPR) (PubMed:10564271, PubMed:11158310, PubMed:11779464). {ECO:0000269|PubMed:10564271, ECO:0000269|PubMed:11158310, ECO:0000269|PubMed:11779464}.; FUNCTION: [Processed cyclic AMP-dependent transcription factor ATF-6 alpha]: Transcription factor that initiates the unfolded protein response (UPR) during endoplasmic reticulum stress by activating transcription of genes involved in the UPR (PubMed:10564271, PubMed:11163209, PubMed:11158310, PubMed:11779464). Binds DNA on the 5'-CCAC[GA]-3'half of the ER stress response element (ERSE) (5'-CCAAT-N(9)-CCAC[GA]-3') and of ERSE II (5'-ATTGG-N-CCACG-3') (PubMed:10564271, PubMed:11158310, PubMed:11779464). Binding to ERSE requires binding of NF-Y to ERSE. Could also be involved in activation of transcription by the serum response factor (PubMed:10564271, PubMed:11158310, PubMed:11779464). May play a role in foveal development and cone function in the retina (PubMed:26029869). {ECO:0000269|PubMed:10564271, ECO:0000269|PubMed:11158310, ECO:0000269|PubMed:11163209, ECO:0000269|PubMed:11779464, ECO:0000269|PubMed:26029869}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Chain (2); Compositional bias (2); Cross-link (1); Domain (1); Glycosylation (3); Mutagenesis (7); Natural variant (6); Region (5); Sequence conflict (9); Site (1); Topological domain (2); Transmembrane (1)
Keywords Activator;DNA-binding;Disease variant;Endoplasmic reticulum;Glycoprotein;Golgi apparatus;Isopeptide bond;Membrane;Nucleus;Reference proteome;Signal-anchor;Transcription;Transcription regulation;Transmembrane;Transmembrane helix;Ubl conjugation;Unfolded protein response
Interact With Itself; Q99941; Q68CJ9; Q53ET0; P11021; P17861; Q3U182
Induction
Subcellular Location SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:10564271, ECO:0000269|PubMed:12782636}; Single-pass type II membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000269|PubMed:12782636}; Single-pass type II membrane protein {ECO:0000255}. Note=Translocates from the endoplasmic reticulum to the Golgi, where it is processed. {ECO:0000269|PubMed:12782636}.; SUBCELLULAR LOCATION: [Processed cyclic AMP-dependent transcription factor ATF-6 alpha]: Nucleus {ECO:0000269|PubMed:10564271, ECO:0000269|PubMed:12782636}. Note=Under ER stress the cleaved N-terminal cytoplasmic domain translocates into the nucleus (PubMed:10564271, PubMed:12782636). THBS4 promotes its nuclear shuttling (By similarity). {ECO:0000250|UniProtKB:F6VAN0, ECO:0000269|PubMed:10564271, ECO:0000269|PubMed:12782636}.
Modified Residue
Post Translational Modification PTM: During unfolded protein response, a fragment of approximately 50 kDa containing the cytoplasmic transcription factor domain is released by proteolysis. The cleavage seems to be performed sequentially by site-1 (MBTPS1, S1P) and site-2 (MBTPS2, S2P) proteases. {ECO:0000269|PubMed:11163209, ECO:0000269|PubMed:12782636}.; PTM: N-glycosylated. The glycosylation status may serve as a sensor for ER homeostasis, resulting in ATF6 activation to trigger the unfolded protein response (UPR). {ECO:0000269|PubMed:14699159}.
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 10085237; 10856300; 10958673; 11805088; 11821395; 11909875; 12014989; 12076252; 12083523; 12097557; 12110171; 12445808; 12713871; 12805554; 14765107; 14973138; 15063770; 15299016; 15598891; 15657421; 16469704; 16505252; 17092596; 17101776; 17327457; 17440018; 17442311; 17522056; 17686766; 18022401; 18635891; 18650380; 18840095; 19122331; 19304306; 19420237; 19667116; 19693772; 19722195; 19723703; 19772629; 19822759; 19913121; 20102225; 20219975; 20628086; 20711500; 20732420; 20800603; 20936779; 21106748; 21211013; 21385877; 21521793; 21841196; 21915095; 21976666; 21988832; 22013072; 22028648; 22099811; 22102412; 22146569; 22577136; 22802018; 22872700; 22917505; 22956602; 23037953; 2377606; 23864652; 23924739; 24043630; 24177270; 24240056; 24269637; 24302549; 24636989; 24664756; 24726443; 25135476; 25302688; 25444553; 25450523; 25593314; 25609649; 25675914; 25754093; 25976933; 26261584; 26707144; 26925648; 27085326; 27117871; 27461470; 27563820; 27590344; 28028229; 28105371; 28157699; 28629319; 28803844; 28812650; 28884228; 28958904; 29061306; 29386036; 29440509; 29483204; 29851562; 30063110; 30063920; 30084354; 30086303; 30287689; 30639234; 30717233; 31029032; 31035281; 31105062; 31227689; 31237654; 31312025; 31368601; 31500833; 31506423; 31852864; 31900015; 31926341; 3194391; 32046286; 32138230; 32234634; 32271167; 32514126; 32724472; 32905769; 33109440; 33397415; 33545358; 33686769; 33919712; 33960419; 34186245; 34561305; 34623328; 8181673; 8754828;
Motif
Gene Encoded By
Mass 74,585
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda