Адипонектин

ADIPOQ
Наявні структури PDB Пошук ортологів: PDBe RCSB Список кодів PDB 4DOU
Ідентифікатори
Символи	ADIPOQ, ACDC, ACRP30, ADIPQTL1, ADPN, APM-1, APM1, GBP28, adiponectin, C1Q and collagen domain containing, Adiponectin
Зовнішні ІД	OMIM: 605441 MGI: 106675 HomoloGene: 3525 GeneCards: ADIPOQ
Онтологія гена Молекулярна функція • hormone activity • signaling receptor binding • cytokine activity • sialic acid binding • protein homodimerization activity • GO:0001948, GO:0016582 protein binding • identical protein binding • extracellular matrix structural constituent Клітинна компонента • cell surface • ендоплазматичний ретикулум • колаген • міжклітинний простір • extracellular region • GO:0009327 protein-containing complex • collagen-containing extracellular matrix Біологічний процес • positive regulation of glucose import • positive regulation of protein phosphorylation • negative regulation of receptor binding • low-density lipoprotein particle clearance • negative regulation of blood pressure • negative regulation of macrophage differentiation • negative regulation of synaptic transmission • generation of precursor metabolites and energy • cellular response to epinephrine stimulus • negative regulation of gluconeogenesis • regulation of glucose metabolic process • циркадний ритм • fatty acid oxidation • positive regulation of interleukin-8 production • glucose metabolic process • protein heterotrimerization • negative regulation of heterotypic cell-cell adhesion • response to ethanol • negative regulation of inflammatory response • cellular response to cAMP • positive regulation of protein kinase A signaling • negative regulation of platelet-derived growth factor receptor signaling pathway • positive regulation of signal transduction • GO:0051247, GO:0051200 positive regulation of protein metabolic process • negative regulation of fat cell differentiation • response to linoleic acid • detection of oxidative stress • glucose homeostasis • adiponectin-activated signaling pathway • response to tumor necrosis factor • positive regulation of blood pressure • response to nutrient levels • positive regulation of cholesterol efflux • negative regulation of MAP kinase activity • cellular response to insulin stimulus • positive regulation of peptidyl-tyrosine phosphorylation • fatty acid beta-oxidation • negative regulation of tumor necrosis factor production • protein localization to plasma membrane • negative regulation of hormone secretion • protein homooligomerization • response to sucrose • positive regulation of metanephric glomerular visceral epithelial cell development • positive regulation of renal albumin absorption • negative regulation of granulocyte differentiation • response to nutrient • negative regulation of protein autophosphorylation • negative regulation of intracellular protein transport • membrane depolarization • response to glucose • positive regulation of myeloid cell apoptotic process • negative regulation of I-kappaB kinase/NF-kappaB signaling • negative regulation of metanephric mesenchymal cell migration • negative regulation of cell migration • positive regulation of fatty acid metabolic process • brown fat cell differentiation • positive regulation of cAMP-dependent protein kinase activity • positive regulation of glycogen (starch) synthase activity • GO:0045996 negative regulation of transcription, DNA-templated • negative regulation of DNA biosynthetic process • positive regulation of protein kinase activity • response to hypoxia • negative regulation of phagocytosis • membrane hyperpolarization • negative regulation of tumor necrosis factor-mediated signaling pathway • positive regulation of monocyte chemotactic protein-1 production • response to glucocorticoid • response to activity • negative regulation of platelet-derived growth factor receptor-alpha signaling pathway • positive regulation of I-kappaB kinase/NF-kappaB signaling • negative regulation of ERK1 and ERK2 cascade • negative regulation of macrophage derived foam cell differentiation • regulation of fatty acid biosynthetic process • regulation of signaling receptor activity • negative regulation of vascular associated smooth muscle cell proliferation • negative regulation of vascular associated smooth muscle cell migration • response to bacterium • positive regulation of cold-induced thermogenesis • negative regulation of cold-induced thermogenesis • GO:0072468 сигнальна трансдукція Джерела:Amigo / QuickGO
Шаблон експресії
Більше даних
Ортологи
Види	Людина	Миша
Entrez	9370	11450
Ensembl	ENSG00000181092	ENSMUSG00000022878
UniProt	Q15848	Q60994
RefSeq (мРНК)	NM_001177800 NM_004797	NM_009605
RefSeq (білок)	NP_001171271 NP_004788	NP_033735
Локус (UCSC)	Хр. 3: 186.84 – 186.86 Mb	Хр. 16: 22.97 – 22.98 Mb
PubMed search
Вікідані
Див./Ред. для людей Див./Ред. для мишей

ADIPOQ (англ. Adiponectin, C1Q and collagen domain containing) – білок, який кодується однойменним геном, розташованим у людей на короткому плечі 3-ї хромосоми. Довжина поліпептидного ланцюга білка становить 244 амінокислот, а молекулярна маса — 26 414.

Послідовність амінокислот

10		20		30		40		50
MLLLGAVLLL		LALPGHDQET		TTQGPGVLLP		LPKGACTGWM		AGIPGHPGHN
GAPGRDGRDG		TPGEKGEKGD		PGLIGPKGDI		GETGVPGAEG		PRGFPGIQGR
KGEPGEGAYV		YRSAFSVGLE		TYVTIPNMPI		RFTKIFYNQQ		NHYDGSTGKF
HCNIPGLYYF		AYHITVYMKD		VKVSLFKKDK		AMLFTYDQYQ		ENNVDQASGS
VLLHLEVGDQ		VWLQVYGEGE		RNGLYADNDN		DSTFTGFLLY		HDTN

A: Аланін
C: Цистеїн
D: Аспарагінова кислота
E: Глутамінова кислота
F: Фенілаланін
G: Гліцин
H: Гістидин
I: Ізолейцин
K: Лізин
L: Лейцин
M: Метіонін
N: Аспарагін
P: Пролін
Q: Глутамін
R: Аргінін
S: Серин
T: Треонін
V: Валін
W: Триптофан

Y: Тирозин

Кодований геном білок за функцією належить до гормонів. Задіяний у такому біологічному процесі як поліморфізм. Секретований назовні.

Література

• The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 14: 2121—2127. 2004. PMID 15489334 DOI:10.1101/gr.2596504
• Zhang Z., Henzel W.J. (2004). Signal peptide prediction based on analysis of experimentally verified cleavage sites. Protein Sci. 13: 2819—2824. PMID 15340161 DOI:10.1110/ps.04682504
• Nakano Y., Tobe T., Choi-Miura N.H., Mazda T., Tomita M. (1996). Isolation and characterization of GBP28, a novel gelatin-binding protein purified from human plasma. J. Biochem. 120: 803—812. PMID 8947845 DOI:10.1093/oxfordjournals.jbchem.a021483

Див. також

• Хромосома 3