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Entry version 192 (13 Feb 2019)
Sequence version 1 (01 Nov 1996)
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Protein

Adiponectin

Gene

ADIPOQ

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

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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

Caution

The expected hydroxylation of Lys-33 was not identified, probably due to poor representation of the N-terminal peptide in mass fingerprinting.1 Publication

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

  • cytokine activity Source: BHF-UCL
  • extracellular matrix structural constituent 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

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionHormone

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-HSA-163680 AMPK inhibits chREBP transcriptional activation activity
R-HSA-381340 Transcriptional regulation of white adipocyte differentiation

SIGNOR Signaling Network Open Resource

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SIGNORi
Q15848

Protein family/group databases

Transport Classification Database

More...
TCDBi
8.A.94.1.1 the adiponectin (adiponectin) family

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>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 protein1 Publication
Short name:
apM-11 Publication
Gelatin-binding protein
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:ADIPOQ
Synonyms:ACDC, ACRP30, APM1, GBP282 Publications
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 3

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
HostDB:ENSG00000181092.9

Human Gene Nomenclature Database

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HGNCi
HGNC:13633 ADIPOQ

Online Mendelian Inheritance in Man (OMIM)

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MIMi
605441 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_Q15848

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>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 & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Secreted

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>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
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>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

<p>This subsection of the ‘Pathology and Biotech’ section describes the use of a protein as a pharmaceutical drug. It indicates the name of the drug, the name of the firm that commercializes it and explains in a few words in which context the drug is used. In some cases, drugs that are under development are also described.<p><a href='/help/pharmaceutical_use' target='_top'>More...</a></p>Pharmaceutical usei

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

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>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

DisGeNET

More...
DisGeNETi
9370

MalaCards human disease database

More...
MalaCardsi
ADIPOQ
MIMi125853 phenotype
612556 phenotype

Open Targets

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OpenTargetsi
ENSG00000181092

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA134933118

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
ADIPOQ

Domain mapping of disease mutations (DMDM)

More...
DMDMi
2493789

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 182 PublicationsAdd BLAST18
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000000354319 – 244AdiponectinAdd BLAST226

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi21O-linked (GalNAc...) threonine1 Publication1
Glycosylationi22O-linked (GalNAc...) threonine1 Publication1
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei335-hydroxylysineBy similarity1
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>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

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

HMW complexes are more extensively glycosylated than smaller oligomers. Hydroxylation and glycosylation of the lysine residues within the collagen-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
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
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei62Not hydroxylated1 Publication1
Sitei86Not hydroxylated1 Publication1
Sitei104Not hydroxylated1 Publication1
Sitei230Not glycosylated1 Publication1

Keywords - PTMi

Disulfide bond, Glycoprotein, Hydroxylation

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
Q15848

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
Q15848

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
Q15848

PeptideAtlas

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PeptideAtlasi
Q15848

PRoteomics IDEntifications database

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PRIDEi
Q15848

ProteomicsDB human proteome resource

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ProteomicsDBi
60791

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
Q15848

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

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PhosphoSitePlusi
Q15848

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Synthesized exclusively by adipocytes and secreted into plasma.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSG00000181092 Expressed in 120 organ(s), highest expression level in adipose tissue of abdominal region

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
Q15848 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
Q15848 HS

Organism-specific databases

Human Protein Atlas

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HPAi
CAB046467
HPA051767

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>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 is also modulated by the degree of 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

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
114771, 22 interactors

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
Q15848

Protein interaction database and analysis system

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IntActi
Q15848, 55 interactors

STRING: functional protein association networks

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STRINGi
9606.ENSP00000320709

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1244
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4DOUX-ray2.00A104-244[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
Q15848

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
Q15848

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini42 – 107Collagen-likeAdd BLAST66
Domaini108 – 244C1qPROSITE-ProRule annotationAdd BLAST137

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The C1q domain is commonly called the globular domain.

Keywords - Domaini

Collagen, Repeat, Signal

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
ENOG410IHSJ Eukaryota
ENOG4111F5K LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000159828

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000085653

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG108220

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q15848

KEGG Orthology (KO)

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KOi
K07296

Identification of Orthologs from Complete Genome Data

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OMAi
QQNHYDG

Database of Orthologous Groups

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OrthoDBi
1110472at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
Q15848

TreeFam database of animal gene trees

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TreeFami
TF329591

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
2.60.120.40, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR001073 C1q_dom
IPR008160 Collagen
IPR008983 Tumour_necrosis_fac-like_dom

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00386 C1q, 1 hit
PF01391 Collagen, 1 hit

Protein Motif fingerprint database; a protein domain database

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PRINTSi
PR00007 COMPLEMNTC1Q

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00110 C1Q, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF49842 SSF49842, 1 hit

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS50871 C1Q, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i64D8C6C1204B1018
GO

<p>This subsection of the ‘Sequence’ section provides information on polymorphic variants. If the variant is associated with a disease state, the description of the latter can be found in the <a href="http://www.uniprot.org/manual/involvement_in_disease">'Involvement in disease'</a> subsection.<p><a href='/help/polymorphism' target='_top'>More...</a></p>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:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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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

The Consensus CDS (CCDS) project

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CCDSi
CCDS3284.1

Protein sequence database of the Protein Information Resource

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PIRi
JC4708

NCBI Reference Sequences

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RefSeqi
NP_001171271.1, NM_001177800.1
NP_004788.1, NM_004797.3

UniGene gene-oriented nucleotide sequence clusters

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UniGenei
Hs.80485

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENST00000320741; ENSP00000320709; ENSG00000181092
ENST00000444204; ENSP00000389814; ENSG00000181092

Database of genes from NCBI RefSeq genomes

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GeneIDi
9370

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
hsa:9370

UCSC genome browser

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UCSCi
uc003fra.4 human

Keywords - Coding sequence diversityi

Polymorphism

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Wikipedia

Adiponectin entry

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4DOUX-ray2.00A104-244[»]
ProteinModelPortaliQ15848
SMRiQ15848
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114771, 22 interactors
CORUMiQ15848
IntActiQ15848, 55 interactors
STRINGi9606.ENSP00000320709

Protein family/group databases

TCDBi8.A.94.1.1 the adiponectin (adiponectin) family

PTM databases

iPTMnetiQ15848
PhosphoSitePlusiQ15848

Polymorphism and mutation databases

BioMutaiADIPOQ
DMDMi2493789

Proteomic databases

EPDiQ15848
jPOSTiQ15848
PaxDbiQ15848
PeptideAtlasiQ15848
PRIDEiQ15848
ProteomicsDBi60791

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
9370
DisGeNETi9370
EuPathDBiHostDB:ENSG00000181092.9

GeneCards: human genes, protein and diseases

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GeneCardsi
ADIPOQ
HGNCiHGNC:13633 ADIPOQ
HPAiCAB046467
HPA051767
MalaCardsiADIPOQ
MIMi125853 phenotype
605441 gene
612556 phenotype
neXtProtiNX_Q15848
OpenTargetsiENSG00000181092
PharmGKBiPA134933118

GenAtlas: human gene database

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GenAtlasi
Search...

Phylogenomic databases

eggNOGiENOG410IHSJ Eukaryota
ENOG4111F5K LUCA
GeneTreeiENSGT00940000159828
HOGENOMiHOG000085653
HOVERGENiHBG108220
InParanoidiQ15848
KOiK07296
OMAiQQNHYDG
OrthoDBi1110472at2759
PhylomeDBiQ15848
TreeFamiTF329591

Enzyme and pathway databases

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

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

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ChiTaRSi
ADIPOQ human

The Gene Wiki collection of pages on human genes and proteins

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GeneWikii
Adiponectin

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

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GenomeRNAii
9370

Protein Ontology

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PROi
PR:Q15848

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
Search...

Gene expression databases

BgeeiENSG00000181092 Expressed in 120 organ(s), highest expression level in adipose tissue of abdominal region
ExpressionAtlasiQ15848 baseline and differential
GenevisibleiQ15848 HS

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

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiADIPO_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q15848
Secondary accession number(s): Q58EX9
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: February 13, 2019
This is version 192 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>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.

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

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

Documents

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