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Protein

Adiponectin

Gene

ADIPOQ

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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).By similarity

GO - Molecular functioni

  • hormone activity Source: UniProtKB
  • receptor binding Source: UniProtKB
  • sialic acid binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hormone

Enzyme and pathway databases

ReactomeiR-BTA-163680. AMPK inhibits chREBP transcriptional activation activity.

Names & Taxonomyi

Protein namesi
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 namesi
Name:ADIPOQ
Synonyms:ACRP30, APM1
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 1

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 172 PublicationsAdd BLAST17
ChainiPRO_000023626918 – 240AdiponectinAdd BLAST223

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei285-hydroxylysine1 Publication1
Glycosylationi28O-linked (Gal...)1 Publication1
Disulfide bondi31Interchain; in form MMW and form HMWBy similarity
Modified residuei394-hydroxyproline1 Publication1
Modified residuei424-hydroxyproline1 Publication1
Modified residuei484-hydroxyproline1 Publication1
Modified residuei605-hydroxylysine1 Publication1
Glycosylationi60O-linked (Gal...)1 Publication1
Modified residuei635-hydroxylysine1 Publication1
Glycosylationi63O-linked (Gal...)1 Publication1
Modified residuei725-hydroxylysine1 Publication1
Glycosylationi72O-linked (Gal...)1 Publication1
Modified residuei864-hydroxyproline1 Publication1
Modified residuei965-hydroxylysine1 Publication1
Glycosylationi96O-linked (Gal...)1 Publication1

Post-translational modificationi

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).By similarity
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.By similarity2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei57Not hydroxylated1
Sitei66Not hydroxylated1
Sitei71Not hydroxylated1
Sitei90Not hydroxylated1
Sitei99Not hydroxylated1
Sitei225Not glycosylated1

Keywords - PTMi

Disulfide bond, Glycoprotein, Hydroxylation

Proteomic databases

PaxDbiQ3Y5Z3.
PeptideAtlasiQ3Y5Z3.
PRIDEiQ3Y5Z3.

Expressioni

Gene expression databases

BgeeiENSBTAG00000019813.

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 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).By similarity

GO - Molecular functioni

Protein-protein interaction databases

MINTiMINT-4563461.
STRINGi9913.ENSBTAP00000026395.

Structurei

3D structure databases

ProteinModelPortaliQ3Y5Z3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini43 – 102Collagen-likeAdd BLAST60
Domaini103 – 240C1qPROSITE-ProRule annotationAdd BLAST138

Sequence similaritiesi

Contains 1 C1q domain.PROSITE-ProRule annotation
Contains 1 collagen-like domain.Curated

Keywords - Domaini

Collagen, Repeat, Signal

Phylogenomic databases

eggNOGiENOG410IHSJ. Eukaryota.
ENOG4111F5K. LUCA.
GeneTreeiENSGT00760000118830.
HOGENOMiHOG000085653.
HOVERGENiHBG108220.
InParanoidiQ3Y5Z3.
KOiK07296.
OMAiKAMLFTY.
OrthoDBiEOG091G0L3Y.
TreeFamiTF329591.

Family and domain databases

Gene3Di2.60.120.40. 1 hit.
InterProiIPR001073. C1q_dom.
IPR008160. Collagen.
IPR008983. Tumour_necrosis_fac-like_dom.
[Graphical view]
PfamiPF00386. C1q. 1 hit.
PF01391. Collagen. 1 hit.
[Graphical view]
PRINTSiPR00007. COMPLEMNTC1Q.
SMARTiSM00110. C1Q. 1 hit.
[Graphical view]
SUPFAMiSSF49842. SSF49842. 1 hit.
PROSITEiPS50871. C1Q. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q3Y5Z3-1 [UniParc]FASTAAdd to basket

« Hide

        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
Length:240
Mass (Da):26,133
Last modified:September 27, 2005 - v1
Checksum:i409122E49F3AF253
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti66P → A in AAK58902 (PubMed:11382781).Curated1
Sequence conflicti69V → L in AAK58902 (PubMed:11382781).Curated1
Sequence conflicti74D → E in AAK58902 (PubMed:11382781).Curated1
Sequence conflicti77 – 83ETGITGI → DVGMTGA in AAK58902 (PubMed:11382781).Curated7
Sequence conflicti102S → A in AAK58902 (PubMed:11382781).Curated1
Sequence conflicti116 – 117RQ → TR in AAK58902 (PubMed:11382781).Curated2
Sequence conflicti141T → S in AAK58902 (PubMed:11382781).Curated1
Sequence conflicti146L → Y in AAK58902 (PubMed:11382781).Curated1
Sequence conflicti163L → M in AAK58902 (PubMed:11382781).Curated1
Sequence conflicti171 – 173YKN → FKK in AAK58902 (PubMed:11382781).Curated3
Sequence conflicti177L → V in AAK58902 (PubMed:11382781).Curated1
Sequence conflicti181H → Y in AAK58902 (PubMed:11382781).Curated1
Sequence conflicti184 – 186FQD → YQE in AAK58902 (PubMed:11382781).Curated3
Sequence conflicti199Y → H in AAK58902 (PubMed:11382781).Curated1
Sequence conflicti202K → V in AAK58902 (PubMed:11382781).Curated1

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.
RefSeqiNP_777167.1. NM_174742.2.
UniGeneiBt.109637.

Genome annotation databases

EnsembliENSBTAT00000026395; ENSBTAP00000026395; ENSBTAG00000019813.
GeneIDi282865.
KEGGibta:282865.

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.
RefSeqiNP_777167.1. NM_174742.2.
UniGeneiBt.109637.

3D structure databases

ProteinModelPortaliQ3Y5Z3.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-4563461.
STRINGi9913.ENSBTAP00000026395.

Proteomic databases

PaxDbiQ3Y5Z3.
PeptideAtlasiQ3Y5Z3.
PRIDEiQ3Y5Z3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000026395; ENSBTAP00000026395; ENSBTAG00000019813.
GeneIDi282865.
KEGGibta:282865.

Organism-specific databases

CTDi9370.

Phylogenomic databases

eggNOGiENOG410IHSJ. Eukaryota.
ENOG4111F5K. LUCA.
GeneTreeiENSGT00760000118830.
HOGENOMiHOG000085653.
HOVERGENiHBG108220.
InParanoidiQ3Y5Z3.
KOiK07296.
OMAiKAMLFTY.
OrthoDBiEOG091G0L3Y.
TreeFamiTF329591.

Enzyme and pathway databases

ReactomeiR-BTA-163680. AMPK inhibits chREBP transcriptional activation activity.

Gene expression databases

BgeeiENSBTAG00000019813.

Family and domain databases

Gene3Di2.60.120.40. 1 hit.
InterProiIPR001073. C1q_dom.
IPR008160. Collagen.
IPR008983. Tumour_necrosis_fac-like_dom.
[Graphical view]
PfamiPF00386. C1q. 1 hit.
PF01391. Collagen. 1 hit.
[Graphical view]
PRINTSiPR00007. COMPLEMNTC1Q.
SMARTiSM00110. C1Q. 1 hit.
[Graphical view]
SUPFAMiSSF49842. SSF49842. 1 hit.
PROSITEiPS50871. C1Q. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiADIPO_BOVIN
AccessioniPrimary (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 5, 2016
This is version 83 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

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

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.