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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) (Adipocyte-specific protein AdipoQ)

 ADIPO_MOUSE             Reviewed;         247 AA.
Q60994; Q62400; Q6GTX4; Q9DC68;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
03-OCT-2012, sequence version 2.
25-OCT-2017, entry version 166.
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=Adipocyte-specific protein AdipoQ;
Flags: Precursor;
Name=Adipoq; Synonyms=Acdc, Acrp30, Apm1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Adipocyte;
PubMed=7592907; DOI=10.1074/jbc.270.45.26746;
Scherer P.E., Williams S., Fogliano M., Baldini G., Lodish H.F.;
"A novel serum protein similar to C1q, produced exclusively in
adipocytes.";
J. Biol. Chem. 270:26746-26749(1995).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Fibroblast;
PubMed=8631877; DOI=10.1074/jbc.271.18.10697;
Hu E., Liang P., Spiegelman B.M.;
"AdipoQ is a novel adipose-specific gene dysregulated in obesity.";
J. Biol. Chem. 271:10697-10703(1996).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=11162643; DOI=10.1006/bbrc.2001.4217;
Das K., Lin Y., Widen E., Zhang Y., Scherer P.E.;
"Chromosomal localization, expression pattern, and promoter analysis
of the mouse gene encoding adipocyte-specific secretory protein
Acrp30.";
Biochem. Biophys. Res. Commun. 280:1120-1129(2001).
[4]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=C57BL/6J, and IRM-2; TISSUE=White adipose tissue;
Wang S.F., Han P.Z., Mu C.J., Zhao M.H.;
"Cloning of murine adipocyte complement-related protein of 30 KDa from
white adipose tissue.";
Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Heart, and Thymus;
PubMed=16141072; DOI=10.1126/science.1112014;
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.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
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.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Thymus;
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).
[9]
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, LACK OF HYDROXYLATION AT PRO-79; PRO-98 AND
PRO-107, LACK OF GLYCOSYLATION AT ASN-233, AND IDENTIFICATION BY MASS
SPECTROMETRY.
PubMed=11912203; DOI=10.1074/jbc.M200601200;
Wang Y., Xu A., Knight C., Xu L.Y., Cooper G.J.S.;
"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.";
J. Biol. Chem. 277:19521-19529(2002).
[10]
STRUCTURE OF CARBOHYDRATES.
PubMed=11382781; DOI=10.1074/jbc.M104148200;
Sato C., Yasukawa Z., Honda N., Matsuda T., Kitajima K.;
"Identification and adipocyte differentiation-dependent expression of
the unique disialic acid residue in an adipose tissue-specific
glycoprotein, adipo Q.";
J. Biol. Chem. 276:28849-28856(2001).
[11]
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).
[12]
FUNCTION.
PubMed=11479628; DOI=10.1038/90992;
Berg A.H., Combs T.P., Du X., Brownlee M., Scherer P.E.;
"The adipocyte-secreted protein Acrp30 enhances hepatic insulin
action.";
Nat. Med. 7:947-953(2001).
[13]
FUNCTION.
PubMed=12840063; DOI=10.1172/JCI200317797;
Xu A., Wang Y., Keshaw H., Xu L.Y., Lam K.S.L., Cooper G.J.S.;
"The fat-derived hormone adiponectin alleviates alcoholic and
nonalcoholic fatty liver diseases in mice.";
J. Clin. Invest. 112:91-100(2003).
[14]
SUBUNIT, AND FUNCTION.
PubMed=15760892; DOI=10.1074/jbc.M414231200;
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.;
"Testosterone selectively reduces the high molecular weight form of
adiponectin by inhibiting its secretion from adipocytes.";
J. Biol. Chem. 280:18073-18080(2005).
[15]
SUBUNIT, AND FUNCTION.
PubMed=15734737; DOI=10.1074/jbc.M501149200;
Wang Y., Lam K.S.L., Xu J.Y., Lu G., Xu L.Y., Cooper G.J.S., Xu A.;
"Adiponectin inhibits cell proliferation by interacting with several
growth factors in an oligomerization-dependent manner.";
J. Biol. Chem. 280:18341-18347(2005).
[16]
SUBUNIT, AND MUTAGENESIS OF LYS-68; LYS-71; LYS-80 AND LYS-104.
PubMed=16621799; DOI=10.1074/jbc.M513907200;
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.;
"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.";
J. Biol. Chem. 281:16391-16400(2006).
[17]
SUBUNIT, INTERACTION WITH CTRP9, AND MUTAGENESIS OF CYS-39.
PubMed=18787108; DOI=10.1096/fj.08-114991;
Wong G.W., Krawczyk S.A., Kitidis-Mitrokostas C., Ge G., Spooner E.,
Hug C., Gimeno R., Lodish H.F.;
"Identification and characterization of CTRP9, a novel secreted
glycoprotein, from adipose tissue that reduces serum glucose in mice
and forms heterotrimers with adiponectin.";
FASEB J. 23:241-258(2009).
[18]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brown adipose tissue, Heart, and Lung;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[19]
GLYCOSYLATION AT THR-23 AND THR-24, AND SUBUNIT.
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).
[20]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 111-247.
PubMed=9512423; DOI=10.1016/S0960-9822(98)70133-2;
Shapiro L., Scherer P.E.;
"The crystal structure of a complement-1q family protein suggests an
evolutionary link to tumor necrosis factor.";
Curr. Biol. 8:335-338(1998).
-!- 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, ECO:0000269|PubMed:11479628,
ECO:0000269|PubMed:12840063, ECO:0000269|PubMed:15734737,
ECO:0000269|PubMed:15760892}.
-!- 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 CTRP9 via the C1q domain (heterotrimeric complex).
{ECO:0000269|PubMed:15734737, ECO:0000269|PubMed:15760892,
ECO:0000269|PubMed:16621799, ECO:0000269|PubMed:18787108,
ECO:0000269|PubMed:19855092}.
-!- INTERACTION:
Self; NbExp=17; IntAct=EBI-7264589, EBI-7264589;
Q9Y2Q3:GSTK1 (xeno); NbExp=2; IntAct=EBI-7264589, EBI-1053767;
Q9DCM2:Gstk1; NbExp=3; IntAct=EBI-7264589, EBI-8369416;
-!- SUBCELLULAR LOCATION: Secreted.
-!- TISSUE SPECIFICITY: Synthesized exclusively by adipocytes and
secreted into plasma.
-!- INDUCTION: During hormone-induced adipose differentiation and
activated by insulin.
-!- 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.
{ECO:0000269|PubMed:11912203}.
-!- PTM: 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. {ECO:0000250}.
-!- 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.
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EMBL; U37222; AAA80543.1; -; mRNA.
EMBL; U49915; AAB06706.1; -; mRNA.
EMBL; AF304466; AAK13417.1; -; Genomic_DNA.
EMBL; AY749429; AAW70555.1; -; mRNA.
EMBL; AY754346; AAW82905.1; -; mRNA.
EMBL; AK003138; BAB22597.1; -; mRNA.
EMBL; AK134112; BAE22019.1; -; mRNA.
EMBL; AC125396; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH466521; EDK97661.1; -; Genomic_DNA.
EMBL; BC028770; AAH28770.1; -; mRNA.
CCDS; CCDS28075.1; -.
RefSeq; NP_033735.3; NM_009605.5.
UniGene; Mm.3969; -.
PDB; 1C28; X-ray; 2.10 A; A/B/C=114-247.
PDB; 1C3H; X-ray; 2.10 A; A/B/C/D/E/F=111-247.
PDBsum; 1C28; -.
PDBsum; 1C3H; -.
ProteinModelPortal; Q60994; -.
SMR; Q60994; -.
BioGrid; 197940; 3.
CORUM; Q60994; -.
DIP; DIP-44111N; -.
IntAct; Q60994; 4.
MINT; MINT-4563800; -.
STRING; 10090.ENSMUSP00000023593; -.
iPTMnet; Q60994; -.
PhosphoSitePlus; Q60994; -.
SwissPalm; Q60994; -.
PaxDb; Q60994; -.
PeptideAtlas; Q60994; -.
PRIDE; Q60994; -.
Ensembl; ENSMUST00000023593; ENSMUSP00000023593; ENSMUSG00000022878.
GeneID; 11450; -.
KEGG; mmu:11450; -.
UCSC; uc007ytk.1; mouse.
CTD; 9370; -.
MGI; MGI:106675; Adipoq.
eggNOG; ENOG410IHSJ; Eukaryota.
eggNOG; ENOG4111F5K; LUCA.
GeneTree; ENSGT00760000118830; -.
HOGENOM; HOG000085653; -.
HOVERGEN; HBG108220; -.
InParanoid; Q60994; -.
KO; K07296; -.
OMA; QQNHYDG; -.
OrthoDB; EOG091G0L3Y; -.
TreeFam; TF329591; -.
Reactome; R-MMU-163680; AMPK inhibits chREBP transcriptional activation activity.
EvolutionaryTrace; Q60994; -.
PRO; PR:Q60994; -.
Proteomes; UP000000589; Chromosome 16.
Bgee; ENSMUSG00000022878; -.
CleanEx; MM_ADIPOQ; -.
ExpressionAtlas; Q60994; baseline and differential.
Genevisible; Q60994; MM.
GO; GO:0071944; C:cell periphery; ISS:UniProtKB.
GO; GO:0009986; C:cell surface; ISS:BHF-UCL.
GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
GO; GO:0070062; C:extracellular exosome; ISO:MGI.
GO; GO:0005615; C:extracellular space; IDA:MGI.
GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
GO; GO:0005179; F:hormone activity; IDA:MGI.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
GO; GO:0005102; F:receptor binding; IDA:MGI.
GO; GO:0033691; F:sialic acid binding; ISO:MGI.
GO; GO:0033211; P:adiponectin-activated signaling pathway; IEA:Ensembl.
GO; GO:0050873; P:brown fat cell differentiation; IDA:MGI.
GO; GO:0071320; P:cellular response to cAMP; IEA:Ensembl.
GO; GO:0035690; P:cellular response to drug; IDA:UniProtKB.
GO; GO:0071872; P:cellular response to epinephrine stimulus; IEA:Ensembl.
GO; GO:0032869; P:cellular response to insulin stimulus; IGI:MGI.
GO; GO:0007623; P:circadian rhythm; IEA:Ensembl.
GO; GO:0070994; P:detection of oxidative stress; IMP:UniProtKB.
GO; GO:0006635; P:fatty acid beta-oxidation; IMP:MGI.
GO; GO:0019395; P:fatty acid oxidation; IDA:MGI.
GO; GO:0042593; P:glucose homeostasis; IDA:MGI.
GO; GO:0006006; P:glucose metabolic process; IDA:MGI.
GO; GO:0034383; P:low-density lipoprotein particle clearance; ISS:UniProtKB.
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; ISS:UniProtKB.
GO; GO:0030336; P:negative regulation of cell migration; IDA:UniProtKB.
GO; GO:2000279; P:negative regulation of DNA biosynthetic process; ISS:UniProtKB.
GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; ISS:UniProtKB.
GO; GO:0045599; P:negative regulation of fat cell differentiation; IDA:BHF-UCL.
GO; GO:0045721; P:negative regulation of gluconeogenesis; IDA:MGI.
GO; GO:0030853; P:negative regulation of granulocyte differentiation; ISS:UniProtKB.
GO; GO:0034115; P:negative regulation of heterotypic cell-cell adhesion; ISS:UniProtKB.
GO; GO:0046888; P:negative regulation of hormone secretion; IEA:Ensembl.
GO; GO:0043124; P:negative regulation of I-kappaB kinase/NF-kappaB signaling; ISS:UniProtKB.
GO; GO:0050728; P:negative regulation of inflammatory response; IDA:UniProtKB.
GO; GO:0090317; P:negative regulation of intracellular protein transport; ISS:UniProtKB.
GO; GO:0045715; P:negative regulation of low-density lipoprotein particle receptor biosynthetic process; ISS:UniProtKB.
GO; GO:0010745; P:negative regulation of macrophage derived foam cell differentiation; ISS:UniProtKB.
GO; GO:0045650; P:negative regulation of macrophage differentiation; ISS:UniProtKB.
GO; GO:0043407; P:negative regulation of MAP kinase activity; IDA:UniProtKB.
GO; GO:2000590; P:negative regulation of metanephric mesenchymal cell migration; IDA:UniProtKB.
GO; GO:0050765; P:negative regulation of phagocytosis; ISS:UniProtKB.
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; IDA:UniProtKB.
GO; GO:0031953; P:negative regulation of protein autophosphorylation; ISS:UniProtKB.
GO; GO:1900121; P:negative regulation of receptor binding; ISS:UniProtKB.
GO; GO:0014912; P:negative regulation of smooth muscle cell migration; ISS:UniProtKB.
GO; GO:0048662; P:negative regulation of smooth muscle cell proliferation; ISS:UniProtKB.
GO; GO:0050805; P:negative regulation of synaptic transmission; ISS:UniProtKB.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:UniProtKB.
GO; GO:0032720; P:negative regulation of tumor necrosis factor production; ISS:UniProtKB.
GO; GO:0010804; P:negative regulation of tumor necrosis factor-mediated signaling pathway; ISS:UniProtKB.
GO; GO:0045777; P:positive regulation of blood pressure; IEA:Ensembl.
GO; GO:2000481; P:positive regulation of cAMP-dependent protein kinase activity; IMP:UniProtKB.
GO; GO:0032270; P:positive regulation of cellular protein metabolic process; ISS:BHF-UCL.
GO; GO:0010875; P:positive regulation of cholesterol efflux; ISS:BHF-UCL.
GO; GO:0045923; P:positive regulation of fatty acid metabolic process; IMP:MGI.
GO; GO:0046326; P:positive regulation of glucose import; IDA:MGI.
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; IDA:MGI.
GO; GO:0032757; P:positive regulation of interleukin-8 production; ISS:UniProtKB.
GO; GO:2000478; P:positive regulation of metanephric glomerular visceral epithelial cell development; IMP:UniProtKB.
GO; GO:0071639; P:positive regulation of monocyte chemotactic protein-1 production; ISS:UniProtKB.
GO; GO:0033034; P:positive regulation of myeloid cell apoptotic process; ISS:UniProtKB.
GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IEA:Ensembl.
GO; GO:0010739; P:positive regulation of protein kinase A signaling; ISS:UniProtKB.
GO; GO:0001934; P:positive regulation of protein phosphorylation; ISS:UniProtKB.
GO; GO:2000534; P:positive regulation of renal albumin absorption; IMP:UniProtKB.
GO; GO:0009967; P:positive regulation of signal transduction; IDA:MGI.
GO; GO:0070208; P:protein heterotrimerization; IPI:MGI.
GO; GO:0051260; P:protein homooligomerization; IDA:MGI.
GO; GO:0072659; P:protein localization to plasma membrane; ISS:UniProtKB.
GO; GO:0010906; P:regulation of glucose metabolic process; ISS: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; IDA:MGI.
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; ISS:UniProtKB.
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; Direct protein sequencing;
Disulfide bond; Glycoprotein; Hormone; Hydroxylation;
Reference proteome; Repeat; Secreted; Signal.
SIGNAL 1 17 {ECO:0000269|PubMed:11912203}.
CHAIN 18 247 Adiponectin.
/FTId=PRO_0000003544.
DOMAIN 45 110 Collagen-like.
DOMAIN 111 247 C1q. {ECO:0000255|PROSITE-
ProRule:PRU00368}.
SITE 79 79 Not hydroxylated.
{ECO:0000269|PubMed:11912203}.
SITE 98 98 Not hydroxylated.
{ECO:0000269|PubMed:11912203}.
SITE 107 107 Not hydroxylated.
{ECO:0000269|PubMed:11912203}.
SITE 233 233 Not glycosylated.
{ECO:0000269|PubMed:11912203}.
MOD_RES 47 47 4-hydroxyproline. {ECO:0000250}.
MOD_RES 50 50 4-hydroxyproline. {ECO:0000250}.
MOD_RES 56 56 4-hydroxyproline. {ECO:0000250}.
MOD_RES 68 68 5-hydroxylysine; alternate.
{ECO:0000269|PubMed:11912203}.
MOD_RES 71 71 5-hydroxylysine; alternate.
{ECO:0000269|PubMed:11912203}.
MOD_RES 80 80 5-hydroxylysine; alternate.
{ECO:0000269|PubMed:11912203}.
MOD_RES 94 94 4-hydroxyproline.
{ECO:0000269|PubMed:11912203}.
MOD_RES 104 104 5-hydroxylysine; alternate.
{ECO:0000269|PubMed:11912203}.
CARBOHYD 23 23 O-linked (GalNAc...) threonine.
{ECO:0000305|PubMed:19855092}.
CARBOHYD 24 24 O-linked (GalNAc...) threonine.
{ECO:0000305|PubMed:19855092}.
CARBOHYD 68 68 O-linked (Gal...) hydroxylysine;
alternate. {ECO:0000269|PubMed:11912203}.
CARBOHYD 71 71 O-linked (Gal...) hydroxylysine;
alternate. {ECO:0000269|PubMed:11912203}.
CARBOHYD 80 80 O-linked (Gal...) hydroxylysine;
alternate. {ECO:0000269|PubMed:11912203}.
CARBOHYD 104 104 O-linked (Gal...) hydroxylysine;
alternate. {ECO:0000269|PubMed:11912203}.
DISULFID 39 39 Interchain. {ECO:0000250}.
MUTAGEN 39 39 C->A: No change in the interaction with
CTRP9. {ECO:0000269|PubMed:18787108}.
MUTAGEN 68 68 K->R: Impaired formation of HMW
multimers; when associated with R-71; R-
80 and R-104.
{ECO:0000269|PubMed:16621799}.
MUTAGEN 71 71 K->R: Impaired formation of HMW
multimers; when associated with R-68; R-
80 and R-104.
{ECO:0000269|PubMed:16621799}.
MUTAGEN 80 80 K->R: Impaired formation of HMW
multimers; when associated with R-68; R-
71 and R-104.
{ECO:0000269|PubMed:16621799}.
MUTAGEN 104 104 K->R: Impaired formation of HMW
multimers; when associated with R-68; R-
71 and R-80.
{ECO:0000269|PubMed:16621799}.
CONFLICT 50 50 P -> S (in Ref. 2; AAB06706).
{ECO:0000305}.
CONFLICT 74 74 A -> S (in Ref. 2; AAB06706).
{ECO:0000305}.
CONFLICT 113 113 V -> M (in Ref. 1; AAA80543 and 3;
AAK13417). {ECO:0000305}.
CONFLICT 117 117 A -> G (in Ref. 2; AAB06706).
{ECO:0000305}.
CONFLICT 148 148 G -> N (in Ref. 2; AAB06706).
{ECO:0000305}.
CONFLICT 243 243 Y -> F (in Ref. 2; AAB06706).
{ECO:0000305}.
STRAND 117 121 {ECO:0000244|PDB:1C28}.
STRAND 130 132 {ECO:0000244|PDB:1C3H}.
STRAND 137 140 {ECO:0000244|PDB:1C28}.
TURN 148 150 {ECO:0000244|PDB:1C28}.
STRAND 152 154 {ECO:0000244|PDB:1C3H}.
STRAND 159 172 {ECO:0000244|PDB:1C28}.
STRAND 174 180 {ECO:0000244|PDB:1C28}.
STRAND 183 190 {ECO:0000244|PDB:1C28}.
STRAND 197 208 {ECO:0000244|PDB:1C28}.
STRAND 213 218 {ECO:0000244|PDB:1C28}.
STRAND 236 244 {ECO:0000244|PDB:1C28}.
SEQUENCE 247 AA; 26809 MW; 0ECC687D9A8E8123 CRC64;
MLLLQALLFL LILPSHAEDD VTTTEELAPA LVPPPKGTCA GWMAGIPGHP GHNGTPGRDG
RDGTPGEKGE KGDAGLLGPK GETGDVGMTG AEGPRGFPGT PGRKGEPGEA AYVYRSAFSV
GLETRVTVPN VPIRFTKIFY NQQNHYDGST GKFYCNIPGL YYFSYHITVY MKDVKVSLFK
KDKAVLFTYD QYQEKNVDQA SGSVLLHLEV GDQVWLQVYG DGDHNGLYAD NVNDSTFTGF
LLYHDTN


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