Adiponectin, C1Q and collagen domain containing

mammalian protein found in Mus musculus

Protein protein Q14864062

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Adiponectin, C1Q and collagen domain containing

Summary

Adiponectin, C1Q and collagen domain containing is a protein^[1].

Key Facts

Adiponectin, C1Q and collagen domain containing's instance of is recorded as protein^[2].
Adiponectin, C1Q and collagen domain containing's subclass of is recorded as protein^[3].
Adiponectin, C1Q and collagen domain containing's UniProt protein ID is recorded as Georg Lindemann^[4].
Adiponectin, C1Q and collagen domain containing's part of is recorded as Tumour necrosis factor-like domain superfamily^[5].
Adiponectin, C1Q and collagen domain containing's part of is recorded as C1q domain, protein family^[6].
Adiponectin, C1Q and collagen domain containing's part of is recorded as collagen triple helix repeat, protein family^[7].
Adiponectin, C1Q and collagen domain containing's has part is recorded as C1q domain^[8].
Adiponectin, C1Q and collagen domain containing's has part is recorded as Collagen triple helix repeat^[9].
Adiponectin, C1Q and collagen domain containing's RefSeq protein ID is recorded as NP_033735^[10].
Adiponectin, C1Q and collagen domain containing's PDB structure ID is recorded as 1C28^[11].
Adiponectin, C1Q and collagen domain containing's PDB structure ID is recorded as 1C3H^[12].
Adiponectin, C1Q and collagen domain containing's molecular function is recorded as hormone activity^[13].
Adiponectin, C1Q and collagen domain containing's molecular function is recorded as signaling receptor binding^[14].
Adiponectin, C1Q and collagen domain containing's molecular function is recorded as sialic acid binding^[15].
Adiponectin, C1Q and collagen domain containing's molecular function is recorded as protein homodimerization activity^[16].
Adiponectin, C1Q and collagen domain containing's molecular function is recorded as protein binding^[17].
Adiponectin, C1Q and collagen domain containing's molecular function is recorded as identical protein binding^[18].
Adiponectin, C1Q and collagen domain containing's molecular function is recorded as extracellular matrix structural constituent^[19].
Adiponectin, C1Q and collagen domain containing's molecular function is recorded as extracellular matrix structural constituent^[20].
Adiponectin, C1Q and collagen domain containing's molecular function is recorded as extracellular matrix structural constituent^[21].
Adiponectin, C1Q and collagen domain containing's cell component is recorded as perinuclear region of cytoplasm^[22].
Adiponectin, C1Q and collagen domain containing's cell component is recorded as cell surface^[23].
Adiponectin, C1Q and collagen domain containing's cell component is recorded as endoplasmic reticulum^[24].
Adiponectin, C1Q and collagen domain containing's cell component is recorded as cell periphery^[25].
Adiponectin, C1Q and collagen domain containing's cell component is recorded as collagen^[26].

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Quick Facts

Instance of protein

Subclass of protein

Part of Tumour necrosis factor-like domain superfamily, C1q domain, protein family, collagen triple helix repeat, protein family

Properties

Biological process positive regulation of glucose import, positive regulation of protein phosphorylation, negative regulation of receptor binding, low-density lipoprotein particle clearance, negative regulation of blood pressure, negative regulation of macrophage differentiation, negative regulation of synaptic transmission, negative regulation of gluconeogenesis, regulation of glucose metabolic process, circadian rhythm, fatty acid oxidation, positive regulation of interleukin-8 production, glucose metabolic process, protein heterotrimerization, negative regulation of heterotypic cell-cell adhesion, response to ethanol, negative regulation of inflammatory response, positive regulation of protein kinase A signaling, negative regulation of platelet-derived growth factor receptor signaling pathway, positive regulation of signal transduction, positive regulation of protein metabolic process, negative regulation of fat cell differentiation, detection of oxidative stress, response to linoleic acid, glucose homeostasis, response to tumor necrosis factor, response to nutrient levels, positive regulation of cholesterol efflux, negative regulation of MAP kinase activity, fatty acid beta-oxidation, negative regulation of tumor necrosis factor production, protein localization to plasma membrane, positive regulation of metanephric glomerular visceral epithelial cell development, response to sucrose, positive regulation of renal albumin absorption, negative regulation of granulocyte differentiation, negative regulation of protein autophosphorylation, response to nutrient, negative regulation of intracellular protein transport, response to glucose, positive regulation of myeloid cell apoptotic process, negative regulation of I-kappaB kinase/NF-kappaB signaling, negative regulation of metanephric mesenchymal cell migration, negative regulation of cell migration, positive regulation of fatty acid metabolic process, brown fat cell differentiation, positive regulation of cAMP-dependent protein kinase activity, negative regulation of transcription, DNA-templated, negative regulation of DNA biosynthetic process, response to hypoxia, negative regulation of phagocytosis, negative regulation of tumor necrosis factor-mediated signaling pathway, positive regulation of monocyte chemotactic protein-1 production, response to glucocorticoid, response to activity, negative regulation of platelet-derived growth factor receptor-alpha signaling pathway, positive regulation of I-kappaB kinase/NF-kappaB signaling, negative regulation of ERK1 and ERK2 cascade, negative regulation of macrophage derived foam cell differentiation, regulation of signaling receptor activity, negative regulation of vascular associated smooth muscle cell proliferation, negative regulation of vascular associated smooth muscle cell migration, cellular response to insulin stimulus, adiponectin-activated signaling pathway, positive regulation of blood pressure, positive regulation of protein kinase activity, negative regulation of hormone secretion, positive regulation of peptidyl-tyrosine phosphorylation, protein homooligomerization, membrane depolarization, membrane hyperpolarization, cellular response to cAMP, cellular response to epinephrine stimulus, positive regulation of glycogen (starch) synthase activity, response to bacterium, positive regulation of cold-induced thermogenesis, negative regulation of cold-induced thermogenesis, signal transduction

Cell component perinuclear region of cytoplasm, cell surface, endoplasmic reticulum, cell periphery, collagen, extracellular space, extracellular region, protein-containing complex, extracellular region

Encoded by Adipoq

Found in taxon house mouse

Has part(s) C1q domain, Collagen triple helix repeat

Imported from wholeness_audit_2026-05-02

Molecular function hormone activity, signaling receptor binding, sialic acid binding, protein homodimerization activity, protein binding, identical protein binding, extracellular matrix structural constituent, extracellular matrix structural constituent, extracellular matrix structural constituent

External References (4)

Ensembl protein id ENSMUSP00000023593, ENSMUSP00000126793

Pdb structure id 1C28, 1C3H

Refseq protein id NP_033735

Uniprot protein id Georg Lindemann

References

Programmatic citations — every numbered marker resolves to a verifiable graph row below.

Direct Wikidata claims

[2] ↑ Adiponectin, C1Q and collagen domain containing — instance of (P31): protein. Q905695. Retrieved 2022-05-25. wikidata.org.
[3] ↑ Adiponectin, C1Q and collagen domain containing — subclass of (P279): protein. Q905695. Retrieved 2017-01-19. wikidata.org.
[4] ↑ Adiponectin, C1Q and collagen domain containing — UniProt protein ID (P352): Georg Lindemann. Q905695. Retrieved 2022-05-25. wikidata.org.
[5] ↑ Adiponectin, C1Q and collagen domain containing — part of (P361): Tumour necrosis factor-like domain superfamily. InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
[6] ↑ Adiponectin, C1Q and collagen domain containing — part of (P361): C1q domain, protein family. wikidata.org.
[7] ↑ Adiponectin, C1Q and collagen domain containing — part of (P361): collagen triple helix repeat, protein family. wikidata.org.
[8] ↑ Adiponectin, C1Q and collagen domain containing — has part(s) (P527): C1q domain. InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
[9] ↑ Adiponectin, C1Q and collagen domain containing — has part(s) (P527): Collagen triple helix repeat. InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
[10] ↑ Adiponectin, C1Q and collagen domain containing — RefSeq protein ID (P637): NP_033735. Q20641742. Retrieved 2022-03-20. wikidata.org.
[11] ↑ Adiponectin, C1Q and collagen domain containing — PDB structure ID (P638): 1C28. Q905695. Retrieved 2016-08-09. wikidata.org.
[12] ↑ Adiponectin, C1Q and collagen domain containing — PDB structure ID (P638): 1C3H. Q905695. Retrieved 2016-08-09. wikidata.org.
[13] ↑ Adiponectin, C1Q and collagen domain containing — molecular function (P680): hormone activity. The fat-derived hormone adiponectin reverses insulin resistance associated with both lipoatrophy and obesity. Retrieved 2019-05-09. ebi.ac.uk. Provenance: wikidata.org.
[14] ↑ Adiponectin, C1Q and collagen domain containing — molecular function (P680): signaling receptor binding. Role of disulfide bonds in Acrp30/adiponectin structure and signaling specificity. Different oligomers activate different signal transduction pathways. Retrieved 2019-05-09. ebi.ac.uk. Provenance: wikidata.org.
[15] ↑ Adiponectin, C1Q and collagen domain containing — molecular function (P680): sialic acid binding. GOA. Retrieved 2019-05-09. ebi.ac.uk. Provenance: wikidata.org.
[16] ↑ Adiponectin, C1Q and collagen domain containing — molecular function (P680): protein homodimerization activity. GOA. Retrieved 2019-05-09. ebi.ac.uk. Provenance: wikidata.org.
[17] ↑ Adiponectin, C1Q and collagen domain containing — molecular function (P680): protein binding. T-cadherin is a receptor for hexameric and high-molecular-weight forms of Acrp30/adiponectin. Retrieved 2019-05-09. ebi.ac.uk. Provenance: wikidata.org.
[18] ↑ Adiponectin, C1Q and collagen domain containing — molecular function (P680): identical protein binding. The oligomeric structure of high molecular weight adiponectin. Retrieved 2019-05-09. ebi.ac.uk. Provenance: wikidata.org.
[19] ↑ Adiponectin, C1Q and collagen domain containing — molecular function (P680): extracellular matrix structural constituent. Quantitative proteomic profiling of the extracellular matrix of pancreatic islets during the angiogenic switch and insulinoma progression.. Retrieved 2018-01-01. ebi.ac.uk. Provenance: wikidata.org.
[20] ↑ Adiponectin, C1Q and collagen domain containing — molecular function (P680): extracellular matrix structural constituent. Quantitative proteomic profiling of the extracellular matrix of pancreatic islets during the angiogenic switch and insulinoma progression.. Retrieved 2019-02-14. ebi.ac.uk. Provenance: wikidata.org.
[21] ↑ Adiponectin, C1Q and collagen domain containing — molecular function (P680): extracellular matrix structural constituent. Quantitative proteomic profiling of the extracellular matrix of pancreatic islets during the angiogenic switch and insulinoma progression.. Retrieved 2019-05-09. ebi.ac.uk. Provenance: wikidata.org.
[22] ↑ Adiponectin, C1Q and collagen domain containing — cell component (P681): perinuclear region of cytoplasm. GOA. Retrieved 2019-05-09. ebi.ac.uk. Provenance: wikidata.org.
[23] ↑ Adiponectin, C1Q and collagen domain containing — cell component (P681): cell surface. GOA. Retrieved 2019-05-09. ebi.ac.uk. Provenance: wikidata.org.
[24] ↑ Adiponectin, C1Q and collagen domain containing — cell component (P681): endoplasmic reticulum. Two compartments for insulin-stimulated exocytosis in 3T3-L1 adipocytes defined by endogenous ACRP30 and GLUT4. Retrieved 2019-05-09. ebi.ac.uk. Provenance: wikidata.org.
[25] ↑ Adiponectin, C1Q and collagen domain containing — cell component (P681): cell periphery. GOA. Retrieved 2019-05-09. ebi.ac.uk. Provenance: wikidata.org.
[26] ↑ Adiponectin, C1Q and collagen domain containing — cell component (P681): collagen. GOA. Retrieved 2019-05-09. ebi.ac.uk. Provenance: wikidata.org.

Class ancestry

[1] ↑ Adiponectin, C1Q and collagen domain containing is an instance of protein (Q8054) [P31, primary]. Wikidata. wikidata.org.

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APA

4ort.xyz Knowledge Graph. (2026). Adiponectin, C1Q and collagen domain containing. Retrieved May 3, 2026, from https://4ort.xyz/entity/adiponectin-c1q-and-collagen-domain-containing

MLA

“Adiponectin, C1Q and collagen domain containing.” 4ort.xyz Knowledge Graph, 4ort.xyz, 3 May. 2026, https://4ort.xyz/entity/adiponectin-c1q-and-collagen-domain-containing.

BibTeX

@misc{4ortxyz_adiponectin-c1q-and-collagen-domain-containing_2026, author = {{4ort.xyz Knowledge Graph}}, title = {{Adiponectin, C1Q and collagen domain containing}}, year = {2026}, url = {https://4ort.xyz/entity/adiponectin-c1q-and-collagen-domain-containing}, note = {Accessed: 2026-05-03}}

LLM prompt

According to 4ort.xyz Knowledge Graph (aggregator of Wikidata, Wikipedia, and authoritative open-data sources): Adiponectin, C1Q and collagen domain containing — https://4ort.xyz/entity/adiponectin-c1q-and-collagen-domain-containing (retrieved 2026-05-03)

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