FAKとは？ わかりやすく解説

新語時事用語辞典
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新語時事用語辞典新語時事用語辞典

FAK

英語：fill and kill

株式取引や外国為替証拠金取引（FX）の注文の際に、約定できる分だけ約定して、約定できなかった分は失効させるという条件。

FAKは、複数単位の注文に対して有効な条件で、成行注文や指値注文、逆指値注文などで用いられる。例えば、ドル/円を5万通貨の成行の買い注文を出して3万通貨のみ約定した場合、残りの2万通貨の注文は取り消される。

ちなみに、注文時における条件にはFAKの他に、FASやFOKなどが挙げられる。
（2015年11月11日更新）

生物学用語辞典
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JabionJabion

チロシンキナーゼ

英訳・(英)同義/類義語：tyrosine kinase, FAK (focal adhesion kinase); Receptor tyrosine kinases; Src family or protein tyrosine kinases

細胞内シグナル伝達に関与するタンパクキナーゼで、標的タンパク質のチロシン残基をリン酸化する酵素の総称。srcタンパクなど、発がん遺伝子の産物として同定されたものも多い。
「生物学用語辞典」の他の用語
酵素タンパク質モチーフなど：  チミジンキナーゼ  チロキシン結合グロブリン  チロキシン結合プレアルブミン  チロシンキナーゼ  チロシンキナーゼ受容体  テストステロン受容体  テトラペプチド

ウィキペディア
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ウィキペディアウィキペディア

FAK

出典: フリー百科事典『ウィキペディア（Wikipedia）』 (2023/01/01 08:07 UTC 版)

FAK（focal adhesion kinase、フォーカルアドヒージョンキナーゼ、焦点接着キナーゼ、接着斑キナーゼ）またはPTK2（protein tyrosine kinase 2）は、ヒトではPTK2遺伝子にコードされるタンパク質である[4]。FAKはフォーカルアドヒージョン（英語版）関連プロテインキナーゼであり、細胞接着（細胞が互いにまたは周囲の環境とどのように結合するか）や拡散過程（細胞がどのように移動するか）に関与している[5]。FAKが遮断されると、がん細胞は移動性が低下し転移能が低下することが示されている[6]。


出典
  1. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000022607 - Ensembl, May 2017
  2. ^ Human PubMed Reference:
  3. ^ Mouse PubMed Reference:
  4. ^ “Expression of an N-terminally truncated form of human focal adhesion kinase in brain”. Biochemical and Biophysical Research Communications 190 (1): 140–7. (January 1993). doi:10.1006/bbrc.1993.1022. PMID 8422239. 
  5. ^ Blackshaw, S. E.; Dow, J. Kamal; Lackie, J. M. (1999). The dictionary of cell and molecular biology (3rd ed.). San Diego: Academic Press. ISBN 978-0-12-432565-4 
  6. ^ “FAK alters invadopodia and focal adhesion composition and dynamics to regulate breast cancer invasion”. The Journal of Cell Biology 185 (2): 357–70. (2009). doi:10.1083/jcb.200809110. PMC 2700377. PMID 19364917. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2700377/. 
  7. ^ “SCOPe 2.07: Protein: Focal adhesion kinase 1” (英語). scop.berkeley.edu. 2021年9月5日閲覧。
  8. ^ “PTK2 - Focal adhesion kinase 1 - Gallus gallus (Chicken) - PTK2 gene & protein” (英語). www.uniprot.org. 2021年9月5日閲覧。
  9. ^ “Entrez Gene: PTK2 PTK2 protein tyrosine kinase 2”. 2008年10月28日閲覧。
  10. ^ “Regulation of focal adhesion-associated protein tyrosine kinase by both cellular adhesion and oncogenic transformation”. Nature 358 (6388): 690–2. (August 1992). Bibcode: 1992Natur.358..690G. doi:10.1038/358690a0. PMID 1379699. 
  11. ^ “Rho-stimulated contractility drives the formation of stress fibers and focal adhesions”. The Journal of Cell Biology 133 (6): 1403–15. (June 1996). doi:10.1083/jcb.133.6.1403. PMC 2120895. PMID 8682874. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2120895/. 
  12. ^ “Vascular endothelial growth factor stimulates tyrosine phosphorylation and recruitment to new focal adhesions of focal adhesion kinase and paxillin in endothelial cells”. The Journal of Biological Chemistry 272 (24): 15442–51. (June 1997). doi:10.1074/jbc.272.24.15442. PMID 9182576. 
  13. ^ “Focal adhesion kinase (p125FAK): a point of convergence in the action of neuropeptides, integrins, and oncogenes”. Cell 71 (6): 891–4. (December 1992). doi:10.1016/0092-8674(92)90385-P. PMID 1458538. 
  14. ^ “Focal adhesions: transmembrane junctions between the extracellular matrix and the cytoskeleton”. Annual Review of Cell Biology 4: 487–525. (1988). doi:10.1146/annurev.cb.04.110188.002415. PMID 3058164. https://cdr.lib.unc.edu/concern/articles/4j03d211n. 
  15. ^ “Tyrosine phosphorylation of paxillin and pp125FAK accompanies cell adhesion to extracellular matrix: a role in cytoskeletal assembly”. The Journal of Cell Biology 119 (4): 893–903. (November 1992). doi:10.1083/jcb.119.4.893. PMC 2289706. PMID 1385444. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2289706/. 
  16. ^ “Selective expression of an endogenous inhibitor of FAK regulates proliferation and migration of vascular smooth muscle cells”. Molecular and Cellular Biology 21 (5): 1565–72. (March 2001). doi:10.1128/MCB.21.5.1565-1572.2001. PMC 86702. PMID 11238893. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC86702/. 
  17. ^ Schlaepfer, D. D.; Hauck, C. R.; Sieg, D. J. (1999). “Signaling through focal adhesion kinase”. Progress in Biophysics and Molecular Biology 71 (3-4): 435–478. doi:10.1016/s0079-6107(98)00052-2. ISSN 0079-6107. PMID 10354709. https://pubmed.ncbi.nlm.nih.gov/10354709. 
  18. ^ a b “Metastasis: a question of life or death”. Nature Reviews. Cancer 6 (6): 449–58. (June 2006). doi:10.1038/nrc1886. PMID 16723991. 
  19. ^ “Cytoskeleton and apoptosis”. Biochemical Pharmacology 76 (1): 11–8. (July 2008). doi:10.1016/j.bcp.2008.03.016. PMID 18462707. 
  20. ^ “Structural basis for the autoinhibition of focal adhesion kinase”. Cell 129 (6): 1177–87. (June 2007). doi:10.1016/j.cell.2007.05.041. PMC 2077847. PMID 17574028. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2077847/. 
  21. ^ “Identification of sequences required for the efficient localization of the focal adhesion kinase, pp125FAK, to cellular focal adhesions”. The Journal of Cell Biology 123 (4): 993–1005. (November 1993). doi:10.1083/jcb.123.4.993. PMC 2200138. PMID 8227154. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2200138/. 
  22. ^ “Paxillin, a tyrosine phosphorylated focal adhesion-associated protein binds to the carboxyl terminal domain of focal adhesion kinase”. Molecular Biology of the Cell 6 (6): 637–47. (June 1995). doi:10.1091/mbc.6.6.637. PMC 301225. PMID 7579684. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC301225/. 
  23. ^ “Focal adhesion kinase and paxillin bind to peptides mimicking beta integrin cytoplasmic domains”. The Journal of Cell Biology 130 (5): 1181–7. (September 1995). doi:10.1083/jcb.130.5.1181. PMC 2120552. PMID 7657702. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2120552/. 
  24. ^ “The role of conserved amino acid motifs within the integrin beta3 cytoplasmic domain in triggering focal adhesion kinase phosphorylation”. The Journal of Biological Chemistry 272 (12): 7892–8. (March 1997). doi:10.1074/jbc.272.12.7892. PMID 9065456. 
  25. ^ “Janus kinases and focal adhesion kinases play in the 4.1 band: a superfamily of band 4.1 domains important for cell structure and signal transduction”. Molecular Medicine 4 (12): 751–69. (December 1998). doi:10.1007/BF03401769. PMC 2230389. PMID 9990861. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2230389/. 
  26. ^ “Tyrosine phosphorylation of focal adhesion kinase at sites in the catalytic domain regulates kinase activity: a role for Src family kinases”. Molecular and Cellular Biology 15 (2): 954–63. (February 1995). doi:10.1128/MCB.15.2.954. PMC 231984. PMID 7529876. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC231984/. 
  27. ^ a b c “FAK in cancer: mechanistic findings and clinical applications”. Nature Reviews. Cancer 14 (9): 598–610. (September 2014). doi:10.1038/nrc3792. PMC 4365862. PMID 25098269. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4365862/. 
  28. ^ a b c “Evolving therapies and FAK inhibitors for the treatment of cancer”. Anti-Cancer Agents in Medicinal Chemistry 10 (10): 722–34. (December 2010). doi:10.2174/187152010794728657. PMC 3274818. PMID 21291406. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3274818/. 
  29. ^ “Researchers Stop Once-Promising Mesothelioma Clinical Trial” (英語). Mesothelioma Center - Vital Services for Cancer Patients & Families. 2021年9月10日閲覧。
  30. ^ “p130CAS forms a signaling complex with the adapter protein CRKL in hematopoietic cells transformed by the BCR/ABL oncogene”. The Journal of Biological Chemistry 271 (41): 25198–203. (October 1996). doi:10.1074/jbc.271.41.25198. PMID 8810278. 
  31. ^ a b c “Differential regulation of cell motility and invasion by FAK”. The Journal of Cell Biology 160 (5): 753–67. (March 2003). doi:10.1083/jcb.200212114. PMC 2173366. PMID 12615911. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2173366/. 
  32. ^ a b “An SH3 domain-containing GTPase-activating protein for Rho and Cdc42 associates with focal adhesion kinase”. Molecular and Cellular Biology 16 (6): 3169–78. (June 1996). doi:10.1128/MCB.16.6.3169. PMC 231310. PMID 8649427. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC231310/. 
  33. ^ “Phosphatidylinositol 3,4,5-trisphosphate directs association of Src homology 2-containing signaling proteins with gelsolin”. The Journal of Biological Chemistry 276 (50): 47434–44. (December 2001). doi:10.1074/jbc.M107494200. PMID 11577104. 
  34. ^ “Activation of Wiskott-Aldrich syndrome protein and its association with other proteins by stromal cell-derived factor-1alpha is associated with cell migration in a T-lymphocyte line”. Experimental Hematology 30 (7): 761–6. (July 2002). doi:10.1016/s0301-472x(02)00823-8. PMID 12135674. 
  35. ^ a b “Stromal cell-derived factor-1alpha stimulates tyrosine phosphorylation of multiple focal adhesion proteins and induces migration of hematopoietic progenitor cells: roles of phosphoinositide-3 kinase and protein kinase C”. Blood 95 (8): 2505–13. (April 2000). doi:10.1182/blood.V95.8.2505. PMID 10753828. 
  36. ^ “Regulation of the PH-domain-containing tyrosine kinase Etk by focal adhesion kinase through the FERM domain”. Nature Cell Biology 3 (5): 439–44. (May 2001). doi:10.1038/35074500. PMID 11331870. 
  37. ^ a b “Src-mediated coupling of focal adhesion kinase to integrin alpha(v)beta5 in vascular endothelial growth factor signaling”. The Journal of Cell Biology 157 (1): 149–60. (April 2002). doi:10.1083/jcb.200109079. PMC 2173263. PMID 11927607. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2173263/. 
  38. ^ a b “Thrombspondin acts via integrin-associated protein to activate the platelet integrin alphaIIbbeta3”. The Journal of Biological Chemistry 272 (23): 14740–6. (June 1997). doi:10.1074/jbc.272.23.14740. PMID 9169439. 
  39. ^ a b c “Protein tyrosine phosphatase-PEST regulates focal adhesion disassembly, migration, and cytokinesis in fibroblasts”. The Journal of Cell Biology 144 (5): 1019–31. (March 1999). doi:10.1083/jcb.144.5.1019. PMC 2148201. PMID 10085298. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2148201/. 
  40. ^ a b “Focal adhesion kinase in netrin-1 signaling”. Nature Neuroscience 7 (11): 1204–12. (November 2004). doi:10.1038/nn1330. PMID 15494733. 
  41. ^ a b c “Specific interactions of neuronal focal adhesion kinase isoforms with Src kinases and amphiphysin”. Journal of Neurochemistry 84 (2): 253–65. (January 2003). doi:10.1046/j.1471-4159.2003.01519.x. PMID 12558988. 
  42. ^ “The role of the Src homology 3-Src homology 2 interface in the regulation of Src kinases”. The Journal of Biological Chemistry 276 (20): 17199–205. (May 2001). doi:10.1074/jbc.M011185200. PMID 11278857. 
  43. ^ “Interaction between liprin-alpha and GIT1 is required for AMPA receptor targeting”. The Journal of Neuroscience 23 (5): 1667–77. (March 2003). doi:10.1523/JNEUROSCI.23-05-01667.2003. PMC 6741975. PMID 12629171. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6741975/. 
  44. ^ “The GIT family of proteins forms multimers and associates with the presynaptic cytomatrix protein Piccolo”. The Journal of Biological Chemistry 278 (8): 6291–300. (February 2003). doi:10.1074/jbc.M212287200. PMID 12473661. 
  45. ^ “Coupling of PAK-interacting exchange factor PIX to GIT1 promotes focal complex disassembly”. Molecular and Cellular Biology 20 (17): 6354–63. (September 2000). doi:10.1128/MCB.20.17.6354-6363.2000. PMC 86110. PMID 10938112. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC86110/. 
  46. ^ “FAK integrates growth-factor and integrin signals to promote cell migration”. Nature Cell Biology 2 (5): 249–56. (May 2000). doi:10.1038/35010517. PMID 10806474. http://nbn-resolving.de/urn:nbn:de:bsz:352-opus-41292. 
  47. ^ “The structural basis of localization and signaling by the focal adhesion targeting domain”. Structure 10 (3): 319–27. (March 2002). doi:10.1016/s0969-2126(02)00717-7. PMID 12005431. 
  48. ^ “Association of focal adhesion kinase with Grb7 and its role in cell migration”. The Journal of Biological Chemistry 274 (34): 24425–30. (August 1999). doi:10.1074/jbc.274.34.24425. PMID 10446223. 
  49. ^ a b “Insulin receptor substrate-1 as a signaling molecule for focal adhesion kinase pp125(FAK) and pp60(src)”. The Journal of Biological Chemistry 273 (48): 32244–53. (November 1998). doi:10.1074/jbc.273.48.32244. PMID 9822703. 
  50. ^ “Growth hormone stimulates the tyrosine phosphorylation and association of p125 focal adhesion kinase (FAK) with JAK2. Fak is not required for stat-mediated transcription”. The Journal of Biological Chemistry 273 (17): 10682–9. (April 1998). doi:10.1074/jbc.273.17.10682. PMID 9553131. 
  51. ^ “Regulation of neutrophil adhesion by pituitary growth hormone accompanies tyrosine phosphorylation of Jak2, p125FAK, and paxillin”. Journal of Immunology 165 (4): 2116–23. (August 2000). doi:10.4049/jimmunol.165.4.2116. PMID 10925297. 
  52. ^ “A scaffold protein in the c-Jun N-terminal kinase signaling pathway is associated with focal adhesion kinase and tyrosine-phosphorylated”. Oncogene 21 (42): 6488–97. (September 2002). doi:10.1038/sj.onc.1205840. PMID 12226752. 
  53. ^ “Structure and function of Cas-L, a 105-kD Crk-associated substrate-related protein that is involved in beta 1 integrin-mediated signaling in lymphocytes”. The Journal of Experimental Medicine 184 (4): 1365–75. (October 1996). doi:10.1084/jem.184.4.1365. PMC 2192828. PMID 8879209. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2192828/. 
  54. ^ a b “Nck-2 interacts with focal adhesion kinase and modulates cell motility”. The International Journal of Biochemistry & Cell Biology 34 (7): 791–805. (July 2002). doi:10.1016/s1357-2725(02)00002-x. PMID 11950595. 
  55. ^ “Human enhancer of filamentation 1, a novel p130cas-like docking protein, associates with focal adhesion kinase and induces pseudohyphal growth in Saccharomyces cerevisiae”. Molecular and Cellular Biology 16 (7): 3327–37. (July 1996). doi:10.1128/mcb.16.7.3327. PMC 231327. PMID 8668148. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC231327/. 
  56. ^ “Nuclear FAK promotes cell proliferation and survival through FERM-enhanced p53 degradation”. Molecular Cell 29 (1): 9–22. (January 2008). doi:10.1016/j.molcel.2007.11.031. PMC 2234035. PMID 18206965. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2234035/. 
  57. ^ “Integrin-dependent translocation of phosphoinositide 3-kinase to the cytoskeleton of thrombin-activated platelets involves specific interactions of p85 alpha with actin filaments and focal adhesion kinase”. The Journal of Cell Biology 129 (3): 831–42. (May 1995). doi:10.1083/jcb.129.3.831. PMC 2120444. PMID 7537275. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2120444/. 
  58. ^ “PTEN interactions with focal adhesion kinase and suppression of the extracellular matrix-dependent phosphatidylinositol 3-kinase/Akt cell survival pathway”. The Journal of Biological Chemistry 274 (29): 20693–703. (July 1999). doi:10.1074/jbc.274.29.20693. PMID 10400703. 
  59. ^ “PTEN regulates tumor cell adhesion of colon carcinoma cells under dynamic conditions of fluid flow”. Oncogene 21 (9): 1450–60. (February 2002). doi:10.1038/sj.onc.1205213. PMID 11857088. 
  60. ^ a b “Differential regulation of Pyk2 and focal adhesion kinase (FAK). The C-terminal domain of FAK confers response to cell adhesion”. The Journal of Biological Chemistry 273 (4): 2384–9. (January 1998). doi:10.1074/jbc.273.4.2384. PMID 9442086. 
  61. ^ a b “Cell adhesion kinase beta forms a complex with a new member, Hic-5, of proteins localized at focal adhesions”. The Journal of Biological Chemistry 273 (2): 1003–14. (January 1998). doi:10.1074/jbc.273.2.1003. PMID 9422762. 
  62. ^ “Focal adhesion kinase and p130Cas mediate both sarcomeric organization and activation of genes associated with cardiac myocyte hypertrophy”. Molecular Biology of the Cell 12 (8): 2290–307. (August 2001). doi:10.1091/mbc.12.8.2290. PMC 58595. PMID 11514617. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC58595/. 
  63. ^ “Paxillin LD4 motif binds PAK and PIX through a novel 95-kD ankyrin repeat, ARF-GAP protein: A role in cytoskeletal remodeling”. The Journal of Cell Biology 145 (4): 851–63. (May 1999). doi:10.1083/jcb.145.4.851. PMC 2133183. PMID 10330411. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2133183/. 
  64. ^ “A fragment of paxillin binds the alpha 4 integrin cytoplasmic domain (tail) and selectively inhibits alpha 4-mediated cell migration”. The Journal of Biological Chemistry 277 (23): 20887–94. (June 2002). doi:10.1074/jbc.M110928200. PMID 11919182. 
  65. ^ “Monocyte cells and cancer cells express novel paxillin isoforms with different binding properties to focal adhesion proteins”. The Journal of Biological Chemistry 272 (11): 7437–44. (March 1997). doi:10.1074/jbc.272.11.7437. PMID 9054445. 
  66. ^ “Identification of LIM3 as the principal determinant of paxillin focal adhesion localization and characterization of a novel motif on paxillin directing vinculin and focal adhesion kinase binding”. The Journal of Cell Biology 135 (4): 1109–23. (November 1996). doi:10.1083/jcb.135.4.1109. PMC 2133378. PMID 8922390. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2133378/. 
  67. ^ “Interaction of Hic-5, A senescence-related protein, with focal adhesion kinase”. The Journal of Biological Chemistry 273 (41): 26516–21. (October 1998). doi:10.1074/jbc.273.41.26516. PMID 9756887. 
  68. ^ “Cytoskeleton-dependent tyrosine phosphorylation of the p130(Cas) family member HEF1 downstream of the G protein-coupled calcitonin receptor. Calcitonin induces the association of HEF1, paxillin, and focal adhesion kinase”. The Journal of Biological Chemistry 274 (35): 25093–8. (August 1999). doi:10.1074/jbc.274.35.25093. PMID 10455189. 
  69. ^ “Suppression of Pyk2 kinase and cellular activities by FIP200”. The Journal of Cell Biology 149 (2): 423–30. (April 2000). doi:10.1083/jcb.149.2.423. PMC 2175150. PMID 10769033. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2175150/. 
  70. ^ “Focal adhesion kinase activates Stat1 in integrin-mediated cell migration and adhesion”. The Journal of Biological Chemistry 276 (22): 19512–23. (June 2001). doi:10.1074/jbc.M009063200. PMID 11278462. 
  71. ^ “Focal adhesion kinase enhances signaling through the Shc/extracellular signal-regulated kinase pathway in anaplastic astrocytoma tumor biopsy samples”. Cancer Research 62 (9): 2699–707. (May 2002). PMID 11980671. 
  72. ^ “Site-specific phosphorylation of platelet focal adhesion kinase by low-density lipoprotein”. The Biochemical Journal 369 (Pt 2): 407–16. (January 2003). doi:10.1042/BJ20020410. PMC 1223094. PMID 12387730. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1223094/. 
  73. ^ “Relocation of Syk protein-tyrosine kinase to the actin filament network and subsequent association with Fak”. European Journal of Biochemistry 248 (3): 827–33. (September 1997). doi:10.1111/j.1432-1033.1997.00827.x. PMID 9342235. 
  74. ^ “Hic-5-reduced cell spreading on fibronectin: competitive effects between paxillin and Hic-5 through interaction with focal adhesion kinase”. Molecular and Cellular Biology 21 (16): 5332–45. (August 2001). doi:10.1128/MCB.21.16.5332-5345.2001. PMC 87257. PMID 11463817. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC87257/. 
  75. ^ “Characterization of a focal adhesion protein, Hic-5, that shares extensive homology with paxillin”. Journal of Cell Science 112 (2): 181–90. (January 1999). PMID 9858471. 
  76. ^ “Interaction of focal adhesion kinase with cytoskeletal protein talin”. The Journal of Biological Chemistry 270 (28): 16995–9. (July 1995). doi:10.1074/jbc.270.28.16995. PMID 7622520. 
  77. ^ “Association of focal adhesion kinase with tuberous sclerosis complex 2 in the regulation of s6 kinase activation and cell growth”. The Journal of Biological Chemistry 281 (49): 37321–9. (December 2006). doi:10.1074/jbc.M605241200. PMID 17043358. 
  78. ^ “FAK controls the mechanical activation of YAP, a transcriptional regulator required for durotaxis” (英語). FASEB Journal 32 (2): 1099–1107. (October 2017). doi:10.1096/fj.201700721r. PMID 29070586. 

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FAKのお隣キーワード

FAITH OF LOVE

FAITH/Thousand Lights

FAITHentertainment

FAIカップ

FAI・ゴールド・エア・メダル

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FAK

FAKE (2016年の映画)

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