Query author contributions in Reactome
Reactome depends on collaboration between our curation team and outside experts to assemble and peer-review its pathway modules. The integration of ORCID within Reactome enables us to meet a key challenge with authoring, curating and reviewing biological information by incentivizing and crediting the external experts that contribute their expertise and time to the Reactome curation process. More information is available at ORCID and Reactome.
If you have an ORCID ID that is not listed on this page, please forward this information to us and we will update your Reactome pathway records.
Details on Person UniProt:Q60994 Adipoq
| Class:Id | ReferenceGeneProduct:85163 |
|---|---|
| _chainChangeLog | signal peptide:1-17 added on Sat February 7 2015;chain:18-247 added on Sat February 7 2015 |
| _displayName | UniProt:Q60994 Adipoq |
| _timestamp | 2026-02-20 22:29:27 |
| chain | signal peptide:1-17 chain:18-247 |
| checksum | 0ECC687D9A8E8123 |
| comment | FUNCTION 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 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.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.SUBUNIT Homomultimer (PubMed:23209641). Forms trimers, hexamers and 12- to 18-mers. The trimers (low molecular weight complexes / LMW) are assembled via non-covalent interactions of the collagen-like domains in a triple helix and hydrophobic interactions within the globular C1q domain. Several trimers can associate to form disulfide-linked hexamers (middle molecular weight complexes / MMW) and larger complexes (higher molecular weight / HMW) (PubMed:23209641). The HMW-complex assembly is also modulated by the degree of lysine hydroxylation and glycosylation (PubMed:23209641). LMW, MMW and HMW complexes bind to HBEGF, MMW and HMW complexes bind to PDGFB, and HMW complex binds to FGF2. Interacts with CTRP9 via the C1q domain (heterotrimeric complex) (PubMed:18787108).INTERACTION Synthesized exclusively by adipocytes and secreted into plasma.INDUCTION During hormone-induced adipose differentiation and activated by insulin.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.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.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.MISCELLANEOUS HMW-complex blood contents are higher in females than in males, are increased in males by castration and decreased again upon subsequent testosterone treatment, which blocks HMW-complex secretion. |
| description | recommendedName: Adiponectin alternativeName: 30 kDa adipocyte complement-related protein alternativeName: Adipocyte complement-related 30 kDa protein shortName: ACRP30 alternativeName: Adipocyte, C1q and collagen domain-containing protein alternativeName: Adipocyte-specific protein AdipoQ |
| geneName | Adipoq Acdc Acrp30 Apm1 |
| identifier | Q60994 |
| isSequenceChanged | FALSE |
| keyword | 3D-structure Collagen Direct protein sequencing Disulfide bond Glycoprotein Hormone Hydroxylation Reference proteome Repeat Secreted Signal |
| modified | [InstanceEdit:143527] Schmidt, EE, 2004-11-12 07:45:10 [InstanceEdit:217385] Schmidt, EE, 2008-03-27 06:23:53 [InstanceEdit:354386] Schmidt, EE, 2008-06-18 04:45:12 [InstanceEdit:384350] Kanapin, AA, 2008-11-26 14:00:39 [InstanceEdit:392885] Kanapin, AA, 2009-03-09 12:07:18 [InstanceEdit:400710] Schmidt, EE, 2009-03-25 05:33:35 [InstanceEdit:423310] Kanapin, AA [InstanceEdit:435478] Kanapin, AA [InstanceEdit:435871] Kanapin, AA [InstanceEdit:447347] Kanapin, AA [InstanceEdit:525883] Kanapin, AA [InstanceEdit:613449] Kanapin, AA [InstanceEdit:797602] Kanapin, AA [InstanceEdit:937368] Yung, CK [InstanceEdit:1042053] Yung, CK [InstanceEdit:1220657] Yung, CK [InstanceEdit:1300696] Yung, CK [InstanceEdit:1301627] Yung, CK [InstanceEdit:1551960] Weiser, JD [InstanceEdit:1995863] Weiser, JD [InstanceEdit:2132304] Weiser, JD [InstanceEdit:2265580] Weiser, JD [InstanceEdit:2587579] Weiser, JD [InstanceEdit:5083144] Weiser, JD [InstanceEdit:5433710] Weiser, JD [InstanceEdit:5618415] Weiser, JD [InstanceEdit:5634237] Weiser, JD [InstanceEdit:5673015] Weiser, JD [InstanceEdit:9037114] Weiser, JD [InstanceEdit:9637257] Weiser, JD [InstanceEdit:9666080] Weiser, JD [InstanceEdit:9676415] Weiser, JD [InstanceEdit:9852000] Weiser, Joel, 2023-11-03 [InstanceEdit:9983091] Weiser, Joel, 2026-02-20 |
| name | Adipoq |
| referenceDatabase | [ReferenceDatabase:2] UniProt |
| secondaryIdentifier | ADIPO_MOUSE Q62400 Q6GTX4 Q9DC68 |
| sequenceLength | 247 |
| species | [Species:48892] Mus musculus |
| (referenceEntity) | [EntityWithAccessionedSequence:9917963] Adipoq [extracellular region] [Mus musculus] |
| [Change default viewing format] | |
No pathways have been reviewed or authored by UniProt:Q60994 Adipoq (85163)
