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UniProtKB - Q15848 (ADIPO_HUMAN)

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Protein

Adiponectin

Gene

ADIPOQ

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -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.1 Publication

Miscellaneous

Variants Arg-84 and Ser-90 show impaired formation of HMW complexes whereas variants Cys-112 and Thr-164 show impaired secretion of adiponectin in any form.
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). In type 2 diabetic patients, both the ratios of HMW to total adiponectin and the degree of adiponectin glycosylation are significantly decreased as compared with healthy controls.By similarity

GO - Molecular functioni

  • cytokine activity Source: BHF-UCL
  • hormone activity Source: BHF-UCL
  • identical protein binding Source: BHF-UCL
  • protein homodimerization activity Source: BHF-UCL
  • sialic acid binding Source: UniProtKB
  • signaling receptor binding Source: UniProtKB
View the complete GO annotation on QuickGO ...

GO - Biological processi

View the complete GO annotation on QuickGO ...

Keywordsi

Molecular functionHormone

Enzyme and pathway databases

ReactomeiR-HSA-163680 AMPK inhibits chREBP transcriptional activation activity
R-HSA-381340 Transcriptional regulation of white adipocyte differentiation
SIGNORiQ15848

Protein family/group databases

TCDBi8.A.94.1.1 the adiponectin (adiponectin) family

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
Gelatin-binding protein
Gene namesi
Name:ADIPOQ
Synonyms:ACDC, ACRP30, APM1, GBP28
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
Proteomesi
  • UP000005640 Componenti: Chromosome 3

Organism-specific databases

EuPathDBiHostDB:ENSG00000181092.9
HGNCiHGNC:13633 ADIPOQ
MIMi605441 gene
neXtProtiNX_Q15848

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Involvement in diseasei

Adiponectin deficiency (ADPND)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA condition that results in very low concentrations of plasma adiponectin.
See also OMIM:612556
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_013274112R → C in ADPND; does not assemble into trimers resulting in impaired secretion from the cell. 3 PublicationsCorresponds to variant dbSNP:rs121917815EnsemblClinVar.1
Diabetes mellitus, non-insulin-dependent (NIDDM)
Disease susceptibility is associated with variations affecting the gene represented in this entry.
Disease descriptionA multifactorial disorder of glucose homeostasis caused by a lack of sensitivity to the body's own insulin. Affected individuals usually have an obese body habitus and manifestations of a metabolic syndrome characterized by diabetes, insulin resistance, hypertension and hypertriglyceridemia. The disease results in long-term complications that affect the eyes, kidneys, nerves, and blood vessels.
See also OMIM:125853

Pharmaceutical usei

Adiponectin might be used in the treatment of diabetes type 2 and insulin resistance.

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi20T → A: No change in sialylated isoforms. 1 Publication1
Mutagenesisi21T → A: Some loss of sialylated isoforms. 1 Publication1
Mutagenesisi22T → A: Abolishes sialylated isoforms. 1 Publication1
Mutagenesisi33K → R: No effect on formation of HMW multimers. 1 Publication1
Mutagenesisi36C → S: Impaired formation of MMW and HMW multimers. 2 Publications1
Mutagenesisi65K → R: Impaired formation of HMW multimers; when associated with R-68. 1 Publication1
Mutagenesisi68K → R: Impaired formation of HMW multimers; when associated with R-65. 1 Publication1
Mutagenesisi77K → R: Impaired formation of HMW multimers; when associated with R-101. 1 Publication1
Mutagenesisi101K → R: Impaired formation of HMW multimers; when associated with R-77. 1 Publication1

Keywords - Diseasei

Diabetes mellitus, Disease mutation, Obesity

Organism-specific databases

DisGeNETi9370
MalaCardsiADIPOQ
MIMi125853 phenotype
612556 phenotype
OpenTargetsiENSG00000181092
PharmGKBiPA134933118

Polymorphism and mutation databases

BioMutaiADIPOQ
DMDMi2493789

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 182 PublicationsAdd BLAST18
ChainiPRO_000000354319 – 244AdiponectinAdd BLAST226

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi21O-linked (GalNAc...) threonine1 Publication1
Glycosylationi22O-linked (GalNAc...) threonine1 Publication1
Modified residuei335-hydroxylysineBy similarity1
Disulfide bondi36Interchain; in form MMW and form HMW2 Publications
Modified residuei444-hydroxyproline1 Publication1
Modified residuei474-hydroxyproline1 Publication1
Modified residuei534-hydroxyproline1 Publication1
Modified residuei655-hydroxylysine1 Publication1
Glycosylationi65O-linked (Gal...) hydroxylysine; partial1 Publication1
Modified residuei685-hydroxylysine1 Publication1
Glycosylationi68O-linked (Gal...) hydroxylysine; partial1 Publication1
Modified residuei714-hydroxyproline; partial1 Publication1
Modified residuei764-hydroxyproline; partial1 Publication1
Modified residuei775-hydroxylysine1 Publication1
Glycosylationi77O-linked (Gal...) hydroxylysine; partial1 Publication1
Modified residuei914-hydroxyproline1 Publication1
Modified residuei954-hydroxyproline; partial1 Publication1
Modified residuei1015-hydroxylysine1 Publication1
Glycosylationi101O-linked (Gal...) hydroxylysine; partial1 Publication1

Post-translational modificationi

Hydroxylated Lys-33 was not identified in PubMed:16497731, probably due to poor representation of the N-terminal peptide in mass fingerprinting.1 Publication
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. Not N-glycosylated. O-linked glycans on hydroxylysines consist of Glc-Gal disaccharides bound to the oxygen atom of post-translationally added hydroxyl groups. Sialylated to varying degrees depending on tissue. Thr-22 appears to be the major site of sialylation. Higher sialylation found in SGBS adipocytes than in HEK fibroblasts. Sialylation is not required neither for heterodimerization nor for secretion. Not sialylated on the glycosylated hydroxylysines. Desialylated forms are rapidly cleared from the circulation.2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei62Not hydroxylated1 Publication1
Sitei86Not hydroxylated1 Publication1
Sitei104Not hydroxylated1 Publication1
Sitei230Not glycosylated1 Publication1

Keywords - PTMi

Disulfide bond, Glycoprotein, Hydroxylation

Proteomic databases

EPDiQ15848
PaxDbiQ15848
PeptideAtlasiQ15848
PRIDEiQ15848
ProteomicsDBi60791

PTM databases

iPTMnetiQ15848
PhosphoSitePlusiQ15848

Expressioni

Tissue specificityi

Synthesized exclusively by adipocytes and secreted into plasma.

Gene expression databases

BgeeiENSG00000181092
CleanExiHS_ADIPOQ
ExpressionAtlasiQ15848 baseline and differential
GenevisibleiQ15848 HS

Organism-specific databases

HPAiCAB046467
HPA051767

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 CTRP9A via the C1q domain (heterotrimeric complex) (By similarity).By similarity

Binary interactionsi

Show more details

GO - Molecular functioni

  • cytokine activity Source: BHF-UCL
  • hormone activity Source: BHF-UCL
  • identical protein binding Source: BHF-UCL
  • protein homodimerization activity Source: BHF-UCL
  • signaling receptor binding Source: UniProtKB
View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridi114771, 21 interactors
IntActiQ15848, 55 interactors
STRINGi9606.ENSP00000320709

Structurei

Secondary structure

1244
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi114 – 118Combined sources5
Beta strandi134 – 137Combined sources4
Turni145 – 147Combined sources3
Beta strandi156 – 177Combined sources22
Beta strandi180 – 187Combined sources8
Beta strandi195 – 205Combined sources11
Beta strandi210 – 215Combined sources6
Beta strandi222 – 225Combined sources4
Beta strandi233 – 241Combined sources9

3D structure databases

ProteinModelPortaliQ15848
SMRiQ15848
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini42 – 107Collagen-likeAdd BLAST66
Domaini108 – 244C1qPROSITE-ProRule annotationAdd BLAST137

Domaini

The C1q domain is commonly called the globular domain.

Keywords - Domaini

Collagen, Repeat, Signal

Phylogenomic databases

eggNOGiENOG410IHSJ Eukaryota
ENOG4111F5K LUCA
GeneTreeiENSGT00760000118830
HOGENOMiHOG000085653
HOVERGENiHBG108220
InParanoidiQ15848
KOiK07296
OMAiQQNHYDG
OrthoDBiEOG091G0L3Y
PhylomeDBiQ15848
TreeFamiTF329591

Family and domain databases

Gene3Di2.60.120.40, 1 hit
InterProiView protein in InterPro
IPR001073 C1q_dom
IPR008160 Collagen
IPR008983 Tumour_necrosis_fac-like_dom
PfamiView protein in Pfam
PF00386 C1q, 1 hit
PF01391 Collagen, 1 hit
PRINTSiPR00007 COMPLEMNTC1Q
SMARTiView protein in SMART
SM00110 C1Q, 1 hit
SUPFAMiSSF49842 SSF49842, 1 hit
PROSITEiView protein in PROSITE
PS50871 C1Q, 1 hit

Sequencei

Sequence statusi: Complete.

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

Q15848-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLLLGAVLLL LALPGHDQET TTQGPGVLLP LPKGACTGWM AGIPGHPGHN 
        60         70         80         90        100
GAPGRDGRDG TPGEKGEKGD PGLIGPKGDI GETGVPGAEG PRGFPGIQGR 
       110        120        130        140        150
KGEPGEGAYV YRSAFSVGLE TYVTIPNMPI RFTKIFYNQQ NHYDGSTGKF 
       160        170        180        190        200
HCNIPGLYYF AYHITVYMKD VKVSLFKKDK AMLFTYDQYQ ENNVDQASGS 
       210        220        230        240 
VLLHLEVGDQ VWLQVYGEGE RNGLYADNDN DSTFTGFLLY HDTN
Length:244
Mass (Da):26,414
Last modified:November 1, 1996 - v1
Checksum:i64D8C6C1204B1018
GO

Polymorphismi

Genetic variations in ADIPOQ influence the variance in adiponectin serum levels and define the adiponectin serum levels quantitative trait locus 1 (ADIPQTL1) [MIMi:612556].

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_01327384G → R Does not form high molecular weight multimers. 3 PublicationsCorresponds to variant dbSNP:rs199646033Ensembl.1
Natural variantiVAR_02739590G → S Does not form high molecular weight multimers. 2 PublicationsCorresponds to variant dbSNP:rs62625753Ensembl.1
Natural variantiVAR_027396111Y → H1 PublicationCorresponds to variant dbSNP:rs17366743Ensembl.1
Natural variantiVAR_013274112R → C in ADPND; does not assemble into trimers resulting in impaired secretion from the cell. 3 PublicationsCorresponds to variant dbSNP:rs121917815EnsemblClinVar.1
Natural variantiVAR_013275117V → M1 PublicationCorresponds to variant dbSNP:rs747223144Ensembl.1
Natural variantiVAR_013276164I → T Associated with low plasma adiponectin concentration and diabetes mellitus type 2; does not assemble into trimers resulting in impaired secretion from the cell. 3 PublicationsCorresponds to variant dbSNP:rs185847354Ensembl.1
Natural variantiVAR_013277221R → S2 PublicationsCorresponds to variant dbSNP:rs138773406Ensembl.1
Natural variantiVAR_013278241H → P2 PublicationsCorresponds to variant dbSNP:rs141205818Ensembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D45371 mRNA Translation: BAA08227.1
AB012165 Genomic DNA Translation: BAA86716.1
AJ131460, AJ131461 Genomic DNA Translation: CAB52413.1
BC054496 mRNA Translation: AAH54496.1
BC096308 mRNA Translation: AAH96308.1
BC096309 mRNA Translation: AAH96309.1
BC096310 mRNA Translation: AAH96310.1
BC096311 mRNA Translation: AAH96311.1
CCDSiCCDS3284.1
PIRiJC4708
RefSeqiNP_001171271.1, NM_001177800.1
NP_004788.1, NM_004797.3
UniGeneiHs.80485

Genome annotation databases

EnsembliENST00000320741; ENSP00000320709; ENSG00000181092
ENST00000444204; ENSP00000389814; ENSG00000181092
GeneIDi9370
KEGGihsa:9370
UCSCiuc003fra.4 human

Keywords - Coding sequence diversityi

Polymorphism

Similar proteinsi

Entry informationi

Entry nameiADIPO_HUMAN
AccessioniPrimary (citable) accession number: Q15848
Secondary accession number(s): Q58EX9
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: July 18, 2018
This is version 186 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

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

Documents

  1. Human chromosome 3
    Human chromosome 3: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references

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