Reviewed, UniProtKB/Swiss-Prot Q3Y5Z3 (ADIPO_BOVIN)

Names and origin

Protein names

Recommended name:
    Adiponectin
Alternative name(s):
    Adipocyte, C1q and collagen domain-containing protein
    30 kDa adipocyte complement-related protein
    Adipocyte complement-related 30 kDa protein
    ACRP30
    Adipose most abundant gene transcript 1 protein
      Short name=apM-1

Gene names

Name:	ADIPOQ
Synonyms:	ACRP30, APM1

Organism

Bos taurus (Bovine)

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length	240 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	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.
Subunit structure	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 aditionnally 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 By similarity.
Subcellular location	Secreted By similarity.
Post-translational modification	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. O-linked glycans consist of Glc-Gal disaccharides bound to the oxygen atom of post-translationally added hydroxyl groups By similarity.
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.
Sequence similarities	Contains 1 C1q domain. Contains 1 collagen-like domain.

Ontologies

Keywords
Cellular component	Secreted
Domain	Collagen Repeat Signal
Molecular function	Hormone
PTM	Disulfide bond Glycoprotein Hydroxylation
Technical term	Direct protein sequencing
Gene Ontology (GO)
Molecular function	hormone activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 17	17	Ref.3
	Chain	18 – 240	223	Adiponectin		PRO_0000236269
Regions
	Domain	43 – 102	60	Collagen-like
	Domain	103 – 240	138	C1q
Sites
	Site	57	1	Not hydroxylated
	Site	66	1	Not hydroxylated
	Site	71	1	Not hydroxylated
	Site	90	1	Not hydroxylated
	Site	99	1	Not hydroxylated
	Site	225	1	Not glycosylated
Amino acid modifications
	Modified residue	28	1	5-hydroxylysine
	Modified residue	39	1	4-hydroxyproline Ref.3
	Modified residue	42	1	4-hydroxyproline Ref.3
	Modified residue	48	1	4-hydroxyproline Ref.3
	Modified residue	60	1	5-hydroxylysine
	Modified residue	63	1	5-hydroxylysine
	Modified residue	72	1	5-hydroxylysine
	Modified residue	86	1	4-hydroxyproline Ref.3
	Modified residue	96	1	5-hydroxylysine
	Glycosylation	28	1	O-linked (Gal...) Ref.3
	Glycosylation	60	1	O-linked (Gal...) Ref.3
	Glycosylation	63	1	O-linked (Gal...) Ref.3
	Glycosylation	72	1	O-linked (Gal...)
	Glycosylation	96	1	O-linked (Gal...) Ref.3
	Disulfide bond	31		Interchain; in form MMW and form HMW By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q3Y5Z3-1 [UniParc]. Last modified September 27, 2005. Version 1. Checksum: 409122E49F3AF253	FASTA	240	26,133
	10 20 30 40 50 60 MLLQGALLLL LALPSHGEDN MEDPPLPKGA CAGWMAGIPG HPGHNGTPGR DGRDGTPGEK 70 80 90 100 110 120 GEKGDPGLVG PKGDTGETGI TGIEGPRGFP GTPGRKGEPG ESAYVYRSAF SVGLERQVTV 130 140 150 160 170 180 PNVPIRFTKI FYNQQNHYDG TTGKFLCNIP GLYYFSYHIT VYLKDVKVSL YKNDKALLFT 190 200 210 220 230 240 HDQFQDKNVD QASGSVLLYL EKGDQVWLQV YEGENHNGVY ADNVNDSTFT GFLLYHNIVE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	Morsci N.S., Schnabel R.D., Taylor J.F. Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	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.
[3]	"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: 15378692] [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, MASS SPECTROMETRY.

Cross-references

Sequence databases
EMBLGenBankDDBJ	DQ156120 Genomic DNA. Translation: AAZ81421.1. BC140488 mRNA. Translation: AAI40489.1.
IPI	IPI00688783.
UniGene	Bt.59365
3D structure databases
SMR	Q3Y5Z3. Positions 103-237.
ModBase	Search...
Protein-protein interaction databases
STRING	Q3Y5Z3.
Genome annotation databases
Ensembl	ENSBTAT00000026395; ENSBTAP00000026395; ENSBTAG00000019813; Bos taurus. [Genome view]
Phylogenomic databases
HOVERGEN	Q3Y5Z3.
OMA	YHITVYM
OrthoDB	EOG91G5PK
Family and domain databases
InterPro	IPR001073. C1q. IPR008160. Collagen. IPR008983. Tumour_necrosis_fac-like. [Graphical view]
Gene3D	G3DSA:2.60.120.40. Tumour_necrosis_fac-like. 1 hit.
Pfam	PF00386. C1q. 1 hit. PF01391. Collagen. 1 hit. [Graphical view]
PRINTS	PR00007. COMPLEMNTC1Q.
SMART	SM00110. C1Q. 1 hit. [Graphical view]
PROSITE	PS50871. C1Q. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ADIPO_BOVIN

Accession

Primary (citable) accession number: Q3Y5Z3
Secondary accession number(s): A5D7A8

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2006
Last sequence update:	September 27, 2005
Last modified:	November 24, 2009
This is version 29 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)