Q3Y5Z3 (ADIPO_BOVIN) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 55.
History...
Clusters with 
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Adiponectin Alternative 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 names |
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| Organism | Bos taurus (Bovine) [Reference proteome] | ||||
| Taxonomic identifier | 9913 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos |
Protein attributes
| Sequence length | 240 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| 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. |
| Subunit structure | 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 aditionally 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. |
| Subcellular location | Secreted By similarity. |
| Post-translational modification | 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. Ref.1 Ref.4 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. Ref.1 Ref.4 |
| 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. |
| Sequence similarities | Contains 1 C1q domain. Contains 1 collagen-like domain. |
Ontologies
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 17 | 17 | Ref.1 Ref.4 | ||||||
| Chain | 18 – 240 | 223 | Adiponectin | PRO_0000236269 | |||||
Regions | |||||||||
| Domain | 43 – 102 | 60 | Collagen-like | ||||||
| Domain | 103 – 240 | 138 | C1q | ||||||
Sites | |||||||||
| Site | 57 | 1 | Not hydroxylated | ||||||
| Site | 66 | 1 | Not hydroxylated | ||||||
| Site | 71 | 1 | Not hydroxylated | ||||||
| Site | 90 | 1 | Not hydroxylated | ||||||
| Site | 99 | 1 | Not hydroxylated | ||||||
| Site | 225 | 1 | Not glycosylated | ||||||
Amino acid modifications | |||||||||
| Modified residue | 28 | 1 | 5-hydroxylysine Ref.4 | ||||||
| Modified residue | 39 | 1 | 4-hydroxyproline Ref.4 | ||||||
| Modified residue | 42 | 1 | 4-hydroxyproline Ref.4 | ||||||
| Modified residue | 48 | 1 | 4-hydroxyproline Ref.4 | ||||||
| Modified residue | 60 | 1 | 5-hydroxylysine Ref.4 | ||||||
| Modified residue | 63 | 1 | 5-hydroxylysine Ref.4 | ||||||
| Modified residue | 72 | 1 | 5-hydroxylysine Ref.4 | ||||||
| Modified residue | 86 | 1 | 4-hydroxyproline Ref.4 | ||||||
| Modified residue | 96 | 1 | 5-hydroxylysine Ref.4 | ||||||
| Glycosylation | 28 | 1 | O-linked (Gal...) Ref.4 | ||||||
| Glycosylation | 60 | 1 | O-linked (Gal...) Ref.4 | ||||||
| Glycosylation | 63 | 1 | O-linked (Gal...) Ref.4 | ||||||
| Glycosylation | 72 | 1 | O-linked (Gal...) | ||||||
| Glycosylation | 96 | 1 | O-linked (Gal...) Ref.4 | ||||||
| Disulfide bond | 31 | Interchain; in form MMW and form HMW By similarity | |||||||
Experimental info | |||||||||
| Sequence conflict | 66 | 1 | P → A in AAK58902. Ref.1 | ||||||
| Sequence conflict | 69 | 1 | V → L in AAK58902. Ref.1 | ||||||
| Sequence conflict | 74 | 1 | D → E in AAK58902. Ref.1 | ||||||
| Sequence conflict | 77 – 83 | 7 | ETGITGI → DVGMTGA in AAK58902. Ref.1 | ||||||
| Sequence conflict | 102 | 1 | S → A in AAK58902. Ref.1 | ||||||
| Sequence conflict | 116 – 117 | 2 | RQ → TR in AAK58902. Ref.1 | ||||||
| Sequence conflict | 141 | 1 | T → S in AAK58902. Ref.1 | ||||||
| Sequence conflict | 146 | 1 | L → Y in AAK58902. Ref.1 | ||||||
| Sequence conflict | 163 | 1 | L → M in AAK58902. Ref.1 | ||||||
| Sequence conflict | 171 – 173 | 3 | YKN → FKK in AAK58902. Ref.1 | ||||||
| Sequence conflict | 177 | 1 | L → V in AAK58902. Ref.1 | ||||||
| Sequence conflict | 181 | 1 | H → Y in AAK58902. Ref.1 | ||||||
| Sequence conflict | 184 – 186 | 3 | FQD → YQE in AAK58902. Ref.1 | ||||||
| Sequence conflict | 199 | 1 | Y → H in AAK58902. Ref.1 | ||||||
| Sequence conflict | 202 | 1 | K → V in AAK58902. Ref.1 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Identification and adipocyte differentiation-dependent expression of the unique disialic acid residue in an adipose tissue-specific glycoprotein, adipo Q." Sato C., Yasukawa Z., Honda N., Matsuda T., Kitajima K. J. Biol. Chem. 276:28849-28856(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 18-26; 194-197; 203-208 AND 221-228, GLYCOSYLATION, STRUCTURE OF CARBOHYDRATES. Tissue: Adipose tissue. |
| [2] | Morsci N.S., Schnabel R.D., Taylor J.F. Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [3] | NIH - Mammalian Gene Collection (MGC) project Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Hereford. Tissue: Ascending colon. |
| [4] | "Proteomic and functional characterization of endogenous adiponectin purified from fetal bovine serum." 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. Proteomics 4:3933-3942(2004) [PubMed] [Europe PMC] [Abstract] Cited for: 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, ABSENCE OF HYDROXYLATION AT PRO-57; PRO-66; PRO-71; PRO-90 AND PRO-99, ABSENCE OF GLYCOSYLATION AT ASN-225, MASS SPECTROMETRY. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AF269230 mRNA. Translation: AAK58902.1. DQ156120 Genomic DNA. Translation: AAZ81421.1. BC140488 mRNA. Translation: AAI40489.1. |
| IPI | IPI00688783. |
| RefSeq | NP_777167.1. NM_174742.2. |
| UniGene | Bt.109637. |
3D structure databases | |
| ProteinModelPortal | Q3Y5Z3. |
| SMR | Q3Y5Z3. Positions 103-237. |
| ModBase | Search... |
Protein-protein interaction databases | |
| MINT | MINT-4563461. |
| STRING | 9913.ENSBTAP00000026395. |
Proteomic databases | |
| PaxDb | Q3Y5Z3. |
| PRIDE | Q3Y5Z3. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| Ensembl | ENSBTAT00000026395; ENSBTAP00000026395; ENSBTAG00000019813. |
| GeneID | 282865. |
| KEGG | bta:282865. |
Organism-specific databases | |
| CTD | 9370. |
Phylogenomic databases | |
| eggNOG | NOG136972. |
| GeneTree | ENSGT00700000104099. |
| HOGENOM | HOG000085653. |
| HOVERGEN | HBG108220. |
| InParanoid | Q3Y5Z3. |
| KO | K07296. |
| OMA | LFTYDQY. |
| OrthoDB | EOG4FXR88. |
Family and domain databases | |
| Gene3D | 2.60.120.40. 1 hit. |
| InterPro | IPR001073. C1q. IPR008160. Collagen. IPR008983. Tumour_necrosis_fac-like_dom. [Graphical view] |
| Pfam | PF00386. C1q. 1 hit. PF01391. Collagen. 1 hit. [Graphical view] |
| PRINTS | PR00007. COMPLEMNTC1Q. |
| SMART | SM00110. C1Q. 1 hit. [Graphical view] |
| SUPFAM | SSF49842. TNF_like. 1 hit. |
| PROSITE | PS50871. C1Q. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other | |
| NextBio | 20806393. |
Entry information
| Entry name | ADIPO_BOVIN | ||||||||
| Accession | Primary (citable) accession number: Q3Y5Z3 Secondary accession number(s): A5D7A8, Q95MQ4 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |