Creb3l1
entrez
26427
canonical
uniprot
Q9Z125
canonical
ensembl
ENSMUSG00000027230
resolver
ensp
ENSMUSP00000028663
resolver
enst
ENSMUST00000028663
resolver
genesymbol
Creb3l1
resolver
genesymbol_syn
Oasis
resolver
uniprot
A0A0R4J082
resolver
uniprot
Q91W70
resolver
uniprot_entry
A0A0R4J082_MOUSE
resolver
uniprot_entry
CR3L1_MOUSE
resolver
uniprot_sec
Q91W70
resolver
amino_acid_sequence
MDAVLEPFPADRLFPGSSFLDLGDLNESDFLNNAHFPEHLDHFVENMEDFSNDLFSSFFDDPVLDEKSALLDMELDSPAPGIQAEHSYSLSGDSAPQSPLVPVKMEDTTQDVEHGAWALGNKLCSIMVKQEQSPELPVDPLAASSAMAAAAAMATPPLLGLSPMPRLPIPHQAPGEMTQLPVIKAEPPEMSQFLKVTPEDLVQMPPTPPSSHGSDSDGSQSPRSLPPSSPVRPMARSSTAISTSPLLTAPHKLQGTSGPLLLTEEEKRTLIAEGYPIPTKLPLTKAEEKALKRVRRKIKNKISAQESRRKKKEYVECLEKKVETYTSENNELWKKVETLETANRTLLQQLQKLQTLVTSKISRPYKMAATQTGTCLMVAALCFVLVLGSLVPCLPAFSSGSMTVKEDPIAADSVYAASQMPSRSLLFYDDGAGSWEDGRGALLPVEPPEGWELKPGGPAEQRPQDHLRHDRADSIHETTKYLRETWPEDTDDNGTSPNFSHPEWFHDRDLGPNTTIKLS
uniprot
proteins
function
FUNCTION: [Cyclic AMP-responsive element-binding protein 3-like protein 1]: Precursor of the transcription factor form (Processed cyclic AMP-responsive element-binding protein 3-like protein 1), which is embedded in the endoplasmic reticulum membrane with N-terminal DNA-binding and transcription activation domains oriented toward the cytosolic face of the membrane. In response to ER stress or DNA damage, transported to the Golgi, where it is cleaved in a site-specific manner by resident proteases S1P/MBTPS1 and S2P/MBTPS2. The released N-terminal cytosolic domain is translocated to the nucleus where it activates transcription of specific target genes involved in the cell-cycle progression inhibition. {ECO:0000269|PubMed:37178686}.; FUNCTION: [Processed cyclic AMP-responsive element-binding protein 3-like protein 1]: Transcription factor involved in cell type specific DNA damage and unfolded protein response (UPR) (PubMed:19767743, PubMed:37178686). Binds the DNA consensus sequence 5'-GTGXGCXGC-3' (By similarity). Plays a critical role in bone formation through the transcription of COL1A1, and possibly COL1A2, and the secretion of bone matrix proteins. Directly binds to the UPR element (UPRE)-like sequence in an osteoblast-specific COL1A1 promoter region and induces its transcription. Does not regulate COL1A1 in other tissues, such as skin (PubMed:19767743). Required to protect astrocytes from ER stress-induced cell death. In astrocytes, binds to the cAMP response element (CRE) of the BiP/HSPA5 promoter and participate in its transcriptional activation (PubMed:12480185, PubMed:15665855). In astrocytes and osteoblasts, upon DNA damage, inhibits cell-cycle progression after G2/M phase by binding to promoters and activating transcription of genes encoding cell-cycle inhibitors, such as p21/CDKN1A (PubMed:37178686). Required for TGFB1 to activate genes involved in the assembly of collagen extracellular matrix (By similarity). {ECO:0000250|UniProtKB:Q96BA8, ECO:0000269|PubMed:12480185, ECO:0000269|PubMed:15665855, ECO:0000269|PubMed:19767743, ECO:0000269|PubMed:37178686}.
uniprot
proteins
mass_dalton
56959
uniprot
proteins
mutagenesis
MUTAGEN 392; /note="P->L: Loss of proteolytic cleavage; when associated with V-423 and V-426."; /evidence="ECO:0000269|PubMed:15665855"; MUTAGEN 423; /note="R->A: Loss of proteolytic cleavage; when associated with L-392 and V-426."; /evidence="ECO:0000269|PubMed:15665855"; MUTAGEN 426; /note="L->V: Loss of proteolytic cleavage; when associated with L-392 and A-423."; /evidence="ECO:0000269|PubMed:15665855
uniprot
proteins
post_translational_modification
PTM: N-glycosylated. {ECO:0000269|PubMed:15665855}.; PTM: Ubiquitinated by HRD1/SYVN1; undergoes 'Lys-48'-linked ubiquitination, followed by rapid proteasomal degradation under normal conditions. Upon ER stress, SYVN1 E3 ubiquitin-protein ligase dissociates from its substrate, ubiquitination does not occur and CREB3L1 is stabilized. {ECO:0000269|PubMed:22705851}.; PTM: Upon ER stress or DNA damage, translocated to the Golgi apparatus, where it is processed by regulated intramembrane proteolysis (RIP) to release the cytosol-facing N-terminal transcription factor domain (PubMed:19767743, PubMed:37178686). The cleavage is performed sequentially by site-1 and site-2 proteases (S1P/MBTPS1 and S2P/MBTPS2). RIP is induced by TGFB1 and ceramide. {ECO:0000250|UniProtKB:Q96BA8, ECO:0000269|PubMed:19767743, ECO:0000269|PubMed:37178686}.
uniprot
proteins
protein_family
ATF subfamily
uniprot
proteins
protein_family
BZIP family
uniprot
proteins
pubmed
10350641
uniprot
proteins
pubmed
12480185
uniprot
proteins
pubmed
12684764
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15665855
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
19767743
uniprot
proteins
pubmed
22705851
uniprot
proteins
pubmed
37178686
uniprot
proteins
sequence_length
519
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:15665855, ECO:0000269|PubMed:19767743}; Single-pass type II membrane protein {ECO:0000269|PubMed:15665855}. Note=ER membrane resident protein. Upon ER stress, translocated to the Golgi apparatus where it is cleaved. The cytosolic N-terminal fragment (processed cyclic AMP-responsive element-binding protein 3-like protein 1) is transported into the nucleus. {ECO:0000269|PubMed:15665855, ECO:0000269|PubMed:19767743}.; SUBCELLULAR LOCATION: [Processed cyclic AMP-responsive element-binding protein 3-like protein 1]: Nucleus {ECO:0000269|PubMed:15665855, ECO:0000269|PubMed:19767743, ECO:0000269|PubMed:37178686}. Note=Upon ER stress or DNA damage, transported into the nucleus. {ECO:0000269|PubMed:15665855, ECO:0000269|PubMed:19767743, ECO:0000269|PubMed:37178686}.
uniprot
proteins
transmembrane_region
TRANSMEM 377..397; /note="Helical; Signal-anchor for type II membrane protein"; /evidence="ECO:0000255
uniprot
proteins