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Q3Y5Z3

- ADIPO_BOVIN

UniProt

Q3Y5Z3 - ADIPO_BOVIN

Protein

Adiponectin

Gene

ADIPOQ

Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 69 (01 Oct 2014)
      Sequence version 1 (27 Sep 2005)
      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 By similarity.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei57 – 571Not hydroxylated
    Sitei66 – 661Not hydroxylated
    Sitei71 – 711Not hydroxylated
    Sitei90 – 901Not hydroxylated
    Sitei99 – 991Not hydroxylated
    Sitei225 – 2251Not glycosylated

    GO - Molecular functioni

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

    GO - Biological processi

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

    Keywords - Molecular functioni

    Hormone

    Enzyme and pathway databases

    ReactomeiREACT_220799. 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
    Gene namesi
    Name:ADIPOQ
    Synonyms:ACRP30, APM1
    OrganismiBos taurus (Bovine)
    Taxonomic identifieri9913 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
    ProteomesiUP000009136: Chromosome 1

    Subcellular locationi

    Secreted By similarity

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 17172 PublicationsAdd
    BLAST
    Chaini18 – 240223AdiponectinPRO_0000236269Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei28 – 2815-hydroxylysine1 Publication
    Glycosylationi28 – 281O-linked (Gal...)2 Publications
    Disulfide bondi31 – 31Interchain; in form MMW and form HMWBy similarity
    Modified residuei39 – 3914-hydroxyproline1 Publication
    Modified residuei42 – 4214-hydroxyproline1 Publication
    Modified residuei48 – 4814-hydroxyproline1 Publication
    Modified residuei60 – 6015-hydroxylysine1 Publication
    Glycosylationi60 – 601O-linked (Gal...)2 Publications
    Modified residuei63 – 6315-hydroxylysine1 Publication
    Glycosylationi63 – 631O-linked (Gal...)2 Publications
    Modified residuei72 – 7215-hydroxylysine1 Publication
    Glycosylationi72 – 721O-linked (Gal...)1 Publication
    Modified residuei86 – 8614-hydroxyproline1 Publication
    Modified residuei96 – 9615-hydroxylysine1 Publication
    Glycosylationi96 – 961O-linked (Gal...)2 Publications

    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 By similarity.By similarity
    O-glycosylated. 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 glycosylations elsewhere disialylated with the structure Neu5Acalpha2->8Neu5Acalpha2->3Gal. Sialylated by alpha 2,8-sialyltransferase III. Desialylated forms are rapidly cleared from the circulation. Not N-glycosylated.By similarity2 Publications

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Hydroxylation

    Proteomic databases

    PaxDbiQ3Y5Z3.
    PRIDEiQ3Y5Z3.

    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) By similarity.By similarity

    Protein-protein interaction databases

    MINTiMINT-4563461.
    STRINGi9913.ENSBTAP00000026395.

    Structurei

    3D structure databases

    ProteinModelPortaliQ3Y5Z3.
    SMRiQ3Y5Z3. Positions 103-237.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini43 – 10260Collagen-likeAdd
    BLAST
    Domaini103 – 240138C1qPROSITE-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.
    InParanoidiQ3Y5Z3.
    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.

    Q3Y5Z3-1 [UniParc]FASTAAdd to Basket

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    MLLQGALLLL LALPSHGEDN MEDPPLPKGA CAGWMAGIPG HPGHNGTPGR    50
    DGRDGTPGEK GEKGDPGLVG PKGDTGETGI TGIEGPRGFP GTPGRKGEPG 100
    ESAYVYRSAF SVGLERQVTV PNVPIRFTKI FYNQQNHYDG TTGKFLCNIP 150
    GLYYFSYHIT VYLKDVKVSL YKNDKALLFT HDQFQDKNVD QASGSVLLYL 200
    EKGDQVWLQV YEGENHNGVY ADNVNDSTFT GFLLYHNIVE 240
    Length:240
    Mass (Da):26,133
    Last modified:September 27, 2005 - v1
    Checksum:i409122E49F3AF253
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti66 – 661P → A in AAK58902. (PubMed:11382781)Curated
    Sequence conflicti69 – 691V → L in AAK58902. (PubMed:11382781)Curated
    Sequence conflicti74 – 741D → E in AAK58902. (PubMed:11382781)Curated
    Sequence conflicti77 – 837ETGITGI → DVGMTGA in AAK58902. (PubMed:11382781)Curated
    Sequence conflicti102 – 1021S → A in AAK58902. (PubMed:11382781)Curated
    Sequence conflicti116 – 1172RQ → TR in AAK58902. (PubMed:11382781)Curated
    Sequence conflicti141 – 1411T → S in AAK58902. (PubMed:11382781)Curated
    Sequence conflicti146 – 1461L → Y in AAK58902. (PubMed:11382781)Curated
    Sequence conflicti163 – 1631L → M in AAK58902. (PubMed:11382781)Curated
    Sequence conflicti171 – 1733YKN → FKK in AAK58902. (PubMed:11382781)Curated
    Sequence conflicti177 – 1771L → V in AAK58902. (PubMed:11382781)Curated
    Sequence conflicti181 – 1811H → Y in AAK58902. (PubMed:11382781)Curated
    Sequence conflicti184 – 1863FQD → YQE in AAK58902. (PubMed:11382781)Curated
    Sequence conflicti199 – 1991Y → H in AAK58902. (PubMed:11382781)Curated
    Sequence conflicti202 – 2021K → V in AAK58902. (PubMed:11382781)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF269230 mRNA. Translation: AAK58902.1.
    DQ156120 Genomic DNA. Translation: AAZ81421.1.
    BC140488 mRNA. Translation: AAI40489.1.
    RefSeqiNP_777167.1. NM_174742.2.
    UniGeneiBt.109637.

    Genome annotation databases

    EnsembliENSBTAT00000026395; ENSBTAP00000026395; ENSBTAG00000019813.
    GeneIDi282865.
    KEGGibta:282865.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF269230 mRNA. Translation: AAK58902.1 .
    DQ156120 Genomic DNA. Translation: AAZ81421.1 .
    BC140488 mRNA. Translation: AAI40489.1 .
    RefSeqi NP_777167.1. NM_174742.2.
    UniGenei Bt.109637.

    3D structure databases

    ProteinModelPortali Q3Y5Z3.
    SMRi Q3Y5Z3. Positions 103-237.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    MINTi MINT-4563461.
    STRINGi 9913.ENSBTAP00000026395.

    Proteomic databases

    PaxDbi Q3Y5Z3.
    PRIDEi Q3Y5Z3.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSBTAT00000026395 ; ENSBTAP00000026395 ; ENSBTAG00000019813 .
    GeneIDi 282865.
    KEGGi bta:282865.

    Organism-specific databases

    CTDi 9370.

    Phylogenomic databases

    eggNOGi NOG136972.
    GeneTreei ENSGT00750000117356.
    HOGENOMi HOG000085653.
    HOVERGENi HBG108220.
    InParanoidi Q3Y5Z3.
    KOi K07296.
    OMAi HITVYLK.
    OrthoDBi EOG70ZZPW.
    TreeFami TF329591.

    Enzyme and pathway databases

    Reactomei REACT_220799. Transcriptional regulation of white adipocyte differentiation.

    Miscellaneous databases

    NextBioi 20806393.

    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. "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: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 18-26; 194-197; 203-208 AND 221-228, GLYCOSYLATION, STRUCTURE OF CARBOHYDRATES.
      Tissue: Adipose tissue.
    2. Morsci N.S., Schnabel R.D., Taylor J.F.
      Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. NIH - Mammalian Gene Collection (MGC) project
      Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: Hereford.
      Tissue: Ascending colon.
    4. "Proteomic and functional characterization of endogenous adiponectin purified from fetal bovine serum."
      Wang Y., Lu G., Wong W.P.S., Vliegenthart J.F.G., Gerwig G.J., Lam K.S.L., Cooper G.J.S., Xu A.
      Proteomics 4:3933-3942(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 18-26, PARTIAL PROTEIN SEQUENCE, HYDROXYLATION AT LYS-28; PRO-39; PRO-42; PRO-48; LYS-60; LYS-63; LYS-72; PRO-86 AND LYS-96, GLYCOSYLATION AT LYS-28; LYS-60; LYS-63 AND LYS-96, ABSENCE OF HYDROXYLATION AT PRO-57; PRO-66; PRO-71; PRO-90 AND PRO-99, ABSENCE OF GLYCOSYLATION AT ASN-225, IDENTIFICATION BY MASS SPECTROMETRY.

    Entry informationi

    Entry nameiADIPO_BOVIN
    AccessioniPrimary (citable) accession number: Q3Y5Z3
    Secondary accession number(s): A5D7A8, Q95MQ4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2006
    Last sequence update: September 27, 2005
    Last modified: October 1, 2014
    This is version 69 of the entry and version 1 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.By similarity

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3