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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)

 ADIPO_BOVIN             Reviewed;         240 AA.
Q3Y5Z3; A5D7A8; Q95MQ4;
30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
27-SEP-2005, sequence version 1.
28-MAR-2018, entry version 91.
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;
Flags: Precursor;
Name=ADIPOQ; Synonyms=ACRP30, APM1;
Bos taurus (Bovine).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Bovinae; Bos.
NCBI_TaxID=9913;
[1]
NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 18-26; 194-197;
203-208 AND 221-228, GLYCOSYLATION, AND STRUCTURE OF CARBOHYDRATES.
TISSUE=Adipose tissue;
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).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Morsci N.S., Schnabel R.D., Taylor J.F.;
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Hereford; TISSUE=Ascending colon;
NIH - Mammalian Gene Collection (MGC) project;
Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
[4]
PROTEIN SEQUENCE OF 18-26, PARTIAL PROTEIN SEQUENCE, HYDROXYLATION AT
LYS-28; PRO-39; PRO-42; PRO-48; LYS-60; LYS-63; LYS-72; PRO-86 AND
LYS-96, GLYCOSYLATION AT LYS-28; LYS-60; LYS-63 AND LYS-96, LACK OF
HYDROXYLATION AT PRO-57; PRO-66; PRO-71; PRO-90 AND PRO-99, LACK OF
GLYCOSYLATION AT ASN-225, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=15378692; DOI=10.1002/pmic.200400826;
Wang Y., Lu G., Wong W.P.S., Vliegenthart J.F.G., Gerwig G.J.,
Lam K.S.L., Cooper G.J.S., Xu A.;
"Proteomic and functional characterization of endogenous adiponectin
purified from fetal bovine serum.";
Proteomics 4:3933-3942(2004).
-!- 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 (By
similarity). {ECO:0000250}.
-!- 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)
(By similarity). {ECO:0000250}.
-!- INTERACTION:
Self; NbExp=2; IntAct=EBI-7264459, EBI-7264459;
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
-!- 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. 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
glycosylations elsewhere disialylated with the structure
Neu5Acalpha2->8Neu5Acalpha2->3Gal. Sialylated by alpha 2,8-
sialyltransferase III. Desialylated forms are rapidly cleared from
the circulation. Not N-glycosylated. {ECO:0000250,
ECO:0000269|PubMed:11382781, ECO:0000269|PubMed:15378692}.
-!- 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. {ECO:0000250}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AF269230; AAK58902.1; -; mRNA.
EMBL; DQ156120; AAZ81421.1; -; Genomic_DNA.
EMBL; BC140488; AAI40489.1; -; mRNA.
RefSeq; NP_777167.1; NM_174742.2.
UniGene; Bt.109637; -.
ProteinModelPortal; Q3Y5Z3; -.
SMR; Q3Y5Z3; -.
MINT; Q3Y5Z3; -.
STRING; 9913.ENSBTAP00000026395; -.
PaxDb; Q3Y5Z3; -.
PeptideAtlas; Q3Y5Z3; -.
PRIDE; Q3Y5Z3; -.
Ensembl; ENSBTAT00000026395; ENSBTAP00000026395; ENSBTAG00000019813.
GeneID; 282865; -.
KEGG; bta:282865; -.
CTD; 9370; -.
VGNC; VGNC:25677; ADIPOQ.
eggNOG; ENOG410IHSJ; Eukaryota.
eggNOG; ENOG4111F5K; LUCA.
GeneTree; ENSGT00760000118830; -.
HOGENOM; HOG000085653; -.
HOVERGEN; HBG108220; -.
InParanoid; Q3Y5Z3; -.
KO; K07296; -.
OMA; QQNHYDG; -.
OrthoDB; EOG091G0L3Y; -.
TreeFam; TF329591; -.
Reactome; R-BTA-163680; AMPK inhibits chREBP transcriptional activation activity.
Proteomes; UP000009136; Chromosome 1.
Bgee; ENSBTAG00000019813; -.
GO; GO:0005623; C:cell; IDA:AgBase.
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; ISS:UniProtKB.
GO; GO:0005615; C:extracellular space; IDA:AgBase.
GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
GO; GO:0005179; F:hormone activity; ISS:UniProtKB.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
GO; GO:0005102; F:receptor binding; ISS:UniProtKB.
GO; GO:0033691; F:sialic acid binding; IDA:UniProtKB.
GO; GO:0050873; P:brown fat cell differentiation; ISS:UniProtKB.
GO; GO:0035690; P:cellular response to drug; ISS:UniProtKB.
GO; GO:0032869; P:cellular response to insulin stimulus; ISS:UniProtKB.
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:0042593; P:glucose homeostasis; ISS:UniProtKB.
GO; GO:0006006; P:glucose metabolic process; ISS:UniProtKB.
GO; GO:0034383; P:low-density lipoprotein particle clearance; ISS:UniProtKB.
GO; GO:0045776; P:negative regulation of blood pressure; ISS:UniProtKB.
GO; GO:0030336; P:negative regulation of cell migration; ISS: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; ISS:UniProtKB.
GO; GO:0045721; P:negative regulation of gluconeogenesis; ISS:UniProtKB.
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:0043124; P:negative regulation of I-kappaB kinase/NF-kappaB signaling; ISS:UniProtKB.
GO; GO:0050728; P:negative regulation of inflammatory response; ISS: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; ISS:UniProtKB.
GO; GO:2000590; P:negative regulation of metanephric mesenchymal cell migration; ISS: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; ISS: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; ISS:UniProtKB.
GO; GO:1900121; P:negative regulation of receptor binding; ISS:UniProtKB.
GO; GO:0050805; P:negative regulation of synaptic transmission; ISS:UniProtKB.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS: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:1904753; P:negative regulation of vascular associated smooth muscle cell migration; ISS:UniProtKB.
GO; GO:1904706; P:negative regulation of vascular smooth muscle cell proliferation; ISS:UniProtKB.
GO; GO:2000481; P:positive regulation of cAMP-dependent protein kinase activity; ISS:UniProtKB.
GO; GO:0032270; P:positive regulation of cellular protein metabolic process; ISS:AgBase.
GO; GO:0010875; P:positive regulation of cholesterol efflux; ISS:AgBase.
GO; GO:0045923; P:positive regulation of fatty acid metabolic process; ISS:UniProtKB.
GO; GO:0046326; P:positive regulation of glucose import; ISS:UniProtKB.
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; ISS: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; ISS:UniProtKB.
GO; GO:0033034; P:positive regulation of myeloid cell apoptotic process; ISS:UniProtKB.
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; ISS:UniProtKB.
GO; GO:0009967; P:positive regulation of signal transduction; ISS:UniProtKB.
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; ISS:UniProtKB.
GO; GO:0010906; P:regulation of glucose metabolic process; ISS:UniProtKB.
GO; GO:0009749; P:response to glucose; ISS:UniProtKB.
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;
Collagen; Complete proteome; Direct protein sequencing;
Disulfide bond; Glycoprotein; Hormone; Hydroxylation;
Reference proteome; Repeat; Secreted; Signal.
SIGNAL 1 17 {ECO:0000269|PubMed:11382781,
ECO:0000269|PubMed:15378692}.
CHAIN 18 240 Adiponectin.
/FTId=PRO_0000236269.
DOMAIN 43 102 Collagen-like.
DOMAIN 103 240 C1q. {ECO:0000255|PROSITE-
ProRule:PRU00368}.
SITE 57 57 Not hydroxylated.
{ECO:0000269|PubMed:15378692}.
SITE 66 66 Not hydroxylated.
{ECO:0000269|PubMed:15378692}.
SITE 71 71 Not hydroxylated.
{ECO:0000269|PubMed:15378692}.
SITE 90 90 Not hydroxylated.
{ECO:0000269|PubMed:15378692}.
SITE 99 99 Not hydroxylated.
{ECO:0000269|PubMed:15378692}.
SITE 225 225 Not glycosylated.
{ECO:0000269|PubMed:15378692}.
MOD_RES 28 28 5-hydroxylysine.
{ECO:0000269|PubMed:15378692}.
MOD_RES 39 39 4-hydroxyproline.
{ECO:0000269|PubMed:15378692}.
MOD_RES 42 42 4-hydroxyproline.
{ECO:0000269|PubMed:15378692}.
MOD_RES 48 48 4-hydroxyproline.
{ECO:0000269|PubMed:15378692}.
MOD_RES 60 60 5-hydroxylysine.
{ECO:0000269|PubMed:15378692}.
MOD_RES 63 63 5-hydroxylysine.
{ECO:0000269|PubMed:15378692}.
MOD_RES 72 72 5-hydroxylysine.
{ECO:0000269|PubMed:15378692}.
MOD_RES 86 86 4-hydroxyproline.
{ECO:0000269|PubMed:15378692}.
MOD_RES 96 96 5-hydroxylysine.
{ECO:0000269|PubMed:15378692}.
CARBOHYD 28 28 O-linked (Gal...) hydroxylysine.
{ECO:0000269|PubMed:15378692}.
CARBOHYD 60 60 O-linked (Gal...) hydroxylysine.
{ECO:0000269|PubMed:15378692}.
CARBOHYD 63 63 O-linked (Gal...) hydroxylysine.
{ECO:0000269|PubMed:15378692}.
CARBOHYD 72 72 O-linked (Gal...) hydroxylysine.
{ECO:0000269|PubMed:11382781}.
CARBOHYD 96 96 O-linked (Gal...) hydroxylysine.
{ECO:0000269|PubMed:15378692}.
DISULFID 31 31 Interchain; in form MMW and form HMW.
{ECO:0000250}.
CONFLICT 66 66 P -> A (in Ref. 1; AAK58902).
{ECO:0000305}.
CONFLICT 69 69 V -> L (in Ref. 1; AAK58902).
{ECO:0000305}.
CONFLICT 74 74 D -> E (in Ref. 1; AAK58902).
{ECO:0000305}.
CONFLICT 77 83 ETGITGI -> DVGMTGA (in Ref. 1; AAK58902).
{ECO:0000305}.
CONFLICT 102 102 S -> A (in Ref. 1; AAK58902).
{ECO:0000305}.
CONFLICT 116 117 RQ -> TR (in Ref. 1; AAK58902).
{ECO:0000305}.
CONFLICT 141 141 T -> S (in Ref. 1; AAK58902).
{ECO:0000305}.
CONFLICT 146 146 L -> Y (in Ref. 1; AAK58902).
{ECO:0000305}.
CONFLICT 163 163 L -> M (in Ref. 1; AAK58902).
{ECO:0000305}.
CONFLICT 171 173 YKN -> FKK (in Ref. 1; AAK58902).
{ECO:0000305}.
CONFLICT 177 177 L -> V (in Ref. 1; AAK58902).
{ECO:0000305}.
CONFLICT 181 181 H -> Y (in Ref. 1; AAK58902).
{ECO:0000305}.
CONFLICT 184 186 FQD -> YQE (in Ref. 1; AAK58902).
{ECO:0000305}.
CONFLICT 199 199 Y -> H (in Ref. 1; AAK58902).
{ECO:0000305}.
CONFLICT 202 202 K -> V (in Ref. 1; AAK58902).
{ECO:0000305}.
SEQUENCE 240 AA; 26133 MW; 409122E49F3AF253 CRC64;
MLLQGALLLL LALPSHGEDN MEDPPLPKGA CAGWMAGIPG HPGHNGTPGR DGRDGTPGEK
GEKGDPGLVG PKGDTGETGI TGIEGPRGFP GTPGRKGEPG ESAYVYRSAF SVGLERQVTV
PNVPIRFTKI FYNQQNHYDG TTGKFLCNIP GLYYFSYHIT VYLKDVKVSL YKNDKALLFT
HDQFQDKNVD QASGSVLLYL EKGDQVWLQV YEGENHNGVY ADNVNDSTFT GFLLYHNIVE


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