ACRP30

Acrp30 is expressed in adipose tissue exclusively. It encodes a protein with similarity to collagens X and VIII and complement factor C1q. The encoded protein circulates in the plasma and is involved with metabolic and hormonal processes. Mutations in thi

adiponectin, C1Q and collagen domain containing

Important adipokine involved in the control of fat metabolism and insulin sensitivity, with direct anti-diabetic, 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. Antagonizes TNF-alpha 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. 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.

Brown fat cell differentiation
Cellular response to cAMP
Cellular response to drug
Cellular response to epinephrine stimulus
Cellular response to insulin stimulus
Circadian rhythm
Detection of oxidative stress
Fatty acid beta-oxidation
Fatty acid oxidation
Gene expression
Generation of precursor metabolites and energy
Glucose homeostasis
Glucose metabolic process
Low-density lipoprotein particle clearance
Negative regulation of blood pressure
Negative regulation of cell migration
Negative regulation of cold-induced thermogenesis
Negative regulation of DNA biosynthetic process
Negative regulation of ERK1 and ERK2 cascade
Negative regulation of fat cell differentiation
Negative regulation of gluconeogenesis
Negative regulation of granulocyte differentiation
Negative regulation of heterotypic cell-cell adhesion
Negative regulation of hormone secretion
Negative regulation of I-kappaB kinase/NF-kappaB signaling
Negative regulation of inflammatory response
Negative regulation of low-density lipoprotein receptor activity
Negative regulation of macrophage derived foam cell differentiation
Negative regulation of macrophage differentiation
Negative regulation of MAP kinase activity
Negative regulation of metanephric mesenchymal cell migration
Negative regulation of phagocytosis Source: BHF-UCL
Negative regulation of platelet-derived growth factor receptor-alpha signaling pathway
Negative regulation of platelet-derived growth factor receptor signaling pathway
Negative regulation of protein autophosphorylation
Negative regulation of receptor binding
Negative regulation of synaptic transmission
Negative regulation of transcription, DNA-templated
Negative regulation of tumor necrosis factor-mediated signaling pathway
Negative regulation of tumor necrosis factor production
Negative regulation of vascular associated smooth muscle cell migration
Negative regulation of vascular associated smooth muscle cell proliferation
Positive regulation of cAMP-dependent protein kinase activity
Positive regulation of cholesterol efflux
Positive regulation of cold-induced thermogenesis
Positive regulation of fatty acid metabolic process
Positive regulation of glucose import
Positive regulation of glycogen (starch) synthase activity
Positive regulation of I-kappaB kinase/NF-kappaB signaling
Positive regulation of interleukin-8 production
Positive regulation of lipid transporter activity
Positive regulation of metanephric glomerular visceral epithelial cell development
Positive regulation of monocyte chemotactic protein-1 production
Positive regulation of myeloid cell apoptotic process
Positive regulation of peptidyl-tyrosine phosphorylation
Positive regulation of protein kinase A signaling
Positive regulation of protein phosphorylation
Positive regulation of renal albumin absorption
Positive regulation of signal transduction
Protein localization to plasma membrane
Regulation of fatty acid biosynthetic process
Regulation of glucose metabolic process
Response to activity
Response to bacterium
Response to ethanol
Response to glucocorticoid
Response to glucose
Response to hypoxia
Response to linoleic acid
Response to nutrient
Response to sucrose
Response to tumor necrosis factor

Secreted

Adiponectin deficiency (ADPND): A condition that results in very low concentrations of plasma adiponectin.
Diabetes mellitus, non-insulin-dependent (NIDDM): A multifactorial disorder of glucose homeostasis caused by a lack of sensitivity to the body's own insulin. Affected individuals usually have an obese body habitus and manifestations of a metabolic syndrome characterized by diabetes, insulin resistance, hypertension and hypertriglyceridemia. The disease results in long-term complications that affect the eyes, kidneys, nerves, and blood vessels.

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.
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.
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.