Gene/Proteome Database (LMPD)

LMPD ID
LMP000440
Gene ID
11450
Species
Mus musculus (Mouse)
Gene Name
adiponectin, C1Q and collagen domain containing
Gene Symbol
Adipoq
Synonyms
30kDa; APN; Acdc; Acrp30; GBP28; adipo; apM1
Alternate Names
adiponectin; adipocyte-specific protein AdipoQ; adipocyte complement related protein; 30 kDa adipocyte complement-related protein; adipocyte complement-related 30 kDa protein; adipocyte, C1Q and collagen domain containing; adipocyte, C1q and collagen domain-containing protein
Chromosome
16
Map Location
16 B3-B4|16 13.96 cM

Proteins

adiponectin precursor
Refseq ID NP_033735
Protein GI 87252711
UniProt ID Q60994
mRNA ID NM_009605
Length 247
RefSeq Status VALIDATED
MLLLQALLFLLILPSHAEDDVTTTEELAPALVPPPKGTCAGWMAGIPGHPGHNGTPGRDGRDGTPGEKGEKGDAGLLGPKGETGDVGMTGAEGPRGFPGTPGRKGEPGEAAYVYRSAFSVGLETRVTVPNVPIRFTKIFYNQQNHYDGSTGKFYCNIPGLYYFSYHITVYMKDVKVSLFKKDKAVLFTYDQYQEKNVDQASGSVLLHLEVGDQVWLQVYGDGDHNGLYADNVNDSTFTGFLLYHDTN
sig_peptide: 1..17 inference: COORDINATES: ab initio prediction:SignalP:4.0 calculated_mol_wt: 1906 peptide sequence: MLLLQALLFLLILPSHA mat_peptide: 18..247 product: Adiponectin experiment: experimental evidence, no additional details recorded note: propagated from UniProtKB/Swiss-Prot (Q60994.2) calculated_mol_wt: 24921 peptide sequence: EDDVTTTEELAPALVPPPKGTCAGWMAGIPGHPGHNGTPGRDGRDGTPGEKGEKGDAGLLGPKGETGDVGMTGAEGPRGFPGTPGRKGEPGEAAYVYRSAFSVGLETRVTVPNVPIRFTKIFYNQQNHYDGSTGKFYCNIPGLYYFSYHITVYMKDVKVSLFKKDKAVLFTYDQYQEKNVDQASGSVLLHLEVGDQVWLQVYGDGDHNGLYADNVNDSTFTGFLLYHDTN

Gene Information

Entrez Gene ID
11450
Gene Name
adiponectin, C1Q and collagen domain containing
Gene Symbol
Adipoq
Species
Mus musculus

Gene Ontology (GO Annotations)

GO ID Source Type Description
GO:0071944 ISS:UniProtKB C cell periphery
GO:0009986 ISS:BHF-UCL C cell surface
GO:0005581 IEA:UniProtKB-KW C collagen trimer
GO:0005783 IDA:MGI C endoplasmic reticulum
GO:0005615 IDA:MGI C extracellular space
GO:0070062 IEA:Ensembl C extracellular vesicular exosome
GO:0048471 ISS:UniProtKB C perinuclear region of cytoplasm
GO:0005179 IDA:MGI F hormone activity
GO:0042802 IPI:IntAct F identical protein binding
GO:0005102 IDA:MGI F receptor binding
GO:0033691 IEA:Ensembl F sialic acid binding
GO:0033211 IEA:Ensembl P adiponectin-activated signaling pathway
GO:0050873 IDA:MGI P brown fat cell differentiation
GO:0071320 IEA:Ensembl P cellular response to cAMP
GO:0035690 IDA:UniProtKB P cellular response to drug
GO:0071872 IEA:Ensembl P cellular response to epinephrine stimulus
GO:0032869 IGI:MGI P cellular response to insulin stimulus
GO:0007623 IEA:Ensembl P circadian rhythm
GO:0070994 IMP:UniProtKB P detection of oxidative stress
GO:0006635 IMP:MGI P fatty acid beta-oxidation
GO:0019395 IDA:MGI P fatty acid oxidation
GO:0042593 IDA:MGI P glucose homeostasis
GO:0006006 IDA:MGI P glucose metabolic process
GO:0034383 ISS:UniProtKB P low-density lipoprotein particle clearance
GO:0051899 IEA:Ensembl P membrane depolarization
GO:0060081 IEA:Ensembl P membrane hyperpolarization
GO:2000279 ISS:UniProtKB P negative regulation of DNA biosynthetic process
GO:0070373 ISS:UniProtKB P negative regulation of ERK1 and ERK2 cascade
GO:0043124 ISS:UniProtKB P negative regulation of I-kappaB kinase/NF-kappaB signaling
GO:0043407 IDA:UniProtKB P negative regulation of MAP kinase activity
GO:0045776 ISS:UniProtKB P negative regulation of blood pressure
GO:0030336 IDA:UniProtKB P negative regulation of cell migration
GO:0045599 IDA:BHF-UCL P negative regulation of fat cell differentiation
GO:0045721 IDA:MGI P negative regulation of gluconeogenesis
GO:0030853 ISS:UniProtKB P negative regulation of granulocyte differentiation
GO:0034115 ISS:UniProtKB P negative regulation of heterotypic cell-cell adhesion
GO:0046888 IEA:Ensembl P negative regulation of hormone secretion
GO:0050728 IDA:UniProtKB P negative regulation of inflammatory response
GO:0090317 ISS:UniProtKB P negative regulation of intracellular protein transport
GO:0045715 ISS:UniProtKB P negative regulation of low-density lipoprotein particle receptor biosynthetic process
GO:0010745 ISS:UniProtKB P negative regulation of macrophage derived foam cell differentiation
GO:0045650 ISS:UniProtKB P negative regulation of macrophage differentiation
GO:2000590 IDA:UniProtKB P negative regulation of metanephric mesenchymal cell migration
GO:0050765 ISS:UniProtKB P negative regulation of phagocytosis
GO:0010642 IDA:UniProtKB P negative regulation of platelet-derived growth factor receptor signaling pathway
GO:2000584 IDA:UniProtKB P negative regulation of platelet-derived growth factor receptor-alpha signaling pathway
GO:0031953 ISS:UniProtKB P negative regulation of protein autophosphorylation
GO:1900121 ISS:UniProtKB P negative regulation of receptor binding
GO:0014912 ISS:UniProtKB P negative regulation of smooth muscle cell migration
GO:0048662 ISS:UniProtKB P negative regulation of smooth muscle cell proliferation
GO:0050805 ISS:UniProtKB P negative regulation of synaptic transmission
GO:0045892 IMP:UniProtKB P negative regulation of transcription, DNA-templated
GO:0032720 ISS:UniProtKB P negative regulation of tumor necrosis factor production
GO:0010804 ISS:UniProtKB P negative regulation of tumor necrosis factor-mediated signaling pathway
GO:0043123 IDA:MGI P positive regulation of I-kappaB kinase/NF-kappaB signaling
GO:0045777 IEA:Ensembl P positive regulation of blood pressure
GO:2000481 IMP:UniProtKB P positive regulation of cAMP-dependent protein kinase activity
GO:0032270 ISS:BHF-UCL P positive regulation of cellular protein metabolic process
GO:0010875 ISS:BHF-UCL P positive regulation of cholesterol efflux
GO:0045923 IMP:MGI P positive regulation of fatty acid metabolic process
GO:0046326 IDA:MGI P positive regulation of glucose import
GO:2000467 ISS:UniProtKB P positive regulation of glycogen (starch) synthase activity
GO:0032757 ISS:UniProtKB P positive regulation of interleukin-8 production
GO:2000478 IMP:UniProtKB P positive regulation of metanephric glomerular visceral epithelial cell development
GO:0071639 ISS:UniProtKB P positive regulation of monocyte chemotactic protein-1 production
GO:0033034 ISS:UniProtKB P positive regulation of myeloid cell apoptotic process
GO:0050731 IEA:Ensembl P positive regulation of peptidyl-tyrosine phosphorylation
GO:0010739 ISS:UniProtKB P positive regulation of protein kinase A signaling
GO:0001934 ISS:UniProtKB P positive regulation of protein phosphorylation
GO:2000534 IMP:UniProtKB P positive regulation of renal albumin absorption
GO:0009967 IDA:MGI P positive regulation of signal transduction
GO:0070208 IPI:MGI P protein heterotrimerization
GO:0051260 IDA:MGI P protein homooligomerization
GO:0072659 ISS:UniProtKB P protein localization to plasma membrane
GO:0010906 ISS:UniProtKB P regulation of glucose metabolic process
GO:0014823 IEA:Ensembl P response to activity
GO:0045471 IEA:Ensembl P response to ethanol
GO:0051384 IEA:Ensembl P response to glucocorticoid
GO:0009749 IDA:MGI P response to glucose
GO:0001666 IEA:Ensembl P response to hypoxia
GO:0070543 IEA:Ensembl P response to linoleic acid
GO:0007584 IEA:Ensembl P response to nutrient
GO:0009744 IEA:Ensembl P response to sucrose
GO:0034612 ISS:UniProtKB P response to tumor necrosis factor

KEGG Pathway Links

KEGG Pathway ID Description
mmu04152 AMPK signaling pathway
mmu04932 Non-alcoholic fatty liver disease (NAFLD)

Domain Information

InterPro Annotations

Accession Description
IPR028572 Adiponectin
IPR008160 Collagen triple helix repeat
IPR001073 Complement C1q protein
IPR008983 Tumour necrosis factor-like domain

UniProt Annotations

Entry Information

Gene Name
adiponectin, C1Q and collagen domain containing
Protein Entry
ADIPO_MOUSE
UniProt ID
Q60994
Species
Mouse

Comments

Comment Type Description
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. {ECO:0000269|PubMed:11479627, ECO:0000269|PubMed:11479628, ECO:0000269|PubMed:12840063, ECO:0000269|PubMed:15734737, ECO:0000269|PubMed:15760892}.
Induction During hormone-induced adipose differentiation and activated by insulin.
Interaction Self; NbExp=12; IntAct=EBI-7264589, EBI-7264589;
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.
Ptm 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. {ECO:0000269|PubMed:11912203}.
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. {ECO:0000250}.
Similarity Contains 1 C1q domain. {ECO:0000255|PROSITE- ProRule:PRU00368}.
Similarity Contains 1 collagen-like domain. {ECO:0000305}.
Subcellular Location Secreted.
Subunit 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 additionally 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. Interacts with CTRP9 via the C1q domain (heterotrimeric complex). {ECO:0000269|PubMed:15734737, ECO:0000269|PubMed:15760892, ECO:0000269|PubMed:16621799, ECO:0000269|PubMed:18787108, ECO:0000269|PubMed:19855092}.
Tissue Specificity Synthesized exclusively by adipocytes and secreted into plasma.

Identical and Related Proteins

Unique RefSeq proteins for LMP000440 (as displayed in Record Overview)

Protein GI Database Accession Length Protein Name
87252711 RefSeq NP_033735 247 adiponectin precursor

Identical Sequences to LMP000440 proteins

Reference Database Accession Length Protein Name
GI:87252711 DBBJ BAE22019.1 247 unnamed protein product [Mus musculus]
GI:87252711 EMBL CBL63520.1 247 unnamed protein product [Mus musculus]
GI:87252711 GenBank AAW70555.1 247 30 kDa adipocyte complement-related protein [Mus musculus]
GI:87252711 GenBank AAW82905.1 247 30 KDa adipocyte complement-related protein [Mus musculus]
GI:87252711 GenBank EDK97661.1 247 adiponectin, C1Q and collagen domain containing [Mus musculus]
GI:87252711 SwissProt Q60994.2 247 RecName: Full=Adiponectin; AltName: Full=30 kDa adipocyte complement-related protein; AltName: Full=Adipocyte complement-related 30 kDa protein; Short=ACRP30; AltName: Full=Adipocyte, C1q and collagen domain-containing protein; AltName: Full=Adipocyte-specific protein AdipoQ; Flags: Precursor [Mus musculus]

Related Sequences to LMP000440 proteins

Reference Database Accession Length Protein Name
GI:87252711 EMBL CAE01098.1 247 unnamed protein product [Mus musculus]
GI:87252711 GenBank AAA80543.1 247 30kDa adipocyte complement-related protein Acrp30 [Mus musculus]
GI:87252711 GenBank AAB35626.1 247 Acrp30=30 kda adipocyte complement-related protein [Mus sp.]
GI:87252711 GenBank AAQ32037.1 247 Sequence 4 from patent US 6566332
GI:87252711 GenBank AAQ41847.1 247 Sequence 4 from patent US 6579852
GI:87252711 GenBank ACJ98018.1 247 Sequence 4 from patent US 7419955