Chymase

Details

Name
Chymase
Synonyms
  • 3.4.21.39
  • Alpha-chymase
  • CYH
  • CYM
  • Mast cell protease I
Gene Name
CMA1
Organism
Humans
Amino acid sequence
>lcl|BSEQ0002067|Chymase
MLLLPLPLLLFLLCSRAEAGEIIGGTECKPHSRPYMAYLEIVTSNGPSKFCGGFLIRRNF
VLTAAHCAGRSITVTLGAHNITEEEDTWQKLEVIKQFRHPKYNTSTLHHDIMLLKLKEKA
SLTLAVGTLPFPSQFNFVPPGRMCRVAGWGRTGVLKPGSDTLQEVKLRLMDPQACSHFRD
FDHNLQLCVGNPRKTKSAFKGDSGGPLLCAGVAQGIVSYGRSDAKPPAVFTRISHYRPWI
NQILQAN
Number of residues
247
Molecular Weight
27324.56
Theoretical pI
9.71
GO Classification
Functions
peptide binding / serine-type endopeptidase activity / serine-type peptidase activity
Processes
angiotensin maturation / cellular protein metabolic process / cellular response to glucose stimulus / extracellular matrix disassembly / extracellular matrix organization / interleukin-1 beta biosynthetic process / midbrain development / positive regulation of angiogenesis / protein processing / regulation of inflammatory response
Components
extracellular region / extracellular space / intracellular
General Function
Serine-type peptidase activity
Specific Function
Major secreted protease of mast cells with suspected roles in vasoactive peptide generation, extracellular matrix degradation, and regulation of gland secretion.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Secreted
Gene sequence
>lcl|BSEQ0010726|Chymase (CMA1)
ATGTTACTAAAGTTGAAGGAGAAAGCCAGCCTGACCCTGGCTGTGGGGACACTCCCCTTC
CCATCCCAATTCAACTTTGTCCCACCTGGGAGAATGTGCCGGGTGGCTGGCTGGGGAAGA
ACAGGTGTGTTGAAGCCGGGCTCAGACACTCTGCAAGAGGTGAAGCTGAGACTCATGGAT
CCCCAGGCCTGCAGCCACTTCAGAGACTTTGACCACAATCTTCAGCTGTGTGTGGGCAAT
CCCAGGAAGACAAAATCTGCATTTAAGGGAGACTCTGGGGGCCCTCTTCTGTGTGCTGGG
GTGGCCCAGGGCATCGTATCCTATGGACGGTCGGATGCAAAGCCCCCTGCTGTCTTCACC
CGAATCTCCCATTACCGGCCCTGGATCAACCAGATCCTGCAGGCAAATTAA
Chromosome Location
14
Locus
14q11.2
External Identifiers
ResourceLink
UniProtKB IDP23946
UniProtKB Entry NameCMA1_HUMAN
GenBank Protein ID180542
GenBank Gene IDM64269
GenAtlas IDCMA1
HGNC IDHGNC:2097
General References
  1. Caughey GH, Zerweck EH, Vanderslice P: Structure, chromosomal assignment, and deduced amino acid sequence of a human gene for mast cell chymase. J Biol Chem. 1991 Jul 15;266(20):12956-63. [Article]
  2. Urata H, Kinoshita A, Perez DM, Misono KS, Bumpus FM, Graham RM, Husain A: Cloning of the gene and cDNA for human heart chymase. J Biol Chem. 1991 Sep 15;266(26):17173-9. [Article]
  3. Schechter NM, Wang ZM, Blacher RW, Lessin SR, Lazarus GS, Rubin H: Determination of the primary structures of human skin chymase and cathepsin G from cutaneous mast cells of urticaria pigmentosa lesions. J Immunol. 1994 Apr 15;152(8):4062-9. [Article]
  4. Goshima N, Kawamura Y, Fukumoto A, Miura A, Honma R, Satoh R, Wakamatsu A, Yamamoto J, Kimura K, Nishikawa T, Andoh T, Iida Y, Ishikawa K, Ito E, Kagawa N, Kaminaga C, Kanehori K, Kawakami B, Kenmochi K, Kimura R, Kobayashi M, Kuroita T, Kuwayama H, Maruyama Y, Matsuo K, Minami K, Mitsubori M, Mori M, Morishita R, Murase A, Nishikawa A, Nishikawa S, Okamoto T, Sakagami N, Sakamoto Y, Sasaki Y, Seki T, Sono S, Sugiyama A, Sumiya T, Takayama T, Takayama Y, Takeda H, Togashi T, Yahata K, Yamada H, Yanagisawa Y, Endo Y, Imamoto F, Kisu Y, Tanaka S, Isogai T, Imai J, Watanabe S, Nomura N: Human protein factory for converting the transcriptome into an in vitro-expressed proteome,. Nat Methods. 2008 Dec;5(12):1011-7. [Article]
  5. Heilig R, Eckenberg R, Petit JL, Fonknechten N, Da Silva C, Cattolico L, Levy M, Barbe V, de Berardinis V, Ureta-Vidal A, Pelletier E, Vico V, Anthouard V, Rowen L, Madan A, Qin S, Sun H, Du H, Pepin K, Artiguenave F, Robert C, Cruaud C, Bruls T, Jaillon O, Friedlander L, Samson G, Brottier P, Cure S, Segurens B, Aniere F, Samain S, Crespeau H, Abbasi N, Aiach N, Boscus D, Dickhoff R, Dors M, Dubois I, Friedman C, Gouyvenoux M, James R, Madan A, Mairey-Estrada B, Mangenot S, Martins N, Menard M, Oztas S, Ratcliffe A, Shaffer T, Trask B, Vacherie B, Bellemere C, Belser C, Besnard-Gonnet M, Bartol-Mavel D, Boutard M, Briez-Silla S, Combette S, Dufosse-Laurent V, Ferron C, Lechaplais C, Louesse C, Muselet D, Magdelenat G, Pateau E, Petit E, Sirvain-Trukniewicz P, Trybou A, Vega-Czarny N, Bataille E, Bluet E, Bordelais I, Dubois M, Dumont C, Guerin T, Haffray S, Hammadi R, Muanga J, Pellouin V, Robert D, Wunderle E, Gauguet G, Roy A, Sainte-Marthe L, Verdier J, Verdier-Discala C, Hillier L, Fulton L, McPherson J, Matsuda F, Wilson R, Scarpelli C, Gyapay G, Wincker P, Saurin W, Quetier F, Waterston R, Hood L, Weissenbach J: The DNA sequence and analysis of human chromosome 14. Nature. 2003 Feb 6;421(6923):601-7. Epub 2003 Jan 1. [Article]
  6. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [Article]
  7. Sukenaga Y, Kido H, Neki A, Enomoto M, Ishida K, Takagi K, Katunuma N: Purification and molecular cloning of chymase from human tonsils. FEBS Lett. 1993 May 24;323(1-2):119-22. [Article]
  8. Jenne DE, Tschopp J: Angiotensin II-forming heart chymase is a mast-cell-specific enzyme. Biochem J. 1991 Jun 1;276 ( Pt 2):567-8. [Article]
  9. Chen R, Jiang X, Sun D, Han G, Wang F, Ye M, Wang L, Zou H: Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry. J Proteome Res. 2009 Feb;8(2):651-61. doi: 10.1021/pr8008012. [Article]
  10. McGrath ME, Mirzadegan T, Schmidt BF: Crystal structure of phenylmethanesulfonyl fluoride-treated human chymase at 1.9 A. Biochemistry. 1997 Nov 25;36(47):14318-24. [Article]
  11. Pereira PJ, Wang ZM, Rubin H, Huber R, Bode W, Schechter NM, Strobl S: The 2.2 A crystal structure of human chymase in complex with succinyl-Ala-Ala-Pro-Phe-chloromethylketone: structural explanation for its dipeptidyl carboxypeptidase specificity. J Mol Biol. 1999 Feb 12;286(1):163-73. [Article]
  12. Pereira PJ, Wang ZM, Rubin H, Huber R, Bode W, Schechter NM, Strobl S: The 2.2 A Crystal Structure of Human Chymase in Complex with Succinyl-Ala-Ala-Pro-Phe-chloromethylketone: Structural Explanation for its Dipeptidyl Carboxypeptidase Specificity. J Mol Biol. 1999 Apr 9;286(4):817. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB03297Benzylsulfonic acidexperimentalunknownDetails
DB038142-(N-morpholino)ethanesulfonic acidexperimentalunknownDetails
DB040162-[3-({Methyl[1-(2-Naphthoyl)Piperidin-4-Yl]Amino}Carbonyl)-2-Naphthyl]-1-(1-Naphthyl)-2-Oxoethylphosphonic AcidexperimentalunknownDetails
DB07680[(1S)-1-(5-CHLORO-1-BENZOTHIEN-3-YL)-2-(2-NAPHTHYLAMINO)-2-OXOETHYL]PHOSPHONIC ACIDexperimentalunknownDetails