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Q60994

- ADIPO_MOUSE

UniProt

Q60994 - ADIPO_MOUSE

Protein

Adiponectin

Gene

Adipoq

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 141 (01 Oct 2014)
      Sequence version 2 (03 Oct 2012)
      Previous versions | rss
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    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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei79 – 791Not hydroxylated
    Sitei98 – 981Not hydroxylated
    Sitei107 – 1071Not hydroxylated
    Sitei233 – 2331Not glycosylated

    GO - Molecular functioni

    1. hormone activity Source: MGI
    2. identical protein binding Source: IntAct
    3. protein binding Source: MGI
    4. receptor binding Source: MGI
    5. sialic acid binding Source: Ensembl

    GO - Biological processi

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

    Keywords - Molecular functioni

    Hormone

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Adiponectin
    Alternative name(s):
    30 kDa adipocyte complement-related protein
    Adipocyte complement-related 30 kDa protein
    Short name:
    ACRP30
    Adipocyte, C1q and collagen domain-containing protein
    Adipocyte-specific protein AdipoQ
    Gene namesi
    Name:Adipoq
    Synonyms:Acdc, Acrp30, Apm1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 16

    Organism-specific databases

    MGIiMGI:106675. Adipoq.

    Subcellular locationi

    GO - Cellular componenti

    1. cell periphery Source: UniProtKB
    2. cell surface Source: BHF-UCL
    3. collagen trimer Source: UniProtKB-KW
    4. endoplasmic reticulum Source: MGI
    5. extracellular space Source: MGI
    6. perinuclear region of cytoplasm Source: UniProtKB

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi39 – 391C → A: No change in the interaction with CTRP9. 1 Publication
    Mutagenesisi68 – 681K → R: Impaired formation of HMW multimers; when associated with R-71; R-80 and R-104. 1 Publication
    Mutagenesisi71 – 711K → R: Impaired formation of HMW multimers; when associated with R-68; R-80 and R-104. 1 Publication
    Mutagenesisi80 – 801K → R: Impaired formation of HMW multimers; when associated with R-68; R-71 and R-104. 1 Publication
    Mutagenesisi104 – 1041K → R: Impaired formation of HMW multimers; when associated with R-68; R-71 and R-80. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 17171 PublicationAdd
    BLAST
    Chaini18 – 247230AdiponectinPRO_0000003544Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi23 – 231O-linked (GalNAc...)1 Publication
    Glycosylationi24 – 241O-linked (GalNAc...)1 Publication
    Disulfide bondi39 – 39InterchainBy similarity
    Modified residuei47 – 4714-hydroxyprolineBy similarity
    Modified residuei50 – 5014-hydroxyprolineBy similarity
    Modified residuei56 – 5614-hydroxyprolineBy similarity
    Modified residuei68 – 6815-hydroxylysine1 Publication
    Glycosylationi68 – 681O-linked (Gal...)1 Publication
    Modified residuei71 – 7115-hydroxylysine1 Publication
    Glycosylationi71 – 711O-linked (Gal...)1 Publication
    Modified residuei80 – 8015-hydroxylysine1 Publication
    Glycosylationi80 – 801O-linked (Gal...)1 Publication
    Modified residuei94 – 9414-hydroxyproline1 Publication
    Modified residuei104 – 10415-hydroxylysine1 Publication
    Glycosylationi104 – 1041O-linked (Gal...)1 Publication

    Post-translational modificationi

    HMW complexes are more extensively glycosylated than smaller oligomers. Hydroxylation and glycosylation of the lysine residues within the collagene-like domain of adiponectin seem to be critically involved in regulating the formation and/or secretion of HMW complexes and consequently contribute to the insulin-sensitizing activity of adiponectin in hepatocytes.1 Publication
    O-glycosylated. Not N-glycosylated By similarity O-linked glycans on hydroxylysine residues consist of Glc-Gal disaccharides bound to the oxygen atom of post-translationally added hydroxyl groups By similarity. O-linked glycosylation in the N-terminal is disialylated with the structure Neu5Acalpha2->8Neu5Acalpha2->3Gal. Sialylated by alpha 2,8-sialyltransferase III.By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Hydroxylation

    Proteomic databases

    MaxQBiQ60994.
    PaxDbiQ60994.
    PRIDEiQ60994.

    Expressioni

    Tissue specificityi

    Synthesized exclusively by adipocytes and secreted into plasma.

    Inductioni

    During hormone-induced adipose differentiation and activated by insulin.

    Gene expression databases

    ArrayExpressiQ60994.
    CleanExiMM_ADIPOQ.
    GenevestigatoriQ60994.

    Interactioni

    Subunit structurei

    Homomultimer. Forms trimers, hexamers and 12- to 18-mers. The trimers (low molecular weight complexes / LMW) are assembled via non-covalent interactions of the collagen-like domains in a triple helix and hydrophobic interactions within the globular C1q domain. Several trimers can associate to form disulfide-linked hexamers (middle molecular weight complexes / MMW) and larger complexes (higher molecular weight / HMW). The HMW-complex assembly may rely additionally on lysine hydroxylation and glycosylation. LMW, MMW and HMW complexes bind to HBEGF, MMW and HMW complexes bind to PDGFB, and HMW complex binds to FGF2. Interacts with CTRP9 via the C1q domain (heterotrimeric complex).5 Publications

    Binary interactionsi

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

    Protein-protein interaction databases

    BioGridi197940. 4 interactions.
    DIPiDIP-44111N.
    IntActiQ60994. 2 interactions.
    MINTiMINT-4563800.

    Structurei

    Secondary structure

    1
    247
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi117 – 1215
    Beta strandi130 – 1323
    Beta strandi137 – 1404
    Turni148 – 1503
    Beta strandi152 – 1543
    Beta strandi159 – 17214
    Beta strandi174 – 1807
    Beta strandi183 – 1908
    Beta strandi197 – 20812
    Beta strandi213 – 2186
    Beta strandi236 – 2449

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1C28X-ray2.10A/B/C114-247[»]
    1C3HX-ray2.10A/B/C/D/E/F111-247[»]
    ProteinModelPortaliQ60994.
    SMRiQ60994. Positions 111-247.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ60994.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini45 – 11066Collagen-likeAdd
    BLAST
    Domaini111 – 247137C1qPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

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

    Keywords - Domaini

    Collagen, Repeat, Signal

    Phylogenomic databases

    eggNOGiNOG136972.
    GeneTreeiENSGT00750000117356.
    HOGENOMiHOG000085653.
    HOVERGENiHBG108220.
    InParanoidiQ60994.
    KOiK07296.
    OMAiHITVYLK.
    OrthoDBiEOG70ZZPW.
    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.

    Q60994-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLLLQALLFL LILPSHAEDD VTTTEELAPA LVPPPKGTCA GWMAGIPGHP    50
    GHNGTPGRDG RDGTPGEKGE KGDAGLLGPK GETGDVGMTG AEGPRGFPGT 100
    PGRKGEPGEA AYVYRSAFSV GLETRVTVPN VPIRFTKIFY NQQNHYDGST 150
    GKFYCNIPGL YYFSYHITVY MKDVKVSLFK KDKAVLFTYD QYQEKNVDQA 200
    SGSVLLHLEV GDQVWLQVYG DGDHNGLYAD NVNDSTFTGF LLYHDTN 247
    Length:247
    Mass (Da):26,809
    Last modified:October 3, 2012 - v2
    Checksum:i0ECC687D9A8E8123
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti50 – 501P → S in AAB06706. (PubMed:8631877)Curated
    Sequence conflicti74 – 741A → S in AAB06706. (PubMed:8631877)Curated
    Sequence conflicti113 – 1131V → M in AAA80543. (PubMed:7592907)Curated
    Sequence conflicti113 – 1131V → M in AAK13417. (PubMed:11162643)Curated
    Sequence conflicti117 – 1171A → G in AAB06706. (PubMed:8631877)Curated
    Sequence conflicti148 – 1481G → N in AAB06706. (PubMed:8631877)Curated
    Sequence conflicti243 – 2431Y → F in AAB06706. (PubMed:8631877)Curated

    Sequence databases

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

    Genome annotation databases

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

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS28075.1.
    RefSeqi NP_033735.3. NM_009605.4.
    UniGenei Mm.3969.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1C28 X-ray 2.10 A/B/C 114-247 [» ]
    1C3H X-ray 2.10 A/B/C/D/E/F 111-247 [» ]
    ProteinModelPortali Q60994.
    SMRi Q60994. Positions 111-247.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 197940. 4 interactions.
    DIPi DIP-44111N.
    IntActi Q60994. 2 interactions.
    MINTi MINT-4563800.

    Proteomic databases

    MaxQBi Q60994.
    PaxDbi Q60994.
    PRIDEi Q60994.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000023593 ; ENSMUSP00000023593 ; ENSMUSG00000022878 .
    GeneIDi 11450.
    KEGGi mmu:11450.
    UCSCi uc007ytk.1. mouse.

    Organism-specific databases

    CTDi 9370.
    MGIi MGI:106675. Adipoq.

    Phylogenomic databases

    eggNOGi NOG136972.
    GeneTreei ENSGT00750000117356.
    HOGENOMi HOG000085653.
    HOVERGENi HBG108220.
    InParanoidi Q60994.
    KOi K07296.
    OMAi HITVYLK.
    OrthoDBi EOG70ZZPW.
    TreeFami TF329591.

    Miscellaneous databases

    EvolutionaryTracei Q60994.
    NextBioi 278770.
    PROi Q60994.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q60994.
    CleanExi MM_ADIPOQ.
    Genevestigatori Q60994.

    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

    1. "A novel serum protein similar to C1q, produced exclusively in adipocytes."
      Scherer P.E., Williams S., Fogliano M., Baldini G., Lodish H.F.
      J. Biol. Chem. 270:26746-26749(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Adipocyte.
    2. "AdipoQ is a novel adipose-specific gene dysregulated in obesity."
      Hu E., Liang P., Spiegelman B.M.
      J. Biol. Chem. 271:10697-10703(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Fibroblast.
    3. "Chromosomal localization, expression pattern, and promoter analysis of the mouse gene encoding adipocyte-specific secretory protein Acrp30."
      Das K., Lin Y., Widen E., Zhang Y., Scherer P.E.
      Biochem. Biophys. Res. Commun. 280:1120-1129(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    4. "Cloning of murine adipocyte complement-related protein of 30 KDa from white adipose tissue."
      Wang S.F., Han P.Z., Mu C.J., Zhao M.H.
      Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: C57BL/6J and IRM-2.
      Tissue: White adipose tissue.
    5. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J.
      Tissue: Heart and Thymus.
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    7. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
      Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "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].
      Strain: C57BL/6J.
      Tissue: Thymus.
    9. "Hydroxylation and glycosylation of the four conserved lysine residues in the collagenous domain of adiponectin. Potential role in the modulation of its insulin-sensitizing activity."
      Wang Y., Xu A., Knight C., Xu L.Y., Cooper G.J.S.
      J. Biol. Chem. 277:19521-19529(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 18-25, HYDROXYLATION AT LYS-68; LYS-71; LYS-80; PRO-94 AND LYS-104, GLYCOSYLATION AT LYS-68; LYS-71; LYS-80 AND LYS-104, GLYCAN STRUCTURE, ABSENCE OF HYDROXYLATION AT PRO-79; PRO-98 AND PRO-107, ABSENCE OF GLYCOSYLATION AT ASN-233, IDENTIFICATION BY MASS SPECTROMETRY.
    10. "Identification and adipocyte differentiation-dependent expression of the unique disialic acid residue in an adipose tissue-specific glycoprotein, adipo Q."
      Sato C., Yasukawa Z., Honda N., Matsuda T., Kitajima K.
      J. Biol. Chem. 276:28849-28856(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE OF CARBOHYDRATES.
    11. Cited for: FUNCTION.
    12. "The adipocyte-secreted protein Acrp30 enhances hepatic insulin action."
      Berg A.H., Combs T.P., Du X., Brownlee M., Scherer P.E.
      Nat. Med. 7:947-953(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    13. "The fat-derived hormone adiponectin alleviates alcoholic and nonalcoholic fatty liver diseases in mice."
      Xu A., Wang Y., Keshaw H., Xu L.Y., Lam K.S.L., Cooper G.J.S.
      J. Clin. Invest. 112:91-100(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    14. "Testosterone selectively reduces the high molecular weight form of adiponectin by inhibiting its secretion from adipocytes."
      Xu A., Chan K.W., Hoo R.L.C., Wang Y., Tan K.C.B., Zhang J., Chen B., Lam M.C., Tse C., Cooper G.J.S., Lam K.S.L.
      J. Biol. Chem. 280:18073-18080(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT, FUNCTION.
    15. "Adiponectin inhibits cell proliferation by interacting with several growth factors in an oligomerization-dependent manner."
      Wang Y., Lam K.S.L., Xu J.Y., Lu G., Xu L.Y., Cooper G.J.S., Xu A.
      J. Biol. Chem. 280:18341-18347(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT, FUNCTION.
    16. "Post-translational modifications of the four conserved lysine residues within the collagenous domain of adiponectin are required for the formation of its high molecular weight oligomeric complex."
      Wang Y., Lam K.S.L., Chan L., Chan K.W., Lam J.B.B., Lam M.C., Hoo R.C.L., Mak W.W.N., Cooper G.J.S., Xu A.
      J. Biol. Chem. 281:16391-16400(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT, MUTAGENESIS OF LYS-68; LYS-71; LYS-80 AND LYS-104.
    17. "Identification and characterization of CTRP9, a novel secreted glycoprotein, from adipose tissue that reduces serum glucose in mice and forms heterotrimers with adiponectin."
      Wong G.W., Krawczyk S.A., Kitidis-Mitrokostas C., Ge G., Spooner E., Hug C., Gimeno R., Lodish H.F.
      FASEB J. 23:241-258(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT, INTERACTION WITH CTRP9, MUTAGENESIS OF CYS-39.
    18. "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-23 AND THR-24, SUBUNIT.
    19. "The crystal structure of a complement-1q family protein suggests an evolutionary link to tumor necrosis factor."
      Shapiro L., Scherer P.E.
      Curr. Biol. 8:335-338(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 111-247.

    Entry informationi

    Entry nameiADIPO_MOUSE
    AccessioniPrimary (citable) accession number: Q60994
    Secondary accession number(s): Q62400, Q6GTX4, Q9DC68
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: October 3, 2012
    Last modified: October 1, 2014
    This is version 141 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    HMW-complex blood contents are higher in females than in males, are increased in males by castration and decreased again upon subsequent testosterone treatment, which blocks HMW-complex secretion.

    Keywords - Technical termi

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

    Documents

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

    External Data

    Dasty 3