Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q15848 (ADIPO_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 146. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·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
Adipose most abundant gene transcript 1 protein
Short name=apM-1
Gelatin-binding protein
Gene names
Name:ADIPOQ
Synonyms:ACDC, ACRP30, APM1, GBP28
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length244 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.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 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 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 componentSecreted
   Coding sequence diversityPolymorphism
   DiseaseDiabetes mellitus
Disease mutation
Obesity
   DomainCollagen
Repeat
Signal
   Molecular functionHormone
   PTMDisulfide bond
Glycoprotein
Hydroxylation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Pharmaceutical
Reference proteome
Gene Ontology (GO)
   Biological_processadiponectin-activated signaling pathway

Inferred from electronic annotation. Source: Ensembl

brown fat cell differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

cellular response to cAMP

Inferred from electronic annotation. Source: Ensembl

cellular response to drug

Inferred from sequence or structural similarity. Source: UniProtKB

cellular response to epinephrine stimulus

Inferred from electronic annotation. Source: Ensembl

cellular response to insulin stimulus

Inferred from sequence or structural similarity. Source: UniProtKB

circadian rhythm

Inferred from electronic annotation. Source: Ensembl

detection of oxidative stress

Inferred from sequence or structural similarity. Source: UniProtKB

fatty acid beta-oxidation

Inferred from sequence or structural similarity. Source: UniProtKB

fatty acid 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: Ensembl

membrane hyperpolarization

Inferred from electronic annotation. Source: Ensembl

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 signaling

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 cell migration

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 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: Ensembl

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 signaling pathway

Inferred from direct assay PubMed 12070119. Source: UniProtKB

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 receptor binding

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-templated

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 signaling

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of blood pressure

Inferred from electronic annotation. Source: Ensembl

positive regulation of cAMP-dependent protein kinase activity

Inferred from direct assay PubMed 18431508PubMed 19524870. Source: UniProtKB

positive regulation of cellular protein metabolic process

Inferred from direct assay PubMed 18703020. Source: BHF-UCL

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: Ensembl

positive regulation of protein kinase A signaling

Inferred from direct assay Ref.8. Source: BHF-UCL

positive regulation of protein phosphorylation

Inferred from direct assay PubMed 18431508. Source: UniProtKB

positive regulation of renal albumin absorption

Inferred from direct assay PubMed 18431508. Source: UniProtKB

positive regulation of signal transduction

Inferred from sequence or structural similarity PubMed 12368907. Source: BHF-UCL

protein heterotrimerization

Inferred from electronic annotation. Source: Ensembl

protein homooligomerization

Inferred from sequence or structural similarity. Source: UniProtKB

protein localization to plasma membrane

Inferred from direct assay PubMed 18431508. Source: UniProtKB

regulation of glucose metabolic process

Inferred from direct assay PubMed 17327472. 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 sequence or structural similarity PubMed 12368907. Source: BHF-UCL

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 direct assay PubMed 10604883. Source: BHF-UCL

   Cellular_componentcell surface

Inferred from direct assay Ref.8. Source: BHF-UCL

collagen

Inferred from electronic annotation. Source: UniProtKB-KW

endoplasmic reticulum

Inferred from sequence or structural similarity. Source: UniProtKB

extracellular region

Traceable author statement. Source: Reactome

extracellular space

Inferred from direct assay PubMed 15585515PubMed 17327472. Source: UniProtKB

   Molecular_functioncytokine activity

Non-traceable author statement PubMed 12611609. 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

protein homodimerization activity

Inferred from physical interaction PubMed 12021245. Source: BHF-UCL

receptor binding

Inferred from sequence or structural similarity. Source: UniProtKB

sialic acid binding

Inferred from direct assay Ref.12. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 Ref.5 Ref.6
Chain19 – 244226Adiponectin
PRO_0000003543

Regions

Domain42 – 10766Collagen-like
Domain108 – 244137C1q

Sites

Site621Not hydroxylated
Site861Not hydroxylated
Site1041Not hydroxylated
Site2301Not glycosylated

Amino acid modifications

Modified residue3315-hydroxylysine Probable
Modified residue4414-hydroxyproline Ref.11
Modified residue4714-hydroxyproline Ref.11
Modified residue5314-hydroxyproline Ref.11
Modified residue6515-hydroxylysine Ref.11
Modified residue6815-hydroxylysine Ref.11
Modified residue7114-hydroxyproline; partial Ref.11
Modified residue7614-hydroxyproline; partial Ref.11
Modified residue7715-hydroxylysine Ref.11
Modified residue9114-hydroxyproline Ref.11
Modified residue9514-hydroxyproline; partial Ref.11
Modified residue10115-hydroxylysine Ref.11
Glycosylation211O-linked (GalNAc...) Ref.12
Glycosylation221O-linked (GalNAc...) Ref.12
Glycosylation651O-linked (Gal...); partial Ref.11
Glycosylation681O-linked (Gal...); partial Ref.11
Glycosylation771O-linked (Gal...); partial Ref.11
Glycosylation1011O-linked (Gal...); partial Ref.11
Disulfide bond36Interchain; in form MMW and form HMW Ref.10 Ref.11

Natural variations

Natural variant841G → R Does not form high molecular weight multimers. Ref.10 Ref.15 Ref.18
VAR_013273
Natural variant901G → S Does not form high molecular weight multimers. Ref.10 Ref.18
Corresponds to variant rs62625753 [ dbSNP | Ensembl ].
VAR_027395
Natural variant1111Y → H. Ref.18
Corresponds to variant rs17366743 [ dbSNP | Ensembl ].
VAR_027396
Natural variant1121R → C in ADPND; does not assemble into trimers resulting in impaired secretion from the cell. Ref.10 Ref.14 Ref.17
VAR_013274
Natural variant1171V → M. Ref.15
VAR_013275
Natural variant1641I → 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
Corresponds to variant rs185847354 [ dbSNP | Ensembl ].
VAR_013276
Natural variant2211R → S. Ref.15 Ref.17
Corresponds to variant rs138773406 [ dbSNP | Ensembl ].
VAR_013277
Natural variant2411H → P. Ref.15 Ref.17
Corresponds to variant rs141205818 [ dbSNP | Ensembl ].
VAR_013278

Experimental info

Mutagenesis201T → A: No change in sialylated isoforms. Ref.12
Mutagenesis211T → A: Some loss of sialylated isoforms. Ref.12
Mutagenesis221T → A: Abolishes sialylated isoforms. Ref.12
Mutagenesis331K → R: No effect on formation of HMW multimers. Ref.11
Mutagenesis361C → S: Impaired formation of MMW and HMW multimers. Ref.10 Ref.11
Mutagenesis651K → R: Impaired formation of HMW multimers; when associated with R-68. Ref.11
Mutagenesis681K → R: Impaired formation of HMW multimers; when associated with R-65. Ref.11
Mutagenesis771K → R: Impaired formation of HMW multimers; when associated with R-101. Ref.11
Mutagenesis1011K → R: Impaired formation of HMW multimers; when associated with R-77. Ref.11

Secondary structure

................... 244
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q15848 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 64D8C6C1204B1018

FASTA24426,414
        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 

« Hide

References

« Hide '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. 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.
[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, IDENTIFICATION BY 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, IDENTIFICATION BY 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. expand/collapse author list , 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. expand/collapse author list , 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.
PIRJC4708.
RefSeqNP_001171271.1. NM_001177800.1.
NP_004788.1. NM_004797.3.
UniGeneHs.80485.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4DOUX-ray2.00A104-244[»]
ProteinModelPortalQ15848.
SMRQ15848. Positions 14-91, 109-243.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114771. 3 interactions.
STRING9606.ENSP00000320709.

Polymorphism databases

DMDM2493789.

Proteomic databases

PaxDbQ15848.
PeptideAtlasQ15848.
PRIDEQ15848.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000320741; ENSP00000320709; ENSG00000181092.
ENST00000412955; ENSP00000405611; ENSG00000181092.
ENST00000444204; ENSP00000389814; ENSG00000181092.
GeneID9370.
KEGGhsa:9370.
UCSCuc003fra.3. human.

Organism-specific databases

CTD9370.
GeneCardsGC03P186560.
HGNCHGNC:13633. ADIPOQ.
HPACAB046467.
MIM125853. phenotype.
605441. gene.
612556. phenotype.
neXtProtNX_Q15848.
PharmGKBPA134933118.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG136972.
HOGENOMHOG000085653.
HOVERGENHBG108220.
InParanoidQ15848.
KOK07296.
OMALFTYDQY.
OrthoDBEOG70ZZPW.
PhylomeDBQ15848.
TreeFamTF329591.

Enzyme and pathway databases

ReactomeREACT_111045. Developmental Biology.

Gene expression databases

ArrayExpressQ15848.
BgeeQ15848.
CleanExHS_ADIPOQ.
GenevestigatorQ15848.

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

ChiTaRSADIPOQ. human.
GeneWikiAdiponectin.
GenomeRNAi9370.
NextBio35094.
PROQ15848.
SOURCESearch...

Entry information

Entry nameADIPO_HUMAN
AccessionPrimary (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: April 16, 2014
This is version 146 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM