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Showing Protein Matrilysin (HMDBP02928)

IdentificationBiological propertiesGene propertiesProtein propertiesExternal linksReferencesXMLShow 2 metabolites
Identification
HMDB Protein ID HMDBP02928
Secondary Accession Numbers
  • 8438
Name Matrilysin
Synonyms
  1. MMP-7
  2. Matrin
  3. Matrix metalloproteinase-7
  4. Pump-1 protease
  5. Uterine metalloproteinase
Gene Name MMP7
Protein Type Unknown
Biological Properties
General Function Involved in metalloendopeptidase activity
Specific Function Degrades casein, gelatins of types I, III, IV, and V, and fibronectin. Activates procollagenase
Pathways Not Available
Reactions Not Available
GO Classification
Component
extracellular region part
extracellular matrix
Function
endopeptidase activity
ion binding
cation binding
metal ion binding
binding
catalytic activity
hydrolase activity
transition metal ion binding
zinc ion binding
metalloendopeptidase activity
peptidase activity
peptidase activity, acting on l-amino acid peptides
metallopeptidase activity
Process
metabolic process
macromolecule metabolic process
protein metabolic process
proteolysis
Cellular Location
  1. Secreted
  2. extracellular space
  3. extracellular matrix (Probable)
Gene Properties
Chromosome Location Chromosome:1
Locus 11q21-q22
SNPs MMP7
Gene Sequence 
>804 bp
ATGCGACTCACCGTGCTGTGTGCTGTGTGCCTGCTGCCTGGCAGCCTGGCCCTGCCGCTG
CCTCAGGAGGCGGGAGGCATGAGTGAGCTACAGTGGGAACAGGCTCAGGACTATCTCAAG
AGATTTTATCTCTATGACTCAGAAACAAAAAATGCCAACAGTTTAGAAGCCAAACTCAAG
GAGATGCAAAAATTCTTTGGCCTACCTATAACTGGAATGTTAAACTCCCGCGTCATAGAA
ATAATGCAGAAGCCCAGATGTGGAGTGCCAGATGTTGCAGAATACTCACTATTTCCAAAT
AGCCCAAAATGGACTTCCAAAGTGGTCACCTACAGGATCGTATCATATACTCGAGACTTA
CCGCATATTACAGTGGATCGATTAGTGTCAAAGGCTTTAAACATGTGGGGCAAAGAGATC
CCCCTGCATTTCAGGAAAGTTGTATGGGGAACTGCTGACATCATGATTGGCTTTGCGCGA
GGAGCTCATGGGGACTCCTACCCATTTGATGGGCCAGGAAACACGCTGGCTCATGCCTTT
GCGCCTGGGACAGGTCTCGGAGGAGATGCTCACTTCGATGAGGATGAACGCTGGACGGAT
GGTAGCAGTCTAGGGATTAACTTCCTGTATGCTGCAACTCATGAACTTGGCCATTCTTTG
GGTATGGGACATTCCTCTGATCCTAATGCAGTGATGTATCCAACCTATGGAAATGGAGAT
CCCCAAAATTTTAAACTTTCCCAGGATGATATTAAAGGCATTCAGAAACTATATGGAAAG
AGAAGTAATTCAAGAAAGAAATAG
Protein Properties
Number of Residues 267
Molecular Weight 29676.6
Theoretical pI 8.09
Pfam Domain Function
Signals
  • 1-17
Transmembrane Regions
  • None
Protein Sequence 
>Matrilysin
MRLTVLCAVCLLPGSLALPLPQEAGGMSELQWEQAQDYLKRFYLYDSETKNANSLEAKLK
EMQKFFGLPITGMLNSRVIEIMQKPRCGVPDVAEYSLFPNSPKWTSKVVTYRIVSYTRDL
PHITVDRLVSKALNMWGKEIPLHFRKVVWGTADIMIGFARGAHGDSYPFDGPGNTLAHAF
APGTGLGGDAHFDEDERWTDGSSLGINFLYAATHELGHSLGMGHSSDPNAVMYPTYGNGD
PQNFKLSQDDIKGIQKLYGKRSNSRKK
GenBank ID Protein 35799
UniProtKB/Swiss-Prot ID P09237
UniProtKB/Swiss-Prot Entry Name MMP7_HUMAN
PDB IDs
GenBank Gene ID X07819
GeneCard ID MMP7
GenAtlas ID MMP7
HGNC ID HGNC:7174
References
General References
  1. 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. [PubMed:15489334 ]
  2. 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. [PubMed:2844164 ]
  3. 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. [PubMed:1497627 ]
  4. 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. [PubMed:8294454 ]
  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. [PubMed:2253219 ]
  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. [PubMed:2550050 ]
  7. Browner MF, Smith WW, Castelhano AL: Matrilysin-inhibitor complexes: common themes among metalloproteases. Biochemistry. 1995 May 23;34(20):6602-10. [PubMed:7756291 ]