Q60994 (ADIPO_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › 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.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 aditionally 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 component	Secreted
Domain	Collagen Repeat Signal
Molecular function	Hormone
PTM	Disulfide bond Glycoprotein Hydroxylation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	adiponectin-mediated signaling pathway Inferred from electronic annotation. Source: Compara brown fat cell differentiation Inferred from direct assay PubMed 18492766. Source: MGI cellular response to cAMP Inferred from electronic annotation. Source: Compara cellular response to drug Inferred from direct assay PubMed 19109165. Source: UniProtKB cellular response to epinephrine stimulus Inferred from electronic annotation. Source: Compara cellular response to insulin stimulus Inferred from genetic interaction PubMed 17693256. Source: MGI circadian rhythm Inferred from electronic annotation. Source: Compara detection of oxidative stress Inferred from mutant phenotype PubMed 18431508. Source: UniProtKB fatty acid beta-oxidation Inferred from mutant phenotype PubMed 12151381. 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: Compara membrane hyperpolarization Inferred from electronic annotation. Source: Compara 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 cascade 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 eukaryotic cell surface binding Inferred from sequence or structural similarity. 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: Compara 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-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 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-dependent 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 cascade Inferred from direct assay PubMed 12087086PubMed 14522956. Source: MGI positive regulation of blood pressure Inferred from electronic annotation. Source: Compara positive regulation of cAMP-dependent protein kinase activity Inferred from mutant phenotype PubMed 18431508. Source: UniProtKB positive regulation of cholesterol efflux Inferred from sequence or structural similarity. Source: UniProtKB 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: Compara positive regulation of protein kinase A signaling cascade Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of renal albumin absorption Inferred from mutant phenotype PubMed 18431508. Source: UniProtKB 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 response to activity Inferred from electronic annotation. Source: Compara response to ethanol Inferred from electronic annotation. Source: Compara response to glucocorticoid stimulus Inferred from electronic annotation. Source: Compara response to glucose stimulus Inferred from direct assay PubMed 12068289. Source: MGI response to hypoxia Inferred from electronic annotation. Source: Compara response to linoleic acid Inferred from electronic annotation. Source: Compara response to nutrient Inferred from electronic annotation. Source: Compara response to sucrose stimulus Inferred from electronic annotation. Source: Compara response to tumor necrosis factor Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	cell periphery Inferred from sequence or structural similarity. Source: UniProtKB 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_function	eukaryotic cell surface binding Inferred from sequence or structural similarity. Source: UniProtKB hormone activity Inferred from direct assay Ref.12. Source: MGI sialic acid binding Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 17

17

Ref.9

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.9

Modified residue

71

1

5-hydroxylysine Ref.9

Modified residue

80

1

5-hydroxylysine Ref.9

Modified residue

94

1

4-hydroxyproline Ref.9

Modified residue

104

1

5-hydroxylysine Ref.9

Glycosylation

23

1

O-linked (GalNAc...) Probable

Glycosylation

24

1

O-linked (GalNAc...) Probable

Glycosylation

68

1

O-linked (Gal...) Ref.9

Glycosylation

71

1

O-linked (Gal...) Ref.9

Glycosylation

80

1

O-linked (Gal...) Ref.9

Glycosylation

104

1

O-linked (Gal...) Ref.9

Disulfide bond

39

Interchain By similarity

Experimental info

Mutagenesis

39

1

C → A: No change in the interaction with CTRP9. Ref.17

Mutagenesis

68

1

K → R: Impaired formation of HMW multimers; when associated with R-71; R-80 and R-104. Ref.16

Mutagenesis

71

1

K → R: Impaired formation of HMW multimers; when associated with R-68; R-80 and R-104. Ref.16

Mutagenesis

80

1

K → R: Impaired formation of HMW multimers; when associated with R-68; R-71 and R-104. Ref.16

Mutagenesis

104

1

K → R: Impaired formation of HMW multimers; when associated with R-68; R-71 and R-80. Ref.16

Sequence conflict

50

1

P → S in AAB06706. Ref.2

Sequence conflict

74

1

A → S in AAB06706. Ref.2

Sequence conflict

113

1

V → M in AAA80543. Ref.1

Sequence conflict

113

1

V → M in AAK13417. Ref.3

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

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

247

Helix Strand Turn

Details...

Beta strand

117 – 121

5

Beta strand

130 – 132

3

Beta strand

137 – 140

4

Turn

148 – 150

3

Beta strand

152 – 154

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

	Sequence		Length	Mass (Da)
	Q60994 [UniParc]. Last modified October 3, 2012. Version 2. Checksum: 0ECC687D9A8E8123	FASTA	247	26,809
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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, 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. , 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.

IPI

IPI00311383.

RefSeq

NP_033735.3. NM_009605.4.

UniGene

Mm.3969.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1C28	X-ray	2.10	A/B/C	114-247	[»]
1C3H	X-ray	2.10	A/B/C/D/E/F	111-247	[»]

ProteinModelPortal

Q60994.

SMR

Q60994. Positions 111-247.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-44111N.

MINT

MINT-4563800.

Proteomic databases

PaxDb

Q60994.

PRIDE

Q60994.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000023593; ENSMUSP00000023593; ENSMUSG00000022878.

GeneID

11450.

KEGG

mmu:11450.

Organism-specific databases

CTD

9370.

MGI

MGI:106675. Adipoq.

Phylogenomic databases

eggNOG

NOG136972.

GeneTree

ENSGT00700000104099.

HOGENOM

HOG000085653.

HOVERGEN

HBG108220.

InParanoid

Q60994.

KO

K07296.

OMA

LFTYDQY.

OrthoDB

EOG4FXR88.

Gene expression databases

CleanEx

MM_ADIPOQ.

Genevestigator

Q60994.

GermOnline

ENSMUSG00000022878. Mus musculus.

Family and domain databases

Gene3D

2.60.120.40. 1 hit.

InterPro

IPR001073. C1q.
IPR008160. Collagen.
IPR008983. Tumour_necrosis_fac-like_dom.
[Graphical view]

Pfam

PF00386. C1q. 1 hit.
PF01391. Collagen. 1 hit.
[Graphical view]

PRINTS

PR00007. COMPLEMNTC1Q.

SMART

SM00110. C1Q. 1 hit.
[Graphical view]

SUPFAM

SSF49842. TNF_like. 1 hit.

PROSITE

PS50871. C1Q. 1 hit.
[Graphical view]

ProtoNet

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Other

EvolutionaryTrace

Q60994.

NextBio

278770.

SOURCE

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Entry information

Entry name

ADIPO_MOUSE

Accession

Primary (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:	May 1, 2013
This is version 128 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program