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Q60994 (ADIPO_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 137. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Adiponectin
Alternative name(s):
30 kDa adipocyte complement-related protein
Adipocyte complement-related 30 kDa protein
Short name=ACRP30
Adipocyte, C1q and collagen domain-containing protein
Adipocyte-specific protein AdipoQ
Gene names
Name:Adipoq
Synonyms:Acdc, Acrp30, Apm1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length247 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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.11 Ref.12 Ref.13 Ref.14 Ref.15

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 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). Ref.14 Ref.15 Ref.16 Ref.17 Ref.18

Subcellular location

Secreted.

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.9 Ref.10 Ref.18

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. Ref.9 Ref.10 Ref.18

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

Keywords
   Cellular componentSecreted
   DomainCollagen
Repeat
Signal
   Molecular functionHormone
   PTMDisulfide bond
Glycoprotein
Hydroxylation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processadiponectin-activated signaling pathway

Inferred from electronic annotation. Source: Ensembl

brown fat cell differentiation

Inferred from direct assay PubMed 18492766. Source: MGI

cellular response to cAMP

Inferred from electronic annotation. Source: Ensembl

cellular response to drug

Inferred from direct assay PubMed 19109165. Source: UniProtKB

cellular response to epinephrine stimulus

Inferred from electronic annotation. Source: Ensembl

cellular response to insulin stimulus

Inferred from genetic interaction PubMed 17693256. Source: MGI

circadian rhythm

Inferred from electronic annotation. Source: Ensembl

detection of oxidative stress

Inferred from mutant phenotype PubMed 18431508. Source: UniProtKB

fatty acid beta-oxidation

Inferred from mutant phenotype PubMed 12151381. Source: MGI

fatty acid oxidation

Inferred from direct assay PubMed 12802337. Source: MGI

glucose homeostasis

Inferred from direct assay Ref.12PubMed 12068289. Source: MGI

glucose metabolic process

Inferred from direct assay Ref.12PubMed 12068289PubMed 12802337. Source: MGI

low-density lipoprotein particle clearance

Inferred from sequence or structural similarity. Source: UniProtKB

membrane depolarization

Inferred from electronic annotation. Source: Ensembl

membrane hyperpolarization

Inferred from electronic annotation. Source: Ensembl

negative regulation of DNA biosynthetic process

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of ERK1 and ERK2 cascade

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of I-kappaB kinase/NF-kappaB signaling

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of MAP kinase activity

Inferred from direct assay PubMed 19460854. Source: UniProtKB

negative regulation of blood pressure

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of cell migration

Inferred from direct assay PubMed 19460854. Source: UniProtKB

negative regulation of fat cell differentiation

Inferred from direct assay PubMed 12021245. Source: BHF-UCL

negative regulation of gluconeogenesis

Inferred from direct assay Ref.12. Source: MGI

negative regulation of granulocyte differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of heterotypic cell-cell adhesion

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of hormone secretion

Inferred from electronic annotation. Source: Ensembl

negative regulation of inflammatory response

Inferred from direct assay PubMed 19109165. Source: UniProtKB

negative regulation of intracellular protein transport

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of low-density lipoprotein particle receptor biosynthetic process

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of macrophage derived foam cell differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of macrophage differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of metanephric mesenchymal cell migration

Inferred from direct assay PubMed 19460854. Source: UniProtKB

negative regulation of phagocytosis

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of platelet-derived growth factor receptor signaling pathway

Inferred from direct assay PubMed 19460854. Source: UniProtKB

negative regulation of platelet-derived growth factor receptor-alpha signaling pathway

Inferred from direct assay PubMed 19460854. Source: UniProtKB

negative regulation of protein autophosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of receptor binding

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of smooth muscle cell migration

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of smooth muscle cell proliferation

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of synaptic transmission

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of transcription, DNA-templated

Inferred from mutant phenotype PubMed 18431508. Source: UniProtKB

negative regulation of tumor necrosis factor production

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of tumor necrosis factor-mediated signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of I-kappaB kinase/NF-kappaB signaling

Inferred from direct assay PubMed 12087086PubMed 14522956. Source: MGI

positive regulation of blood pressure

Inferred from electronic annotation. Source: Ensembl

positive regulation of cAMP-dependent protein kinase activity

Inferred from mutant phenotype PubMed 18431508. Source: UniProtKB

positive regulation of cellular protein metabolic process

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of cholesterol efflux

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of fatty acid metabolic process

Inferred from mutant phenotype PubMed 12068289. Source: MGI

positive regulation of glucose import

Inferred from direct assay PubMed 12068289. Source: MGI

positive regulation of glycogen (starch) synthase activity

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of interleukin-8 production

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of metanephric glomerular visceral epithelial cell development

Inferred from mutant phenotype PubMed 18431508. Source: UniProtKB

positive regulation of monocyte chemotactic protein-1 production

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of myeloid cell apoptotic process

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of peptidyl-tyrosine phosphorylation

Inferred from electronic annotation. Source: Ensembl

positive regulation of protein kinase A signaling

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of protein phosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of renal albumin absorption

Inferred from mutant phenotype PubMed 18431508. Source: UniProtKB

positive regulation of signal transduction

Inferred from direct assay PubMed 12087086PubMed 14522956. Source: MGI

protein heterotrimerization

Inferred from physical interaction PubMed 18783346. Source: MGI

protein homooligomerization

Inferred from direct assay PubMed 12087086PubMed 14522956PubMed 15210937Ref.1. Source: MGI

protein localization to plasma membrane

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of glucose metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

response to activity

Inferred from electronic annotation. Source: Ensembl

response to ethanol

Inferred from electronic annotation. Source: Ensembl

response to glucocorticoid

Inferred from electronic annotation. Source: Ensembl

response to glucose

Inferred from direct assay PubMed 12068289. Source: MGI

response to hypoxia

Inferred from electronic annotation. Source: Ensembl

response to linoleic acid

Inferred from electronic annotation. Source: Ensembl

response to nutrient

Inferred from electronic annotation. Source: Ensembl

response to sucrose

Inferred from electronic annotation. Source: Ensembl

response to tumor necrosis factor

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentcell periphery

Inferred from sequence or structural similarity. Source: UniProtKB

cell surface

Inferred from sequence or structural similarity. Source: BHF-UCL

collagen

Inferred from electronic annotation. Source: UniProtKB-KW

endoplasmic reticulum

Inferred from direct assay PubMed 10444069. Source: MGI

extracellular space

Inferred from direct assay PubMed 10444069Ref.12PubMed 12087086PubMed 14522956PubMed 14578283PubMed 15210937PubMed 15231994PubMed 17693256Ref.1. Source: MGI

perinuclear region of cytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionhormone activity

Inferred from direct assay Ref.12. Source: MGI

identical protein binding

Inferred from physical interaction PubMed 17292892PubMed 21536037PubMed 22583869. Source: IntAct

receptor binding

Inferred from direct assay PubMed 12087086PubMed 12802337PubMed 14522956. Source: MGI

sialic acid binding

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

itself12EBI-7264589,EBI-7264589

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1717 Ref.9
Chain18 – 247230Adiponectin
PRO_0000003544

Regions

Domain45 – 11066Collagen-like
Domain111 – 247137C1q

Sites

Site791Not hydroxylated
Site981Not hydroxylated
Site1071Not hydroxylated
Site2331Not glycosylated

Amino acid modifications

Modified residue4714-hydroxyproline By similarity
Modified residue5014-hydroxyproline By similarity
Modified residue5614-hydroxyproline By similarity
Modified residue6815-hydroxylysine Ref.9
Modified residue7115-hydroxylysine Ref.9
Modified residue8015-hydroxylysine Ref.9
Modified residue9414-hydroxyproline Ref.9
Modified residue10415-hydroxylysine Ref.9
Glycosylation231O-linked (GalNAc...) Probable
Glycosylation241O-linked (GalNAc...) Probable
Glycosylation681O-linked (Gal...) Ref.9
Glycosylation711O-linked (Gal...) Ref.9
Glycosylation801O-linked (Gal...) Ref.9
Glycosylation1041O-linked (Gal...) Ref.9
Disulfide bond39Interchain By similarity

Experimental info

Mutagenesis391C → A: No change in the interaction with CTRP9. Ref.17
Mutagenesis681K → R: Impaired formation of HMW multimers; when associated with R-71; R-80 and R-104. Ref.16
Mutagenesis711K → R: Impaired formation of HMW multimers; when associated with R-68; R-80 and R-104. Ref.16
Mutagenesis801K → R: Impaired formation of HMW multimers; when associated with R-68; R-71 and R-104. Ref.16
Mutagenesis1041K → R: Impaired formation of HMW multimers; when associated with R-68; R-71 and R-80. Ref.16
Sequence conflict501P → S in AAB06706. Ref.2
Sequence conflict741A → S in AAB06706. Ref.2
Sequence conflict1131V → M in AAA80543. Ref.1
Sequence conflict1131V → M in AAK13417. Ref.3
Sequence conflict1171A → G in AAB06706. Ref.2
Sequence conflict1481G → N in AAB06706. Ref.2
Sequence conflict2431Y → F in AAB06706. Ref.2

Secondary structure

....................... 247
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q60994 [UniParc].

Last modified October 3, 2012. Version 2.
Checksum: 0ECC687D9A8E8123

FASTA24726,809
        10         20         30         40         50         60 
MLLLQALLFL LILPSHAEDD VTTTEELAPA LVPPPKGTCA GWMAGIPGHP GHNGTPGRDG 

        70         80         90        100        110        120 
RDGTPGEKGE KGDAGLLGPK GETGDVGMTG AEGPRGFPGT PGRKGEPGEA AYVYRSAFSV 

       130        140        150        160        170        180 
GLETRVTVPN VPIRFTKIFY NQQNHYDGST GKFYCNIPGL YYFSYHITVY MKDVKVSLFK 

       190        200        210        220        230        240 
KDKAVLFTYD QYQEKNVDQA SGSVLLHLEV GDQVWLQVYG DGDHNGLYAD NVNDSTFTGF 


LLYHDTN 

« Hide

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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"Cloning of murine adipocyte complement-related protein of 30 KDa from white adipose tissue."
Wang S.F., Han P.Z., Mu C.J., Zhao M.H.
Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: C57BL/6J and IRM-2.
Tissue: White adipose tissue.
[5]"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. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Heart and Thymus.
[6]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[7]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Thymus.
[9]"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] [Europe PMC] [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, IDENTIFICATION BY MASS SPECTROMETRY.
[10]"Identification and adipocyte differentiation-dependent expression of the unique disialic acid residue in an adipose tissue-specific glycoprotein, adipo Q."
Sato C., Yasukawa Z., Honda N., Matsuda T., Kitajima K.
J. Biol. Chem. 276:28849-28856(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE OF CARBOHYDRATES.
[11]"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. expand/collapse author list , Nakano Y., Tobe K., Nagai R., Kimura S., Tomita M., Froguel P., Kadowaki T.
Nat. Med. 7:941-946(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[12]"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] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[13]"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] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[14]"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] [Europe PMC] [Abstract]
Cited for: SUBUNIT, FUNCTION.
[15]"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] [Europe PMC] [Abstract]
Cited for: SUBUNIT, FUNCTION.
[16]"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] [Europe PMC] [Abstract]
Cited for: SUBUNIT, MUTAGENESIS OF LYS-68; LYS-71; LYS-80 AND LYS-104.
[17]"Identification and characterization of CTRP9, a novel secreted glycoprotein, from adipose tissue that reduces serum glucose in mice and forms heterotrimers with adiponectin."
Wong G.W., Krawczyk S.A., Kitidis-Mitrokostas C., Ge G., Spooner E., Hug C., Gimeno R., Lodish H.F.
FASEB J. 23:241-258(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT, INTERACTION WITH CTRP9, MUTAGENESIS OF CYS-39.
[18]"Sialic acid modification of adiponectin is not required for multimerization or secretion but determines half-life in circulation."
Richards A.A., Colgrave M.L., Zhang J., Webster J., Simpson F., Preston E., Wilks D., Hoehn K.L., Stephenson M., Macdonald G.A., Prins J.B., Cooney G.J., Xu A., Whitehead J.P.
Mol. Endocrinol. 24:229-239(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT THR-23 AND THR-24, SUBUNIT.
[19]"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] [Europe PMC] [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.
AY749429 mRNA. Translation: AAW70555.1.
AY754346 mRNA. Translation: AAW82905.1.
AK003138 mRNA. Translation: BAB22597.1.
AK134112 mRNA. Translation: BAE22019.1.
AC125396 Genomic DNA. No translation available.
CH466521 Genomic DNA. Translation: EDK97661.1.
BC028770 mRNA. Translation: AAH28770.1.
RefSeqNP_033735.3. NM_009605.4.
UniGeneMm.3969.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1C28X-ray2.10A/B/C114-247[»]
1C3HX-ray2.10A/B/C/D/E/F111-247[»]
ProteinModelPortalQ60994.
SMRQ60994. Positions 28-99, 111-247.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid197940. 4 interactions.
DIPDIP-44111N.
IntActQ60994. 2 interactions.
MINTMINT-4563800.

Proteomic databases

PaxDbQ60994.
PRIDEQ60994.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000023593; ENSMUSP00000023593; ENSMUSG00000022878.
GeneID11450.
KEGGmmu:11450.
UCSCuc007ytk.1. mouse.

Organism-specific databases

CTD9370.
MGIMGI:106675. Adipoq.

Phylogenomic databases

eggNOGNOG136972.
GeneTreeENSGT00750000117356.
HOGENOMHOG000085653.
HOVERGENHBG108220.
InParanoidQ60994.
KOK07296.
OMALFTYDQY.
OrthoDBEOG70ZZPW.
TreeFamTF329591.

Gene expression databases

ArrayExpressQ60994.
CleanExMM_ADIPOQ.
GenevestigatorQ60994.

Family and domain databases

Gene3D2.60.120.40. 1 hit.
InterProIPR028572. Adiponectin.
IPR001073. C1q.
IPR008160. Collagen.
IPR008983. Tumour_necrosis_fac-like_dom.
[Graphical view]
PANTHERPTHR24022:SF2. PTHR24022:SF2. 1 hit.
PfamPF00386. C1q. 1 hit.
PF01391. Collagen. 1 hit.
[Graphical view]
PRINTSPR00007. COMPLEMNTC1Q.
SMARTSM00110. C1Q. 1 hit.
[Graphical view]
SUPFAMSSF49842. SSF49842. 1 hit.
PROSITEPS50871. C1Q. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ60994.
NextBio278770.
PROQ60994.
SOURCESearch...

Entry information

Entry nameADIPO_MOUSE
AccessionPrimary (citable) accession number: Q60994
Secondary accession number(s): Q62400, Q6GTX4, Q9DC68
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: October 3, 2012
Last modified: April 16, 2014
This is version 137 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot