ADIPO_MOUSE
ID ADIPO_MOUSE Reviewed; 247 AA.
AC Q60994; Q62400; Q6GTX4; Q9DC68;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 2.
DT 03-AUG-2022, entry version 198.
DE RecName: Full=Adiponectin;
DE AltName: Full=30 kDa adipocyte complement-related protein;
DE AltName: Full=Adipocyte complement-related 30 kDa protein;
DE Short=ACRP30;
DE AltName: Full=Adipocyte, C1q and collagen domain-containing protein;
DE AltName: Full=Adipocyte-specific protein AdipoQ;
DE Flags: Precursor;
GN Name=Adipoq; Synonyms=Acdc, Acrp30, Apm1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Adipocyte;
RX PubMed=7592907; DOI=10.1074/jbc.270.45.26746;
RA Scherer P.E., Williams S., Fogliano M., Baldini G., Lodish H.F.;
RT "A novel serum protein similar to C1q, produced exclusively in
RT adipocytes.";
RL J. Biol. Chem. 270:26746-26749(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Fibroblast;
RX PubMed=8631877; DOI=10.1074/jbc.271.18.10697;
RA Hu E., Liang P., Spiegelman B.M.;
RT "AdipoQ is a novel adipose-specific gene dysregulated in obesity.";
RL J. Biol. Chem. 271:10697-10703(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11162643; DOI=10.1006/bbrc.2001.4217;
RA Das K., Lin Y., Widen E., Zhang Y., Scherer P.E.;
RT "Chromosomal localization, expression pattern, and promoter analysis of the
RT mouse gene encoding adipocyte-specific secretory protein Acrp30.";
RL Biochem. Biophys. Res. Commun. 280:1120-1129(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J, and IRM-2; TISSUE=White adipose tissue;
RA Wang S.F., Han P.Z., Mu C.J., Zhao M.H.;
RT "Cloning of murine adipocyte complement-related protein of 30 KDa from
RT white adipose tissue.";
RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Heart, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Thymus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP PROTEIN SEQUENCE OF 18-25, HYDROXYLATION AT LYS-68; LYS-71; LYS-80; PRO-94
RP AND LYS-104, GLYCOSYLATION AT LYS-68; LYS-71; LYS-80 AND LYS-104, GLYCAN
RP STRUCTURE, LACK OF HYDROXYLATION AT PRO-79; PRO-98 AND PRO-107, LACK OF
RP GLYCOSYLATION AT ASN-233, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=11912203; DOI=10.1074/jbc.m200601200;
RA Wang Y., Xu A., Knight C., Xu L.Y., Cooper G.J.S.;
RT "Hydroxylation and glycosylation of the four conserved lysine residues in
RT the collagenous domain of adiponectin. Potential role in the modulation of
RT its insulin-sensitizing activity.";
RL J. Biol. Chem. 277:19521-19529(2002).
RN [10]
RP STRUCTURE OF CARBOHYDRATES.
RX PubMed=11382781; DOI=10.1074/jbc.m104148200;
RA Sato C., Yasukawa Z., Honda N., Matsuda T., Kitajima K.;
RT "Identification and adipocyte differentiation-dependent expression of the
RT unique disialic acid residue in an adipose tissue-specific glycoprotein,
RT adipo Q.";
RL J. Biol. Chem. 276:28849-28856(2001).
RN [11]
RP FUNCTION.
RX PubMed=11479627; DOI=10.1038/90984;
RA Yamauchi T., Kamon J., Waki H., Terauchi Y., Kubota N., Hara K., Mori Y.,
RA Ide T., Murakami K., Tsuboyama-Kasaoka N., Ezaki O., Akanuma Y.,
RA Gavrilova O., Vinson C., Reitman M.L., Kagechika H., Shudo K., Yoda M.,
RA Nakano Y., Tobe K., Nagai R., Kimura S., Tomita M., Froguel P.,
RA Kadowaki T.;
RT "The fat-derived hormone adiponectin reverses insulin resistance associated
RT with both lipoatrophy and obesity.";
RL Nat. Med. 7:941-946(2001).
RN [12]
RP FUNCTION.
RX PubMed=11479628; DOI=10.1038/90992;
RA Berg A.H., Combs T.P., Du X., Brownlee M., Scherer P.E.;
RT "The adipocyte-secreted protein Acrp30 enhances hepatic insulin action.";
RL Nat. Med. 7:947-953(2001).
RN [13]
RP FUNCTION.
RX PubMed=12840063; DOI=10.1172/jci200317797;
RA Xu A., Wang Y., Keshaw H., Xu L.Y., Lam K.S.L., Cooper G.J.S.;
RT "The fat-derived hormone adiponectin alleviates alcoholic and nonalcoholic
RT fatty liver diseases in mice.";
RL J. Clin. Invest. 112:91-100(2003).
RN [14]
RP SUBUNIT, AND FUNCTION.
RX PubMed=15760892; DOI=10.1074/jbc.m414231200;
RA Xu A., Chan K.W., Hoo R.L.C., Wang Y., Tan K.C.B., Zhang J., Chen B.,
RA Lam M.C., Tse C., Cooper G.J.S., Lam K.S.L.;
RT "Testosterone selectively reduces the high molecular weight form of
RT adiponectin by inhibiting its secretion from adipocytes.";
RL J. Biol. Chem. 280:18073-18080(2005).
RN [15]
RP SUBUNIT, AND FUNCTION.
RX PubMed=15734737; DOI=10.1074/jbc.m501149200;
RA Wang Y., Lam K.S.L., Xu J.Y., Lu G., Xu L.Y., Cooper G.J.S., Xu A.;
RT "Adiponectin inhibits cell proliferation by interacting with several growth
RT factors in an oligomerization-dependent manner.";
RL J. Biol. Chem. 280:18341-18347(2005).
RN [16]
RP SUBUNIT, AND MUTAGENESIS OF LYS-68; LYS-71; LYS-80 AND LYS-104.
RX PubMed=16621799; DOI=10.1074/jbc.m513907200;
RA Wang Y., Lam K.S.L., Chan L., Chan K.W., Lam J.B.B., Lam M.C., Hoo R.C.L.,
RA Mak W.W.N., Cooper G.J.S., Xu A.;
RT "Post-translational modifications of the four conserved lysine residues
RT within the collagenous domain of adiponectin are required for the formation
RT of its high molecular weight oligomeric complex.";
RL J. Biol. Chem. 281:16391-16400(2006).
RN [17]
RP SUBUNIT, INTERACTION WITH CTRP9, AND MUTAGENESIS OF CYS-39.
RX PubMed=18787108; DOI=10.1096/fj.08-114991;
RA Wong G.W., Krawczyk S.A., Kitidis-Mitrokostas C., Ge G., Spooner E.,
RA Hug C., Gimeno R., Lodish H.F.;
RT "Identification and characterization of CTRP9, a novel secreted
RT glycoprotein, from adipose tissue that reduces serum glucose in mice and
RT forms heterotrimers with adiponectin.";
RL FASEB J. 23:241-258(2009).
RN [18]
RP SUCCINATION AT CYS-39, AND ACTIVITY REGULATION.
RX PubMed=19592500; DOI=10.1074/jbc.m109.019257;
RA Frizzell N., Rajesh M., Jepson M.J., Nagai R., Carson J.A., Thorpe S.R.,
RA Baynes J.W.;
RT "Succination of thiol groups in adipose tissue proteins in diabetes:
RT succination inhibits polymerization and secretion of adiponectin.";
RL J. Biol. Chem. 284:25772-25781(2009).
RN [19]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, and Lung;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [20]
RP GLYCOSYLATION AT THR-23 AND THR-24, AND SUBUNIT.
RX PubMed=19855092; DOI=10.1210/me.2009-0133;
RA Richards A.A., Colgrave M.L., Zhang J., Webster J., Simpson F., Preston E.,
RA Wilks D., Hoehn K.L., Stephenson M., Macdonald G.A., Prins J.B.,
RA Cooney G.J., Xu A., Whitehead J.P.;
RT "Sialic acid modification of adiponectin is not required for
RT multimerization or secretion but determines half-life in circulation.";
RL Mol. Endocrinol. 24:229-239(2010).
RN [21]
RP SUBUNIT, SUBCELLULAR LOCATION, HYDROXYLATION AT LYS-68; LYS-71; LYS-80 AND
RP LYS-104, GLYCOSYLATION AT LYS-68; LYS-71; LYS-80 AND LYS-104, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=23209641; DOI=10.1371/journal.pone.0050045;
RA Ruotsalainen H., Risteli M., Wang C., Wang Y., Karppinen M., Bergmann U.,
RA Kvist A.P., Pospiech H., Herzig K.H., Myllylae R.;
RT "The activities of lysyl hydroxylase 3 (LH3) regulate the amount and
RT oligomerization status of adiponectin.";
RL PLoS ONE 7:E50045-E50045(2012).
RN [22]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 111-247.
RX PubMed=9512423; DOI=10.1016/s0960-9822(98)70133-2;
RA Shapiro L., Scherer P.E.;
RT "The crystal structure of a complement-1q family protein suggests an
RT evolutionary link to tumor necrosis factor.";
RL Curr. Biol. 8:335-338(1998).
CC -!- FUNCTION: Important adipokine involved in the control of fat metabolism
CC and insulin sensitivity, with direct anti-diabetic, anti-atherogenic
CC and anti-inflammatory activities. Stimulates AMPK phosphorylation and
CC activation in the liver and the skeletal muscle, enhancing glucose
CC utilization and fatty-acid combustion. Antagonizes TNF-alpha by
CC negatively regulating its expression in various tissues such as liver
CC and macrophages, and also by counteracting its effects. Inhibits
CC endothelial NF-kappa-B signaling through a cAMP-dependent pathway. May
CC play a role in cell growth, angiogenesis and tissue remodeling by
CC binding and sequestering various growth factors with distinct binding
CC affinities, depending on the type of complex, LMW, MMW or HMW.
CC {ECO:0000269|PubMed:11479627, ECO:0000269|PubMed:11479628,
CC ECO:0000269|PubMed:12840063, ECO:0000269|PubMed:15734737,
CC ECO:0000269|PubMed:15760892}.
CC -!- ACTIVITY REGULATION: Polymerization and secretion of adiponectin is
CC inhibited by succination of cysteine residues by the Krebs cycle
CC intermediate fumarate, which leads to S-(2-succinyl)cysteine residues.
CC {ECO:0000269|PubMed:19592500}.
CC -!- SUBUNIT: Homomultimer (PubMed:23209641). Forms trimers, hexamers and
CC 12- to 18-mers. The trimers (low molecular weight complexes / LMW) are
CC assembled via non-covalent interactions of the collagen-like domains in
CC a triple helix and hydrophobic interactions within the globular C1q
CC domain. Several trimers can associate to form disulfide-linked hexamers
CC (middle molecular weight complexes / MMW) and larger complexes (higher
CC molecular weight / HMW) (PubMed:23209641). The HMW-complex assembly is
CC also modulated by the degree of lysine hydroxylation and glycosylation
CC (PubMed:23209641). LMW, MMW and HMW complexes bind to HBEGF, MMW and
CC HMW complexes bind to PDGFB, and HMW complex binds to FGF2. Interacts
CC with CTRP9 via the C1q domain (heterotrimeric complex)
CC (PubMed:18787108). {ECO:0000269|PubMed:15734737,
CC ECO:0000269|PubMed:15760892, ECO:0000269|PubMed:16621799,
CC ECO:0000269|PubMed:18787108, ECO:0000269|PubMed:19855092,
CC ECO:0000269|PubMed:23209641}.
CC -!- INTERACTION:
CC Q60994; Q60994: Adipoq; NbExp=17; IntAct=EBI-7264589, EBI-7264589;
CC Q60994; Q9DCM2: Gstk1; NbExp=3; IntAct=EBI-7264589, EBI-8369416;
CC Q60994; Q9Y2Q3: GSTK1; Xeno; NbExp=2; IntAct=EBI-7264589, EBI-1053767;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:23209641}.
CC -!- TISSUE SPECIFICITY: Synthesized exclusively by adipocytes and secreted
CC into plasma.
CC -!- INDUCTION: During hormone-induced adipose differentiation and activated
CC by insulin.
CC -!- PTM: HMW complexes are more extensively glycosylated than smaller
CC oligomers. Hydroxylation and glycosylation of the lysine residues
CC within the collagen-like domain of adiponectin seem to be critically
CC involved in regulating the formation and/or secretion of HMW complexes
CC and consequently contribute to the insulin-sensitizing activity of
CC adiponectin in hepatocytes. {ECO:0000269|PubMed:11912203,
CC ECO:0000269|PubMed:23209641}.
CC -!- PTM: O-glycosylated. Not N-glycosylated (By similarity) O-linked
CC glycans on hydroxylysine residues consist of Glc-Gal disaccharides
CC bound to the oxygen atom of post-translationally added hydroxyl groups
CC (By similarity). O-linked glycosylation in the N-terminal is
CC disialylated with the structure Neu5Acalpha2->8Neu5Acalpha2->3Gal.
CC Sialylated by alpha 2,8-sialyltransferase III. {ECO:0000250}.
CC -!- PTM: Succination of Cys-39 by the Krebs cycle intermediate fumarate,
CC which leads to S-(2-succinyl)cysteine residues, inhibits polymerization
CC and secretion of adiponectin. Adiponectin is a major target for
CC succination in both adipocytes and adipose tissue of diabetic mice. It
CC was proposed that succination of proteins is a biomarker of
CC mitochondrial stress and accumulation of Krebs cycle intermediates in
CC adipose tissue in diabetes and that succination of adiponectin may
CC contribute to the decrease in plasma adiponectin in diabetes.
CC {ECO:0000269|PubMed:19592500}.
CC -!- MISCELLANEOUS: HMW-complex blood contents are higher in females than in
CC males, are increased in males by castration and decreased again upon
CC subsequent testosterone treatment, which blocks HMW-complex secretion.
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DR EMBL; U37222; AAA80543.1; -; mRNA.
DR EMBL; U49915; AAB06706.1; -; mRNA.
DR EMBL; AF304466; AAK13417.1; -; Genomic_DNA.
DR EMBL; AY749429; AAW70555.1; -; mRNA.
DR EMBL; AY754346; AAW82905.1; -; mRNA.
DR EMBL; AK003138; BAB22597.1; -; mRNA.
DR EMBL; AK134112; BAE22019.1; -; mRNA.
DR EMBL; AC125396; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466521; EDK97661.1; -; Genomic_DNA.
DR EMBL; BC028770; AAH28770.1; -; mRNA.
DR CCDS; CCDS28075.1; -.
DR RefSeq; NP_033735.3; NM_009605.5.
DR PDB; 1C28; X-ray; 2.10 A; A/B/C=114-247.
DR PDB; 1C3H; X-ray; 2.10 A; A/B/C/D/E/F=111-247.
DR PDBsum; 1C28; -.
DR PDBsum; 1C3H; -.
DR AlphaFoldDB; Q60994; -.
DR SMR; Q60994; -.
DR BioGRID; 197940; 6.
DR CORUM; Q60994; -.
DR DIP; DIP-44111N; -.
DR IntAct; Q60994; 5.
DR MINT; Q60994; -.
DR STRING; 10090.ENSMUSP00000023593; -.
DR GlyGen; Q60994; 6 sites.
DR iPTMnet; Q60994; -.
DR PhosphoSitePlus; Q60994; -.
DR SwissPalm; Q60994; -.
DR CPTAC; non-CPTAC-3294; -.
DR CPTAC; non-CPTAC-3335; -.
DR CPTAC; non-CPTAC-3336; -.
DR jPOST; Q60994; -.
DR PaxDb; Q60994; -.
DR PeptideAtlas; Q60994; -.
DR PRIDE; Q60994; -.
DR ProteomicsDB; 296185; -.
DR Antibodypedia; 19310; 1898 antibodies from 49 providers.
DR DNASU; 11450; -.
DR Ensembl; ENSMUST00000023593; ENSMUSP00000023593; ENSMUSG00000022878.
DR GeneID; 11450; -.
DR KEGG; mmu:11450; -.
DR UCSC; uc007ytk.1; mouse.
DR CTD; 9370; -.
DR MGI; MGI:106675; Adipoq.
DR VEuPathDB; HostDB:ENSMUSG00000022878; -.
DR eggNOG; ENOG502QRY3; Eukaryota.
DR GeneTree; ENSGT00940000159828; -.
DR HOGENOM; CLU_001074_0_2_1; -.
DR InParanoid; Q60994; -.
DR OMA; DSTFMGF; -.
DR OrthoDB; 1258047at2759; -.
DR PhylomeDB; Q60994; -.
DR TreeFam; TF329591; -.
DR Reactome; R-MMU-163680; AMPK inhibits chREBP transcriptional activation activity.
DR BioGRID-ORCS; 11450; 1 hit in 74 CRISPR screens.
DR EvolutionaryTrace; Q60994; -.
DR PRO; PR:Q60994; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q60994; protein.
DR Bgee; ENSMUSG00000022878; Expressed in gonadal fat pad and 105 other tissues.
DR ExpressionAtlas; Q60994; baseline and differential.
DR Genevisible; Q60994; MM.
DR GO; GO:0071944; C:cell periphery; ISS:UniProtKB.
DR GO; GO:0009986; C:cell surface; ISS:UniProtKB.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
DR GO; GO:0005615; C:extracellular space; IDA:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0005179; F:hormone activity; IDA:MGI.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0033691; F:sialic acid binding; ISO:MGI.
DR GO; GO:0005102; F:signaling receptor binding; IDA:MGI.
DR GO; GO:0050873; P:brown fat cell differentiation; IDA:MGI.
DR GO; GO:0071320; P:cellular response to cAMP; ISO:MGI.
DR GO; GO:0071872; P:cellular response to epinephrine stimulus; ISO:MGI.
DR GO; GO:0032869; P:cellular response to insulin stimulus; IGI:MGI.
DR GO; GO:0071466; P:cellular response to xenobiotic stimulus; IDA:UniProtKB.
DR GO; GO:0007623; P:circadian rhythm; IEA:Ensembl.
DR GO; GO:0070994; P:detection of oxidative stress; IMP:UniProtKB.
DR GO; GO:0006635; P:fatty acid beta-oxidation; IMP:MGI.
DR GO; GO:0019395; P:fatty acid oxidation; IDA:MGI.
DR GO; GO:0010467; P:gene expression; IDA:MGI.
DR GO; GO:0042593; P:glucose homeostasis; IDA:MGI.
DR GO; GO:0006006; P:glucose metabolic process; IDA:MGI.
DR GO; GO:0034383; P:low-density lipoprotein particle clearance; ISS:UniProtKB.
DR GO; GO:0045776; P:negative regulation of blood pressure; ISS:UniProtKB.
DR GO; GO:0030336; P:negative regulation of cell migration; IDA:UniProtKB.
DR GO; GO:0120163; P:negative regulation of cold-induced thermogenesis; IMP:YuBioLab.
DR GO; GO:2000279; P:negative regulation of DNA biosynthetic process; ISS:UniProtKB.
DR GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; ISS:UniProtKB.
DR GO; GO:0045599; P:negative regulation of fat cell differentiation; IDA:BHF-UCL.
DR GO; GO:0045721; P:negative regulation of gluconeogenesis; IDA:MGI.
DR GO; GO:0030853; P:negative regulation of granulocyte differentiation; ISS:UniProtKB.
DR GO; GO:0034115; P:negative regulation of heterotypic cell-cell adhesion; ISS:UniProtKB.
DR GO; GO:0046888; P:negative regulation of hormone secretion; ISO:MGI.
DR GO; GO:0043124; P:negative regulation of I-kappaB kinase/NF-kappaB signaling; ISS:UniProtKB.
DR GO; GO:0050728; P:negative regulation of inflammatory response; IDA:UniProtKB.
DR GO; GO:0090317; P:negative regulation of intracellular protein transport; ISS:UniProtKB.
DR GO; GO:1905598; P:negative regulation of low-density lipoprotein receptor activity; ISO:MGI.
DR GO; GO:0010745; P:negative regulation of macrophage derived foam cell differentiation; ISS:UniProtKB.
DR GO; GO:0045650; P:negative regulation of macrophage differentiation; ISS:UniProtKB.
DR GO; GO:0043407; P:negative regulation of MAP kinase activity; IDA:UniProtKB.
DR GO; GO:2000590; P:negative regulation of metanephric mesenchymal cell migration; IDA:UniProtKB.
DR GO; GO:0050765; P:negative regulation of phagocytosis; ISS:UniProtKB.
DR GO; GO:0010642; P:negative regulation of platelet-derived growth factor receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:2000584; P:negative regulation of platelet-derived growth factor receptor-alpha signaling pathway; IDA:UniProtKB.
DR GO; GO:0031953; P:negative regulation of protein autophosphorylation; ISS:UniProtKB.
DR GO; GO:1900121; P:negative regulation of receptor binding; ISS:UniProtKB.
DR GO; GO:0050805; P:negative regulation of synaptic transmission; ISS:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:UniProtKB.
DR GO; GO:0032720; P:negative regulation of tumor necrosis factor production; ISS:UniProtKB.
DR GO; GO:0010804; P:negative regulation of tumor necrosis factor-mediated signaling pathway; ISS:UniProtKB.
DR GO; GO:1904753; P:negative regulation of vascular associated smooth muscle cell migration; ISS:UniProtKB.
DR GO; GO:1904706; P:negative regulation of vascular associated smooth muscle cell proliferation; ISS:UniProtKB.
DR GO; GO:2000481; P:positive regulation of cAMP-dependent protein kinase activity; IMP:UniProtKB.
DR GO; GO:0010875; P:positive regulation of cholesterol efflux; ISS:UniProtKB.
DR GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; IMP:YuBioLab.
DR GO; GO:0045923; P:positive regulation of fatty acid metabolic process; IMP:MGI.
DR GO; GO:0046326; P:positive regulation of glucose import; IDA:MGI.
DR GO; GO:2000467; P:positive regulation of glycogen (starch) synthase activity; ISS:UniProtKB.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IDA:MGI.
DR GO; GO:0032757; P:positive regulation of interleukin-8 production; ISS:UniProtKB.
DR GO; GO:0110113; P:positive regulation of lipid transporter activity; ISS:UniProtKB.
DR GO; GO:2000478; P:positive regulation of metanephric podocyte development; IMP:UniProtKB.
DR GO; GO:0071639; P:positive regulation of monocyte chemotactic protein-1 production; ISS:UniProtKB.
DR GO; GO:0033034; P:positive regulation of myeloid cell apoptotic process; ISS:UniProtKB.
DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; ISO:MGI.
DR GO; GO:0010739; P:positive regulation of protein kinase A signaling; ISS:UniProtKB.
DR GO; GO:0045860; P:positive regulation of protein kinase activity; ISO:MGI.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; ISS:UniProtKB.
DR GO; GO:2000534; P:positive regulation of renal albumin absorption; IMP:UniProtKB.
DR GO; GO:0009967; P:positive regulation of signal transduction; IDA:MGI.
DR GO; GO:0072659; P:protein localization to plasma membrane; ISS:UniProtKB.
DR GO; GO:0010906; P:regulation of glucose metabolic process; ISS:UniProtKB.
DR GO; GO:0014823; P:response to activity; IEA:Ensembl.
DR GO; GO:0009617; P:response to bacterium; IEP:MGI.
DR GO; GO:0045471; P:response to ethanol; IEA:Ensembl.
DR GO; GO:0051384; P:response to glucocorticoid; IEA:Ensembl.
DR GO; GO:0009749; P:response to glucose; IDA:MGI.
DR GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
DR GO; GO:0070543; P:response to linoleic acid; IEA:Ensembl.
DR GO; GO:0007584; P:response to nutrient; IEA:Ensembl.
DR GO; GO:0009744; P:response to sucrose; IEA:Ensembl.
DR GO; GO:0034612; P:response to tumor necrosis factor; ISS:UniProtKB.
DR Gene3D; 2.60.120.40; -; 1.
DR InterPro; IPR028572; Adiponectin.
DR InterPro; IPR001073; C1q_dom.
DR InterPro; IPR008160; Collagen.
DR InterPro; IPR008983; Tumour_necrosis_fac-like_dom.
DR PANTHER; PTHR15427:SF20; PTHR15427:SF20; 1.
DR Pfam; PF00386; C1q; 1.
DR Pfam; PF01391; Collagen; 1.
DR PRINTS; PR00007; COMPLEMNTC1Q.
DR SMART; SM00110; C1Q; 1.
DR SUPFAM; SSF49842; SSF49842; 1.
DR PROSITE; PS50871; C1Q; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Collagen; Direct protein sequencing; Disulfide bond;
KW Glycoprotein; Hormone; Hydroxylation; Reference proteome; Repeat; Secreted;
KW Signal.
FT SIGNAL 1..17
FT /evidence="ECO:0000269|PubMed:11912203"
FT CHAIN 18..247
FT /note="Adiponectin"
FT /id="PRO_0000003544"
FT DOMAIN 45..110
FT /note="Collagen-like"
FT DOMAIN 111..247
FT /note="C1q"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00368"
FT REGION 44..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 61..75
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 79
FT /note="Not hydroxylated"
FT /evidence="ECO:0000269|PubMed:11912203"
FT SITE 98
FT /note="Not hydroxylated"
FT /evidence="ECO:0000269|PubMed:11912203"
FT SITE 107
FT /note="Not hydroxylated"
FT /evidence="ECO:0000269|PubMed:11912203"
FT SITE 233
FT /note="Not glycosylated"
FT /evidence="ECO:0000269|PubMed:11912203"
FT MOD_RES 36
FT /note="5-hydroxylysine"
FT /evidence="ECO:0000250|UniProtKB:Q3Y5Z3"
FT MOD_RES 39
FT /note="S-(2-succinyl)cysteine"
FT /evidence="ECO:0000269|PubMed:19592500"
FT MOD_RES 47
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 50
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 56
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 68
FT /note="5-hydroxylysine; alternate"
FT /evidence="ECO:0000269|PubMed:11912203,
FT ECO:0000269|PubMed:23209641"
FT MOD_RES 71
FT /note="5-hydroxylysine; alternate"
FT /evidence="ECO:0000269|PubMed:11912203,
FT ECO:0000269|PubMed:23209641"
FT MOD_RES 80
FT /note="5-hydroxylysine; alternate"
FT /evidence="ECO:0000269|PubMed:11912203,
FT ECO:0000269|PubMed:23209641"
FT MOD_RES 94
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:11912203"
FT MOD_RES 104
FT /note="5-hydroxylysine; alternate"
FT /evidence="ECO:0000269|PubMed:11912203,
FT ECO:0000269|PubMed:23209641"
FT CARBOHYD 23
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000305|PubMed:19855092"
FT CARBOHYD 24
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000305|PubMed:19855092"
FT CARBOHYD 68
FT /note="O-linked (Gal...) hydroxylysine; alternate"
FT /evidence="ECO:0000269|PubMed:11912203,
FT ECO:0000269|PubMed:23209641"
FT CARBOHYD 71
FT /note="O-linked (Gal...) hydroxylysine; alternate"
FT /evidence="ECO:0000269|PubMed:11912203,
FT ECO:0000269|PubMed:23209641"
FT CARBOHYD 80
FT /note="O-linked (Gal...) hydroxylysine; alternate"
FT /evidence="ECO:0000269|PubMed:11912203,
FT ECO:0000269|PubMed:23209641"
FT CARBOHYD 104
FT /note="O-linked (Gal...) hydroxylysine; alternate"
FT /evidence="ECO:0000269|PubMed:11912203,
FT ECO:0000269|PubMed:23209641"
FT DISULFID 39
FT /note="Interchain"
FT /evidence="ECO:0000250"
FT MUTAGEN 39
FT /note="C->A: No change in the interaction with CTRP9."
FT /evidence="ECO:0000269|PubMed:18787108"
FT MUTAGEN 68
FT /note="K->R: Impaired formation of HMW multimers; when
FT associated with R-71; R-80 and R-104."
FT /evidence="ECO:0000269|PubMed:16621799"
FT MUTAGEN 71
FT /note="K->R: Impaired formation of HMW multimers; when
FT associated with R-68; R-80 and R-104."
FT /evidence="ECO:0000269|PubMed:16621799"
FT MUTAGEN 80
FT /note="K->R: Impaired formation of HMW multimers; when
FT associated with R-68; R-71 and R-104."
FT /evidence="ECO:0000269|PubMed:16621799"
FT MUTAGEN 104
FT /note="K->R: Impaired formation of HMW multimers; when
FT associated with R-68; R-71 and R-80."
FT /evidence="ECO:0000269|PubMed:16621799"
FT CONFLICT 50
FT /note="P -> S (in Ref. 2; AAB06706)"
FT /evidence="ECO:0000305"
FT CONFLICT 74
FT /note="A -> S (in Ref. 2; AAB06706)"
FT /evidence="ECO:0000305"
FT CONFLICT 113
FT /note="V -> M (in Ref. 1; AAA80543 and 3; AAK13417)"
FT /evidence="ECO:0000305"
FT CONFLICT 117
FT /note="A -> G (in Ref. 2; AAB06706)"
FT /evidence="ECO:0000305"
FT CONFLICT 148
FT /note="G -> N (in Ref. 2; AAB06706)"
FT /evidence="ECO:0000305"
FT CONFLICT 243
FT /note="Y -> F (in Ref. 2; AAB06706)"
FT /evidence="ECO:0000305"
FT STRAND 117..121
FT /evidence="ECO:0007829|PDB:1C28"
FT STRAND 130..132
FT /evidence="ECO:0007829|PDB:1C3H"
FT STRAND 137..140
FT /evidence="ECO:0007829|PDB:1C28"
FT TURN 148..150
FT /evidence="ECO:0007829|PDB:1C28"
FT STRAND 152..154
FT /evidence="ECO:0007829|PDB:1C3H"
FT STRAND 159..172
FT /evidence="ECO:0007829|PDB:1C28"
FT STRAND 174..180
FT /evidence="ECO:0007829|PDB:1C28"
FT STRAND 183..190
FT /evidence="ECO:0007829|PDB:1C28"
FT STRAND 197..208
FT /evidence="ECO:0007829|PDB:1C28"
FT STRAND 213..218
FT /evidence="ECO:0007829|PDB:1C28"
FT STRAND 236..244
FT /evidence="ECO:0007829|PDB:1C28"
SQ 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
