ADIPOQ
entrez
9370
canonical
uniprot
Q15848
canonical
ensembl
ENSG00000181092
resolver
ensp
ENSP00000320709
resolver
ensp
ENSP00000389814
resolver
ensp
ENSP00000551806
resolver
ensp
ENSP00000626744
resolver
enst
ENST00000320741
resolver
enst
ENST00000444204
resolver
enst
ENST00000881747
resolver
enst
ENST00000956685
resolver
genesymbol
ADIPOQ
resolver
genesymbol_syn
ACDC
resolver
genesymbol_syn
ACRP30
resolver
genesymbol_syn
APM1
resolver
genesymbol_syn
GBP28
resolver
hgnc
HGNC:13633
resolver
uniprot
A8K660
resolver
uniprot
B2R773
resolver
uniprot
Q58EX9
resolver
uniprot_entry
A8K660_HUMAN
resolver
uniprot_entry
ADIPO_HUMAN
resolver
uniprot_entry
B2R773_HUMAN
resolver
uniprot_sec
Q58EX9
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:0000250|UniProtKB:Q60994}.
uniprot
proteins
amino_acid_sequence
MLLLGAVLLLLALPGHDQETTTQGPGVLLPLPKGACTGWMAGIPGHPGHNGAPGRDGRDGTPGEKGEKGDPGLIGPKGDIGETGVPGAEGPRGFPGIQGRKGEPGEGAYVYRSAFSVGLETYVTIPNMPIRFTKIFYNQQNHYDGSTGKFHCNIPGLYYFAYHITVYMKDVKVSLFKKDKAMLFTYDQYQENNVDQASGSVLLHLEVGDQVWLQVYGEGERNGLYADNDNDSTFTGFLLYHDTN
uniprot
proteins
disease_involvement
DISEASE: Adiponectin deficiency (ADPOD) [MIM:612556]: An autosomal dominant condition characterized by very low concentrations of plasma adiponectin. Levels of adiponectin are decreased in obesity and may contribute to a chronic state of inflammation that leads to insulin resistance, type 2 diabetes, coronary artery disease, myocardial infarction, non-alcoholic steatohepatitis, and kidney disease. {ECO:0000269|PubMed:10918532, ECO:0000269|PubMed:11812766, ECO:0000269|PubMed:12086969}. Note=The disease is caused by variants affecting the gene represented in this entry.
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. Also has anti-atherogenic and anti-inflammatory activities (By similarity). Stimulates AMPK phosphorylation and activation in the liver and the skeletal muscle, enhancing glucose utilization and fatty-acid combustion (By similarity). 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 (PubMed:10982546). 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 (By similarity). {ECO:0000250|UniProtKB:Q60994, ECO:0000269|PubMed:10982546}.
uniprot
proteins
mass_dalton
26414
uniprot
proteins
mutagenesis
MUTAGEN 20; /note="T->A: No change in sialylated isoforms."; /evidence="ECO:0000269|PubMed:19855092"; MUTAGEN 21; /note="T->A: Some loss of sialylated isoforms."; /evidence="ECO:0000269|PubMed:19855092"; MUTAGEN 22; /note="T->A: Abolishes sialylated isoforms."; /evidence="ECO:0000269|PubMed:19855092"; MUTAGEN 33; /note="K->R: No effect on formation of HMW multimers."; /evidence="ECO:0000269|PubMed:16497731"; MUTAGEN 36; /note="C->S: Impaired formation of MMW and HMW multimers."; /evidence="ECO:0000269|PubMed:12878598, ECO:0000269|PubMed:16497731"; MUTAGEN 65; /note="K->R: Impaired formation of HMW multimers; when associated with R-68."; /evidence="ECO:0000269|PubMed:16497731"; MUTAGEN 68; /note="K->R: Impaired formation of HMW multimers; when associated with R-65."; /evidence="ECO:0000269|PubMed:16497731"; MUTAGEN 77; /note="K->R: Impaired formation of HMW multimers; when associated with R-101."; /evidence="ECO:0000269|PubMed:16497731"; MUTAGEN 101; /note="K->R: Impaired formation of HMW multimers; when associated with R-77."; /evidence="ECO:0000269|PubMed:16497731
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:0000250|UniProtKB:Q60994}.; PTM: O-glycosylated. Not N-glycosylated. O-linked glycans on hydroxylysines consist of Glc-Gal disaccharides bound to the oxygen atom of post-translationally added hydroxyl groups. Sialylated to varying degrees depending on tissue. Thr-22 appears to be the major site of sialylation. Higher sialylation found in SGBS adipocytes than in HEK fibroblasts. Sialylation is not required neither for heterodimerization nor for secretion. Not sialylated on the glycosylated hydroxylysines. Desialylated forms are rapidly cleared from the circulation. {ECO:0000269|PubMed:16497731, ECO:0000269|PubMed:19855092}.; PTM: Succination of Cys-36 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 mammals. 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:0000250|UniProtKB:Q60994}.
uniprot
proteins
pubmed
10095105
uniprot
proteins
pubmed
10403784
uniprot
proteins
pubmed
10918532
uniprot
proteins
pubmed
10961870
uniprot
proteins
pubmed
10982546
uniprot
proteins
pubmed
11812766
uniprot
proteins
pubmed
12086969
uniprot
proteins
pubmed
12354786
uniprot
proteins
pubmed
12878598
uniprot
proteins
pubmed
15340161
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16497731
uniprot
proteins
pubmed
19855092
uniprot
proteins
pubmed
22449980
uniprot
proteins
pubmed
22905912
uniprot
proteins
pubmed
35869090
uniprot
proteins
pubmed
8619847
uniprot
proteins
pubmed
8947845
uniprot
proteins
sequence_length
244
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:8947845}.
uniprot
proteins