カベオリン1

CAV1
識別子
記号	CAV1, BSCL3, CGL3, LCCNS, MSTP085, PPH3, VIP21, Caveolin 1
外部ID	OMIM: 601047 MGI: 102709 HomoloGene: 1330 GeneCards: CAV1
遺伝子の位置 (ヒト)
染色体	7番染色体 (ヒト)
終点	116,561,179 bp
遺伝子の位置 (マウス)
染色体	6番染色体 (マウス)
終点	17,341,451 bp
RNA発現パターン
	; ;
	さらなる参照発現データ
遺伝子オントロジー
分子機能	• protein-macromolecule adaptor activity; • transmembrane transporter binding; • 構造分子活性; • 受容体結合; • nitric-oxide synthase binding; • patched binding; • 酵素結合; • peptidase activator activity; • 血漿タンパク結合; • molecular adaptor activity; • プロテインキナーゼ結合; • ATPase binding; • cholesterol binding; • inward rectifier potassium channel inhibitor activity; • identical protein binding; • protein heterodimerization activity; • protein-containing complex binding;
細胞の構成要素	• endocytic vesicle membrane; • エンドソーム; • 膜; • 焦点接着; • VCP-NPL4-UFD1 AAA ATPase complex; • perinuclear region of cytoplasm; • カベオラ; • 繊毛; • apical plasma membrane; • 小胞体; • 脂質ラフト; • integral component of membrane; • ゴルジ体; • early endosome membrane; • 細胞膜; • 細胞内; • 細胞皮質; • endoplasmic reticulum membrane; • ゴルジ膜; • integral component of plasma membrane; • acrosomal membrane; • basolateral plasma membrane; • cytoplasmic vesicle; • 脂肪滴; • 細胞質; • 高分子複合体; • 筋鞘;
生物学的プロセス	• caveolin-mediated endocytosis; • positive regulation of calcium ion transport into cytosol; • 血管収縮; • response to progesterone; • negative regulation of protein binding; • regulation of peptidase activity; • protein localization to plasma membrane raft; • 乳房発達; • 脈管形成; • negative regulation of pinocytosis; • response to ischemia; • 血管新生; • 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; • negative regulation of MAP kinase activity; • positive regulation of vasoconstriction; • negative regulation of potassium ion transmembrane transport; • 授乳; • receptor-mediated endocytosis of virus by host cell; • regulation of blood coagulation; • regulation of ventricular cardiac muscle cell action potential; • protein homooligomerization; • 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; • 膜脱分極; • negative regulation of cytokine-mediated signaling pathway; • cellular calcium ion homeostasis; • 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; • タンパク質局在化; • positive regulation of cell adhesion molecule production; • 低酸素症への反応; • negative regulation of nitric-oxide synthase activity; • 細菌への反応; • 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; • 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; • 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; • 細胞分化; • positive regulation of cell migration; • positive regulation of cold-induced thermogenesis; • positive regulation of NF-kappaB transcription factor activity;
	出典:Amigo / QuickGO
オルソログ
	857
	12389
	ENSG00000105974
	ENSMUSG00000007655
	Q03135,C9JKI3
	P49817
	NM_001753; NM_001172895; NM_001172896; NM_001172897
	NM_001243064; NM_007616
	NP_001166366; NP_001166367; NP_001166368; NP_001744
	NP_001229993; NP_031642
	ウィキデータ
閲覧/編集ヒト	閲覧/編集マウス

カベオリン1（英: caveolin 1）は、ヒトではCAV1遺伝子によってコードされるタンパク質である^[5]。

機能編集

CAV1遺伝子にコードされるカベオリン1は足場タンパク質であり、大部分の細胞種における細胞膜のカベオラの主要な構成要素である。カベオリン1はインテグリンサブユニットとチロシンキナーゼ FYNを連結し、インテグリンとRas-ERK経路の共役と細胞周期の進行の促進の開始段階となる。CAV1遺伝子はがん抑制遺伝子の候補であり、Ras-p42/44MAPキナーゼカスケードの負の調節因子である。CAV1とCAV2（英語版）は7番染色体（英語版）上に隣接して位置ており、安定なヘテロオリゴマー複合体を形成して共局在するタンパク質を発現する。同じリーディングフレームを利用する代替的開始コドンの存在によって、この遺伝子に由来する1つの転写産物には2つのアイソフォーム（αとβ）がコードされている^[6]。

相互作用編集

カベオリン1は、ヘテロ三量体Gタンパク質^[7]、Srcチロシンキナーゼ（Src、Lyn（英語版））^[8]、H-Ras（英語版）^[8]、コレステロール^[9]、TGF-β受容体1（英語版）^[10]、eNOS^[11]、iNOS^[12]、アンドロゲン受容体^[13]、アミロイド前駆体タンパク質^[14]、GJA1^[15]、EGFR^[16]、エンドセリンB型受容体（英語版）^[17]、PDGFRA（英語版）^[18]、PDGFRB（英語版）^[18]、PTGS2^[19]、TRAF2（英語版）^[20]^[21]、エストロゲン受容体α^[22]、カベオリン2（英語版）^[23]^[24]、PLD2（英語版）^[25]^[26]、ブルトン型チロシンキナーゼ^[27]、SCP2（英語版）^[28]と相互作用することが示されている。これらの相互作用は全て、カベオリン足場ドメイン（caveolin-scaffolding domain、CSD）を介して行われる^[8]。カベオリン1と相互作用する分子にはカベオリン結合モチーフ（caveolin-binding motif、CBM）が存在する^[29]。

出典編集

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000105974 - Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000007655 - Ensembl, May 2017
^ Human PubMed Reference:
^ Mouse PubMed Reference:
^ “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. (March 1999). doi:10.1006/geno.1998.5723. PMID 10087206.
^ “Entrez Gene: CAV1 caveolin 1, caveolae protein, 22kDa”. 2021年10月16日閲覧。
^ “Evidence for a regulated interaction between heterotrimeric G proteins and caveolin”. The Journal of Biological Chemistry 270 (26): 15693–701. (June 1995). doi:10.1074/jbc.270.26.15693. PMID 7797570.
^ ^a ^b ^c “Src tyrosine kinases, Galpha subunits, and H-Ras share a common membrane-anchored scaffolding protein, caveolin. Caveolin binding negatively regulates the auto-activation of Src tyrosine kinases”. The Journal of Biological Chemistry 271 (46): 29182–90. (November 1996). doi:10.1074/jbc.271.46.29182. PMC 6687395. PMID 8910575.
^ “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. (January 1996). doi:10.1074/jbc.271.1.568. PMID 8550621.
^ “Caveolin-1 regulates transforming growth factor (TGF)-beta/SMAD signaling through an interaction with the TGF-beta type I receptor”. The Journal of Biological Chemistry 276 (9): 6727–38. (March 2001). doi:10.1074/jbc.M008340200. PMID 11102446.
^ “Endothelial nitric oxide synthase is regulated by tyrosine phosphorylation and interacts with caveolin-1”. The Journal of Biological Chemistry 271 (44): 27237–40. (November 1996). doi:10.1074/jbc.271.44.27237. PMID 8910295.
^ “Caveolin-1 down-regulates inducible nitric oxide synthase via the proteasome pathway in human colon carcinoma cells”. Proceedings of the National Academy of Sciences of the United States of America 97 (26): 14334–9. (December 2000). Bibcode: 2000PNAS...9714334F. doi:10.1073/pnas.250406797. PMC 18919. PMID 11114180.
^ “Caveolin-1 interacts with androgen receptor. A positive modulator of androgen receptor mediated transactivation”. The Journal of Biological Chemistry 276 (16): 13442–51. (April 2001). doi:10.1074/jbc.M006598200. PMID 11278309.
^ “Caveolae, plasma membrane microdomains for alpha-secretase-mediated processing of the amyloid precursor protein”. The Journal of Biological Chemistry 273 (17): 10485–95. (April 1998). doi:10.1074/jbc.273.17.10485. PMID 9553108.
^ “Connexin family members target to lipid raft domains and interact with caveolin-1”. Biochemistry 41 (18): 5754–64. (May 2002). doi:10.1021/bi0121656. PMID 11980479.
^ “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. (November 1997). doi:10.1074/jbc.272.48.30429. PMID 9374534.
^ “Regulated interaction of endothelin B receptor with caveolin-1”. European Journal of Biochemistry 270 (8): 1816–27. (April 2003). doi:10.1046/j.1432-1033.2003.03544.x. PMID 12694195.
^ ^a ^b “Caveolin is an inhibitor of platelet-derived growth factor receptor signaling”. Experimental Cell Research 247 (2): 380–8. (March 1999). doi:10.1006/excr.1998.4379. PMID 10066366.
^ “Colocalization and interaction of cyclooxygenase-2 with caveolin-1 in human fibroblasts”. The Journal of Biological Chemistry 276 (37): 34975–82. (September 2001). doi:10.1074/jbc.M105946200. PMID 11432874.
^ “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. (March 2001). doi:10.1074/jbc.M007116200. PMID 11112773.
^ “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. (March 2002). doi:10.1074/jbc.C100661200. PMID 11805080.
^ “Ligand-independent activation of oestrogen receptor alpha by caveolin-1”. The Biochemical Journal 359 (Pt 1): 203–10. (October 2001). doi:10.1042/0264-6021:3590203. PMC 1222136. PMID 11563984.
^ “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. (December 2002). doi:10.1242/jcs.00130. PMID 12414992.
^ “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. (November 1997). doi:10.1074/jbc.272.46.29337. PMID 9361015.
^ “Aquaporin 3 colocates with phospholipase d2 in caveolin-rich membrane microdomains and is downregulated upon keratinocyte differentiation”. The Journal of Investigative Dermatology 121 (6): 1487–95. (December 2003). doi:10.1111/j.1523-1747.2003.12614.x. PMID 14675200.
^ “Phospholipase D2: functional interaction with caveolin in low-density membrane microdomains”. FEBS Letters 467 (2–3): 326–32. (February 2000). doi:10.1016/S0014-5793(00)01174-1. PMID 10675563.
^ “Functional interaction of caveolin-1 with Bruton's tyrosine kinase and Bmx”. The Journal of Biological Chemistry 277 (11): 9351–7. (March 2002). doi:10.1074/jbc.M108537200. PMID 11751885.
^ “Sterol carrier protein-2 directly interacts with caveolin-1 in vitro and in vivo”. Biochemistry 43 (23): 7288–306. (June 2004). doi:10.1021/bi035914n. PMID 15182174.
^ “Identification of peptide and protein ligands for the caveolin-scaffolding domain. Implications for the interaction of caveolin with caveolae-associated proteins”. The Journal of Biological Chemistry 272 (10): 6525–33. (March 1997). doi:10.1074/jbc.272.10.6525. PMID 9045678.

カベオリン1

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カベオリン1

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