A0A0C5B5G6
uniprot
A0A0C5B5G6
canonical
amino_acid_sequence
MRWQEMGYIFYPRKLR
uniprot
proteins
function
FUNCTION: Regulates insulin sensitivity and metabolic homeostasis (PubMed:25738459, PubMed:33468709). Inhibits the folate cycle, thereby reducing de novo purine biosynthesis which leads to the accumulation of the de novo purine synthesis intermediate 5-aminoimidazole-4-carboxamide (AICAR) and the activation of the metabolic regulator 5'-AMP-activated protein kinase (AMPK) (PubMed:25738459). Protects against age-dependent and diet-induced insulin resistance as well as diet-induced obesity (PubMed:25738459). In response to metabolic stress, translocates to the nucleus where it binds to antioxidant response elements (ARE) present in the promoter regions of a number of genes and plays a role in regulating nuclear gene expression in an NFE2L2-dependent manner and increasing cellular resistance to metabolic stress (PubMed:29983246). Increases mitochondrial respiration and levels of CPT1A and cytokines IL1B, IL6, IL8, IL10 and TNF in senescent cells (PubMed:29886458). Increases activity of the serine/threonine protein kinase complex mTORC2 and reduces activity of the PTEN phosphatase, thus promoting phosphorylation of AKT (PubMed:33554779). This promotes AKT-mediated phosphorylation of transcription factor FOXO1 which reduces FOXO1 activity, leading to reduced levels of MSTN and promotion of skeletal muscle growth (PubMed:33554779). Promotes osteogenic differentiation of bone marrow mesenchymal stem cells via the TGFB/SMAD pathway (PubMed:30468456). Promotes osteoblast proliferation and osteoblast synthesis of type I collagens COL1A1 and COL1A2 via the TGFB/SMAD pathway (PubMed:31081069). {ECO:0000269|PubMed:25738459, ECO:0000269|PubMed:29886458, ECO:0000269|PubMed:29983246, ECO:0000269|PubMed:30468456, ECO:0000269|PubMed:31081069, ECO:0000269|PubMed:33468709, ECO:0000269|PubMed:33554779}.
uniprot
proteins
mass_dalton
2175
uniprot
proteins
mutagenesis
MUTAGEN 5; /note="E->A: Lack of enhanced glycolytic response to glucose stimulation."; /evidence="ECO:0000269|PubMed:25738459"; MUTAGEN 7; /note="G->A: Lack of enhanced glycolytic response to glucose stimulation."; /evidence="ECO:0000269|PubMed:25738459"; MUTAGEN 11..14; /note="YPRK->AAAA: Abolishes nuclear localization and DNA-binding activity."; /evidence="ECO:0000269|PubMed:29983246"; MUTAGEN 13..16; /note="RKLR->AAAA: Does not affect nuclear localization or interaction with NFE2L2 but abolishes DNA-binding activity."; /evidence="ECO:0000269|PubMed:29983246
uniprot
proteins
pubmed
25738459
uniprot
proteins
pubmed
26289118
uniprot
proteins
pubmed
29096170
uniprot
proteins
pubmed
29886458
uniprot
proteins
pubmed
29983246
uniprot
proteins
pubmed
30468456
uniprot
proteins
pubmed
30725119
uniprot
proteins
pubmed
31081069
uniprot
proteins
pubmed
31109005
uniprot
proteins
pubmed
31369811
uniprot
proteins
pubmed
31694019
uniprot
proteins
pubmed
31931370
uniprot
proteins
pubmed
32182209
uniprot
proteins
pubmed
33468709
uniprot
proteins
pubmed
33473109
uniprot
proteins
pubmed
33554779
uniprot
proteins
pubmed
7219534
uniprot
proteins
sequence_length
16
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:25738459}. Mitochondrion {ECO:0000269|PubMed:29983246}. Nucleus {ECO:0000269|PubMed:29983246, ECO:0000269|PubMed:33473109}. Note=Translocates to the nucleus in response to metabolic stress in an AMPK-dependent manner. {ECO:0000269|PubMed:29983246}.
uniprot
proteins