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Adiponectin (30 kDa adipocyte complement-related protein) (Adipocyte complement-related 30 kDa protein) (ACRP30) (Adipocyte, C1q and collagen domain-containing protein) (Adipose most abundant gene transcript 1 protein) (apM-1) (Gelatin-binding protein)

 ADIPO_HUMAN             Reviewed;         244 AA.
Q15848; Q58EX9;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
22-NOV-2017, entry version 179.
RecName: Full=Adiponectin;
AltName: Full=30 kDa adipocyte complement-related protein;
AltName: Full=Adipocyte complement-related 30 kDa protein;
Short=ACRP30;
AltName: Full=Adipocyte, C1q and collagen domain-containing protein;
AltName: Full=Adipose most abundant gene transcript 1 protein;
Short=apM-1;
AltName: Full=Gelatin-binding protein;
Flags: Precursor;
Name=ADIPOQ; Synonyms=ACDC, ACRP30, APM1, GBP28;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Adipose tissue;
PubMed=8619847; DOI=10.1006/bbrc.1996.0587;
Maeda K., Okubo K., Shimomura I., Funahashi T., Matsuzawa Y.,
Matsubara K.;
"cDNA cloning and expression of a novel adipose specific collagen-like
factor, apM1 (AdiPose Most abundant Gene transcript 1).";
Biochem. Biophys. Res. Commun. 221:286-289(1996).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=10095105; DOI=10.1016/S0378-1119(99)00041-4;
Saito K., Tobe T., Minoshima S., Asakawa S., Sumiya J., Yoda M.,
Nakano Y., Shimizu N., Tomita M.;
"Organization of the gene for gelatin-binding protein (GBP28).";
Gene 229:67-73(1999).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=10403784; DOI=10.1006/bbrc.1999.0865;
Schaeffler A., Orso E., Palitzsch K.D., Buechler C., Drobnik W.,
Fuerst A., Schoelmerich J., Schmitz G.;
"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).";
Biochem. Biophys. Res. Commun. 260:416-425(1999).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
PROTEIN SEQUENCE OF 19-33.
PubMed=15340161; DOI=10.1110/ps.04682504;
Zhang Z., Henzel W.J.;
"Signal peptide prediction based on analysis of experimentally
verified cleavage sites.";
Protein Sci. 13:2819-2824(2004).
[6]
PROTEIN SEQUENCE OF N-TERMINUS, AND PARTIAL PROTEIN SEQUENCE.
PubMed=8947845; DOI=10.1093/oxfordjournals.jbchem.a021483;
Nakano Y., Tobe T., Choi-Miura N.H., Mazda T., Tomita M.;
"Isolation and characterization of GBP28, a novel gelatin-binding
protein purified from human plasma.";
J. Biochem. 120:803-812(1996).
[7]
CHARACTERIZATION.
PubMed=10961870;
Yokota T., Oritani K., Takahashi I., Ishikawa J., Matsuyama A.,
Ouchi N., Kihara S., Funahashi T., Tenner A.J., Tomiyama Y.,
Matsuzawa Y.;
"Adiponectin, a new member of the family of soluble defense collagens,
negatively regulates the growth of myelomonocytic progenitors and the
functions of macrophages.";
Blood 96:1723-1732(2000).
[8]
CHARACTERIZATION.
PubMed=10982546; DOI=10.1161/01.CIR.102.11.1296;
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.;
"Adiponectin, an adipocyte-derived plasma protein, inhibits
endothelial NF-kappaB signaling through a cAMP-dependent pathway.";
Circulation 102:1296-1301(2000).
[9]
FUNCTION.
PubMed=11479627; DOI=10.1038/90984;
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.;
"The fat-derived hormone adiponectin reverses insulin resistance
associated with both lipoatrophy and obesity.";
Nat. Med. 7:941-946(2001).
[10]
SUBUNIT, DISULFIDE BOND, MUTAGENESIS OF CYS-36, AND CHARACTERIZATION
OF VARIANTS ARG-84; SER-90; CYS-112 AND THR-164.
PubMed=12878598; DOI=10.1074/jbc.M300365200;
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.;
"Impaired multimerization of human adiponectin mutants associated with
diabetes. Molecular structure and multimer formation of adiponectin.";
J. Biol. Chem. 278:40352-40363(2003).
[11]
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, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=16497731; DOI=10.1210/me.2005-0390;
Richards A.A., Stephens T., Charlton H.K., Jones A., Macdonald G.A.,
Prins J.B., Whitehead J.P.;
"Adiponectin multimerization is dependent on conserved lysines in the
collagenous domain: evidence for regulation of multimerization by
alterations in posttranslational modifications.";
Mol. Endocrinol. 20:1673-1687(2006).
[12]
GLYCOSYLATION AT THR-21 AND THR-22, SUBUNIT, IDENTIFICATION BY MASS
SPECTROMETRY, AND MUTAGENESIS OF THR-20; THR-21 AND THR-22.
PubMed=19855092; DOI=10.1210/me.2009-0133;
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.;
"Sialic acid modification of adiponectin is not required for
multimerization or secretion but determines half-life in
circulation.";
Mol. Endocrinol. 24:229-239(2010).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22905912; DOI=10.1021/pr300539b;
Rosenow A., Noben J.P., Jocken J., Kallendrusch S.,
Fischer-Posovszky P., Mariman E.C., Renes J.;
"Resveratrol-induced changes of the human adipocyte secretion
profile.";
J. Proteome Res. 11:4733-4743(2012).
[14]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 104-244, AND SUBUNIT.
PubMed=22449980; DOI=10.1016/j.febslet.2012.02.024;
Min X., Lemon B., Tang J., Liu Q., Zhang R., Walker N., Li Y.,
Wang Z.;
"Crystal structure of a single-chain trimer of human adiponectin
globular domain.";
FEBS Lett. 586:912-917(2012).
[15]
VARIANT ADPND CYS-112.
PubMed=10918532; DOI=10.1038/sj.ijo.0801244;
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.;
"Genomic structure and mutations in adipose-specific gene,
adiponectin.";
Int. J. Obes. Relat. Metab. Disord. 24:861-868(2000).
[16]
VARIANTS ARG-84; MET-117; THR-164; SER-221 AND PRO-241.
PubMed=11812766; DOI=10.2337/diabetes.51.2.536;
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.;
"Genetic variation in the gene encoding adiponectin is associated with
an increased risk of type 2 diabetes in the Japanese population.";
Diabetes 51:536-540(2002).
[17]
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).
[18]
VARIANTS CYS-112; THR-164; SER-221 AND PRO-241, AND ASSOCIATION WITH
LOW PLASMA ADIPONECTIN CONCENTRATION AND DIABETES MELLITUS TYPE 2.
PubMed=12086969; DOI=10.2337/diabetes.51.7.2325;
Kondo H., Shimomura I., Matsukawa Y., Kumada M., Takahashi M.,
Matsuda M., Ouchi N., Kihara S., Kawamoto T., Sumitsuji S.,
Funahashi T., Matsuzawa Y.;
"Association of adiponectin mutation with type 2 diabetes: a candidate
gene for the insulin resistance syndrome.";
Diabetes 51:2325-2328(2002).
[19]
VARIANTS ARG-84; SER-90 AND HIS-111.
PubMed=12354786; DOI=10.1093/hmg/11.21.2607;
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.;
"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.";
Hum. Mol. Genet. 11:2607-2614(2002).
-!- FUNCTION: Important adipokine involved in the control of fat
metabolism and insulin sensitivity, with direct anti-diabetic,
anti-atherogenic and anti-inflammatory activities. Stimulates AMPK
phosphorylation and activation in the liver and the skeletal
muscle, enhancing glucose utilization and fatty-acid combustion.
Antagonizes TNF-alpha by negatively regulating its expression in
various tissues such as liver and macrophages, and also by
counteracting its effects. Inhibits endothelial NF-kappa-B
signaling through a cAMP-dependent pathway. May play a role in
cell growth, angiogenesis and tissue remodeling by binding and
sequestering various growth factors with distinct binding
affinities, depending on the type of complex, LMW, MMW or HMW.
{ECO:0000269|PubMed:11479627}.
-!- SUBUNIT: Homomultimer. Forms trimers, hexamers and 12- to 18-mers.
The trimers (low molecular weight complexes / LMW) are assembled
via non-covalent interactions of the collagen-like domains in a
triple helix and hydrophobic interactions within the globular C1q
domain. Several trimers can associate to form disulfide-linked
hexamers (middle molecular weight complexes / MMW) and larger
complexes (higher molecular weight / HMW). The HMW-complex
assembly may rely additionally on lysine hydroxylation and
glycosylation. LMW, MMW and HMW complexes bind to HBEGF, MMW and
HMW complexes bind to PDGFB, and HMW complex binds to FGF2.
Interacts with CTRP9A via the C1q domain (heterotrimeric complex)
(By similarity). {ECO:0000250}.
-!- INTERACTION:
O60238:BNIP3L; NbExp=3; IntAct=EBI-10827839, EBI-849893;
Q8N6L0:CCDC155; NbExp=3; IntAct=EBI-10827839, EBI-749265;
Q9UHP7-3:CLEC2D; NbExp=4; IntAct=EBI-10827839, EBI-11749983;
O43765:SGTA; NbExp=5; IntAct=EBI-10827839, EBI-347996;
Q8N205-2:SYNE4; NbExp=5; IntAct=EBI-10827839, EBI-12099160;
-!- SUBCELLULAR LOCATION: Secreted.
-!- TISSUE SPECIFICITY: Synthesized exclusively by adipocytes and
secreted into plasma.
-!- DOMAIN: The C1q domain is commonly called the globular domain.
-!- PTM: Hydroxylated Lys-33 was not identified in PubMed:16497731,
probably due to poor representation of the N-terminal peptide in
mass fingerprinting. {ECO:0000269|PubMed:16497731}.
-!- PTM: HMW complexes are more extensively glycosylated than smaller
oligomers. Hydroxylation and glycosylation of the lysine residues
within the collagene-like domain of adiponectin seem to be
critically involved in regulating the formation and/or secretion
of HMW complexes and consequently contribute to the insulin-
sensitizing activity of adiponectin in hepatocytes (By
similarity). {ECO:0000250}.
-!- PTM: 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.
{ECO:0000269|PubMed:16497731, ECO:0000269|PubMed:19855092}.
-!- 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].
-!- DISEASE: Adiponectin deficiency (ADPND) [MIM:612556]: A condition
that results in very low concentrations of plasma adiponectin.
{ECO:0000269|PubMed:10918532}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: 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: 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.
-!- 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 (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. {ECO:0000250}.
-!- WEB RESOURCE: Name=Wikipedia; Note=Adiponectin entry;
URL="https://en.wikipedia.org/wiki/Adiponectin";
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EMBL; D45371; BAA08227.1; -; mRNA.
EMBL; AB012165; BAA86716.1; -; Genomic_DNA.
EMBL; AJ131460; CAB52413.1; -; Genomic_DNA.
EMBL; AJ131461; CAB52413.1; JOINED; Genomic_DNA.
EMBL; BC054496; AAH54496.1; -; mRNA.
EMBL; BC096308; AAH96308.1; -; mRNA.
EMBL; BC096309; AAH96309.1; -; mRNA.
EMBL; BC096310; AAH96310.1; -; mRNA.
EMBL; BC096311; AAH96311.1; -; mRNA.
CCDS; CCDS3284.1; -.
PIR; JC4708; JC4708.
RefSeq; NP_001171271.1; NM_001177800.1.
RefSeq; NP_004788.1; NM_004797.3.
UniGene; Hs.80485; -.
PDB; 4DOU; X-ray; 2.00 A; A=104-244.
PDBsum; 4DOU; -.
ProteinModelPortal; Q15848; -.
SMR; Q15848; -.
BioGrid; 114771; 21.
IntAct; Q15848; 21.
STRING; 9606.ENSP00000320709; -.
iPTMnet; Q15848; -.
PhosphoSitePlus; Q15848; -.
BioMuta; ADIPOQ; -.
DMDM; 2493789; -.
PaxDb; Q15848; -.
PeptideAtlas; Q15848; -.
PRIDE; Q15848; -.
Ensembl; ENST00000320741; ENSP00000320709; ENSG00000181092.
Ensembl; ENST00000444204; ENSP00000389814; ENSG00000181092.
GeneID; 9370; -.
KEGG; hsa:9370; -.
UCSC; uc003fra.4; human.
CTD; 9370; -.
DisGeNET; 9370; -.
EuPathDB; HostDB:ENSG00000181092.9; -.
GeneCards; ADIPOQ; -.
HGNC; HGNC:13633; ADIPOQ.
HPA; CAB046467; -.
HPA; HPA051767; -.
MalaCards; ADIPOQ; -.
MIM; 125853; phenotype.
MIM; 605441; gene.
MIM; 612556; phenotype.
neXtProt; NX_Q15848; -.
OpenTargets; ENSG00000181092; -.
PharmGKB; PA134933118; -.
eggNOG; ENOG410IHSJ; Eukaryota.
eggNOG; ENOG4111F5K; LUCA.
GeneTree; ENSGT00760000118830; -.
HOGENOM; HOG000085653; -.
HOVERGEN; HBG108220; -.
InParanoid; Q15848; -.
KO; K07296; -.
OMA; QQNHYDG; -.
OrthoDB; EOG091G0L3Y; -.
PhylomeDB; Q15848; -.
TreeFam; TF329591; -.
Reactome; R-HSA-163680; AMPK inhibits chREBP transcriptional activation activity.
Reactome; R-HSA-381340; Transcriptional regulation of white adipocyte differentiation.
SIGNOR; Q15848; -.
ChiTaRS; ADIPOQ; human.
GeneWiki; Adiponectin; -.
GenomeRNAi; 9370; -.
PRO; PR:Q15848; -.
Proteomes; UP000005640; Chromosome 3.
Bgee; ENSG00000181092; -.
CleanEx; HS_ADIPOQ; -.
ExpressionAtlas; Q15848; baseline and differential.
Genevisible; Q15848; HS.
GO; GO:0009986; C:cell surface; IDA:BHF-UCL.
GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005576; C:extracellular region; IDA:BHF-UCL.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:0005125; F:cytokine activity; NAS:BHF-UCL.
GO; GO:0005179; F:hormone activity; IDA:BHF-UCL.
GO; GO:0042802; F:identical protein binding; TAS:BHF-UCL.
GO; GO:0042803; F:protein homodimerization activity; IPI:BHF-UCL.
GO; GO:0005102; F:receptor binding; ISS:UniProtKB.
GO; GO:0033691; F:sialic acid binding; IDA:UniProtKB.
GO; GO:0033211; P:adiponectin-activated signaling pathway; IEA:Ensembl.
GO; GO:0050873; P:brown fat cell differentiation; ISS:UniProtKB.
GO; GO:0071320; P:cellular response to cAMP; IEA:Ensembl.
GO; GO:0035690; P:cellular response to drug; ISS:UniProtKB.
GO; GO:0071872; P:cellular response to epinephrine stimulus; IEA:Ensembl.
GO; GO:0032869; P:cellular response to insulin stimulus; ISS:UniProtKB.
GO; GO:0007623; P:circadian rhythm; IEA:Ensembl.
GO; GO:0070994; P:detection of oxidative stress; ISS:UniProtKB.
GO; GO:0006635; P:fatty acid beta-oxidation; ISS:UniProtKB.
GO; GO:0019395; P:fatty acid oxidation; ISS:UniProtKB.
GO; GO:0006091; P:generation of precursor metabolites and energy; TAS:ProtInc.
GO; GO:0042593; P:glucose homeostasis; ISS:UniProtKB.
GO; GO:0006006; P:glucose metabolic process; ISS:UniProtKB.
GO; GO:0034383; P:low-density lipoprotein particle clearance; IDA:BHF-UCL.
GO; GO:0051899; P:membrane depolarization; IEA:Ensembl.
GO; GO:0060081; P:membrane hyperpolarization; IEA:Ensembl.
GO; GO:0045776; P:negative regulation of blood pressure; IDA:UniProtKB.
GO; GO:0030336; P:negative regulation of cell migration; ISS:UniProtKB.
GO; GO:2000279; P:negative regulation of DNA biosynthetic process; IDA:UniProtKB.
GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; IDA:UniProtKB.
GO; GO:0045599; P:negative regulation of fat cell differentiation; IDA:BHF-UCL.
GO; GO:0045721; P:negative regulation of gluconeogenesis; ISS:BHF-UCL.
GO; GO:0030853; P:negative regulation of granulocyte differentiation; IDA:BHF-UCL.
GO; GO:0034115; P:negative regulation of heterotypic cell-cell adhesion; IDA:BHF-UCL.
GO; GO:0046888; P:negative regulation of hormone secretion; IEA:Ensembl.
GO; GO:0043124; P:negative regulation of I-kappaB kinase/NF-kappaB signaling; IDA:BHF-UCL.
GO; GO:0050728; P:negative regulation of inflammatory response; ISS:UniProtKB.
GO; GO:0090317; P:negative regulation of intracellular protein transport; IDA:UniProtKB.
GO; GO:0045715; P:negative regulation of low-density lipoprotein particle receptor biosynthetic process; IDA:BHF-UCL.
GO; GO:0010745; P:negative regulation of macrophage derived foam cell differentiation; IDA:BHF-UCL.
GO; GO:0045650; P:negative regulation of macrophage differentiation; IDA:BHF-UCL.
GO; GO:0043407; P:negative regulation of MAP kinase activity; ISS:UniProtKB.
GO; GO:2000590; P:negative regulation of metanephric mesenchymal cell migration; ISS:UniProtKB.
GO; GO:0050765; P:negative regulation of phagocytosis; IDA:BHF-UCL.
GO; GO:0010642; P:negative regulation of platelet-derived growth factor receptor signaling pathway; IDA:UniProtKB.
GO; GO:2000584; P:negative regulation of platelet-derived growth factor receptor-alpha signaling pathway; ISS:UniProtKB.
GO; GO:0031953; P:negative regulation of protein autophosphorylation; IDA:UniProtKB.
GO; GO:1900121; P:negative regulation of receptor binding; IDA:UniProtKB.
GO; GO:0014912; P:negative regulation of smooth muscle cell migration; IDA:UniProtKB.
GO; GO:0048662; P:negative regulation of smooth muscle cell proliferation; IDA:UniProtKB.
GO; GO:0050805; P:negative regulation of synaptic transmission; IDA:UniProtKB.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0032720; P:negative regulation of tumor necrosis factor production; IDA:BHF-UCL.
GO; GO:0010804; P:negative regulation of tumor necrosis factor-mediated signaling pathway; IDA:BHF-UCL.
GO; GO:0045777; P:positive regulation of blood pressure; IEA:Ensembl.
GO; GO:2000481; P:positive regulation of cAMP-dependent protein kinase activity; IDA:UniProtKB.
GO; GO:0032270; P:positive regulation of cellular protein metabolic process; IDA:BHF-UCL.
GO; GO:0010875; P:positive regulation of cholesterol efflux; IDA:BHF-UCL.
GO; GO:0045923; P:positive regulation of fatty acid metabolic process; ISS:BHF-UCL.
GO; GO:0046326; P:positive regulation of glucose import; ISS:BHF-UCL.
GO; GO:2000467; P:positive regulation of glycogen (starch) synthase activity; ISS:UniProtKB.
GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; ISS:UniProtKB.
GO; GO:0032757; P:positive regulation of interleukin-8 production; IDA:UniProtKB.
GO; GO:2000478; P:positive regulation of metanephric glomerular visceral epithelial cell development; ISS:UniProtKB.
GO; GO:0071639; P:positive regulation of monocyte chemotactic protein-1 production; IDA:UniProtKB.
GO; GO:0033034; P:positive regulation of myeloid cell apoptotic process; IDA:BHF-UCL.
GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IEA:Ensembl.
GO; GO:0010739; P:positive regulation of protein kinase A signaling; IDA:BHF-UCL.
GO; GO:0001934; P:positive regulation of protein phosphorylation; IDA:UniProtKB.
GO; GO:2000534; P:positive regulation of renal albumin absorption; IDA:UniProtKB.
GO; GO:0009967; P:positive regulation of signal transduction; ISS:BHF-UCL.
GO; GO:0070208; P:protein heterotrimerization; IEA:Ensembl.
GO; GO:0051260; P:protein homooligomerization; ISS:UniProtKB.
GO; GO:0072659; P:protein localization to plasma membrane; IDA:UniProtKB.
GO; GO:0042304; P:regulation of fatty acid biosynthetic process; TAS:Reactome.
GO; GO:0010906; P:regulation of glucose metabolic process; IDA:UniProtKB.
GO; GO:0014823; P:response to activity; IEA:Ensembl.
GO; GO:0045471; P:response to ethanol; IEA:Ensembl.
GO; GO:0051384; P:response to glucocorticoid; IEA:Ensembl.
GO; GO:0009749; P:response to glucose; ISS:BHF-UCL.
GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
GO; GO:0070543; P:response to linoleic acid; IEA:Ensembl.
GO; GO:0007584; P:response to nutrient; IEA:Ensembl.
GO; GO:0009744; P:response to sucrose; IEA:Ensembl.
GO; GO:0034612; P:response to tumor necrosis factor; IDA:BHF-UCL.
Gene3D; 2.60.120.40; -; 1.
InterPro; IPR001073; C1q_dom.
InterPro; IPR008160; Collagen.
InterPro; IPR008983; Tumour_necrosis_fac-like_dom.
Pfam; PF00386; C1q; 1.
Pfam; PF01391; Collagen; 1.
PRINTS; PR00007; COMPLEMNTC1Q.
SMART; SM00110; C1Q; 1.
SUPFAM; SSF49842; SSF49842; 1.
PROSITE; PS50871; C1Q; 1.
1: Evidence at protein level;
3D-structure; Collagen; Complete proteome; Diabetes mellitus;
Direct protein sequencing; Disease mutation; Disulfide bond;
Glycoprotein; Hormone; Hydroxylation; Obesity; Pharmaceutical;
Polymorphism; Reference proteome; Repeat; Secreted; Signal.
SIGNAL 1 18 {ECO:0000269|PubMed:15340161,
ECO:0000269|PubMed:8947845}.
CHAIN 19 244 Adiponectin.
/FTId=PRO_0000003543.
DOMAIN 42 107 Collagen-like.
DOMAIN 108 244 C1q. {ECO:0000255|PROSITE-
ProRule:PRU00368}.
SITE 62 62 Not hydroxylated.
{ECO:0000269|PubMed:16497731}.
SITE 86 86 Not hydroxylated.
{ECO:0000269|PubMed:16497731}.
SITE 104 104 Not hydroxylated.
{ECO:0000269|PubMed:16497731}.
SITE 230 230 Not glycosylated.
{ECO:0000269|PubMed:16497731}.
MOD_RES 33 33 5-hydroxylysine. {ECO:0000305}.
MOD_RES 44 44 4-hydroxyproline.
{ECO:0000269|PubMed:16497731}.
MOD_RES 47 47 4-hydroxyproline.
{ECO:0000269|PubMed:16497731}.
MOD_RES 53 53 4-hydroxyproline.
{ECO:0000269|PubMed:16497731}.
MOD_RES 65 65 5-hydroxylysine.
{ECO:0000269|PubMed:16497731}.
MOD_RES 68 68 5-hydroxylysine.
{ECO:0000269|PubMed:16497731}.
MOD_RES 71 71 4-hydroxyproline; partial.
{ECO:0000269|PubMed:16497731}.
MOD_RES 76 76 4-hydroxyproline; partial.
{ECO:0000269|PubMed:16497731}.
MOD_RES 77 77 5-hydroxylysine.
{ECO:0000269|PubMed:16497731}.
MOD_RES 91 91 4-hydroxyproline.
{ECO:0000269|PubMed:16497731}.
MOD_RES 95 95 4-hydroxyproline; partial.
{ECO:0000269|PubMed:16497731}.
MOD_RES 101 101 5-hydroxylysine.
{ECO:0000269|PubMed:16497731}.
CARBOHYD 21 21 O-linked (GalNAc...) threonine.
{ECO:0000269|PubMed:19855092}.
CARBOHYD 22 22 O-linked (GalNAc...) threonine.
{ECO:0000269|PubMed:19855092}.
CARBOHYD 65 65 O-linked (Gal...) hydroxylysine; partial.
{ECO:0000269|PubMed:16497731}.
CARBOHYD 68 68 O-linked (Gal...) hydroxylysine; partial.
{ECO:0000269|PubMed:16497731}.
CARBOHYD 77 77 O-linked (Gal...) hydroxylysine; partial.
{ECO:0000269|PubMed:16497731}.
CARBOHYD 101 101 O-linked (Gal...) hydroxylysine; partial.
{ECO:0000269|PubMed:16497731}.
DISULFID 36 36 Interchain; in form MMW and form HMW.
{ECO:0000269|PubMed:12878598,
ECO:0000269|PubMed:16497731}.
VARIANT 84 84 G -> R (does not form high molecular
weight multimers; dbSNP:rs199646033).
{ECO:0000269|PubMed:11812766,
ECO:0000269|PubMed:12354786,
ECO:0000269|PubMed:12878598}.
/FTId=VAR_013273.
VARIANT 90 90 G -> S (does not form high molecular
weight multimers; dbSNP:rs62625753).
{ECO:0000269|PubMed:12354786,
ECO:0000269|PubMed:12878598}.
/FTId=VAR_027395.
VARIANT 111 111 Y -> H (in dbSNP:rs17366743).
{ECO:0000269|PubMed:12354786}.
/FTId=VAR_027396.
VARIANT 112 112 R -> C (in ADPND; does not assemble into
trimers resulting in impaired secretion
from the cell; dbSNP:rs121917815).
{ECO:0000269|PubMed:10918532,
ECO:0000269|PubMed:12086969,
ECO:0000269|PubMed:12878598}.
/FTId=VAR_013274.
VARIANT 117 117 V -> M (in dbSNP:rs747223144).
{ECO:0000269|PubMed:11812766}.
/FTId=VAR_013275.
VARIANT 164 164 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; dbSNP:rs185847354).
{ECO:0000269|PubMed:11812766,
ECO:0000269|PubMed:12086969,
ECO:0000269|PubMed:12878598}.
/FTId=VAR_013276.
VARIANT 221 221 R -> S (in dbSNP:rs138773406).
{ECO:0000269|PubMed:11812766,
ECO:0000269|PubMed:12086969}.
/FTId=VAR_013277.
VARIANT 241 241 H -> P (in dbSNP:rs141205818).
{ECO:0000269|PubMed:11812766,
ECO:0000269|PubMed:12086969}.
/FTId=VAR_013278.
MUTAGEN 20 20 T->A: No change in sialylated isoforms.
{ECO:0000269|PubMed:19855092}.
MUTAGEN 21 21 T->A: Some loss of sialylated isoforms.
{ECO:0000269|PubMed:19855092}.
MUTAGEN 22 22 T->A: Abolishes sialylated isoforms.
{ECO:0000269|PubMed:19855092}.
MUTAGEN 33 33 K->R: No effect on formation of HMW
multimers. {ECO:0000269|PubMed:16497731}.
MUTAGEN 36 36 C->S: Impaired formation of MMW and HMW
multimers. {ECO:0000269|PubMed:12878598,
ECO:0000269|PubMed:16497731}.
MUTAGEN 65 65 K->R: Impaired formation of HMW
multimers; when associated with R-68.
{ECO:0000269|PubMed:16497731}.
MUTAGEN 68 68 K->R: Impaired formation of HMW
multimers; when associated with R-65.
{ECO:0000269|PubMed:16497731}.
MUTAGEN 77 77 K->R: Impaired formation of HMW
multimers; when associated with R-101.
{ECO:0000269|PubMed:16497731}.
MUTAGEN 101 101 K->R: Impaired formation of HMW
multimers; when associated with R-77.
{ECO:0000269|PubMed:16497731}.
STRAND 114 118 {ECO:0000244|PDB:4DOU}.
STRAND 134 137 {ECO:0000244|PDB:4DOU}.
TURN 145 147 {ECO:0000244|PDB:4DOU}.
STRAND 156 177 {ECO:0000244|PDB:4DOU}.
STRAND 180 187 {ECO:0000244|PDB:4DOU}.
STRAND 195 205 {ECO:0000244|PDB:4DOU}.
STRAND 210 225 {ECO:0000244|PDB:4DOU}.
STRAND 233 241 {ECO:0000244|PDB:4DOU}.
SEQUENCE 244 AA; 26414 MW; 64D8C6C1204B1018 CRC64;
MLLLGAVLLL LALPGHDQET TTQGPGVLLP LPKGACTGWM AGIPGHPGHN GAPGRDGRDG
TPGEKGEKGD PGLIGPKGDI GETGVPGAEG PRGFPGIQGR KGEPGEGAYV YRSAFSVGLE
TYVTIPNMPI RFTKIFYNQQ NHYDGSTGKF HCNIPGLYYF AYHITVYMKD VKVSLFKKDK
AMLFTYDQYQ ENNVDQASGS VLLHLEVGDQ VWLQVYGEGE RNGLYADNDN DSTFTGFLLY
HDTN


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