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Protein

Adiponectin

Gene

Adipoq

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: 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.5 Publications

Sites

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

GO - Molecular functioni

  • hormone activity Source: MGI
  • identical protein binding Source: IntAct
  • protein homodimerization activity Source: MGI
  • receptor binding Source: MGI
  • sialic acid binding Source: MGI

GO - Biological processi

Complete GO annotation...

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 Componenti: Chromosome 16

Organism-specific databases

MGIiMGI:106675. Adipoq.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

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

CleanExiMM_ADIPOQ.
ExpressionAtlasiQ60994. baseline and differential.
GenevisibleiQ60994. MM.

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. 3 interactions.
DIPiDIP-44111N.
IntActiQ60994. 2 interactions.
MINTiMINT-4563800.
STRINGi10090.ENSMUSP00000023593.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00760000118830.
HOGENOMiHOG000085653.
HOVERGENiHBG108220.
InParanoidiQ60994.
KOiK07296.
OMAiKAMLFTY.
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

        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
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:
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_009605.4.
UniGeneiMm.3969.

Genome annotation databases

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

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_009605.4.
UniGeneiMm.3969.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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...

Protein-protein interaction databases

BioGridi197940. 3 interactions.
DIPiDIP-44111N.
IntActiQ60994. 2 interactions.
MINTiMINT-4563800.
STRINGi10090.ENSMUSP00000023593.

Proteomic databases

MaxQBiQ60994.
PaxDbiQ60994.
PRIDEiQ60994.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi9370.
MGIiMGI:106675. Adipoq.

Phylogenomic databases

eggNOGiNOG136972.
GeneTreeiENSGT00760000118830.
HOGENOMiHOG000085653.
HOVERGENiHBG108220.
InParanoidiQ60994.
KOiK07296.
OMAiKAMLFTY.
OrthoDBiEOG70ZZPW.
TreeFamiTF329591.

Miscellaneous databases

EvolutionaryTraceiQ60994.
NextBioi278770.
PROiQ60994.
SOURCEiSearch...

Gene expression databases

CleanExiMM_ADIPOQ.
ExpressionAtlasiQ60994. baseline and differential.
GenevisibleiQ60994. MM.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: July 22, 2015
This is version 149 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.