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Identification
HMDB Protein ID HMDBP07814
Secondary Accession Numbers
  • 13523
Name Neutrophil collagenase
Synonyms
  1. MMP-8
  2. Matrix metalloproteinase-8
  3. PMNL collagenase
  4. PMNL-CL
Gene Name MMP8
Protein Type Unknown
Biological Properties
General Function Involved in metalloendopeptidase activity
Specific Function Can degrade fibrillar type I, II, and III collagens
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
calcium ion binding
Process
metabolic process
macromolecule metabolic process
protein metabolic process
proteolysis
Cellular Location
  1. Secreted
  2. Cytoplasmic granule
  3. extracellular space
  4. extracellular matrix (Probable)
Gene Properties
Chromosome Location Chromosome:1
Locus 11q22.3
SNPs MMP8
Gene Sequence
>1404 bp
ATGTTCTCCCTGAAGACGCTTCCATTTCTGCTCTTACTCCATGTGCAGATTTCCAAGGCC
TTTCCTGTATCTTCTAAAGAGAAAAATACAAAAACTGTTCAGGACTACCTGGAAAAGTTC
TACCAATTACCAAGCAACCAGTATCAGTCTACAAGGAAGAATGGCACTAATGTGATCGTT
GAAAAGCTTAAAGAAATGCAGCGATTTTTTGGGTTGAATGTGACGGGGAAGCCAAATGAG
GAAACTCTGGACATGATGAAAAAGCCTCGCTGTGGAGTGCCTGACAGTGGTGGTTTTATG
TTAACCCCAGGAAACCCCAAGTGGGAACGCACTAACTTGACCTACAGGATTCGAAACTAT
ACCCCACAGCTGTCAGAGGCTGAGGTAGAAAGAGCTATCAAGGATGCCTTTGAACTCTGG
AGTGTTGCATCACCTCTCATCTTCACCAGGATCTCACAGGGAGAGGCAGATATCAACATT
GCTTTTTACCAAAGAGATCACGGTGACAATTCTCCATTTGATGGACCCAATGGAATCCTT
GCTCATGCCTTTCAGCCAGGCCAAGGTATTGGAGGAGATGCTCATTTTGATGCCGAAGAA
ACATGGACCAACACCTCCGCAAATTACAACTTGTTTCTTGTTGCTGCTCATGAATTTGGC
CATTCTTTGGGGCTCGCTCACTCCTCTGACCCTGGTGCCTTGATGTATCCCAACTATGCT
TTCAGGGAAACCAGCAACTACTCACTCCCTCAAGATGACATCGATGGCATTCAGGCCATC
TATGGACTTTCAAGCAACCCTATCCAACCTACTGGACCAAGCACACCCAAACCCTGTGAC
CCCAGTTTGACATTTGATGCTATCACCACACTCCGTGGAGAAATACTTTTCTTTAAAGAC
AGGTACTTCTGGAGAAGGCATCCTCAGCTACAAAGAGTCGAAATGAATTTTATTTCTCTA
TTCTGGCCATCCCTTCCAACTGGTATACAGGCTGCTTATGAAGATTTTGACAGAGACCTC
ATTTTCCTATTTAAAGGCAACCAATACTGGGCTCTGAGTGGCTATGATATTCTGCAAGGT
TATCCCAAGGATATATCAAACTATGGCTTCCCCAGCAGCGTCCAAGCAATTGACGCAGCT
GTTTTCTACAGAAGTAAAACATACTTCTTTGTAAATGACCAATTCTGGAGATATGATAAC
CAAAGACAATTCATGGAGCCAGGTTATCCCAAAAGCATATCAGGTGCCTTTCCAGGAATA
GAGAGTAAAGTTGATGCAGTTTTCCAGCAAGAACATTTCTTCCATGTCTTCAGTGGACCA
AGATATTACGCATTTGATCTTATTGCTCAGAGAGTTACCAGAGTTGCAAGAGGCAATAAA
TGGCTTAACTGTAGATATGGCTGA
Protein Properties
Number of Residues 467
Molecular Weight 53411.7
Theoretical pI 6.86
Pfam Domain Function
Signals
  • 1-20
Transmembrane Regions
  • None
Protein Sequence
>Neutrophil collagenase
MFSLKTLPFLLLLHVQISKAFPVSSKEKNTKTVQDYLEKFYQLPSNQYQSTRKNGTNVIV
EKLKEMQRFFGLNVTGKPNEETLDMMKKPRCGVPDSGGFMLTPGNPKWERTNLTYRIRNY
TPQLSEAEVERAIKDAFELWSVASPLIFTRISQGEADINIAFYQRDHGDNSPFDGPNGIL
AHAFQPGQGIGGDAHFDAEETWTNTSANYNLFLVAAHEFGHSLGLAHSSDPGALMYPNYA
FRETSNYSLPQDDIDGIQAIYGLSSNPIQPTGPSTPKPCDPSLTFDAITTLRGEILFFKD
RYFWRRHPQLQRVEMNFISLFWPSLPTGIQAAYEDFDRDLIFLFKGNQYWALSGYDILQG
YPKDISNYGFPSSVQAIDAAVFYRSKTYFFVNDQFWRYDNQRQFMEPGYPKSISGAFPGI
ESKVDAVFQQEHFFHVFSGPRYYAFDLIAQRVTRVARGNKWLNCRYG
GenBank ID Protein Not Available
UniProtKB/Swiss-Prot ID P22894
UniProtKB/Swiss-Prot Entry Name MMP8_HUMAN
PDB IDs Not Available
GenBank Gene ID J05556
GeneCard ID MMP8
GenAtlas ID MMP8
HGNC ID HGNC:7175
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. Hasty KA, Pourmotabbed TF, Goldberg GI, Thompson JP, Spinella DG, Stevens RM, Mainardi CL: Human neutrophil collagenase. A distinct gene product with homology to other matrix metalloproteinases. J Biol Chem. 1990 Jul 15;265(20):11421-4. [PubMed:2164002 ]
  3. Knauper V, Kramer S, Reinke H, Tschesche H: Characterization and activation of procollagenase from human polymorphonuclear leucocytes. N-terminal sequence determination of the proenzyme and various proteolytically activated forms. Eur J Biochem. 1990 Apr 30;189(2):295-300. [PubMed:2159879 ]
  4. Blaser J, Knauper V, Osthues A, Reinke H, Tschesche H: Mercurial activation of human polymorphonuclear leucocyte procollagenase. Eur J Biochem. 1991 Dec 18;202(3):1223-30. [PubMed:1662606 ]
  5. Mallya SK, Mookhtiar KA, Gao Y, Brew K, Dioszegi M, Birkedal-Hansen H, Van Wart HE: Characterization of 58-kilodalton human neutrophil collagenase: comparison with human fibroblast collagenase. Biochemistry. 1990 Nov 27;29(47):10628-34. [PubMed:2176876 ]
  6. Knauper V, Kramer S, Reinke H, Tschesche H: Partial amino acid sequence of human PMN leukocyte procollagenase. Biol Chem Hoppe Seyler. 1990 May;371 Suppl:295-304. [PubMed:2169256 ]
  7. Knauper V, Kramer S, Reinke H, Tschesche H: Partial amino-acid sequence of human PMN leukocyte procollagenase. Biol Chem Hoppe Seyler. 1990 Aug;371(8):733. [PubMed:2169766 ]
  8. Blaser J, Triebel S, Reinke H, Tschesche H: Formation of a covalent Hg-Cys-bond during mercurial activation of PMNL procollagenase gives evidence of a cysteine-switch mechanism. FEBS Lett. 1992 Nov 16;313(1):59-61. [PubMed:1330697 ]
  9. Bode W, Reinemer P, Huber R, Kleine T, Schnierer S, Tschesche H: The X-ray crystal structure of the catalytic domain of human neutrophil collagenase inhibited by a substrate analogue reveals the essentials for catalysis and specificity. EMBO J. 1994 Mar 15;13(6):1263-9. [PubMed:8137810 ]
  10. Reinemer P, Grams F, Huber R, Kleine T, Schnierer S, Piper M, Tschesche H, Bode W: Structural implications for the role of the N terminus in the 'superactivation' of collagenases. A crystallographic study. FEBS Lett. 1994 Jan 31;338(2):227-33. [PubMed:8307185 ]
  11. Stams T, Spurlino JC, Smith DL, Wahl RC, Ho TF, Qoronfleh MW, Banks TM, Rubin B: Structure of human neutrophil collagenase reveals large S1' specificity pocket. Nat Struct Biol. 1994 Feb;1(2):119-23. [PubMed:7656015 ]
  12. Betz M, Huxley P, Davies SJ, Mushtaq Y, Pieper M, Tschesche H, Bode W, Gomis-Ruth FX: 1.8-A crystal structure of the catalytic domain of human neutrophil collagenase (matrix metalloproteinase-8) complexed with a peptidomimetic hydroxamate primed-side inhibitor with a distinct selectivity profile. Eur J Biochem. 1997 Jul 1;247(1):356-63. [PubMed:9249047 ]
  13. Brandstetter H, Engh RA, Von Roedern EG, Moroder L, Huber R, Bode W, Grams F: Structure of malonic acid-based inhibitors bound to human neutrophil collagenase. A new binding mode explains apparently anomalous data. Protein Sci. 1998 Jun;7(6):1303-9. [PubMed:9655333 ]