Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q15848

- ADIPO_HUMAN

UniProt

Q15848 - ADIPO_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Adiponectin

Gene

ADIPOQ

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei62 – 621Not hydroxylated
Sitei86 – 861Not hydroxylated
Sitei104 – 1041Not hydroxylated
Sitei230 – 2301Not glycosylated

GO - Molecular functioni

  1. cytokine activity Source: BHF-UCL
  2. hormone activity Source: BHF-UCL
  3. identical protein binding Source: BHF-UCL
  4. protein homodimerization activity Source: BHF-UCL
  5. receptor binding Source: UniProtKB
  6. sialic acid binding Source: UniProtKB

GO - Biological processi

  1. adiponectin-activated signaling pathway Source: Ensembl
  2. brown fat cell differentiation Source: UniProtKB
  3. cellular response to cAMP Source: Ensembl
  4. cellular response to drug Source: UniProtKB
  5. cellular response to epinephrine stimulus Source: Ensembl
  6. cellular response to insulin stimulus Source: UniProtKB
  7. circadian rhythm Source: Ensembl
  8. detection of oxidative stress Source: UniProtKB
  9. fatty acid beta-oxidation Source: UniProtKB
  10. fatty acid oxidation Source: UniProtKB
  11. generation of precursor metabolites and energy Source: ProtInc
  12. glucose homeostasis Source: UniProtKB
  13. glucose metabolic process Source: UniProtKB
  14. low-density lipoprotein particle clearance Source: BHF-UCL
  15. membrane depolarization Source: Ensembl
  16. membrane hyperpolarization Source: Ensembl
  17. negative regulation of blood pressure Source: UniProtKB
  18. negative regulation of cell migration Source: UniProtKB
  19. negative regulation of DNA biosynthetic process Source: UniProtKB
  20. negative regulation of ERK1 and ERK2 cascade Source: UniProtKB
  21. negative regulation of fat cell differentiation Source: BHF-UCL
  22. negative regulation of gluconeogenesis Source: BHF-UCL
  23. negative regulation of granulocyte differentiation Source: BHF-UCL
  24. negative regulation of heterotypic cell-cell adhesion Source: BHF-UCL
  25. negative regulation of hormone secretion Source: Ensembl
  26. negative regulation of I-kappaB kinase/NF-kappaB signaling Source: BHF-UCL
  27. negative regulation of inflammatory response Source: UniProtKB
  28. negative regulation of intracellular protein transport Source: UniProtKB
  29. negative regulation of low-density lipoprotein particle receptor biosynthetic process Source: BHF-UCL
  30. negative regulation of macrophage derived foam cell differentiation Source: BHF-UCL
  31. negative regulation of macrophage differentiation Source: BHF-UCL
  32. negative regulation of MAP kinase activity Source: UniProtKB
  33. negative regulation of metanephric mesenchymal cell migration Source: UniProtKB
  34. negative regulation of phagocytosis Source: BHF-UCL
  35. negative regulation of platelet-derived growth factor receptor-alpha signaling pathway Source: UniProtKB
  36. negative regulation of platelet-derived growth factor receptor signaling pathway Source: UniProtKB
  37. negative regulation of protein autophosphorylation Source: UniProtKB
  38. negative regulation of receptor binding Source: UniProtKB
  39. negative regulation of smooth muscle cell migration Source: UniProtKB
  40. negative regulation of smooth muscle cell proliferation Source: UniProtKB
  41. negative regulation of synaptic transmission Source: UniProtKB
  42. negative regulation of transcription, DNA-templated Source: UniProtKB
  43. negative regulation of tumor necrosis factor-mediated signaling pathway Source: BHF-UCL
  44. negative regulation of tumor necrosis factor production Source: BHF-UCL
  45. positive regulation of blood pressure Source: Ensembl
  46. positive regulation of cAMP-dependent protein kinase activity Source: UniProtKB
  47. positive regulation of cellular protein metabolic process Source: BHF-UCL
  48. positive regulation of cholesterol efflux Source: BHF-UCL
  49. positive regulation of fatty acid metabolic process Source: BHF-UCL
  50. positive regulation of glucose import Source: BHF-UCL
  51. positive regulation of glycogen (starch) synthase activity Source: UniProtKB
  52. positive regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
  53. positive regulation of interleukin-8 production Source: UniProtKB
  54. positive regulation of metanephric glomerular visceral epithelial cell development Source: UniProtKB
  55. positive regulation of monocyte chemotactic protein-1 production Source: UniProtKB
  56. positive regulation of myeloid cell apoptotic process Source: BHF-UCL
  57. positive regulation of peptidyl-tyrosine phosphorylation Source: Ensembl
  58. positive regulation of protein kinase A signaling Source: BHF-UCL
  59. positive regulation of protein phosphorylation Source: UniProtKB
  60. positive regulation of renal albumin absorption Source: UniProtKB
  61. positive regulation of signal transduction Source: BHF-UCL
  62. protein heterotrimerization Source: Ensembl
  63. protein homooligomerization Source: UniProtKB
  64. protein localization to plasma membrane Source: UniProtKB
  65. regulation of glucose metabolic process Source: UniProtKB
  66. response to activity Source: Ensembl
  67. response to ethanol Source: Ensembl
  68. response to glucocorticoid Source: Ensembl
  69. response to glucose Source: BHF-UCL
  70. response to hypoxia Source: Ensembl
  71. response to linoleic acid Source: Ensembl
  72. response to nutrient Source: Ensembl
  73. response to sucrose Source: Ensembl
  74. response to tumor necrosis factor Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

Hormone

Enzyme and pathway databases

ReactomeiREACT_27161. Transcriptional regulation of white adipocyte differentiation.

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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 3

Organism-specific databases

HGNCiHGNC:13633. ADIPOQ.

Subcellular locationi

GO - Cellular componenti

  1. cell surface Source: BHF-UCL
  2. collagen trimer Source: UniProtKB-KW
  3. endoplasmic reticulum Source: UniProtKB
  4. extracellular region Source: Reactome
  5. extracellular space Source: UniProtKB
  6. extracellular vesicular exosome Source: UniProt
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Involvement in diseasei

Adiponectin deficiency (ADPND) [MIM:612556]: A condition that results in very low concentrations of plasma adiponectin.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti112 – 1121R → C in ADPND; does not assemble into trimers resulting in impaired secretion from the cell. 2 Publications
VAR_013274
Diabetes mellitus, non-insulin-dependent (NIDDM) [MIM:125853]: A 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.
Note: Disease susceptibility is associated with variations affecting the gene represented in this entry.

Pharmaceutical usei

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

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi20 – 201T → A: No change in sialylated isoforms. 1 Publication
Mutagenesisi21 – 211T → A: Some loss of sialylated isoforms. 1 Publication
Mutagenesisi22 – 221T → A: Abolishes sialylated isoforms. 1 Publication
Mutagenesisi33 – 331K → R: No effect on formation of HMW multimers. 1 Publication
Mutagenesisi36 – 361C → S: Impaired formation of MMW and HMW multimers. 2 Publications
Mutagenesisi65 – 651K → R: Impaired formation of HMW multimers; when associated with R-68. 1 Publication
Mutagenesisi68 – 681K → R: Impaired formation of HMW multimers; when associated with R-65. 1 Publication
Mutagenesisi77 – 771K → R: Impaired formation of HMW multimers; when associated with R-101. 1 Publication
Mutagenesisi101 – 1011K → R: Impaired formation of HMW multimers; when associated with R-77. 1 Publication

Keywords - Diseasei

Diabetes mellitus, Disease mutation, Obesity

Organism-specific databases

MIMi125853. phenotype.
612556. phenotype.
PharmGKBiPA134933118.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 18182 PublicationsAdd
BLAST
Chaini19 – 244226AdiponectinPRO_0000003543Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi21 – 211O-linked (GalNAc...)1 Publication
Glycosylationi22 – 221O-linked (GalNAc...)1 Publication
Modified residuei33 – 3315-hydroxylysineCurated
Disulfide bondi36 – 36Interchain; in form MMW and form HMW2 Publications
Modified residuei44 – 4414-hydroxyproline1 Publication
Modified residuei47 – 4714-hydroxyproline1 Publication
Modified residuei53 – 5314-hydroxyproline1 Publication
Modified residuei65 – 6515-hydroxylysine1 Publication
Glycosylationi65 – 651O-linked (Gal...); partial1 Publication
Modified residuei68 – 6815-hydroxylysine1 Publication
Glycosylationi68 – 681O-linked (Gal...); partial1 Publication
Modified residuei71 – 7114-hydroxyproline; partial1 Publication
Modified residuei76 – 7614-hydroxyproline; partial1 Publication
Modified residuei77 – 7715-hydroxylysine1 Publication
Glycosylationi77 – 771O-linked (Gal...); partial1 Publication
Modified residuei91 – 9114-hydroxyproline1 Publication
Modified residuei95 – 9514-hydroxyproline; partial1 Publication
Modified residuei101 – 10115-hydroxylysine1 Publication
Glycosylationi101 – 1011O-linked (Gal...); partial1 Publication

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

Keywords - PTMi

Disulfide bond, Glycoprotein, Hydroxylation

Proteomic databases

PaxDbiQ15848.
PeptideAtlasiQ15848.
PRIDEiQ15848.

Expressioni

Tissue specificityi

Synthesized exclusively by adipocytes and secreted into plasma.

Gene expression databases

BgeeiQ15848.
CleanExiHS_ADIPOQ.
ExpressionAtlasiQ15848. baseline and differential.
GenevestigatoriQ15848.

Organism-specific databases

HPAiCAB046467.

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

Protein-protein interaction databases

BioGridi114771. 3 interactions.
STRINGi9606.ENSP00000320709.

Structurei

Secondary structure

1
244
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi114 – 1185
Beta strandi134 – 1374
Turni145 – 1473
Beta strandi156 – 17722
Beta strandi180 – 1878
Beta strandi195 – 20511
Beta strandi210 – 2156
Beta strandi222 – 2254
Beta strandi233 – 2419

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4DOUX-ray2.00A104-244[»]
ProteinModelPortaliQ15848.
SMRiQ15848. Positions 109-243.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini42 – 10766Collagen-likeAdd
BLAST
Domaini108 – 244137C1qPROSITE-ProRule annotationAdd
BLAST

Domaini

The C1q domain is commonly called the globular domain.

Sequence similaritiesi

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

Keywords - Domaini

Collagen, Repeat, Signal

Phylogenomic databases

eggNOGiNOG136972.
GeneTreeiENSGT00760000118830.
HOGENOMiHOG000085653.
HOVERGENiHBG108220.
InParanoidiQ15848.
KOiK07296.
OMAiNANDEGH.
OrthoDBiEOG70ZZPW.
PhylomeDBiQ15848.
TreeFamiTF329591.

Family and domain databases

Gene3Di2.60.120.40. 1 hit.
InterProiIPR028572. Adiponectin.
IPR001073. C1q.
IPR008160. Collagen.
IPR008983. Tumour_necrosis_fac-like_dom.
[Graphical view]
PANTHERiPTHR24022:SF81. PTHR24022:SF81. 1 hit.
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.

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)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti84 – 841G → R Does not form high molecular weight multimers. 2 Publications
VAR_013273
Natural varianti90 – 901G → S Does not form high molecular weight multimers. 1 Publication
Corresponds to variant rs62625753 [ dbSNP | Ensembl ].
VAR_027395
Natural varianti111 – 1111Y → H.1 Publication
Corresponds to variant rs17366743 [ dbSNP | Ensembl ].
VAR_027396
Natural varianti112 – 1121R → C in ADPND; does not assemble into trimers resulting in impaired secretion from the cell. 2 Publications
VAR_013274
Natural varianti117 – 1171V → M.1 Publication
VAR_013275
Natural varianti164 – 1641I → T Associated with low plasma adiponectin concentration and diabetes mellitus type 2; does not assemble into trimers resulting in impaired secretion from the cell. 2 Publications
Corresponds to variant rs185847354 [ dbSNP | Ensembl ].
VAR_013276
Natural varianti221 – 2211R → S.2 Publications
Corresponds to variant rs138773406 [ dbSNP | Ensembl ].
VAR_013277
Natural varianti241 – 2411H → P.2 Publications
Corresponds to variant rs141205818 [ dbSNP | Ensembl ].
VAR_013278

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.3. human.

Polymorphism databases

DMDMi2493789.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Wikipedia

Adiponectin entry

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS3284.1.
PIRi JC4708.
RefSeqi NP_001171271.1. NM_001177800.1.
NP_004788.1. NM_004797.3.
UniGenei Hs.80485.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4DOU X-ray 2.00 A 104-244 [» ]
ProteinModelPortali Q15848.
SMRi Q15848. Positions 109-243.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 114771. 3 interactions.
STRINGi 9606.ENSP00000320709.

Polymorphism databases

DMDMi 2493789.

Proteomic databases

PaxDbi Q15848.
PeptideAtlasi Q15848.
PRIDEi Q15848.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000320741 ; ENSP00000320709 ; ENSG00000181092 .
ENST00000444204 ; ENSP00000389814 ; ENSG00000181092 .
GeneIDi 9370.
KEGGi hsa:9370.
UCSCi uc003fra.3. human.

Organism-specific databases

CTDi 9370.
GeneCardsi GC03P186560.
HGNCi HGNC:13633. ADIPOQ.
HPAi CAB046467.
MIMi 125853. phenotype.
605441. gene.
612556. phenotype.
neXtProti NX_Q15848.
PharmGKBi PA134933118.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG136972.
GeneTreei ENSGT00760000118830.
HOGENOMi HOG000085653.
HOVERGENi HBG108220.
InParanoidi Q15848.
KOi K07296.
OMAi NANDEGH.
OrthoDBi EOG70ZZPW.
PhylomeDBi Q15848.
TreeFami TF329591.

Enzyme and pathway databases

Reactomei REACT_27161. Transcriptional regulation of white adipocyte differentiation.

Miscellaneous databases

ChiTaRSi ADIPOQ. human.
GeneWikii Adiponectin.
GenomeRNAii 9370.
NextBioi 35094.
PROi Q15848.
SOURCEi Search...

Gene expression databases

Bgeei Q15848.
CleanExi HS_ADIPOQ.
ExpressionAtlasi Q15848. baseline and differential.
Genevestigatori Q15848.

Family and domain databases

Gene3Di 2.60.120.40. 1 hit.
InterProi IPR028572. Adiponectin.
IPR001073. C1q.
IPR008160. Collagen.
IPR008983. Tumour_necrosis_fac-like_dom.
[Graphical view ]
PANTHERi PTHR24022:SF81. PTHR24022:SF81. 1 hit.
Pfami PF00386. C1q. 1 hit.
PF01391. Collagen. 1 hit.
[Graphical view ]
PRINTSi PR00007. COMPLEMNTC1Q.
SMARTi SM00110. C1Q. 1 hit.
[Graphical view ]
SUPFAMi SSF49842. SSF49842. 1 hit.
PROSITEi PS50871. C1Q. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "cDNA cloning and expression of a novel adipose specific collagen-like factor, apM1 (AdiPose Most abundant Gene transcript 1)."
    Maeda K., Okubo K., Shimomura I., Funahashi T., Matsuzawa Y., Matsubara K.
    Biochem. Biophys. Res. Commun. 221:286-289(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Adipose tissue.
  2. "Organization of the gene for gelatin-binding protein (GBP28)."
    Saito K., Tobe T., Minoshima S., Asakawa S., Sumiya J., Yoda M., Nakano Y., Shimizu N., Tomita M.
    Gene 229:67-73(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "The human apM-1, an adipocyte-specific gene linked to the family of TNF's and to genes expressed in activated T cells, is mapped to chromosome 1q21.3-q23, a susceptibility locus identified for familial combined hyperlipidemia (FCH)."
    Schaeffler A., Orso E., Palitzsch K.D., Buechler C., Drobnik W., Fuerst A., Schoelmerich J., Schmitz G.
    Biochem. Biophys. Res. Commun. 260:416-425(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  5. "Signal peptide prediction based on analysis of experimentally verified cleavage sites."
    Zhang Z., Henzel W.J.
    Protein Sci. 13:2819-2824(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 19-33.
  6. "Isolation and characterization of GBP28, a novel gelatin-binding protein purified from human plasma."
    Nakano Y., Tobe T., Choi-Miura N.H., Mazda T., Tomita M.
    J. Biochem. 120:803-812(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF N-TERMINUS, PARTIAL PROTEIN SEQUENCE.
  7. "Adiponectin, a new member of the family of soluble defense collagens, negatively regulates the growth of myelomonocytic progenitors and the functions of macrophages."
    Yokota T., Oritani K., Takahashi I., Ishikawa J., Matsuyama A., Ouchi N., Kihara S., Funahashi T., Tenner A.J., Tomiyama Y., Matsuzawa Y.
    Blood 96:1723-1732(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  8. "Adiponectin, an adipocyte-derived plasma protein, inhibits endothelial NF-kappaB signaling through a cAMP-dependent pathway."
    Ouchi N., Kihara S., Arita Y., Okamoto Y., Maeda K., Kuriyama H., Hotta K., Nishida M., Takahashi M., Muraguchi M., Ohmoto Y., Nakamura T., Yamashita S., Funahashi T., Matsuzawa Y.
    Circulation 102:1296-1301(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  9. Cited for: FUNCTION.
  10. "Impaired multimerization of human adiponectin mutants associated with diabetes. Molecular structure and multimer formation of adiponectin."
    Waki H., Yamauchi T., Kamon J., Ito Y., Uchida S., Kita S., Hara K., Hada Y., Vasseur F., Froguel P., Kimura S., Nagai R., Kadowaki T.
    J. Biol. Chem. 278:40352-40363(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT, DISULFIDE BOND, MUTAGENESIS OF CYS-36, CHARACTERIZATION OF VARIANTS ARG-84; SER-90; CYS-112 AND THR-164.
  11. "Adiponectin multimerization is dependent on conserved lysines in the collagenous domain: evidence for regulation of multimerization by alterations in posttranslational modifications."
    Richards A.A., Stephens T., Charlton H.K., Jones A., Macdonald G.A., Prins J.B., Whitehead J.P.
    Mol. Endocrinol. 20:1673-1687(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT, HYDROXYLATION AT PRO-44; PRO-47; PRO-53; LYS-65; LYS-68; PRO-71; PRO-76; LYS-77; PRO-91; PRO-95 AND LYS-101, GLYCOSYLATION AT LYS-65; LYS-68; LYS-77 AND LYS-101, DISULFIDE BOND, LACK OF HYDROXYLATION AT PRO-62; PRO-86 AND PRO-104, LACK OF GLYCOSYLATION AT ASN-230, MUTAGENESIS OF LYS-33; CYS-36; LYS-65; LYS-68; LYS-77 AND LYS-101, IDENTIFICATION BY MASS SPECTROMETRY.
  12. "Sialic acid modification of adiponectin is not required for multimerization or secretion but determines half-life in circulation."
    Richards A.A., Colgrave M.L., Zhang J., Webster J., Simpson F., Preston E., Wilks D., Hoehn K.L., Stephenson M., Macdonald G.A., Prins J.B., Cooney G.J., Xu A., Whitehead J.P.
    Mol. Endocrinol. 24:229-239(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION AT THR-21 AND THR-22, SUBUNIT, IDENTIFICATION BY MASS SPECTROMETRY, MUTAGENESIS OF THR-20; THR-21 AND THR-22.
  13. "Crystal structure of a single-chain trimer of human adiponectin globular domain."
    Min X., Lemon B., Tang J., Liu Q., Zhang R., Walker N., Li Y., Wang Z.
    FEBS Lett. 586:912-917(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 104-244, SUBUNIT.
  14. Cited for: VARIANT ADPND CYS-112.
  15. "Genetic variation in the gene encoding adiponectin is associated with an increased risk of type 2 diabetes in the Japanese population."
    Hara K., Boutin P., Mori Y., Tobe K., Dina C., Yasuda K., Yamauchi T., Otabe S., Okada T., Eto K., Kadowaki H., Hagura R., Akanuma Y., Yazaki Y., Nagai R., Taniyama M., Matsubara K., Yoda M.
    , Nakano Y., Kimura S., Tomita M., Kimura S., Ito C., Froguel P., Kadowaki T.
    Diabetes 51:536-540(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS ARG-84; MET-117; THR-164; SER-221 AND PRO-241.
  16. "Association of adiponectin mutation with type 2 diabetes: a candidate gene for the insulin resistance syndrome."
    Kondo H., Shimomura I., Matsukawa Y., Kumada M., Takahashi M., Matsuda M., Ouchi N., Kihara S., Kawamoto T., Sumitsuji S., Funahashi T., Matsuzawa Y.
    Diabetes 51:2325-2328(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS CYS-112; THR-164; SER-221 AND PRO-241, ASSOCIATION WITH LOW PLASMA ADIPONECTIN CONCENTRATION AND DIABETES MELLITUS TYPE 2.
  17. "Single-nucleotide polymorphism haplotypes in the both proximal promoter and exon 3 of the APM1 gene modulate adipocyte-secreted adiponectin hormone levels and contribute to the genetic risk for type 2 diabetes in French Caucasians."
    Vasseur F., Helbecque N., Dina C., Lobbens S., Delannoy V., Gaget S., Boutin P., Vaxillaire M., Lepretre F., Dupont S., Hara K., Clement K., Bihain B., Kadowaki T., Froguel P.
    Hum. Mol. Genet. 11:2607-2614(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS ARG-84; SER-90 AND HIS-111.

Entry informationi

Entry nameiADIPO_HUMAN
AccessioniPrimary (citable) accession number: Q15848
Secondary accession number(s): Q58EX9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: October 29, 2014
This is version 152 of the entry and version 1 of the sequence. [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

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

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
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3