Matrilysin

Details

Name
Matrilysin
Synonyms
  • 3.4.24.23
  • Matrin
  • Matrix metalloproteinase-7
  • MMP-7
  • MPSL1
  • Pump-1 protease
  • PUMP1
  • Uterine metalloproteinase
Gene Name
MMP7
Organism
Humans
Amino acid sequence
>lcl|BSEQ0012566|Matrilysin
MRLTVLCAVCLLPGSLALPLPQEAGGMSELQWEQAQDYLKRFYLYDSETKNANSLEAKLK
EMQKFFGLPITGMLNSRVIEIMQKPRCGVPDVAEYSLFPNSPKWTSKVVTYRIVSYTRDL
PHITVDRLVSKALNMWGKEIPLHFRKVVWGTADIMIGFARGAHGDSYPFDGPGNTLAHAF
APGTGLGGDAHFDEDERWTDGSSLGINFLYAATHELGHSLGMGHSSDPNAVMYPTYGNGD
PQNFKLSQDDIKGIQKLYGKRSNSRKK
Number of residues
267
Molecular Weight
29676.62
Theoretical pI
8.09
GO Classification
Functions
heparin binding / metalloendopeptidase activity / zinc ion binding
Processes
aging / antibacterial peptide biosynthetic process / antibacterial peptide secretion / cellular response to mechanical stimulus / collagen catabolic process / defense response to Gram-negative bacterium / defense response to Gram-positive bacterium / estrous cycle / extracellular matrix disassembly / extracellular matrix organization / maternal process involved in female pregnancy / proteolysis / regulation of cell proliferation / response to drug / response to nutrient levels
Components
cell surface / extracellular exosome / extracellular region / extracellular space / proteinaceous extracellular matrix
General Function
Zinc ion binding
Specific Function
Degrades casein, gelatins of types I, III, IV, and V, and fibronectin. Activates procollagenase.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Secreted
Gene sequence
>lcl|BSEQ0012567|Matrilysin (MMP7)
ATGCGACTCACCGTGCTGTGTGCTGTGTGCCTGCTGCCTGGCAGCCTGGCCCTGCCGCTG
CCTCAGGAGGCGGGAGGCATGAGTGAGCTACAGTGGGAACAGGCTCAGGACTATCTCAAG
AGATTTTATCTCTATGACTCAGAAACAAAAAATGCCAACAGTTTAGAAGCCAAACTCAAG
GAGATGCAAAAATTCTTTGGCCTACCTATAACTGGAATGTTAAACTCCCGCGTCATAGAA
ATAATGCAGAAGCCCAGATGTGGAGTGCCAGATGTTGCAGAATACTCACTATTTCCAAAT
AGCCCAAAATGGACTTCCAAAGTGGTCACCTACAGGATCGTATCATATACTCGAGACTTA
CCGCATATTACAGTGGATCGATTAGTGTCAAAGGCTTTAAACATGTGGGGCAAAGAGATC
CCCCTGCATTTCAGGAAAGTTGTATGGGGAACTGCTGACATCATGATTGGCTTTGCGCGA
GGAGCTCATGGGGACTCCTACCCATTTGATGGGCCAGGAAACACGCTGGCTCATGCCTTT
GCGCCTGGGACAGGTCTCGGAGGAGATGCTCACTTCGATGAGGATGAACGCTGGACGGAT
GGTAGCAGTCTAGGGATTAACTTCCTGTATGCTGCAACTCATGAACTTGGCCATTCTTTG
GGTATGGGACATTCCTCTGATCCTAATGCAGTGATGTATCCAACCTATGGAAATGGAGAT
CCCCAAAATTTTAAACTTTCCCAGGATGATATTAAAGGCATTCAGAAACTATATGGAAAG
AGAAGTAATTCAAGAAAGAAATAG
Chromosome Location
11
Locus
11q21-q22
External Identifiers
ResourceLink
UniProtKB IDP09237
UniProtKB Entry NameMMP7_HUMAN
GenBank Protein ID35799
GenBank Gene IDX07819
HGNC IDHGNC:7174
General References
  1. Muller D, Quantin B, Gesnel MC, Millon-Collard R, Abecassis J, Breathnach R: The collagenase gene family in humans consists of at least four members. Biochem J. 1988 Jul 1;253(1):187-92. [Article]
  2. Marti HP, McNeil L, Thomas G, Davies M, Lovett DH: Molecular characterization of a low-molecular-mass matrix metalloproteinase secreted by glomerular mesangial cells as PUMP-1. Biochem J. 1992 Aug 1;285 ( Pt 3):899-905. [Article]
  3. Gaire M, Magbanua Z, McDonnell S, McNeil L, Lovett DH, Matrisian LM: Structure and expression of the human gene for the matrix metalloproteinase matrilysin. J Biol Chem. 1994 Jan 21;269(3):2032-40. [Article]
  4. 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]
  5. Miyazaki K, Hattori Y, Umenishi F, Yasumitsu H, Umeda M: Purification and characterization of extracellular matrix-degrading metalloproteinase, matrin (pump-1), secreted from human rectal carcinoma cell line. Cancer Res. 1990 Dec 15;50(24):7758-64. [Article]
  6. Quantin B, Murphy G, Breathnach R: Pump-1 cDNA codes for a protein with characteristics similar to those of classical collagenase family members. Biochemistry. 1989 Jun 27;28(13):5327-34. [Article]
  7. Browner MF, Smith WW, Castelhano AL: Matrilysin-inhibitor complexes: common themes among metalloproteases. Biochemistry. 1995 May 23;34(20):6602-10. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB00786MarimastatinvestigationalyesantagonistDetails
DB08170(1R)-N,6-DIHYDROXY-7-METHOXY-2-[(4-METHOXYPHENYL)SULFONYL]-1,2,3,4-TETRAHYDROISOQUINOLINE-1-CARBOXAMIDEexperimentalunknownDetails
DB08489N4-HYDROXY-2-ISOBUTYL-N1-(9-OXO-1,8-DIAZA-TRICYCLO[10.6.1.013,18]NONADECA-12(19),13,15,17-TETRAEN-10-YL)-SUCCINAMIDEexperimentalunknownDetails
DB084935-METHYL-3-(9-OXO-1,8-DIAZA-TRICYCLO[10.6.1.013,18]NONADECA-12(19),13,15,17-TETRAEN-10-YLCARBAMOYL)-HEXANOIC ACIDexperimentalunknownDetails