Q15848 (ADIPO_HUMAN) 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
Adipose most abundant gene transcript 1 protein
Short name=apM-1
Gelatin-binding protein

Gene names

Name:	ADIPOQ
Synonyms:	ACDC, ACRP30, APM1, GBP28

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	244 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.9
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 CTRP9A via the C1q domain (heterotrimeric complex) By similarity. Ref.10 Ref.11 Ref.12 Ref.13
Subcellular location	Secreted.
Tissue specificity	Synthesized exclusively by adipocytes and secreted into plasma.
Domain	The C1q domain is commonly called the globular domain.
Post-translational modification	Hydroxylated Lys-33 was not identified in Ref.11, probably due to poor representation of the N-terminal peptide in mass fingerprinting. 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 By similarity. Ref.11 Ref.12 O-glycosylated. Not N-glycosylated. O-linked glycans on hydroxylysines consist of Glc-Gal disaccharides bound to the oxygen atom of post-translationally added hydroxyl groups. Sialylated to varying degrees depending on tissue. Thr-22 appears to be the major site of sialylation. Higher sialylation found in SGBS adipocytes than in HEK fibroblasts. Sialylation is not required neither for heterodimerization nor for secretion. Not sialylated on the glycosylated hydroxylysines. Desialylated forms are rapidly cleared from the circulation. Ref.11 Ref.12
Polymorphism	Genetic variations in ADIPOQ influence the variance in adiponectin serum levels and define the adiponectin serum levels quantitative trait locus 1 (ADIPQTL1) [MIM:612556].
Involvement in disease	Adiponectin deficiency (ADPND) [MIM:612556]: A condition that results in very low concentrations of plasma adiponectin. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.14 Diabetes mellitus, non-insulin-dependent (NIDDM) [MIM:125853]: A multifactorial disorder of glucose homeostasis caused by a lack of sensitivity to the body's own insulin. Affected individuals usually have an obese body habitus and manifestations of a metabolic syndrome characterized by diabetes, insulin resistance, hypertension and hypertriglyceridemia. The disease results in long-term complications that affect the eyes, kidneys, nerves, and blood vessels. Note: Disease susceptibility is associated with variations affecting the gene represented in this entry.
Pharmaceutical use	Adiponectin might be used in the treatment of diabetes type 2 and insulin resistance.
Miscellaneous	Variants Arg-84 and Ser-90 show impaired formation of HMW complexes whereas variants Cys-112 and Thr-164 show impaired secretion of adiponectin in any form. 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 By similarity. In type 2 diabetic patients, both the ratios of HMW to total adiponectin and the degree of adiponectin glycosylation are significantly decreased as compared with healthy controls.
Sequence similarities	Contains 1 C1q domain. Contains 1 collagen-like domain.

Ontologies

Keywords
Cellular component	Secreted
Coding sequence diversity	Polymorphism
Disease	Diabetes mellitus Disease mutation Obesity
Domain	Collagen Repeat Signal
Molecular function	Hormone
PTM	Disulfide bond Glycoprotein Hydroxylation
Technical term	3D-structure Complete proteome Direct protein sequencing Pharmaceutical Reference proteome
Gene Ontology (GO)
Biological_process	adiponectin-mediated signaling pathway Inferred from electronic annotation. Source: Compara brown fat cell differentiation Inferred from sequence or structural similarity. Source: UniProtKB cellular response to cAMP Inferred from electronic annotation. Source: Compara cellular response to drug Inferred from sequence or structural similarity. Source: UniProtKB cellular response to epinephrine stimulus Inferred from electronic annotation. Source: Compara cellular response to insulin stimulus Inferred from sequence or structural similarity. Source: UniProtKB circadian rhythm Inferred from electronic annotation. Source: Compara detection of oxidative stress Inferred from sequence or structural similarity. Source: UniProtKB fatty acid beta-oxidation Inferred from sequence or structural similarity. Source: UniProtKB generation of precursor metabolites and energy Traceable author statement Ref.2. Source: ProtInc glucose homeostasis Inferred from sequence or structural similarity. Source: UniProtKB glucose metabolic process Inferred from sequence or structural similarity. Source: UniProtKB low-density lipoprotein particle clearance Inferred from direct assay PubMed 11222466. Source: BHF-UCL membrane depolarization Inferred from electronic annotation. Source: Compara membrane hyperpolarization Inferred from electronic annotation. Source: Compara negative regulation of DNA biosynthetic process Inferred from direct assay PubMed 12070119. Source: UniProtKB negative regulation of ERK1 and ERK2 cascade Inferred from direct assay PubMed 12070119. Source: UniProtKB negative regulation of I-kappaB kinase/NF-kappaB cascade Inferred from direct assay Ref.8. Source: BHF-UCL negative regulation of MAP kinase activity Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of blood pressure Inferred from direct assay PubMed 17327472. Source: UniProtKB negative regulation of eukaryotic cell surface binding Inferred from direct assay PubMed 12070119. Source: UniProtKB negative regulation of fat cell differentiation Inferred from direct assay PubMed 12021245. Source: BHF-UCL negative regulation of gluconeogenesis Inferred from sequence or structural similarity PubMed 12368907. Source: BHF-UCL negative regulation of granulocyte differentiation Inferred from direct assay Ref.7. Source: BHF-UCL negative regulation of heterotypic cell-cell adhesion Inferred from direct assay PubMed 10604883. Source: BHF-UCL negative regulation of hormone secretion Inferred from electronic annotation. Source: Compara negative regulation of inflammatory response Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of intracellular protein transport Inferred from direct assay PubMed 18431508. Source: UniProtKB negative regulation of low-density lipoprotein particle receptor biosynthetic process Inferred from direct assay PubMed 11222466. Source: BHF-UCL negative regulation of macrophage derived foam cell differentiation Inferred from direct assay PubMed 11222466. Source: BHF-UCL negative regulation of macrophage differentiation Inferred from direct assay Ref.7. Source: BHF-UCL negative regulation of metanephric mesenchymal cell migration Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of phagocytosis Inferred from direct assay Ref.7. Source: BHF-UCL negative regulation of platelet-derived growth factor receptor-alpha signaling pathway Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of protein autophosphorylation Inferred from direct assay PubMed 12070119. Source: UniProtKB negative regulation of smooth muscle cell migration Inferred from direct assay PubMed 12070119. Source: UniProtKB negative regulation of smooth muscle cell proliferation Inferred from direct assay PubMed 12070119. Source: UniProtKB negative regulation of synaptic transmission Inferred from direct assay PubMed 17327472. Source: UniProtKB negative regulation of transcription, DNA-dependent Inferred from direct assay PubMed 18431508. Source: UniProtKB negative regulation of tumor necrosis factor production Inferred from direct assay Ref.7. Source: BHF-UCL negative regulation of tumor necrosis factor-mediated signaling pathway Inferred from direct assay PubMed 10604883. Source: BHF-UCL positive regulation of I-kappaB kinase/NF-kappaB cascade Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of blood pressure Inferred from electronic annotation. Source: Compara positive regulation of cAMP-dependent protein kinase activity Inferred from direct assay PubMed 18431508PubMed 19524870. Source: UniProtKB positive regulation of cholesterol efflux Inferred from direct assay PubMed 18703020. Source: BHF-UCL positive regulation of fatty acid metabolic process Inferred from sequence or structural similarity PubMed 12368907. Source: BHF-UCL positive regulation of glucose import Inferred from sequence or structural similarity PubMed 12368907. Source: BHF-UCL positive regulation of glycogen (starch) synthase activity Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of interleukin-8 production Inferred from direct assay PubMed 19524870. Source: UniProtKB positive regulation of metanephric glomerular visceral epithelial cell development Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of monocyte chemotactic protein-1 production Inferred from direct assay PubMed 19524870. Source: UniProtKB positive regulation of myeloid cell apoptotic process Inferred from direct assay Ref.7. Source: BHF-UCL positive regulation of peptidyl-tyrosine phosphorylation Inferred from electronic annotation. Source: Compara positive regulation of protein kinase A signaling cascade Inferred from direct assay Ref.8. Source: BHF-UCL positive regulation of renal albumin absorption Inferred from direct assay PubMed 18431508. Source: UniProtKB protein heterotrimerization Inferred from electronic annotation. Source: Compara protein homooligomerization Inferred from sequence or structural similarity. Source: UniProtKB protein localization to plasma membrane Inferred from direct assay PubMed 18431508. 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 sequence or structural similarity PubMed 12368907. Source: BHF-UCL 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 direct assay PubMed 10604883. Source: BHF-UCL
Cellular_component	collagen Inferred from electronic annotation. Source: UniProtKB-KW endoplasmic reticulum Inferred from sequence or structural similarity. Source: UniProtKB extracellular space Inferred from direct assay PubMed 15585515PubMed 17327472. Source: UniProtKB
Molecular_function	cytokine activity Non-traceable author statement PubMed 12611609. Source: BHF-UCL eukaryotic cell surface binding Inferred from direct assay Ref.8. Source: BHF-UCL hormone activity Inferred from direct assay PubMed 11222466. Source: BHF-UCL identical protein binding Traceable author statement Ref.7. Source: BHF-UCL sialic acid binding Inferred from direct assay Ref.12. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 18

18

Ref.5 Ref.6

Chain

19 – 244

226

Adiponectin

PRO_0000003543

Regions

Domain

42 – 107

66

Collagen-like

Domain

108 – 244

137

C1q

Sites

Site

62

1

Not hydroxylated

Site

86

1

Not hydroxylated

Site

104

1

Not hydroxylated

Site

230

1

Not glycosylated

Amino acid modifications

Modified residue

33

1

5-hydroxylysine Probable

Modified residue

44

1

4-hydroxyproline Ref.11

Modified residue

47

1

4-hydroxyproline Ref.11

Modified residue

53

1

4-hydroxyproline Ref.11

Modified residue

65

1

5-hydroxylysine Ref.11

Modified residue

68

1

5-hydroxylysine Ref.11

Modified residue

71

1

4-hydroxyproline; partial Ref.11

Modified residue

76

1

4-hydroxyproline; partial Ref.11

Modified residue

77

1

5-hydroxylysine Ref.11

Modified residue

91

1

4-hydroxyproline Ref.11

Modified residue

95

1

4-hydroxyproline; partial Ref.11

Modified residue

101

1

5-hydroxylysine Ref.11

Glycosylation

21

1

O-linked (GalNAc...) Ref.12

Glycosylation

22

1

O-linked (GalNAc...) Ref.12

Glycosylation

65

1

O-linked (Gal...); partial Ref.11

Glycosylation

68

1

O-linked (Gal...); partial Ref.11

Glycosylation

77

1

O-linked (Gal...); partial Ref.11

Glycosylation

101

1

O-linked (Gal...); partial Ref.11

Disulfide bond

36

Interchain; in form MMW and form HMW Ref.10 Ref.11

Natural variations

Natural variant

84

1

G → R Does not form high molecular weight multimers. Ref.10 Ref.15 Ref.18

VAR_013273

Natural variant

90

1

G → S Does not form high molecular weight multimers. Ref.10 Ref.18

VAR_027395

Natural variant

111

1

Y → H. Ref.18
Corresponds to variant rs17366743 [ dbSNP | Ensembl ].

VAR_027396

Natural variant

112

1

R → C in ADPND; does not assemble into trimers resulting in impaired secretion from the cell. Ref.10 Ref.14 Ref.17

VAR_013274

Natural variant

117

1

V → M. Ref.15

VAR_013275

Natural variant

164

1

I → T Associated with low plasma adiponectin concentration and diabetes mellitus type 2; does not assemble into trimers resulting in impaired secretion from the cell. Ref.10 Ref.15 Ref.17

VAR_013276

Natural variant

221

1

R → S. Ref.15 Ref.17

VAR_013277

Natural variant

241

1

H → P. Ref.15 Ref.17

VAR_013278

Experimental info

Mutagenesis

20

1

T → A: No change in sialylated isoforms. Ref.12

Mutagenesis

21

1

T → A: Some loss of sialylated isoforms. Ref.12

Mutagenesis

22

1

T → A: Abolishes sialylated isoforms. Ref.12

Mutagenesis

33

1

K → R: No effect on formation of HMW multimers. Ref.11

Mutagenesis

36

1

C → S: Impaired formation of MMW and HMW multimers. Ref.10 Ref.11

Mutagenesis

65

1

K → R: Impaired formation of HMW multimers; when associated with R-68. Ref.11

Mutagenesis

68

1

K → R: Impaired formation of HMW multimers; when associated with R-65. Ref.11

Mutagenesis

77

1

K → R: Impaired formation of HMW multimers; when associated with R-101. Ref.11

Mutagenesis

101

1

K → R: Impaired formation of HMW multimers; when associated with R-77. Ref.11

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

244

Helix Strand Turn

Details...

Beta strand

114 – 118

5

Beta strand

134 – 137

4

Turn

145 – 147

3

Beta strand

156 – 177

22

Beta strand

180 – 187

8

Beta strand

195 – 205

11

Beta strand

210 – 216

7

Beta strand

220 – 225

6

Beta strand

233 – 241

9

Sequences

	Sequence		Length	Mass (Da)
	Q15848 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 64D8C6C1204B1018	FASTA	244	26,414
	10 20 30 40 50 60 MLLLGAVLLL LALPGHDQET TTQGPGVLLP LPKGACTGWM AGIPGHPGHN GAPGRDGRDG 70 80 90 100 110 120 TPGEKGEKGD PGLIGPKGDI GETGVPGAEG PRGFPGIQGR KGEPGEGAYV YRSAFSVGLE 130 140 150 160 170 180 TYVTIPNMPI RFTKIFYNQQ NHYDGSTGKF HCNIPGLYYF AYHITVYMKD VKVSLFKKDK 190 200 210 220 230 240 AMLFTYDQYQ ENNVDQASGS VLLHLEVGDQ VWLQVYGEGE RNGLYADNDN DSTFTGFLLY HDTN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"cDNA cloning and expression of a novel adipose specific collagen-like factor, apM1 (AdiPose Most abundant Gene transcript 1)." Maeda K., Okubo K., Shimomura I., Funahashi T., Matsuzawa Y., Matsubara K. Biochem. Biophys. Res. Commun. 221:286-289(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Adipose tissue.
[2]	"Organization of the gene for gelatin-binding protein (GBP28)." Saito K., Tobe T., Minoshima S., Asakawa S., Sumiya J., Yoda M., Nakano Y., Shimizu N., Tomita M. Gene 229:67-73(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"The human apM-1, an adipocyte-specific gene linked to the family of TNF's and to genes expressed in activated T cells, is mapped to chromosome 1q21.3-q23, a susceptibility locus identified for familial combined hyperlipidemia (FCH)." Schaeffler A., Orso E., Palitzsch K.D., Buechler C., Drobnik W., Fuerst A., Schoelmerich J., Schmitz G. Biochem. Biophys. Res. Commun. 260:416-425(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]	"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].
[5]	"Signal peptide prediction based on analysis of experimentally verified cleavage sites." Zhang Z., Henzel W.J. Protein Sci. 13:2819-2824(2004) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 19-33.
[6]	"Isolation and characterization of GBP28, a novel gelatin-binding protein purified from human plasma." Nakano Y., Tobe T., Choi-Miura N.H., Mazda T., Tomita M. J. Biochem. 120:803-812(1996) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF N-TERMINUS, PARTIAL PROTEIN SEQUENCE.
[7]	"Adiponectin, a new member of the family of soluble defense collagens, negatively regulates the growth of myelomonocytic progenitors and the functions of macrophages." Yokota T., Oritani K., Takahashi I., Ishikawa J., Matsuyama A., Ouchi N., Kihara S., Funahashi T., Tenner A.J., Tomiyama Y., Matsuzawa Y. Blood 96:1723-1732(2000) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION.
[8]	"Adiponectin, an adipocyte-derived plasma protein, inhibits endothelial NF-kappaB signaling through a cAMP-dependent pathway." Ouchi N., Kihara S., Arita Y., Okamoto Y., Maeda K., Kuriyama H., Hotta K., Nishida M., Takahashi M., Muraguchi M., Ohmoto Y., Nakamura T., Yamashita S., Funahashi T., Matsuzawa Y. Circulation 102:1296-1301(2000) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION.
[9]	"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.
[10]	"Impaired multimerization of human adiponectin mutants associated with diabetes. Molecular structure and multimer formation of adiponectin." Waki H., Yamauchi T., Kamon J., Ito Y., Uchida S., Kita S., Hara K., Hada Y., Vasseur F., Froguel P., Kimura S., Nagai R., Kadowaki T. J. Biol. Chem. 278:40352-40363(2003) [PubMed] [Europe PMC] [Abstract] Cited for: SUBUNIT, DISULFIDE BOND, MUTAGENESIS OF CYS-36, CHARACTERIZATION OF VARIANTS ARG-84; SER-90; CYS-112 AND THR-164.
[11]	"Adiponectin multimerization is dependent on conserved lysines in the collagenous domain: evidence for regulation of multimerization by alterations in posttranslational modifications." Richards A.A., Stephens T., Charlton H.K., Jones A., Macdonald G.A., Prins J.B., Whitehead J.P. Mol. Endocrinol. 20:1673-1687(2006) [PubMed] [Europe PMC] [Abstract] Cited for: SUBUNIT, HYDROXYLATION AT PRO-44; PRO-47; PRO-53; LYS-65; LYS-68; PRO-71; PRO-76; LYS-77; PRO-91; PRO-95 AND LYS-101, GLYCOSYLATION AT LYS-65; LYS-68; LYS-77 AND LYS-101, DISULFIDE BOND, LACK OF HYDROXYLATION AT PRO-62; PRO-86 AND PRO-104, LACK OF GLYCOSYLATION AT ASN-230, MUTAGENESIS OF LYS-33; CYS-36; LYS-65; LYS-68; LYS-77 AND LYS-101, MASS SPECTROMETRY.
[12]	"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-21 AND THR-22, SUBUNIT, MASS SPECTROMETRY, MUTAGENESIS OF THR-20; THR-21 AND THR-22.
[13]	"Crystal structure of a single-chain trimer of human adiponectin globular domain." Min X., Lemon B., Tang J., Liu Q., Zhang R., Walker N., Li Y., Wang Z. FEBS Lett. 586:912-917(2012) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 104-244, SUBUNIT.
[14]	"Genomic structure and mutations in adipose-specific gene, adiponectin." Takahashi M., Arita Y., Yamagata K., Matsukawa Y., Okutomi K., Horie M., Shimomura I., Hotta K., Kuriyama H., Kihara S., Nakamura T., Yamashita S., Funahashi T., Matsuzawa Y. Int. J. Obes. Relat. Metab. Disord. 24:861-868(2000) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT ADPND CYS-112.
[15]	"Genetic variation in the gene encoding adiponectin is associated with an increased risk of type 2 diabetes in the Japanese population." Hara K., Boutin P., Mori Y., Tobe K., Dina C., Yasuda K., Yamauchi T., Otabe S., Okada T., Eto K., Kadowaki H., Hagura R., Akanuma Y., Yazaki Y., Nagai R., Taniyama M., Matsubara K., Yoda M. , Nakano Y., Kimura S., Tomita M., Kimura S., Ito C., Froguel P., Kadowaki T. Diabetes 51:536-540(2002) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS ARG-84; MET-117; THR-164; SER-221 AND PRO-241.
[16]	Erratum Hara K., Boutin P., Mori Y., Tobe K., Dina C., Yasuda K., Yamauchi T., Otabe S., Okada T., Eto K., Kadowaki H., Hagura R., Akanuma Y., Yazaki Y., Nagai R., Taniyama M., Matsubara K., Yoda M. , Nakano Y., Kimura S., Tomita M., Kimura S., Ito C., Froguel P., Kadowaki T. Diabetes 51:1294-1294(2002)
[17]	"Association of adiponectin mutation with type 2 diabetes: a candidate gene for the insulin resistance syndrome." Kondo H., Shimomura I., Matsukawa Y., Kumada M., Takahashi M., Matsuda M., Ouchi N., Kihara S., Kawamoto T., Sumitsuji S., Funahashi T., Matsuzawa Y. Diabetes 51:2325-2328(2002) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS CYS-112; THR-164; SER-221 AND PRO-241, ASSOCIATION WITH LOW PLASMA ADIPONECTIN CONCENTRATION AND DIABETES MELLITUS TYPE 2.
[18]	"Single-nucleotide polymorphism haplotypes in the both proximal promoter and exon 3 of the APM1 gene modulate adipocyte-secreted adiponectin hormone levels and contribute to the genetic risk for type 2 diabetes in French Caucasians." Vasseur F., Helbecque N., Dina C., Lobbens S., Delannoy V., Gaget S., Boutin P., Vaxillaire M., Lepretre F., Dupont S., Hara K., Clement K., Bihain B., Kadowaki T., Froguel P. Hum. Mol. Genet. 11:2607-2614(2002) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS ARG-84; SER-90 AND HIS-111.
+	Additional computationally mapped references.

Web resources

Wikipedia

Adiponectin entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

D45371 mRNA. Translation: BAA08227.1.
AB012165 Genomic DNA. Translation: BAA86716.1.
AJ131460, AJ131461 Genomic DNA. Translation: CAB52413.1.
BC054496 mRNA. Translation: AAH54496.1.
BC096308 mRNA. Translation: AAH96308.1.
BC096309 mRNA. Translation: AAH96309.1.
BC096310 mRNA. Translation: AAH96310.1.
BC096311 mRNA. Translation: AAH96311.1.

IPI

IPI00020019.

PIR

JC4708.

RefSeq

NP_001171271.1. NM_001177800.1.
NP_004788.1. NM_004797.3.

UniGene

Hs.80485.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
4DOU	X-ray	2.00	A	104-244	[»]

ProteinModelPortal

Q15848.

ModBase

Search...

Protein-protein interaction databases

STRING

9606.ENSP00000320709.

Polymorphism databases

DMDM

2493789.

Proteomic databases

PaxDb

Q15848.

PeptideAtlas

Q15848.

PRIDE

Q15848.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000320741; ENSP00000320709; ENSG00000181092.
ENST00000412955; ENSP00000405611; ENSG00000181092.
ENST00000444204; ENSP00000389814; ENSG00000181092.

GeneID

9370.

KEGG

hsa:9370.

UCSC

uc003fra.3. human.

Organism-specific databases

CTD

9370.

GeneCards

GC03P186560.

HGNC

HGNC:13633. ADIPOQ.

HPA

CAB046467.

MIM

125853. phenotype.
605441. gene.
612556. phenotype.

neXtProt

NX_Q15848.

PharmGKB

PA134933118.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG136972.

HOGENOM

HOG000085653.

HOVERGEN

HBG108220.

InParanoid

Q15848.

KO

K07296.

OMA

LFTYDQY.

OrthoDB

EOG4FXR88.

PhylomeDB

Q15848.

Enzyme and pathway databases

Reactome

REACT_111045. Developmental Biology.

Gene expression databases

ArrayExpress

Q15848.

Bgee

Q15848.

CleanEx

HS_ADIPOQ.

Genevestigator

Q15848.

GermOnline

ENSG00000181092. Homo sapiens.

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

Search...

Other

ChiTaRS

ADIPOQ. human.

GenomeRNAi

9370.

NextBio

35094.

SOURCE

Search...

Entry information

Entry name

ADIPO_HUMAN

Accession

Primary (citable) accession number: Q15848
Secondary accession number(s): Q58EX9

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1996
Last modified:	May 1, 2013
This is version 137 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.