کاویئولین ۱

CAV1
معین‌کننده‌ها
نام‌های دیگر	CAV1, BSCL3, CGL3, LCCNS, MSTP085, PPH3, VIP21, Caveolin 1
شناسه‌های بیرونی	OMIM: 601047 MGI: 102709 HomoloGene: 1330 GeneCards: CAV1
موقعیت ژن (موش) کروموزوم کروموزوم ۶ (موش)[۱] نوار 6|6 A2 شروع 17,306,334 bp[۱] پایان 17,341,451 bp[۱]
الگوی گسترش RNA More reference expression data
هستی‌شناسی ژن عملکرد ملکولی • protein-macromolecule adaptor activity • transmembrane transporter binding • structural molecule activity • signaling receptor binding • nitric-oxide synthase binding • patched binding • enzyme binding • peptidase activator activity • GO:0001948، GO:0016582 پیوند پروتئینی • GO:0032947 molecular adaptor activity • protein kinase binding • ATPase binding • cholesterol binding • inward rectifier potassium channel inhibitor activity • identical protein binding • protein heterodimerization activity • GO:0032403 protein-containing complex binding ترکیبات سلولی • endocytic vesicle membrane • اندوزوم • membrane • focal adhesion • VCP-NPL4-UFD1 AAA ATPase complex • perinuclear region of cytoplasm • حفره غشایی • مژک • apical plasma membrane • شبکه آندوپلاسمی • لیپید رفت • integral component of membrane • دستگاه گلژی • early endosome membrane • پوسته یاخته • intracellular anatomical structure • cell cortex • endoplasmic reticulum membrane • Golgi membrane • integral component of plasma membrane • acrosomal membrane • basolateral plasma membrane • GO:0016023 cytoplasmic vesicle • lipid droplet • سیتوپلاسم • GO:0009327 protein-containing complex • سارکولما فرایند زیستی • caveolin-mediated endocytosis • positive regulation of calcium ion transport into cytosol • انقباض عروق • response to progesterone • negative regulation of protein binding • regulation of peptidase activity • protein localization to plasma membrane raft • mammary gland development • vasculogenesis • negative regulation of pinocytosis • پاسخ به ایسکمی • رگ‌زایی • apoptotic signaling pathway • positive regulation of extrinsic apoptotic signaling pathway • cholesterol homeostasis • triglyceride metabolic process • negative regulation of canonical Wnt signaling pathway • calcium ion transport • negative regulation of cell population proliferation • cellular response to transforming growth factor beta stimulus • positive regulation of toll-like receptor 3 signaling pathway • regulation of cytosolic calcium ion concentration • regulation of smooth muscle contraction • vesicle organization • negative regulation of peptidyl-tyrosine autophosphorylation • regulation of cardiac muscle cell action potential involved in regulation of contraction • negative regulation of transforming growth factor beta receptor signaling pathway • protein localization to basolateral plasma membrane • receptor internalization involved in canonical Wnt signaling pathway • regulation of membrane repolarization during action potential • positive regulation of peptidyl-serine phosphorylation • negative regulation of protein tyrosine kinase activity • regulation of entry of bacterium into host cell • مپ کیناز • positive regulation of vasoconstriction • negative regulation of potassium ion transmembrane transport • lactation • receptor-mediated endocytosis of virus by host cell • regulation of blood coagulation • regulation of ventricular cardiac muscle cell action potential • protein homooligomerization • GO:0022415 viral process • positive regulation of intrinsic apoptotic signaling pathway • negative regulation of receptor signaling pathway via JAK-STAT • mammary gland involution • calcium ion homeostasis • negative regulation of necroptotic process • regulation of the force of heart contraction • lipid storage • nitric oxide homeostasis • membrane depolarization • negative regulation of cytokine-mediated signaling pathway • cellular calcium ion homeostasis • GO:1901227 negative regulation of transcription by RNA polymerase II • response to estrogen • response to calcium ion • regulation of fatty acid metabolic process • cellular response to exogenous dsRNA • negative regulation of MAPK cascade • regulation of ruffle assembly • positive regulation of protein binding • positive regulation of protein ubiquitination • negative regulation of anoikis • leukocyte migration • GO:0034613 protein localization • positive regulation of cell adhesion molecule production • response to hypoxia • negative regulation of nitric-oxide synthase activity • response to bacterium • caveola assembly • cellular response to hyperoxia • cholesterol transport • cellular response to starvation • T cell costimulation • regulation of nitric-oxide synthase activity • receptor internalization • positive regulation of peptidase activity • positive regulation of ER-associated ubiquitin-dependent protein catabolic process • negative regulation of endothelial cell proliferation • negative regulation of BMP signaling pathway • negative regulation of protein ubiquitination • cellular response to peptide hormone stimulus • GO:1901313 positive regulation of gene expression • negative regulation of nitric oxide biosynthetic process • angiotensin-activated signaling pathway involved in heart process • protein complex oligomerization • negative regulation of peptidyl-serine phosphorylation • posttranscriptional regulation of gene expression • positive regulation of gap junction assembly • maintenance of protein location in cell • negative regulation of signal transduction • regulation of the force of heart contraction by chemical signal • regulation of cell communication by electrical coupling involved in cardiac conduction • regulation of heart rate by cardiac conduction • negative regulation of epithelial cell differentiation • skeletal muscle tissue development • beta-catenin destruction complex disassembly • GO:0048554 positive regulation of catalytic activity • positive regulation of canonical Wnt signaling pathway • negative regulation of tyrosine phosphorylation of STAT protein • negative regulation of inward rectifier potassium channel activity • دگرگونی یاخته‌ • positive regulation of cell migration • positive regulation of cold-induced thermogenesis • positive regulation of NF-kappaB transcription factor activity منابع: آمیگو / کوئیک‌گو
هم‌ساخت‌شناسی
گونه‌ها	انسان	موش
Entrez	857	12389
آنسامبل	ENSG00000105974	ENSMUSG00000007655
یونی‌پروت	Q03135	P49817
RefSeq (mRNA)	NM_001172895، NM_001172896، NM_001172897 NM_001753، NM_001172895، NM_001172896، NM_001172897	NM_007616، XM_006504974، XM_006504975، XM_006504976 NM_001243064، NM_007616، XM_006504974، XM_006504975، XM_006504976
RefSeq (پروتئین)	NP_001166367، NP_001166368، NP_001744 NP_001166366، NP_001166367، NP_001166368، NP_001744	NP_031642، XP_006505037، XP_006505038، XP_006505039 NP_001229993، NP_031642، XP_006505037، XP_006505038، XP_006505039
موقعیت (UCSC)	ن/م	Chr : 17.31 – 17.34 Mb
جستجوی PubMed	[۲]	[۳]
ویکی‌داده
مشاهده/ویرایش انسان مشاهده/ویرایش موش

کاویئولین ۱ (به انگلیسی: Caveolin 1) یک پروتئین است که در انسان توسط ژن «CAV1» واقع بر بازوی بلند کروموزوم ۷ کُدگذاری می‌شود.^[۴]

این پروتئین داربستی مهمترین بخش سازندهٔ حفره غشایی است و احتمالاً نقش سرکوب‌گر تومور را نیز می‌تواند ایفا کند.

کاویئولین ۱ با مولکول‌های تیروزین-پروتئین کیناز CSK، کلسترول،^[۵] گیرنده آندروژن،^[۶] گیرنده فاکتور رشد اپیدرمی،^[۷] گیرنده اندوتلین بی،^[۸] TRAF2،^[۹][۱۰] کاویئولین ۲^[۱۱][۱۲] و SCP2^[۱۳] تعامل پروتئین-پروتئین دارد.

منابع

1. GRCm38: Ensembl release 89: ENSMUSG00000007655 - Ensembl, May 2017
2. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
3. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. Fra AM, Mastroianni N, Mancini M, Pasqualetto E, Sitia R (March 1999). "Human caveolin-1 and caveolin-2 are closely linked genes colocalized with WI-5336 in a region of 7q31 frequently deleted in tumors". Genomics. 56 (3): 355–6. doi:10.1006/geno.1998.5723. PMID 10087206.
5. Li S, Song KS, Lisanti MP (January 1996). "Expression and characterization of recombinant caveolin. Purification by polyhistidine tagging and cholesterol-dependent incorporation into defined lipid membranes". The Journal of Biological Chemistry. 271 (1): 568–73. doi:10.1074/jbc.271.1.568. PMID 8550621.
6. Lu ML, Schneider MC, Zheng Y, Zhang X, Richie JP (April 2001). "Caveolin-1 interacts with androgen receptor. A positive modulator of androgen receptor mediated transactivation". The Journal of Biological Chemistry. 276 (16): 13442–51. doi:10.1074/jbc.M006598200. PMID 11278309.
7. Couet J, Sargiacomo M, Lisanti MP (November 1997). "Interaction of a receptor tyrosine kinase, EGF-R, with caveolins. Caveolin binding negatively regulates tyrosine and serine/threonine kinase activities". The Journal of Biological Chemistry. 272 (48): 30429–38. doi:10.1074/jbc.272.48.30429. PMID 9374534.
8. Yamaguchi T, Murata Y, Fujiyoshi Y, Doi T (April 2003). "Regulated interaction of endothelin B receptor with caveolin-1". European Journal of Biochemistry. 270 (8): 1816–27. doi:10.1046/j.1432-1033.2003.03544.x. PMID 12694195.
9. Feng X, Gaeta ML, Madge LA, Yang JH, Bradley JR, Pober JS (March 2001). "Caveolin-1 associates with TRAF2 to form a complex that is recruited to tumor necrosis factor receptors". The Journal of Biological Chemistry. 276 (11): 8341–9. doi:10.1074/jbc.M007116200. PMID 11112773.
10. Cao H, Courchesne WE, Mastick CC (March 2002). "A phosphotyrosine-dependent protein interaction screen reveals a role for phosphorylation of caveolin-1 on tyrosine 14: recruitment of C-terminal Src kinase". The Journal of Biological Chemistry. 277 (11): 8771–4. doi:10.1074/jbc.C100661200. PMID 11805080.
11. Breuza L, Corby S, Arsanto JP, Delgrossi MH, Scheiffele P, Le Bivic A (December 2002). "The scaffolding domain of caveolin 2 is responsible for its Golgi localization in Caco-2 cells". Journal of Cell Science. 115 (Pt 23): 4457–67. doi:10.1242/jcs.00130. PMID 12414992.
12. Scherer PE, Lewis RY, Volonte D, Engelman JA, Galbiati F, Couet J, Kohtz DS, van Donselaar E, Peters P, Lisanti MP (November 1997). "Cell-type and tissue-specific expression of caveolin-2. Caveolins 1 and 2 co-localize and form a stable hetero-oligomeric complex in vivo". The Journal of Biological Chemistry. 272 (46): 29337–46. doi:10.1074/jbc.272.46.29337. PMID 9361015.
13. Zhou M, Parr RD, Petrescu AD, Payne HR, Atshaves BP, Kier AB, Ball JM, Schroeder F (June 2004). "Sterol carrier protein-2 directly interacts with caveolin-1 in vitro and in vivo". Biochemistry. 43 (23): 7288–306. doi:10.1021/bi035914n. PMID 15182174.

• مشارکت‌کنندگان ویکی‌پدیا. «Caveolin 1». در دانشنامهٔ ویکی‌پدیای انگلیسی.

برای مطالعهٔ بیشتر

• Engelman JA, Zhang X, Galbiati F, Volonte D, Sotgia F, Pestell RG, Minetti C, Scherer PE, Okamoto T, Lisanti MP (December 1998). "Molecular genetics of the caveolin gene family: implications for human cancers, diabetes, Alzheimer disease, and muscular dystrophy". American Journal of Human Genetics. 63 (6): 1578–87. doi:10.1086/302172. PMC 1377628. PMID 9837809.
• Razani B, Schlegel A, Liu J, Lisanti MP (August 2001). "Caveolin-1, a putative tumour suppressor gene". Biochemical Society Transactions. 29 (Pt 4): 494–9. doi:10.1042/BST0290494. PMID 11498016.
• Fujimoto T, Kogo H, Nakamura N, Ozeki S (March 2002). "[Microdomains and caveolin]". Tanpakushitsu Kakusan Koso. Protein, Nucleic Acid, Enzyme. 47 (4 Suppl): 326–32. PMID 11915322.
• Shatz M, Liscovitch M (September 2004). "Caveolin-1 and cancer multidrug resistance: coordinate regulation of pro-survival proteins?". Leukemia Research. 28 (9): 907–8. doi:10.1016/j.leukres.2004.03.013. PMID 15234566.
• Frank PG, Lisanti MP (January 2007). "Caveolin-1 and liver regeneration: role in proliferation and lipogenesis". Cell Cycle. 6 (2): 115–6. doi:10.4161/cc.6.2.3722. PMID 17314510.