UniProtKB - Q3Y5Z3 (ADIPO_BOVIN)
Adiponectin
ADIPOQ
Functioni
Miscellaneous
Activity regulationi
GO - Molecular functioni
- hormone activity Source: UniProtKB
- identical protein binding Source: IntAct
- sialic acid binding Source: UniProtKB
- signaling receptor binding Source: UniProtKB
GO - Biological processi
- brown fat cell differentiation Source: UniProtKB
- cellular response to drug Source: UniProtKB
- cellular response to insulin stimulus Source: UniProtKB
- detection of oxidative stress Source: UniProtKB
- fatty acid beta-oxidation Source: UniProtKB
- fatty acid oxidation Source: UniProtKB
- glucose homeostasis Source: UniProtKB
- glucose metabolic process Source: UniProtKB
- low-density lipoprotein particle clearance Source: UniProtKB
- negative regulation of blood pressure Source: UniProtKB
- negative regulation of cell migration Source: UniProtKB
- negative regulation of DNA biosynthetic process Source: UniProtKB
- negative regulation of ERK1 and ERK2 cascade Source: UniProtKB
- negative regulation of fat cell differentiation Source: UniProtKB
- negative regulation of gluconeogenesis Source: UniProtKB
- negative regulation of granulocyte differentiation Source: UniProtKB
- negative regulation of heterotypic cell-cell adhesion Source: UniProtKB
- negative regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
- negative regulation of inflammatory response Source: UniProtKB
- negative regulation of intracellular protein transport Source: UniProtKB
- negative regulation of low-density lipoprotein particle receptor biosynthetic process Source: UniProtKB
- negative regulation of macrophage derived foam cell differentiation Source: UniProtKB
- negative regulation of macrophage differentiation Source: UniProtKB
- negative regulation of MAP kinase activity Source: UniProtKB
- negative regulation of metanephric mesenchymal cell migration Source: UniProtKB
- negative regulation of phagocytosis Source: UniProtKB
- negative regulation of platelet-derived growth factor receptor-alpha signaling pathway Source: UniProtKB
- negative regulation of platelet-derived growth factor receptor signaling pathway Source: UniProtKB
- negative regulation of protein autophosphorylation Source: UniProtKB
- negative regulation of receptor binding Source: UniProtKB
- negative regulation of synaptic transmission Source: UniProtKB
- negative regulation of transcription, DNA-templated Source: UniProtKB
- negative regulation of tumor necrosis factor-mediated signaling pathway Source: UniProtKB
- negative regulation of tumor necrosis factor production Source: UniProtKB
- negative regulation of vascular associated smooth muscle cell migration Source: UniProtKB
- negative regulation of vascular associated smooth muscle cell proliferation Source: UniProtKB
- positive regulation of cAMP-dependent protein kinase activity Source: UniProtKB
- positive regulation of cellular protein metabolic process Source: AgBase
- positive regulation of cholesterol efflux Source: AgBase
- positive regulation of fatty acid metabolic process Source: UniProtKB
- positive regulation of glucose import Source: UniProtKB
- positive regulation of glycogen (starch) synthase activity Source: UniProtKB
- positive regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
- positive regulation of interleukin-8 production Source: UniProtKB
- positive regulation of metanephric glomerular visceral epithelial cell development Source: UniProtKB
- positive regulation of monocyte chemotactic protein-1 production Source: UniProtKB
- positive regulation of myeloid cell apoptotic process Source: UniProtKB
- positive regulation of protein kinase A signaling Source: UniProtKB
- positive regulation of protein phosphorylation Source: UniProtKB
- positive regulation of renal albumin absorption Source: UniProtKB
- positive regulation of signal transduction Source: UniProtKB
- protein localization to plasma membrane Source: UniProtKB
- regulation of glucose metabolic process Source: UniProtKB
- response to glucose Source: UniProtKB
- response to tumor necrosis factor Source: UniProtKB
Keywordsi
Molecular function | Hormone |
Enzyme and pathway databases
Reactomei | R-BTA-163680, AMPK inhibits chREBP transcriptional activation activity |
Names & Taxonomyi
Protein namesi | Recommended name: AdiponectinAlternative name(s): 30 kDa adipocyte complement-related protein Adipocyte complement-related 30 kDa protein Short name: ACRP30 Adipocyte, C1q and collagen domain-containing protein Adipose most abundant gene transcript 1 protein Short name: apM-1 |
Gene namesi | Name:ADIPOQ Synonyms:ACRP30, APM1 |
Organismi | Bos taurus (Bovine) |
Taxonomic identifieri | 9913 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Artiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos |
Proteomesi |
|
Subcellular locationi
Extracellular region or secreted
- Secreted 1 Publication
Endoplasmic reticulum
- endoplasmic reticulum Source: UniProtKB
Extracellular region or secreted
- extracellular space Source: AgBase
Other locations
- cell periphery Source: UniProtKB
- cell surface Source: BHF-UCL
- collagen trimer Source: UniProtKB-KW
- perinuclear region of cytoplasm Source: UniProtKB
Keywords - Cellular componenti
SecretedPTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Signal peptidei | 1 – 17 | 2 PublicationsAdd BLAST | 17 | |
ChainiPRO_0000236269 | 18 – 240 | AdiponectinAdd BLAST | 223 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 28 | 5-hydroxylysine1 Publication | 1 | |
Glycosylationi | 28 | O-linked (Gal...) hydroxylysine1 Publication | 1 | |
Modified residuei | 31 | S-(2-succinyl)cysteineBy similarity | 1 | |
Disulfide bondi | 31 | Interchain; in form MMW and form HMWBy similarity | ||
Modified residuei | 39 | 4-hydroxyproline1 Publication | 1 | |
Modified residuei | 42 | 4-hydroxyproline1 Publication | 1 | |
Modified residuei | 48 | 4-hydroxyproline1 Publication | 1 | |
Modified residuei | 60 | 5-hydroxylysine1 Publication | 1 | |
Glycosylationi | 60 | O-linked (Gal...) hydroxylysine1 Publication | 1 | |
Modified residuei | 63 | 5-hydroxylysine1 Publication | 1 | |
Glycosylationi | 63 | O-linked (Gal...) hydroxylysine1 Publication | 1 | |
Modified residuei | 72 | 5-hydroxylysine1 Publication | 1 | |
Glycosylationi | 72 | O-linked (Gal...) hydroxylysine1 Publication | 1 | |
Modified residuei | 86 | 4-hydroxyproline1 Publication | 1 | |
Modified residuei | 96 | 5-hydroxylysine1 Publication | 1 | |
Glycosylationi | 96 | O-linked (Gal...) hydroxylysine1 Publication | 1 |
Post-translational modificationi
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sitei | 57 | Not hydroxylated1 Publication | 1 | |
Sitei | 66 | Not hydroxylated1 Publication | 1 | |
Sitei | 71 | Not hydroxylated1 Publication | 1 | |
Sitei | 90 | Not hydroxylated1 Publication | 1 | |
Sitei | 99 | Not hydroxylated1 Publication | 1 | |
Sitei | 225 | Not glycosylated1 Publication | 1 |
Keywords - PTMi
Disulfide bond, Glycoprotein, HydroxylationProteomic databases
PaxDbi | Q3Y5Z3 |
PeptideAtlasi | Q3Y5Z3 |
PRIDEi | Q3Y5Z3 |
Expressioni
Gene expression databases
Bgeei | ENSBTAG00000019813, Expressed in intercostal muscle and 11 other tissues |
Interactioni
Subunit structurei
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 is also modulated by the degree of 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 similarityBinary interactionsi
Q3Y5Z3
With | #Exp. | IntAct |
---|---|---|
itself | 2 | EBI-7264459,EBI-7264459 |
GO - Molecular functioni
- hormone activity Source: UniProtKB
- identical protein binding Source: IntAct
- signaling receptor binding Source: UniProtKB
Protein-protein interaction databases
MINTi | Q3Y5Z3 |
STRINGi | 9913.ENSBTAP00000026395 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 43 – 102 | Collagen-likeAdd BLAST | 60 | |
Domaini | 103 – 240 | C1qPROSITE-ProRule annotationAdd BLAST | 138 |
Keywords - Domaini
Collagen, Repeat, SignalPhylogenomic databases
eggNOGi | ENOG502QRY3, Eukaryota |
HOGENOMi | CLU_001074_0_2_1 |
InParanoidi | Q3Y5Z3 |
OMAi | NDSTFMG |
OrthoDBi | 1258047at2759 |
TreeFami | TF329591 |
Family and domain databases
Gene3Di | 2.60.120.40, 1 hit |
InterProi | View protein in InterPro IPR001073, C1q_dom IPR008160, Collagen IPR008983, Tumour_necrosis_fac-like_dom |
Pfami | View protein in Pfam PF00386, C1q, 1 hit PF01391, Collagen, 1 hit |
PRINTSi | PR00007, COMPLEMNTC1Q |
SMARTi | View protein in SMART SM00110, C1Q, 1 hit |
SUPFAMi | SSF49842, SSF49842, 1 hit |
PROSITEi | View protein in PROSITE PS50871, C1Q, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
10 20 30 40 50
MLLQGALLLL LALPSHGEDN MEDPPLPKGA CAGWMAGIPG HPGHNGTPGR
60 70 80 90 100
DGRDGTPGEK GEKGDPGLVG PKGDTGETGI TGIEGPRGFP GTPGRKGEPG
110 120 130 140 150
ESAYVYRSAF SVGLERQVTV PNVPIRFTKI FYNQQNHYDG TTGKFLCNIP
160 170 180 190 200
GLYYFSYHIT VYLKDVKVSL YKNDKALLFT HDQFQDKNVD QASGSVLLYL
210 220 230 240
EKGDQVWLQV YEGENHNGVY ADNVNDSTFT GFLLYHNIVE
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 66 | P → A in AAK58902 (PubMed:11382781).Curated | 1 | |
Sequence conflicti | 69 | V → L in AAK58902 (PubMed:11382781).Curated | 1 | |
Sequence conflicti | 74 | D → E in AAK58902 (PubMed:11382781).Curated | 1 | |
Sequence conflicti | 77 – 83 | ETGITGI → DVGMTGA in AAK58902 (PubMed:11382781).Curated | 7 | |
Sequence conflicti | 102 | S → A in AAK58902 (PubMed:11382781).Curated | 1 | |
Sequence conflicti | 116 – 117 | RQ → TR in AAK58902 (PubMed:11382781).Curated | 2 | |
Sequence conflicti | 141 | T → S in AAK58902 (PubMed:11382781).Curated | 1 | |
Sequence conflicti | 146 | L → Y in AAK58902 (PubMed:11382781).Curated | 1 | |
Sequence conflicti | 163 | L → M in AAK58902 (PubMed:11382781).Curated | 1 | |
Sequence conflicti | 171 – 173 | YKN → FKK in AAK58902 (PubMed:11382781).Curated | 3 | |
Sequence conflicti | 177 | L → V in AAK58902 (PubMed:11382781).Curated | 1 | |
Sequence conflicti | 181 | H → Y in AAK58902 (PubMed:11382781).Curated | 1 | |
Sequence conflicti | 184 – 186 | FQD → YQE in AAK58902 (PubMed:11382781).Curated | 3 | |
Sequence conflicti | 199 | Y → H in AAK58902 (PubMed:11382781).Curated | 1 | |
Sequence conflicti | 202 | K → V in AAK58902 (PubMed:11382781).Curated | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AF269230 mRNA Translation: AAK58902.1 DQ156120 Genomic DNA Translation: AAZ81421.1 BC140488 mRNA Translation: AAI40489.1 |
RefSeqi | NP_777167.1, NM_174742.2 |
Genome annotation databases
GeneIDi | 282865 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AF269230 mRNA Translation: AAK58902.1 DQ156120 Genomic DNA Translation: AAZ81421.1 BC140488 mRNA Translation: AAI40489.1 |
RefSeqi | NP_777167.1, NM_174742.2 |
3D structure databases
SMRi | Q3Y5Z3 |
ModBasei | Search... |
Protein-protein interaction databases
MINTi | Q3Y5Z3 |
STRINGi | 9913.ENSBTAP00000026395 |
Proteomic databases
PaxDbi | Q3Y5Z3 |
PeptideAtlasi | Q3Y5Z3 |
PRIDEi | Q3Y5Z3 |
Genome annotation databases
GeneIDi | 282865 |
Organism-specific databases
CTDi | 9370 |
Phylogenomic databases
eggNOGi | ENOG502QRY3, Eukaryota |
HOGENOMi | CLU_001074_0_2_1 |
InParanoidi | Q3Y5Z3 |
OMAi | NDSTFMG |
OrthoDBi | 1258047at2759 |
TreeFami | TF329591 |
Enzyme and pathway databases
Reactomei | R-BTA-163680, AMPK inhibits chREBP transcriptional activation activity |
Gene expression databases
Bgeei | ENSBTAG00000019813, Expressed in intercostal muscle and 11 other tissues |
Family and domain databases
Gene3Di | 2.60.120.40, 1 hit |
InterProi | View protein in InterPro IPR001073, C1q_dom IPR008160, Collagen IPR008983, Tumour_necrosis_fac-like_dom |
Pfami | View protein in Pfam PF00386, C1q, 1 hit PF01391, Collagen, 1 hit |
PRINTSi | PR00007, COMPLEMNTC1Q |
SMARTi | View protein in SMART SM00110, C1Q, 1 hit |
SUPFAMi | SSF49842, SSF49842, 1 hit |
PROSITEi | View protein in PROSITE PS50871, C1Q, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | ADIPO_BOVIN | |
Accessioni | Q3Y5Z3Primary (citable) accession number: Q3Y5Z3 Secondary accession number(s): A5D7A8, Q95MQ4 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | May 30, 2006 |
Last sequence update: | September 27, 2005 | |
Last modified: | October 7, 2020 | |
This is version 110 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |