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Protein

Adiponectin

Gene

Adipoq

Organism
Mus musculus (Mouse)
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.5 Publications

GO - Molecular functioni

  • hormone activity Source: MGI
  • identical protein binding Source: IntAct
  • protein homodimerization activity Source: MGI
  • receptor binding Source: MGI
  • sialic acid binding Source: MGI

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hormone

Enzyme and pathway databases

ReactomeiR-MMU-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
Adipocyte-specific protein AdipoQ
Gene namesi
Name:Adipoq
Synonyms:Acdc, Acrp30, Apm1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 16

Organism-specific databases

MGIiMGI:106675. Adipoq.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi39C → A: No change in the interaction with CTRP9. 1 Publication1
Mutagenesisi68K → R: Impaired formation of HMW multimers; when associated with R-71; R-80 and R-104. 1 Publication1
Mutagenesisi71K → R: Impaired formation of HMW multimers; when associated with R-68; R-80 and R-104. 1 Publication1
Mutagenesisi80K → R: Impaired formation of HMW multimers; when associated with R-68; R-71 and R-104. 1 Publication1
Mutagenesisi104K → R: Impaired formation of HMW multimers; when associated with R-68; R-71 and R-80. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 171 PublicationAdd BLAST17
ChainiPRO_000000354418 – 247AdiponectinAdd BLAST230

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi23O-linked (GalNAc...)1 Publication1
Glycosylationi24O-linked (GalNAc...)1 Publication1
Disulfide bondi39InterchainBy similarity
Modified residuei474-hydroxyprolineBy similarity1
Modified residuei504-hydroxyprolineBy similarity1
Modified residuei564-hydroxyprolineBy similarity1
Modified residuei685-hydroxylysine; alternate1 Publication1
Glycosylationi68O-linked (Gal...); alternate1 Publication1
Modified residuei715-hydroxylysine; alternate1 Publication1
Glycosylationi71O-linked (Gal...); alternate1 Publication1
Modified residuei805-hydroxylysine; alternate1 Publication1
Glycosylationi80O-linked (Gal...); alternate1 Publication1
Modified residuei944-hydroxyproline1 Publication1
Modified residuei1045-hydroxylysine; alternate1 Publication1
Glycosylationi104O-linked (Gal...); alternate1 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.1 Publication
O-glycosylated. Not N-glycosylated (By similarity) 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 glycosylation in the N-terminal is disialylated with the structure Neu5Acalpha2->8Neu5Acalpha2->3Gal. Sialylated by alpha 2,8-sialyltransferase III.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei79Not hydroxylated1
Sitei98Not hydroxylated1
Sitei107Not hydroxylated1
Sitei233Not glycosylated1

Keywords - PTMi

Disulfide bond, Glycoprotein, Hydroxylation

Proteomic databases

PaxDbiQ60994.
PeptideAtlasiQ60994.
PRIDEiQ60994.

PTM databases

PhosphoSitePlusiQ60994.
SwissPalmiQ60994.

Expressioni

Tissue specificityi

Synthesized exclusively by adipocytes and secreted into plasma.

Inductioni

During hormone-induced adipose differentiation and activated by insulin.

Gene expression databases

BgeeiENSMUSG00000022878.
CleanExiMM_ADIPOQ.
ExpressionAtlasiQ60994. baseline and differential.
GenevisibleiQ60994. MM.

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).5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself12EBI-7264589,EBI-7264589

GO - Molecular functioni

  • hormone activity Source: MGI
  • identical protein binding Source: IntAct
  • protein homodimerization activity Source: MGI
  • receptor binding Source: MGI

Protein-protein interaction databases

BioGridi197940. 3 interactors.
DIPiDIP-44111N.
IntActiQ60994. 2 interactors.
MINTiMINT-4563800.
STRINGi10090.ENSMUSP00000023593.

Structurei

Secondary structure

1247
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi117 – 121Combined sources5
Beta strandi130 – 132Combined sources3
Beta strandi137 – 140Combined sources4
Turni148 – 150Combined sources3
Beta strandi152 – 154Combined sources3
Beta strandi159 – 172Combined sources14
Beta strandi174 – 180Combined sources7
Beta strandi183 – 190Combined sources8
Beta strandi197 – 208Combined sources12
Beta strandi213 – 218Combined sources6
Beta strandi236 – 244Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1C28X-ray2.10A/B/C114-247[»]
1C3HX-ray2.10A/B/C/D/E/F111-247[»]
ProteinModelPortaliQ60994.
SMRiQ60994.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ60994.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini45 – 110Collagen-likeAdd BLAST66
Domaini111 – 247C1qPROSITE-ProRule annotationAdd BLAST137

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.
InParanoidiQ60994.
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.

Q60994-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLLLQALLFL LILPSHAEDD VTTTEELAPA LVPPPKGTCA GWMAGIPGHP
60 70 80 90 100
GHNGTPGRDG RDGTPGEKGE KGDAGLLGPK GETGDVGMTG AEGPRGFPGT
110 120 130 140 150
PGRKGEPGEA AYVYRSAFSV GLETRVTVPN VPIRFTKIFY NQQNHYDGST
160 170 180 190 200
GKFYCNIPGL YYFSYHITVY MKDVKVSLFK KDKAVLFTYD QYQEKNVDQA
210 220 230 240
SGSVLLHLEV GDQVWLQVYG DGDHNGLYAD NVNDSTFTGF LLYHDTN
Length:247
Mass (Da):26,809
Last modified:October 3, 2012 - v2
Checksum:i0ECC687D9A8E8123
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti50P → S in AAB06706 (PubMed:8631877).Curated1
Sequence conflicti74A → S in AAB06706 (PubMed:8631877).Curated1
Sequence conflicti113V → M in AAA80543 (PubMed:7592907).Curated1
Sequence conflicti113V → M in AAK13417 (PubMed:11162643).Curated1
Sequence conflicti117A → G in AAB06706 (PubMed:8631877).Curated1
Sequence conflicti148G → N in AAB06706 (PubMed:8631877).Curated1
Sequence conflicti243Y → F in AAB06706 (PubMed:8631877).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U37222 mRNA. Translation: AAA80543.1.
U49915 mRNA. Translation: AAB06706.1.
AF304466 Genomic DNA. Translation: AAK13417.1.
AY749429 mRNA. Translation: AAW70555.1.
AY754346 mRNA. Translation: AAW82905.1.
AK003138 mRNA. Translation: BAB22597.1.
AK134112 mRNA. Translation: BAE22019.1.
AC125396 Genomic DNA. No translation available.
CH466521 Genomic DNA. Translation: EDK97661.1.
BC028770 mRNA. Translation: AAH28770.1.
CCDSiCCDS28075.1.
RefSeqiNP_033735.3. NM_009605.4.
UniGeneiMm.3969.

Genome annotation databases

EnsembliENSMUST00000023593; ENSMUSP00000023593; ENSMUSG00000022878.
GeneIDi11450.
KEGGimmu:11450.
UCSCiuc007ytk.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U37222 mRNA. Translation: AAA80543.1.
U49915 mRNA. Translation: AAB06706.1.
AF304466 Genomic DNA. Translation: AAK13417.1.
AY749429 mRNA. Translation: AAW70555.1.
AY754346 mRNA. Translation: AAW82905.1.
AK003138 mRNA. Translation: BAB22597.1.
AK134112 mRNA. Translation: BAE22019.1.
AC125396 Genomic DNA. No translation available.
CH466521 Genomic DNA. Translation: EDK97661.1.
BC028770 mRNA. Translation: AAH28770.1.
CCDSiCCDS28075.1.
RefSeqiNP_033735.3. NM_009605.4.
UniGeneiMm.3969.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1C28X-ray2.10A/B/C114-247[»]
1C3HX-ray2.10A/B/C/D/E/F111-247[»]
ProteinModelPortaliQ60994.
SMRiQ60994.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi197940. 3 interactors.
DIPiDIP-44111N.
IntActiQ60994. 2 interactors.
MINTiMINT-4563800.
STRINGi10090.ENSMUSP00000023593.

PTM databases

PhosphoSitePlusiQ60994.
SwissPalmiQ60994.

Proteomic databases

PaxDbiQ60994.
PeptideAtlasiQ60994.
PRIDEiQ60994.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000023593; ENSMUSP00000023593; ENSMUSG00000022878.
GeneIDi11450.
KEGGimmu:11450.
UCSCiuc007ytk.1. mouse.

Organism-specific databases

CTDi9370.
MGIiMGI:106675. Adipoq.

Phylogenomic databases

eggNOGiENOG410IHSJ. Eukaryota.
ENOG4111F5K. LUCA.
GeneTreeiENSGT00760000118830.
HOGENOMiHOG000085653.
HOVERGENiHBG108220.
InParanoidiQ60994.
KOiK07296.
OMAiKAMLFTY.
OrthoDBiEOG091G0L3Y.
TreeFamiTF329591.

Enzyme and pathway databases

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

Miscellaneous databases

EvolutionaryTraceiQ60994.
PROiQ60994.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000022878.
CleanExiMM_ADIPOQ.
ExpressionAtlasiQ60994. baseline and differential.
GenevisibleiQ60994. MM.

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_MOUSE
AccessioniPrimary (citable) accession number: Q60994
Secondary accession number(s): Q62400, Q6GTX4, Q9DC68
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: October 3, 2012
Last modified: November 2, 2016
This is version 159 of the entry and version 2 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.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.