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Q3Y5Z3 (ADIPO_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 63. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
Name:ADIPOQ
Synonyms:ACRP30, APM1
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length240 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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 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.

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

Keywords
   Cellular componentSecreted
   DomainCollagen
Repeat
Signal
   Molecular functionHormone
   PTMDisulfide bond
Glycoprotein
Hydroxylation
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processadiponectin-activated signaling pathway

Inferred from electronic annotation. Source: InterPro

brown fat cell differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

cellular response to drug

Inferred from sequence or structural similarity. Source: UniProtKB

cellular response to insulin stimulus

Inferred from sequence or structural similarity. Source: UniProtKB

detection of oxidative stress

Inferred from sequence or structural similarity. Source: UniProtKB

fatty acid beta-oxidation

Inferred from sequence or structural similarity. Source: UniProtKB

glucose homeostasis

Inferred from sequence or structural similarity. Source: UniProtKB

glucose metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

low-density lipoprotein particle clearance

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of DNA biosynthetic process

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of ERK1 and ERK2 cascade

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of I-kappaB kinase/NF-kappaB signaling

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of MAP kinase activity

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of blood pressure

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of fat cell differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of gluconeogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of granulocyte differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of heterotypic cell-cell adhesion

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of inflammatory response

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of intracellular protein transport

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of low-density lipoprotein particle receptor biosynthetic process

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of macrophage derived foam cell differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of macrophage differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of metanephric mesenchymal cell migration

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of phagocytosis

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of platelet-derived growth factor receptor-alpha signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of protein autophosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of receptor binding

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of smooth muscle cell migration

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of smooth muscle cell proliferation

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of synaptic transmission

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of transcription, DNA-templated

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of tumor necrosis factor production

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of tumor necrosis factor-mediated signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of I-kappaB kinase/NF-kappaB signaling

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of cAMP-dependent protein kinase activity

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of cholesterol efflux

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of fatty acid metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of glucose import

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of glycogen (starch) synthase activity

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of interleukin-8 production

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of metanephric glomerular visceral epithelial cell development

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of monocyte chemotactic protein-1 production

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of myeloid cell apoptotic process

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of protein kinase A signaling

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of renal albumin absorption

Inferred from sequence or structural similarity. Source: UniProtKB

protein heterotrimerization

Inferred from electronic annotation. Source: Ensembl

protein homooligomerization

Inferred from sequence or structural similarity. Source: UniProtKB

protein localization to plasma membrane

Inferred from sequence or structural similarity. Source: UniProtKB

response to glucose

Inferred from sequence or structural similarity. Source: UniProtKB

response to tumor necrosis factor

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentcell periphery

Inferred from sequence or structural similarity. Source: UniProtKB

cell surface

Inferred from sequence or structural similarity. Source: BHF-UCL

collagen

Inferred from electronic annotation. Source: UniProtKB-KW

endoplasmic reticulum

Inferred from sequence or structural similarity. Source: UniProtKB

extracellular space

Inferred from sequence or structural similarity. Source: UniProtKB

perinuclear region of cytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionhormone activity

Inferred from sequence or structural similarity. Source: UniProtKB

sialic acid binding

Inferred from direct assay Ref.1. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

itself2EBI-7264459,EBI-7264459

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1717 Ref.1 Ref.4
Chain18 – 240223Adiponectin
PRO_0000236269

Regions

Domain43 – 10260Collagen-like
Domain103 – 240138C1q

Sites

Site571Not hydroxylated
Site661Not hydroxylated
Site711Not hydroxylated
Site901Not hydroxylated
Site991Not hydroxylated
Site2251Not glycosylated

Amino acid modifications

Modified residue2815-hydroxylysine Ref.4
Modified residue3914-hydroxyproline Ref.4
Modified residue4214-hydroxyproline Ref.4
Modified residue4814-hydroxyproline Ref.4
Modified residue6015-hydroxylysine Ref.4
Modified residue6315-hydroxylysine Ref.4
Modified residue7215-hydroxylysine Ref.4
Modified residue8614-hydroxyproline Ref.4
Modified residue9615-hydroxylysine Ref.4
Glycosylation281O-linked (Gal...) Ref.4
Glycosylation601O-linked (Gal...) Ref.4
Glycosylation631O-linked (Gal...) Ref.4
Glycosylation721O-linked (Gal...)
Glycosylation961O-linked (Gal...) Ref.4
Disulfide bond31Interchain; in form MMW and form HMW By similarity

Experimental info

Sequence conflict661P → A in AAK58902. Ref.1
Sequence conflict691V → L in AAK58902. Ref.1
Sequence conflict741D → E in AAK58902. Ref.1
Sequence conflict77 – 837ETGITGI → DVGMTGA in AAK58902. Ref.1
Sequence conflict1021S → A in AAK58902. Ref.1
Sequence conflict116 – 1172RQ → TR in AAK58902. Ref.1
Sequence conflict1411T → S in AAK58902. Ref.1
Sequence conflict1461L → Y in AAK58902. Ref.1
Sequence conflict1631L → M in AAK58902. Ref.1
Sequence conflict171 – 1733YKN → FKK in AAK58902. Ref.1
Sequence conflict1771L → V in AAK58902. Ref.1
Sequence conflict1811H → Y in AAK58902. Ref.1
Sequence conflict184 – 1863FQD → YQE in AAK58902. Ref.1
Sequence conflict1991Y → H in AAK58902. Ref.1
Sequence conflict2021K → V in AAK58902. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q3Y5Z3 [UniParc].

Last modified September 27, 2005. Version 1.
Checksum: 409122E49F3AF253

FASTA24026,133
        10         20         30         40         50         60 
MLLQGALLLL LALPSHGEDN MEDPPLPKGA CAGWMAGIPG HPGHNGTPGR DGRDGTPGEK 

        70         80         90        100        110        120 
GEKGDPGLVG PKGDTGETGI TGIEGPRGFP GTPGRKGEPG ESAYVYRSAF SVGLERQVTV 

       130        140        150        160        170        180 
PNVPIRFTKI FYNQQNHYDG TTGKFLCNIP GLYYFSYHIT VYLKDVKVSL YKNDKALLFT 

       190        200        210        220        230        240 
HDQFQDKNVD QASGSVLLYL EKGDQVWLQV YEGENHNGVY ADNVNDSTFT GFLLYHNIVE 

« Hide

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.
RefSeqNP_777167.1. NM_174742.2.
UniGeneBt.109637.

3D structure databases

ProteinModelPortalQ3Y5Z3.
SMRQ3Y5Z3. Positions 103-237.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

MINTMINT-4563461.
STRING9913.ENSBTAP00000026395.

Proteomic databases

PaxDbQ3Y5Z3.
PRIDEQ3Y5Z3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSBTAT00000026395; ENSBTAP00000026395; ENSBTAG00000019813.
GeneID282865.
KEGGbta:282865.

Organism-specific databases

CTD9370.

Phylogenomic databases

eggNOGNOG136972.
GeneTreeENSGT00730000110732.
HOGENOMHOG000085653.
HOVERGENHBG108220.
InParanoidQ3Y5Z3.
KOK07296.
OMALFTYDQY.
OrthoDBEOG70ZZPW.
TreeFamTF329591.

Family and domain databases

Gene3D2.60.120.40. 1 hit.
InterProIPR028572. Adiponectin.
IPR001073. C1q.
IPR008160. Collagen.
IPR008983. Tumour_necrosis_fac-like_dom.
[Graphical view]
PANTHERPTHR24022:SF2. PTHR24022:SF2. 1 hit.
PfamPF00386. C1q. 1 hit.
PF01391. Collagen. 1 hit.
[Graphical view]
PRINTSPR00007. COMPLEMNTC1Q.
SMARTSM00110. C1Q. 1 hit.
[Graphical view]
SUPFAMSSF49842. SSF49842. 1 hit.
PROSITEPS50871. C1Q. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20806393.

Entry information

Entry nameADIPO_BOVIN
AccessionPrimary (citable) accession number: Q3Y5Z3
Secondary accession number(s): A5D7A8, Q95MQ4
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2006
Last sequence update: September 27, 2005
Last modified: February 19, 2014
This is version 63 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families