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 protein binding; • identical protein binding; • extracellular matrix structural constituent;
Клітинна компонента	• cell surface; • Ендоплазматичний ретикулум; • Колаген; • extracellular space; • extracellular region; • 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; • positive regulation of cellular 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; • 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; • Сигнальна трансдукція;
	Джерела:Amigo / QuickGO
Шаблон експресії
	Більше даних
Ортологи
	9370
	11450
	ENSG00000181092
	ENSMUSG00000022878
	Q15848
	Q60994
	NM_001177800; NM_004797
	NM_009605
	NP_001171271; NP_004788
	NP_033735
	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. [3] Довжина поліпептидного ланцюга білка становить 244 амінокислот, а молекулярна маса — 26 414[4].

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. PubMed 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. PubMed 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. PubMed DOI:10.1093/oxfordjournals.jbchem.a021483

Примітки

Human PubMed Reference:.
Mouse PubMed Reference:.
HUGO Gene Nomenclature Commitee, HGNC:13633 (англ.). Процитовано 30 серпня 2017.
UniProt, Q15848 (англ.). Процитовано 30 серпня 2017.

Див. також

Хромосома 3

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[1] Human PubMed Reference:.

[2] Mouse PubMed Reference:.

[HGNC-3] HUGO Gene Nomenclature Commitee, HGNC:13633 (англ.). Процитовано 30 серпня 2017.

[UniProt-4] UniProt, Q15848 (англ.). Процитовано 30 серпня 2017.