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cyclic AMP-dependent transcription factor ATF-6 beta; activating transcription factor 6 beta; ATF6-beta; cAMP-responsive element-binding protein-like 1; cAMP response element-binding protein-related protein; Creb-rp; protein G13 (CREBL1, G13, ATF6B)
Function:
1) transcription factor
2) role in unfolded protein response pathway (UPR)
3) activates UPR target genes induced during ER stress
4) binds DNA on the 5'-CCAC[GA]-3' half of the ER stress response element (ERSE) (5'-CCAATN(9)CCAC[GA]-3') when NF-Y is bound to ERSE
5) homodimer & heterodimer with ATF6-alpha
6) dimer interacts with the nuclear transcription factor Y (NF-Y) trimer via direct binding to NF-Y subunit C (NF-YC)
7) during unfolded protein response an approximative 60 kD fragment containing the cytoplasmic transcription factor domain is released by proteolysis - cleavage is probably performed sequentially by site-1 & site-2 proteases
Structure:
- belongs to the bZIP family, ATF subfamily
- contains 1 bZIP domain
- basic domain functions as a nuclear localization signal
- basic leucine-zipper domain is sufficient for association with NF-Y trimer & binding to ERSE
- N-glycosylated
Compartment:
- endoplasmic reticulum membrane
- processed form: nucleus
- under ER stress the cleaved N-terminal cytoplasmic domain translocates into the nucleus
Alternative splicing: named isoforms=2
Expression: ubiquitous
General
DNA-binding protein
glycoprotein
membrane protein
transcription factor (TF)
Properties
SIZE: MW = 77 kD
entity length = 703 aa
COMPARTMENT: cytoplasm
cell nucleus
endoplasmic reticulum
MOTIF: transcriptional activation domain
SITE: 1-86
serine-rich region {96-105}
MOTIF: serine residue (SEVERAL)
DNA-binding motif
SITE: 327-347
leucine zipper
SITE: 367-388
FOR-BINDING-VIA: leucine zipper
transmembrane domain {397-417}
MOTIF: proteolytic site {410-410}
proteolytic site {413-413}
proteolytic site {440-441}
N-glycosylation site {N476}
N-glycosylation site {N505}
N-glycosylation site {N610}
N-glycosylation site {N627}
N-glycosylation site {N676}
Database Correlations
OMIM 600984
UniProt Q99941
Pfam PF00170
References
UniProt :accession Q99941