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Protein

Adiponectin

Gene

Adipoq

Organism
Mus musculus (Mouse)
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.5 Publications

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.

<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

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-MMU-163680 AMPK inhibits chREBP transcriptional activation activity

<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
Adipocyte-specific protein AdipoQ
<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
<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>OrganismiMus musculus (Mouse)
<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 identifieri10090 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
<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
  • UP000000589 <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 16

Organism-specific databases

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

More...
MGIi
MGI:106675 Adipoq

<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; 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

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>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

<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 – 171 PublicationAdd BLAST17
<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_000000354418 – 247AdiponectinAdd BLAST230

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>Glycosylationi23O-linked (GalNAc...) threonine1 Publication1
Glycosylationi24O-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 residuei365-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 bondi39InterchainBy similarity
Modified residuei474-hydroxyprolineBy similarity1
Modified residuei504-hydroxyprolineBy similarity1
Modified residuei564-hydroxyprolineBy similarity1
Modified residuei685-hydroxylysine; alternate2 Publications1
Glycosylationi68O-linked (Gal...) hydroxylysine; alternate2 Publications1
Modified residuei715-hydroxylysine; alternate2 Publications1
Glycosylationi71O-linked (Gal...) hydroxylysine; alternate2 Publications1
Modified residuei805-hydroxylysine; alternate2 Publications1
Glycosylationi80O-linked (Gal...) hydroxylysine; alternate2 Publications1
Modified residuei944-hydroxyproline1 Publication1
Modified residuei1045-hydroxylysine; alternate2 Publications1
Glycosylationi104O-linked (Gal...) hydroxylysine; alternate2 Publications1

<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.2 Publications
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
<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>Sitei79Not hydroxylated1 Publication1
Sitei98Not hydroxylated1 Publication1
Sitei107Not hydroxylated1 Publication1
Sitei233Not glycosylated1 Publication1

Keywords - PTMi

Disulfide bond, Glycoprotein, Hydroxylation

Proteomic databases

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

More...
PaxDbi
Q60994

PeptideAtlas

More...
PeptideAtlasi
Q60994

PRoteomics IDEntifications database

More...
PRIDEi
Q60994

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q60994

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

More...
PhosphoSitePlusi
Q60994

SwissPalm database of S-palmitoylation events

More...
SwissPalmi
Q60994

<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.

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

During hormone-induced adipose differentiation and activated by insulin.

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSMUSG00000022878 Expressed in 122 organ(s), highest expression level in subcutaneous adipose tissue

CleanEx database of gene expression profiles

More...
CleanExi
MM_ADIPOQ

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
Q60994 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
Q60994 MM

<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 (PubMed:23209641). 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) (PubMed:23209641). The HMW-complex assembly is also modulated by the degree of lysine hydroxylation and glycosylation (PubMed:23209641). 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) (PubMed:18787108).6 Publications

<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)

More...
BioGridi
197940, 3 interactors

CORUM comprehensive resource of mammalian protein complexes

More...
CORUMi
Q60994

Database of interacting proteins

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DIPi
DIP-44111N

Protein interaction database and analysis system

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IntActi
Q60994, 5 interactors

Molecular INTeraction database

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MINTi
Q60994

STRING: functional protein association networks

More...
STRINGi
10090.ENSMUSP00000023593

<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

1247
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
Q60994

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

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SMRi
Q60994

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
Q60994

<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>Domaini45 – 110Collagen-likeAdd BLAST66
Domaini111 – 247C1qPROSITE-ProRule annotationAdd BLAST137

Keywords - Domaini

Collagen, Repeat, Signal

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG410IHSJ Eukaryota
ENOG4111F5K LUCA

Ensembl GeneTree

More...
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
Q60994

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
EOG091G0L3Y

TreeFam database of animal gene trees

More...
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

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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

More...
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>Sequence (1+)i

<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.

This entry has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All

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
<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:i0ECC687D9A8E8123
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
E9PWU4E9PWU4_MOUSE
Adiponectin
Adipoq
168Annotation score:

Annotation score:4 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 Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>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:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
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

The Consensus CDS (CCDS) project

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CCDSi
CCDS28075.1

NCBI Reference Sequences

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RefSeqi
NP_033735.3, NM_009605.5

UniGene gene-oriented nucleotide sequence clusters

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UniGenei
Mm.3969

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENSMUST00000023593; ENSMUSP00000023593; ENSMUSG00000022878

Database of genes from NCBI RefSeq genomes

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GeneIDi
11450

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
mmu:11450

UCSC genome browser

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UCSCi
uc007ytk.1 mouse

<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

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_009605.5
UniGeneiMm.3969

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
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
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
CORUMiQ60994
DIPiDIP-44111N
IntActiQ60994, 5 interactors
MINTiQ60994
STRINGi10090.ENSMUSP00000023593

PTM databases

iPTMnetiQ60994
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

Comparative Toxicogenomics Database

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CTDi
9370
MGIiMGI:106675 Adipoq

Phylogenomic databases

eggNOGiENOG410IHSJ Eukaryota
ENOG4111F5K LUCA
GeneTreeiENSGT00940000159828
HOGENOMiHOG000085653
HOVERGENiHBG108220
InParanoidiQ60994
KOiK07296
OMAiQQNHYDG
OrthoDBiEOG091G0L3Y
TreeFamiTF329591

Enzyme and pathway databases

ReactomeiR-MMU-163680 AMPK inhibits chREBP transcriptional activation activity

Miscellaneous databases

EvolutionaryTraceiQ60994

Protein Ontology

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PROi
PR:Q60994

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
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Gene expression databases

BgeeiENSMUSG00000022878 Expressed in 122 organ(s), highest expression level in subcutaneous adipose tissue
CleanExiMM_ADIPOQ
ExpressionAtlasiQ60994 baseline and differential
GenevisibleiQ60994 MM

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
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<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_MOUSE
<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: Q60994
Secondary accession number(s): Q62400, Q6GTX4, Q9DC68
<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: October 3, 2012
Last modified: December 5, 2018
This is version 176 of the entry and version 2 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

<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, Reference proteome

Documents

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