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维基百科

胱抑素A

行進 07, 2024

胱抑素A是一种在人体中由CSTA基因编码的蛋白质。[6][7]

血清胱抑素A
已知的結構
PDB直系同源搜索: PDBe RCSB
識別號
别名CSTA；, AREI, STF1, STFA, Cystatin A, PSS4
外部IDOMIM：184600 MGI：3645124 HomoloGene：3819 GeneCards：CSTA
相關疾病
Exfoliative ichthyosis[1]
基因位置（人类）
染色体3號染色體[2]
基因座3q21.1起始122,325,248 bp[2]
终止122,341,969 bp[2]
RNA表达模式
查阅更多表达数据
直系同源
物種人類小鼠
Entrez

1475

433016

Ensembl

ENSG00000121552

ENSMUSG00000079597

UniProt

P01040

B2RV77

mRNA​序列

NM_005213

NM_001082547

蛋白序列

NP_005204

NP_001076016

基因位置​（UCSC）Chr 3: 122.33 – 122.34 MbChr 16: 36 – 36.01 Mb
PubMed​查找[4][5]
維基數據
檢視/編輯人類檢視/編輯小鼠

胱抑素超家族包括含有多个胱抑素样序列的蛋白质。一些成员是活性半胱氨酸蛋白酶抑制剂，而其他成员已经失去或可能从未获得这种抑制活性。超家族中有3个抑制家族，包括1型胱抑素（stefin）、2型胱抑素和激肽原。该基因编码一种stefin，起半胱氨酸蛋白酶抑制剂的作用，与木瓜蛋白酶和组织蛋白酶B、H和L形成紧密复合物。该蛋白是角质形成细胞中角化细胞包膜的前体蛋白之一，在表皮发育和维护。Stefin已被提议作为癌症的预后和诊断工具。[7]

相互作用 编辑

胱抑素A已被证明与胱抑素B[8][9]和组织蛋白酶L1[9][10]产生相互作用。

参见 编辑

  • 肽转运蛋白碳饥饿家族

参考文献 编辑

  1. ^ 與血清胱抑素A相關的疾病；在維基數據上查看/編輯參考. 
  2. ^ 2.0 2.1 2.2 GRCh38: Ensembl release 89: ENSG00000121552 - Ensembl, May 2017
  3. ^ 3.0 3.1 3.2 GRCm38: Ensembl release 89: ENSMUSG00000079597 - Ensembl, May 2017
  4. ^ Human PubMed Reference:. National Center for Biotechnology Information, U.S. National Library of Medicine. 
  5. ^ Mouse PubMed Reference:. National Center for Biotechnology Information, U.S. National Library of Medicine. 
  6. ^ Hsieh WT, Barrick JL, Berrettini WH, Chan MM, Fong D. A PstI DNA polymorphism in the human stefin A gene (STF 1). Nucleic Acids Res. Jun 1991, 19 (7): 1722. PMC 333958  . PMID 1674139. doi:10.1093/nar/19.7.1722-a. 
  7. ^ 7.0 7.1 Entrez Gene: CSTA cystatin A (stefin A). 
  8. ^ Pavlova, Alona; Björk Ingemar. Grafting of features of cystatins C or B into the N-terminal region or second binding loop of cystatin A (stefin A) substantially enhances inhibition of cysteine proteinases. Biochemistry (United States). Sep 2003, 42 (38): 11326–33. ISSN 0006-2960. PMID 14503883. doi:10.1021/bi030119v. 
  9. ^ 9.0 9.1 Estrada, S; Nycander M; Hill N J; Craven C J; Waltho J P; Björk I. The role of Gly-4 of human cystatin A (stefin A) in the binding of target proteinases. Characterization by kinetic and equilibrium methods of the interactions of cystatin A Gly-4 mutants with papain, cathepsin B, and cathepsin L. Biochemistry (UNITED STATES). May 1998, 37 (20): 7551–60. ISSN 0006-2960. PMID 9585570. doi:10.1021/bi980026r. 
  10. ^ Majerle, Andreja; Jerala Roman. Protein inhibitors form complexes with procathepsin L and augment cleavage of the propeptide. Arch. Biochem. Biophys. (United States). Sep 2003, 417 (1): 53–8. ISSN 0003-9861. PMID 12921779. doi:10.1016/S0003-9861(03)00319-9. 

阅读 编辑

  • Järvinen M, Rinne A, Hopsu-Havu VK. Human cystatins in normal and diseased tissues--a review. Acta Histochem. 1988, 82 (1): 5–18. PMID 3122506. doi:10.1016/s0065-1281(87)80043-0. 
  • Brown WM, Dziegielewska KM. Friends and relations of the cystatin superfamily--new members and their evolution. Protein Sci. 1997, 6 (1): 5–12. PMC 2143511  . PMID 9007972. doi:10.1002/pro.5560060102. 
  • Kos J, Lah TT. Cysteine proteinases and their endogenous inhibitors: target proteins for prognosis, diagnosis and therapy in cancer (review). Oncol. Rep. 1998, 5 (6): 1349–61. PMID 9769367. doi:10.3892/or.5.6.1349. 
  • Rinne A, Järvinen M, Räsänen O. A protein reminiscent of the epidermal SH-protease inhibitor occurs in squamous epithelia of man and rat. Acta Histochem. 1979, 63 (2): 183–92. PMID 107702. doi:10.1016/s0065-1281(78)80024-5. 
  • Räsänen O, Järvinen M, Rinne A. Localization of the human SH-protease inhibitor in the epidermis. Immunofluorescent studies. Acta Histochem. 1979, 63 (2): 193–6. PMID 107703. doi:10.1016/s0065-1281(78)80025-7. 
  • Rasmussen HH, van Damme J, Puype M, et al. Microsequences of 145 proteins recorded in the two-dimensional gel protein database of normal human epidermal keratinocytes. Electrophoresis. 1993, 13 (12): 960–9. PMID 1286667. S2CID 41855774. doi:10.1002/elps.11501301199. 
  • Madsen P, Rasmussen HH, Leffers H, et al. Molecular cloning, occurrence, and expression of a novel partially secreted protein "psoriasin" that is highly up-regulated in psoriatic skin. J. Invest. Dermatol. 1991, 97 (4): 701–12. PMID 1940442. doi:10.1111/1523-1747.ep12484041. 
  • Hsieh WT, Fong D, Sloane BF, et al. Mapping of the gene for human cysteine proteinase inhibitor stefin A, STF1, to chromosome 3cen-q21. Genomics. 1991, 9 (1): 207–9. PMID 2004763. doi:10.1016/0888-7543(91)90241-6. 
  • Rinne A, Järvinen M, Dorn A, et al. [Low-molecular cysteine protease inhibitors in the human palatal tonsil]. Anatomischer Anzeiger. 1986, 161 (3): 215–30. PMID 2424340. 
  • Kartasova T, Cornelissen BJ, Belt P, van de Putte P. Effects of UV, 4-NQO and TPA on gene expression in cultured human epidermal keratinocytes. Nucleic Acids Res. 1987, 15 (15): 5945–62. PMC 306060  . PMID 2442723. doi:10.1093/nar/15.15.5945. 
  • Takeda A, Kaji H, Nakaya K, et al. Comparative studies on the primary structure of human cystatin as from epidermis, liver, spleen, and leukocytes. J. Biochem. 1989, 105 (6): 986–91. PMID 2768224. doi:10.1093/oxfordjournals.jbchem.a122792. 
  • Strauss M, Stollwerk J, Lenarcic B, et al. Chemical synthesis of a gene for human stefin A and its expression in E. coli. Biol. Chem. Hoppe-Seyler. 1989, 369 (9): 1019–30. PMID 3067731. doi:10.1515/bchm3.1988.369.2.1019. 
  • Davies ME, Barrett AJ. Immunolocalization of human cystatins in neutrophils and lymphocytes. Histochemistry. 1984, 80 (4): 373–7. PMID 6429090. S2CID 13559202. doi:10.1007/BF00495420. 
  • Machleidt W, Borchart U, Fritz H, et al. Protein inhibitors of cysteine proteinases. II. Primary structure of stefin, a cytosolic protein inhibitor of cysteine proteinases from human polymorphonuclear granulocytes. Hoppe-Seyler's Z. Physiol. Chem. 1984, 364 (11): 1481–6. PMID 6689312. doi:10.1515/bchm2.1983.364.2.1481. 
  • Söderström KO, Laato M, Wu P, et al. Expression of acid cysteine proteinase inhibitor (ACPI) in the normal human prostate, benign prostatic hyperplasia and adenocarcinoma. Int. J. Cancer. 1995, 62 (1): 1–4. PMID 7541394. S2CID 25265556. doi:10.1002/ijc.2910620102. 
  • Tate S, Ushioda T, Utsunomiya-Tate N, et al. Solution structure of a human cystatin A variant, cystatin A2-98 M65L, by NMR spectroscopy. A possible role of the interactions between the N- and C-termini to maintain the inhibitory active form of cystatin A. Biochemistry. 1995, 34 (45): 14637–48. PMID 7578072. doi:10.1021/bi00045a004. 
  • Martin JR, Craven CJ, Jerala R, et al. The three-dimensional solution structure of human stefin A. J. Mol. Biol. 1995, 246 (2): 331–43. PMID 7869384. doi:10.1006/jmbi.1994.0088. 
  • Steinert PM, Marekov LN. Direct evidence that involucrin is a major early isopeptide cross-linked component of the keratinocyte cornified cell envelope. J. Biol. Chem. 1997, 272 (3): 2021–30. PMID 8999895. doi:10.1074/jbc.272.3.2021  . 

外部链接 编辑

  • 相当有趣的PDB结构文章在PDBe （页面存档备份，存于互联网档案馆）
  • 肽酶及其抑制剂的MEROPS在线数据库：I25.001

行進 07, 2024
胱抑素a, 是一种在人体中由csta基因编码的蛋白质, 血清已知的結構pdb直系同源搜索, pdbe, rcsbpdbid列表1cyu, 1cyv, 1dvc, 1dvd, 1gd3, 1gd4, 1n9j, 1nb3, 1nb5, 3k9m, 3kfq, 3kse識別號别名csta, arei, stf1, stfa, cystatin, pss4外部idomim, 184600, 3645124, homologene, 3819, genecards, csta相關疾病exfoliative, ichthyo. 胱抑素A是一种在人体中由CSTA基因编码的蛋白质 6 7 血清胱抑素A已知的結構PDB直系同源搜索 PDBe RCSBPDBID列表1CYU 1CYV 1DVC 1DVD 1GD3 1GD4 1N9J 1NB3 1NB5 3K9M 3KFQ 3KSE識別號别名CSTA AREI STF1 STFA Cystatin A PSS4外部IDOMIM 184600 MGI 3645124 HomoloGene 3819 GeneCards CSTA相關疾病Exfoliative ichthyosis 1 基因位置 人类 染色体3號染色體 2 基因座3q21 1起始122 325 248 bp 2 终止122 341 969 bp 2 基因位置 小鼠 染色体小鼠16号染色体 3 基因座16 16 B3起始36 004 582 bp 3 终止36 008 481 bp 3 RNA表达模式查阅更多表达数据基因本體分子功能 peptidase inhibitor activity 蛋白酶結合 protein macromolecule adaptor activity endopeptidase inhibitor activity structural molecule activity cysteine type endopeptidase inhibitor activity細胞組分 細胞質 胞內 cornified envelope 細胞外空間 细胞核 细胞质基质生物學過程 negative regulation of proteolysis peptide cross linking negative regulation of peptidase activity 細胞粘附 keratinocyte differentiation negative regulation of endopeptidase activity cornification cell cell adhesionSources Amigo QuickGO直系同源物種人類小鼠Entrez1475433016EnsemblENSG00000121552ENSMUSG00000079597UniProtP01040B2RV77mRNA 序列NM 005213NM 001082547蛋白序列NP 005204NP 001076016基因位置 UCSC Chr 3 122 33 122 34 MbChr 16 36 36 01 MbPubMed 查找 4 5 維基數據檢視 編輯人類檢視 編輯小鼠胱抑素超家族包括含有多个胱抑素样序列的蛋白质 一些成员是活性半胱氨酸蛋白酶抑制剂 而其他成员已经失去或可能从未获得这种抑制活性 超家族中有3个抑制家族 包括1型胱抑素 stefin 2型胱抑素和激肽原 该基因编码一种stefin 起半胱氨酸蛋白酶抑制剂的作用 与木瓜蛋白酶和组织蛋白酶B H和L形成紧密复合物 该蛋白是角质形成细胞中角化细胞包膜的前体蛋白之一 在表皮发育和维护 Stefin已被提议作为癌症的预后和诊断工具 7 目录 1 相互作用 2 参见 3 参考文献 4 阅读 5 外部链接相互作用 编辑胱抑素A已被证明与胱抑素B 8 9 和组织蛋白酶L1 9 10 产生相互作用 参见 编辑肽转运蛋白碳饥饿家族参考文献 编辑 與血清胱抑素A相關的疾病 在維基數據上查看 編輯參考 2 0 2 1 2 2 GRCh38 Ensembl release 89 ENSG00000121552 Ensembl May 2017 3 0 3 1 3 2 GRCm38 Ensembl release 89 ENSMUSG00000079597 Ensembl May 2017 Human PubMed Reference National Center for Biotechnology Information U S National Library of Medicine Mouse PubMed Reference National Center for Biotechnology Information U S National Library of Medicine Hsieh WT Barrick JL Berrettini WH Chan MM Fong D A PstI DNA polymorphism in the human stefin A gene STF 1 Nucleic Acids Res Jun 1991 19 7 1722 PMC 333958 nbsp PMID 1674139 doi 10 1093 nar 19 7 1722 a 7 0 7 1 Entrez Gene CSTA cystatin A stefin A Pavlova Alona Bjork Ingemar Grafting of features of cystatins C or B into the N terminal region or second binding loop of cystatin A stefin A substantially enhances inhibition of cysteine proteinases Biochemistry United States Sep 2003 42 38 11326 33 ISSN 0006 2960 PMID 14503883 doi 10 1021 bi030119v 9 0 9 1 Estrada S Nycander M Hill N J Craven C J Waltho J P Bjork I The role of Gly 4 of human cystatin A stefin A in the binding of target proteinases Characterization by kinetic and equilibrium methods of the interactions of cystatin A Gly 4 mutants with papain cathepsin B and cathepsin L Biochemistry UNITED STATES May 1998 37 20 7551 60 ISSN 0006 2960 PMID 9585570 doi 10 1021 bi980026r Majerle Andreja Jerala Roman Protein inhibitors form complexes with procathepsin L and augment cleavage of the propeptide Arch Biochem Biophys United States Sep 2003 417 1 53 8 ISSN 0003 9861 PMID 12921779 doi 10 1016 S0003 9861 03 00319 9 阅读 编辑Jarvinen M Rinne A Hopsu Havu VK Human cystatins in normal and diseased tissues a review Acta Histochem 1988 82 1 5 18 PMID 3122506 doi 10 1016 s0065 1281 87 80043 0 Brown WM Dziegielewska KM Friends and relations of the cystatin superfamily new members and their evolution Protein Sci 1997 6 1 5 12 PMC 2143511 nbsp PMID 9007972 doi 10 1002 pro 5560060102 Kos J Lah TT Cysteine proteinases and their endogenous inhibitors target proteins for prognosis diagnosis and therapy in cancer review Oncol Rep 1998 5 6 1349 61 PMID 9769367 doi 10 3892 or 5 6 1349 Rinne A Jarvinen M Rasanen O A protein reminiscent of the epidermal SH protease inhibitor occurs in squamous epithelia of man and rat Acta Histochem 1979 63 2 183 92 PMID 107702 doi 10 1016 s0065 1281 78 80024 5 Rasanen O Jarvinen M Rinne A Localization of the human SH protease inhibitor in the epidermis Immunofluorescent studies Acta Histochem 1979 63 2 193 6 PMID 107703 doi 10 1016 s0065 1281 78 80025 7 Rasmussen HH van Damme J Puype M et al Microsequences of 145 proteins recorded in the two dimensional gel protein database of normal human epidermal keratinocytes Electrophoresis 1993 13 12 960 9 PMID 1286667 S2CID 41855774 doi 10 1002 elps 11501301199 Madsen P Rasmussen HH Leffers H et al Molecular cloning occurrence and expression of a novel partially secreted protein psoriasin that is highly up regulated in psoriatic skin J Invest Dermatol 1991 97 4 701 12 PMID 1940442 doi 10 1111 1523 1747 ep12484041 Hsieh WT Fong D Sloane BF et al Mapping of the gene for human cysteine proteinase inhibitor stefin A STF1 to chromosome 3cen q21 Genomics 1991 9 1 207 9 PMID 2004763 doi 10 1016 0888 7543 91 90241 6 Rinne A Jarvinen M Dorn A et al Low molecular cysteine protease inhibitors in the human palatal tonsil Anatomischer Anzeiger 1986 161 3 215 30 PMID 2424340 Kartasova T Cornelissen BJ Belt P van de Putte P Effects of UV 4 NQO and TPA on gene expression in cultured human epidermal keratinocytes Nucleic Acids Res 1987 15 15 5945 62 PMC 306060 nbsp PMID 2442723 doi 10 1093 nar 15 15 5945 Takeda A Kaji H Nakaya K et al Comparative studies on the primary structure of human cystatin as from epidermis liver spleen and leukocytes J Biochem 1989 105 6 986 91 PMID 2768224 doi 10 1093 oxfordjournals jbchem a122792 Strauss M Stollwerk J Lenarcic B et al Chemical synthesis of a gene for human stefin A and its expression in E coli Biol Chem Hoppe Seyler 1989 369 9 1019 30 PMID 3067731 doi 10 1515 bchm3 1988 369 2 1019 Davies ME Barrett AJ Immunolocalization of human cystatins in neutrophils and lymphocytes Histochemistry 1984 80 4 373 7 PMID 6429090 S2CID 13559202 doi 10 1007 BF00495420 Machleidt W Borchart U Fritz H et al Protein inhibitors of cysteine proteinases II Primary structure of stefin a cytosolic protein inhibitor of cysteine proteinases from human polymorphonuclear granulocytes Hoppe Seyler s Z Physiol Chem 1984 364 11 1481 6 PMID 6689312 doi 10 1515 bchm2 1983 364 2 1481 Soderstrom KO Laato M Wu P et al Expression of acid cysteine proteinase inhibitor ACPI in the normal human prostate benign prostatic hyperplasia and adenocarcinoma Int J Cancer 1995 62 1 1 4 PMID 7541394 S2CID 25265556 doi 10 1002 ijc 2910620102 Tate S Ushioda T Utsunomiya Tate N et al Solution structure of a human cystatin A variant cystatin A2 98 M65L by NMR spectroscopy A possible role of the interactions between the N and C termini to maintain the inhibitory active form of cystatin A Biochemistry 1995 34 45 14637 48 PMID 7578072 doi 10 1021 bi00045a004 Martin JR Craven CJ Jerala R et al The three dimensional solution structure of human stefin A J Mol Biol 1995 246 2 331 43 PMID 7869384 doi 10 1006 jmbi 1994 0088 Steinert PM Marekov LN Direct evidence that involucrin is a major early isopeptide cross linked component of the keratinocyte cornified cell envelope J Biol Chem 1997 272 3 2021 30 PMID 8999895 doi 10 1074 jbc 272 3 2021 nbsp 外部链接 编辑Cystatin a protein that flips out 相当有趣的PDB结构文章在PDBe 页面存档备份 存于互联网档案馆 肽酶及其抑制剂的MEROPS在线数据库 I25 001 取自 https zh wikipedia org w index php title 胱抑素A amp oldid 75103248, 维基百科，wiki，书籍，书籍，图书馆，

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