Adipoq
entrez
11450
canonical
uniprot
Q60994
canonical
ensembl
ENSMUSG00000022878
resolver
ensp
ENSMUSP00000023593
resolver
enst
ENSMUST00000023593
resolver
genesymbol
Adipoq
resolver
genesymbol_syn
Acdc
resolver
genesymbol_syn
Acrp30
resolver
genesymbol_syn
Apm1
resolver
uniprot
Q62400
resolver
uniprot
Q6GTX4
resolver
uniprot
Q9DC68
resolver
uniprot_entry
ADIPO_MOUSE
resolver
uniprot_sec
Q62400
resolver
uniprot_sec
Q6GTX4
resolver
uniprot_sec
Q9DC68
resolver
activity_regulation
ACTIVITY REGULATION: Polymerization and secretion of adiponectin is inhibited by succination of cysteine residues by the Krebs cycle intermediate fumarate, which leads to S-(2-succinyl)cysteine residues. {ECO:0000269|PubMed:19592500}.
uniprot
proteins
amino_acid_sequence
MLLLQALLFLLILPSHAEDDVTTTEELAPALVPPPKGTCAGWMAGIPGHPGHNGTPGRDGRDGTPGEKGEKGDAGLLGPKGETGDVGMTGAEGPRGFPGTPGRKGEPGEAAYVYRSAFSVGLETRVTVPNVPIRFTKIFYNQQNHYDGSTGKFYCNIPGLYYFSYHITVYMKDVKVSLFKKDKAVLFTYDQYQEKNVDQASGSVLLHLEVGDQVWLQVYGDGDHNGLYADNVNDSTFTGFLLYHDTN
uniprot
proteins
function
FUNCTION: Important adipokine involved in the control of fat metabolism and insulin sensitivity upon binding to its receptors ADIPOR1 or ADIPOR2, with direct anti-diabetic effect (PubMed:12802337). Also has anti-atherogenic and anti-inflammatory activities. Stimulates AMPK phosphorylation and activation in the liver and the skeletal muscle, enhancing glucose utilization and fatty-acid combustion (PubMed:12368907). Antagonizes TNF by negatively regulating its expression in various tissues such as liver and macrophages, and also by counteracting its effects. Inhibits endothelial NF-kappa-B signaling through a cAMP-dependent pathway (By similarity). May play a role in cell growth, angiogenesis and tissue remodeling by binding and sequestering various growth factors with distinct binding affinities, depending on the type of complex, LMW, MMW or HMW (PubMed:15734737). {ECO:0000250|UniProtKB:Q15848, ECO:0000269|PubMed:11479627, ECO:0000269|PubMed:11479628, ECO:0000269|PubMed:12368907, ECO:0000269|PubMed:12802337, ECO:0000269|PubMed:12840063, ECO:0000269|PubMed:15734737, ECO:0000269|PubMed:15760892}.
uniprot
proteins
mass_dalton
26809
uniprot
proteins
mutagenesis
MUTAGEN 39; /note="C->A: No change in the interaction with CTRP9."; /evidence="ECO:0000269|PubMed:18787108"; MUTAGEN 68; /note="K->R: Impaired formation of HMW multimers; when associated with R-71; R-80 and R-104."; /evidence="ECO:0000269|PubMed:16621799"; MUTAGEN 71; /note="K->R: Impaired formation of HMW multimers; when associated with R-68; R-80 and R-104."; /evidence="ECO:0000269|PubMed:16621799"; MUTAGEN 80; /note="K->R: Impaired formation of HMW multimers; when associated with R-68; R-71 and R-104."; /evidence="ECO:0000269|PubMed:16621799"; MUTAGEN 104; /note="K->R: Impaired formation of HMW multimers; when associated with R-68; R-71 and R-80."; /evidence="ECO:0000269|PubMed:16621799
uniprot
proteins
post_translational_modification
PTM: HMW complexes are more extensively glycosylated than smaller oligomers. Hydroxylation and glycosylation of the lysine residues within the collagen-like domain of adiponectin seem to be critically involved in regulating the formation and/or secretion of HMW complexes and consequently contribute to the insulin-sensitizing activity of adiponectin in hepatocytes. {ECO:0000269|PubMed:11912203, ECO:0000269|PubMed:23209641}.; PTM: O-glycosylated. Not N-glycosylated (By similarity) O-linked glycans on hydroxylysine residues consist of Glc-Gal disaccharides bound to the oxygen atom of post-translationally added hydroxyl groups (By similarity). O-linked glycosylation in the N-terminal is disialylated with the structure Neu5Acalpha2->8Neu5Acalpha2->3Gal. Sialylated by alpha 2,8-sialyltransferase III. {ECO:0000250}.; PTM: Succination of Cys-39 by the Krebs cycle intermediate fumarate, which leads to S-(2-succinyl)cysteine residues, inhibits polymerization and secretion of adiponectin. Adiponectin is a major target for succination in both adipocytes and adipose tissue of diabetic mice. It was proposed that succination of proteins is a biomarker of mitochondrial stress and accumulation of Krebs cycle intermediates in adipose tissue in diabetes and that succination of adiponectin may contribute to the decrease in plasma adiponectin in diabetes. {ECO:0000269|PubMed:19592500}.
uniprot
proteins
pubmed
11162643
uniprot
proteins
pubmed
11382781
uniprot
proteins
pubmed
11479627
uniprot
proteins
pubmed
11479628
uniprot
proteins
pubmed
11912203
uniprot
proteins
pubmed
12368907
uniprot
proteins
pubmed
12802337
uniprot
proteins
pubmed
12840063
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15734737
uniprot
proteins
pubmed
15760892
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
16621799
uniprot
proteins
pubmed
18787108
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
19592500
uniprot
proteins
pubmed
19855092
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
23209641
uniprot
proteins
pubmed
7592907
uniprot
proteins
pubmed
8631877
uniprot
proteins
pubmed
9512423
uniprot
proteins
sequence_length
247
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:23209641}.
uniprot
proteins