Reviewed,
UniProtKB/Swiss-Prot Q60994 (ADIPO_MOUSE)
Last modified
January 19, 2010.
Version 98.
History...
Clusters with 100%,
90%,
50% identity |
Documents (3) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Adiponectin Alternative name(s): Adipocyte, C1q and collagen domain-containing protein 30 kDa adipocyte complement-related protein Adipocyte complement-related 30 kDa protein Short name=ACRP30 Adipocyte-specific protein AdipoQ | ||||
| Gene names |
| ||||
| Organism | Mus musculus (Mouse) | ||||
| Taxonomic identifier | 10090 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus |
Protein attributes
| Sequence length | 247 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| 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-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. Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 |
| Subunit structure | Homomultimer. 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). The HMW-complex assembly may rely aditionnally on lysine hydroxylation and glycosylation. LMW, MMW and HMW complexes bind to HBEGF, MMW and HMW complexes bind to PDGFB, and HMW complex binds to FGF2. Ref.9 Ref.10 Ref.11 |
| Subcellular location | |
| Tissue specificity | Synthesized exclusively by adipocytes and secreted into plasma. |
| Induction | During hormone-induced adipose differentiation and activated by insulin. |
| Post-translational modification | HMW complexes are more extensively glycosylated than smaller oligomers. Hydroxylation and glycosylation of the lysine residues within the collagene-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. Ref.5 O-linked glycans consist of Glc-Gal disaccharides bound to the oxygen atom of post-translationally added hydroxyl groups. Not N-glycosylated. Ref.5 |
| 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. |
| Sequence similarities | Contains 1 C1q domain. Contains 1 collagen-like domain. |
Ontologies
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||||||||||||||||||
Molecule processing | |||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 17 | 17 | Ref.5 | ||||||||||||||||||||||||
| Chain | 18 – 247 | 230 | Adiponectin | PRO_0000003544 | |||||||||||||||||||||||
Regions | |||||||||||||||||||||||||||
| Domain | 45 – 110 | 66 | Collagen-like | ||||||||||||||||||||||||
| Domain | 111 – 247 | 137 | C1q | ||||||||||||||||||||||||
Sites | |||||||||||||||||||||||||||
| Site | 79 | 1 | Not hydroxylated | ||||||||||||||||||||||||
| Site | 98 | 1 | Not hydroxylated | ||||||||||||||||||||||||
| Site | 107 | 1 | Not hydroxylated | ||||||||||||||||||||||||
| Site | 233 | 1 | Not glycosylated | ||||||||||||||||||||||||
Amino acid modifications | |||||||||||||||||||||||||||
| Modified residue | 47 | 1 | 4-hydroxyproline By similarity | ||||||||||||||||||||||||
| Modified residue | 50 | 1 | 4-hydroxyproline By similarity | ||||||||||||||||||||||||
| Modified residue | 56 | 1 | 4-hydroxyproline By similarity | ||||||||||||||||||||||||
| Modified residue | 68 | 1 | 5-hydroxylysine Ref.5 | ||||||||||||||||||||||||
| Modified residue | 71 | 1 | 5-hydroxylysine Ref.5 | ||||||||||||||||||||||||
| Modified residue | 80 | 1 | 5-hydroxylysine Ref.5 | ||||||||||||||||||||||||
| Modified residue | 94 | 1 | 4-hydroxyproline Ref.5 | ||||||||||||||||||||||||
| Modified residue | 104 | 1 | 5-hydroxylysine Ref.5 | ||||||||||||||||||||||||
| Glycosylation | 68 | 1 | O-linked (Gal...) Ref.5 | ||||||||||||||||||||||||
| Glycosylation | 71 | 1 | O-linked (Gal...) Ref.5 | ||||||||||||||||||||||||
| Glycosylation | 80 | 1 | O-linked (Gal...) Ref.5 | ||||||||||||||||||||||||
| Glycosylation | 104 | 1 | O-linked (Gal...) Ref.5 | ||||||||||||||||||||||||
| Disulfide bond | 39 | Interchain By similarity | |||||||||||||||||||||||||
Natural variations | |||||||||||||||||||||||||||
| Natural variant | 113 | 1 | M → V | ||||||||||||||||||||||||
Experimental info | |||||||||||||||||||||||||||
| Mutagenesis | 68 | 1 | K → R: Impaired formation of HMW multimers; when associated with R-71; R-80 and R-104. Ref.11 | ||||||||||||||||||||||||
| Mutagenesis | 71 | 1 | K → R: Impaired formation of HMW multimers; when associated with R-68; R-80 and R-104. Ref.11 | ||||||||||||||||||||||||
| Mutagenesis | 80 | 1 | K → R: Impaired formation of HMW multimers; when associated with R-68; R-71 and R-104. Ref.11 | ||||||||||||||||||||||||
| Mutagenesis | 104 | 1 | K → R: Impaired formation of HMW multimers; when associated with R-68; R-71 and R-80. Ref.11 | ||||||||||||||||||||||||
| Sequence conflict | 50 | 1 | P → S in AAB06706. Ref.2 | ||||||||||||||||||||||||
| Sequence conflict | 74 | 1 | A → S in AAB06706. Ref.2 | ||||||||||||||||||||||||
| Sequence conflict | 117 | 1 | A → G in AAB06706. Ref.2 | ||||||||||||||||||||||||
| Sequence conflict | 148 | 1 | G → N in AAB06706. Ref.2 | ||||||||||||||||||||||||
| Sequence conflict | 243 | 1 | Y → F in AAB06706. Ref.2 | ||||||||||||||||||||||||
Secondary structure | |||||||||||||||||||||||||||
Helix Strand Turn | |||||||||||||||||||||||||||
| Beta strand | 117 – 121 | 5 | |||||||||||||||||||||||||
| Beta strand | 137 – 140 | 4 | |||||||||||||||||||||||||
| Turn | 148 – 150 | 3 | |||||||||||||||||||||||||
| Beta strand | 159 – 172 | 14 | |||||||||||||||||||||||||
| Beta strand | 174 – 180 | 7 | |||||||||||||||||||||||||
| Beta strand | 183 – 190 | 8 | |||||||||||||||||||||||||
| Beta strand | 197 – 208 | 12 | |||||||||||||||||||||||||
| Beta strand | 213 – 218 | 6 | |||||||||||||||||||||||||
| Beta strand | 236 – 244 | 9 | |||||||||||||||||||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "A novel serum protein similar to C1q, produced exclusively in adipocytes." Scherer P.E., Williams S., Fogliano M., Baldini G., Lodish H.F. J. Biol. Chem. 270:26746-26749(1995) [PubMed: 7592907] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Adipocyte. |
| [2] | "AdipoQ is a novel adipose-specific gene dysregulated in obesity." Hu E., Liang P., Spiegelman B.M. J. Biol. Chem. 271:10697-10703(1996) [PubMed: 8631877] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Fibroblast. |
| [3] | "Chromosomal localization, expression pattern, and promoter analysis of the mouse gene encoding adipocyte-specific secretory protein Acrp30." Das K., Lin Y., Widen E., Zhang Y., Scherer P.E. Biochem. Biophys. Res. Commun. 280:1120-1129(2001) [PubMed: 11162643] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [4] | "The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. Hayashizaki Y.Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Heart. |
| [5] | "Hydroxylation and glycosylation of the four conserved lysine residues in the collagenous domain of adiponectin. Potential role in the modulation of its insulin-sensitizing activity." Wang Y., Xu A., Knight C., Xu L.Y., Cooper G.J.S. J. Biol. Chem. 277:19521-19529(2002) [PubMed: 11912203] [Abstract] Cited for: PROTEIN SEQUENCE OF 18-25, HYDROXYLATION AT LYS-68; LYS-71; LYS-80; PRO-94 AND LYS-104, GLYCOSYLATION AT LYS-68; LYS-71; LYS-80 AND LYS-104, GLYCAN STRUCTURE, ABSENCE OF HYDROXYLATION AT PRO-79; PRO-98 AND PRO-107, ABSENCE OF GLYCOSYLATION AT ASN-233, MASS SPECTROMETRY. |
| [6] | "The fat-derived hormone adiponectin reverses insulin resistance associated with both lipoatrophy and obesity." Yamauchi T., Kamon J., Waki H., Terauchi Y., Kubota N., Hara K., Mori Y., Ide T., Murakami K., Tsuboyama-Kasaoka N., Ezaki O., Akanuma Y., Gavrilova O., Vinson C., Reitman M.L., Kagechika H., Shudo K., Yoda M. Kadowaki T.Nat. Med. 7:941-946(2001) [PubMed: 11479627] [Abstract] Cited for: FUNCTION. |
| [7] | "The adipocyte-secreted protein Acrp30 enhances hepatic insulin action." Berg A.H., Combs T.P., Du X., Brownlee M., Scherer P.E. Nat. Med. 7:947-953(2001) [PubMed: 11479628] [Abstract] Cited for: FUNCTION. |
| [8] | "The fat-derived hormone adiponectin alleviates alcoholic and nonalcoholic fatty liver diseases in mice." Xu A., Wang Y., Keshaw H., Xu L.Y., Lam K.S.L., Cooper G.J.S. J. Clin. Invest. 112:91-100(2003) [PubMed: 12840063] [Abstract] Cited for: FUNCTION. |
| [9] | "Testosterone selectively reduces the high molecular weight form of adiponectin by inhibiting its secretion from adipocytes." Xu A., Chan K.W., Hoo R.L.C., Wang Y., Tan K.C.B., Zhang J., Chen B., Lam M.C., Tse C., Cooper G.J.S., Lam K.S.L. J. Biol. Chem. 280:18073-18080(2005) [PubMed: 15760892] [Abstract] Cited for: SUBUNIT, FUNCTION. |
| [10] | "Adiponectin inhibits cell proliferation by interacting with several growth factors in an oligomerization-dependent manner." Wang Y., Lam K.S.L., Xu J.Y., Lu G., Xu L.Y., Cooper G.J.S., Xu A. J. Biol. Chem. 280:18341-18347(2005) [PubMed: 15734737] [Abstract] Cited for: SUBUNIT, FUNCTION. |
| [11] | "Post-translational modifications of the four conserved lysine residues within the collagenous domain of adiponectin are required for the formation of its high molecular weight oligomeric complex." Wang Y., Lam K.S.L., Chan L., Chan K.W., Lam J.B.B., Lam M.C., Hoo R.C.L., Mak W.W.N., Cooper G.J.S., Xu A. J. Biol. Chem. 281:16391-16400(2006) [PubMed: 16621799] [Abstract] Cited for: SUBUNIT, MUTAGENESIS OF LYS-68; LYS-71; LYS-80 AND LYS-104. |
| [12] | "The crystal structure of a complement-1q family protein suggests an evolutionary link to tumor necrosis factor." Shapiro L., Scherer P.E. Curr. Biol. 8:335-338(1998) [PubMed: 9512423] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 111-247. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| EMBL GenBank DDBJ | U37222 mRNA. Translation: AAA80543.1. U49915 mRNA. Translation: AAB06706.1. AF304466 Genomic DNA. Translation: AAK13417.1. AK003138 mRNA. Translation: BAB22597.1. | ||||||||||||||||||
| IPI | IPI00311383. | ||||||||||||||||||
| RefSeq | NP_033735.3. | ||||||||||||||||||
| UniGene | Mm.3969 | ||||||||||||||||||
3D structure databases | |||||||||||||||||||
| PDBe RCSB PDB PDBj |
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| ModBase | Search... | ||||||||||||||||||
Protein-protein interaction databases | |||||||||||||||||||
| STRING | Q60994. | ||||||||||||||||||
Proteomic databases | |||||||||||||||||||
| PRIDE | Q60994. | ||||||||||||||||||
Genome annotation databases | |||||||||||||||||||
| Ensembl | ENSMUST00000023593; ENSMUSP00000023593; ENSMUSG00000022878; Mus musculus. [Genome view] | ||||||||||||||||||
| GeneID | 11450. | ||||||||||||||||||
| KEGG | mmu:11450. | ||||||||||||||||||
Organism-specific databases | |||||||||||||||||||
| CTD | 11450. | ||||||||||||||||||
| MGI | MGI:106675. Adipoq. | ||||||||||||||||||
Phylogenomic databases | |||||||||||||||||||
| eggNOG | roNOG04854. | ||||||||||||||||||
| HOGENOM | HBG444750. | ||||||||||||||||||
| HOVERGEN | Q60994. | ||||||||||||||||||
| InParanoid | Q60994. | ||||||||||||||||||
Gene expression databases | |||||||||||||||||||
| ArrayExpress | Q60994. | ||||||||||||||||||
| Bgee | Q60994. | ||||||||||||||||||
| CleanEx | MM_ADIPOQ. | ||||||||||||||||||
| Genevestigator | Q60994. | ||||||||||||||||||
| GermOnline | ENSMUSG00000022878. Mus musculus. | ||||||||||||||||||
Family and domain databases | |||||||||||||||||||
| InterPro | IPR001073. C1q. IPR008160. Collagen. IPR008983. Tumour_necrosis_fac-like. [Graphical view] | ||||||||||||||||||
| Gene3D | G3DSA:2.60.120.40. Tumour_necrosis_fac-like. 1 hit. | ||||||||||||||||||
| Pfam | PF00386. C1q. 1 hit. PF01391. Collagen. 1 hit. [Graphical view] | ||||||||||||||||||
| PRINTS | PR00007. COMPLEMNTC1Q. | ||||||||||||||||||
| SMART | SM00110. C1Q. 1 hit. [Graphical view] | ||||||||||||||||||
| PROSITE | PS50871. C1Q. 1 hit. [Graphical view] | ||||||||||||||||||
| ProtoNet | Search... | ||||||||||||||||||
Other Resources | |||||||||||||||||||
| SOURCE | Search... | ||||||||||||||||||
Entry information
| Entry name | ADIPO_MOUSE | ||||||||
| Accession | Primary (citable) accession number: Q60994 Secondary accession number(s): Q62400, Q9DC68 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
Relevant documents
| MGD cross-references Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot |
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with


