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Identification
HMDB Protein ID HMDBP07804
Secondary Accession Numbers
  • 13513
Name Matrix metalloproteinase-15
Synonyms
  1. MMP-15
  2. MT-MMP 2
  3. MT2-MMP
  4. MT2MMP
  5. MTMMP2
  6. Membrane-type matrix metalloproteinase 2
  7. Membrane-type-2 matrix metalloproteinase
  8. SMCP-2
Gene Name MMP15
Protein Type Unknown
Biological Properties
General Function Involved in metalloendopeptidase activity
Specific Function Endopeptidase that degrades various components of the extracellular matrix. May activate progelatinase A
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. Membrane
  2. Single-pass type I membrane protein
  3. Extracellular side (Potential)
Gene Properties
Chromosome Location Chromosome:1
Locus 16q13
SNPs MMP15
Gene Sequence
>2010 bp
ATGGGCAGCGACCCGAGCGCGCCCGGACGGCCGGGCTGGACGGGCAGCCTCCTCGGCGAC
CGGGAGGAGGCGGCGCGGCCGCGACTGCTGCCGCTGCTCCTGGTGCTTCTGGGCTGCCTG
GGCCTTGGCGTAGCGGCCGAAGACGCGGAGGTCCATGCCGAGAACTGGCTGCGGCTTTAT
GGCTACCTGCCTCAGCCCAGCCGCCATATGTCCACCATGCGTTCCGCCCAGATCTTGGCC
TCGGCCCTTGCAGAGATGCAGCGCTTCTACGGGATCCCAGTCACCGGTGTGCTCGACGAA
GAGACCAAGGAGTGGATGAAGCGGCCCCGCTGTGGGGTGCCAGACCAGTTCGGGGTACGA
GTGAAAGCCAACCTGCGGCGGCGTCGGAAGCGCTACGCCCTCACCGGGAGGAAGTGGAAC
AACCACCATCTGACCTTTAGCATCCAGAACTACACGGAGAAGTTGGGCTGGTACCACTCG
ATGGAGGCGGTGCGCAGGGCCTTCCGCGTGTGGGAGCAGGCCACGCCCCTGGTCTTCCAG
GAGGTGCCCTATGAGGACATCCGGCTGCGGCGACAGAAGGAGGCCGACATCATGGTACTC
TTTGCCTCTGGCTTCCACGGCGACAGCTCGCCGTTTGATGGCACCGGTGGCTTTCTGGCC
CACGCCTATTTCCCTGGCCCCGGCCTAGGCGGGGACACCCATTTTGACGCAGATGAGCCC
TGGACCTTCTCCAGCACTGACCTGCATGGAAACAACCTCTTCCTGGTGGCAGTGCATGAG
CTGGGCCACGCGCTGGGGCTGGAGCACTCCAGCAACCCCAATGCCATCATGGCGCCGTTC
TACCAGTGGAAGGACGTTGACAACTTCAAGCTGCCCGAGGACGATCTCCGTGGCATCCAG
CAGCTCTACGGTACCCCAGACGGTCAGCCACAGCCTACCCAGCCTCTCCCCACTGTGACG
CCACGGCGGCCAGGCCGGCCTGACCACCGGCCGCCCCGGCCTCCCCAGCCACCACCCCCA
GGTGGGAAGCCAGAGCGGCCCCCAAAGCCGGGCCCCCCAGTCCAGCCCCGAGCCACAGAG
CGGCCCGACCAGTATGGCCCCAACATCTGCGACGGGGACTTTGACACAGTGGCCATGCTT
CGCGGGGAGATGTTCGTGTTCAAGGGCCGCTGGTTCTGGCGAGTCCGGCACAACCGCGTC
CTGGACAACTATCCCATGCCCATCGGGCACTTCTGGCGTGGTCTGCCCGGTGACATCAGT
GCTGCCTACGAGCGCCAAGACGGTCGTTTTGTCTTTTTCAAAGGTGACCGCTACTGGCTC
TTTCGAGAAGCGAACCTGGAGCCCGGCTACCCACAGCCGCTGACCAGCTATGGCCTGGGC
ATCCCCTATGACCGCATTGACACGGCCATCTGGTGGGAGCCCACAGGCCACACCTTCTTC
TTCCAAGAGGACAGGTACTGGCGCTTCAACGAGGAGACACAGCGTGGAGACCCTGGGTAC
CCCAAGCCCATCAGTGTCTGGCAGGGGATCCCTGCCTCCCCTAAAGGGGCCTTCCTGAGC
AATGACGCAGCCTACACCTACTTCTACAAGGGCACCAAATACTGGAAATTCGACAATGAG
CGCCTGCGGATGGAGCCCGGCTACCCCAAGTCCATCCTGCGGGACTTCATGGGCTGCCAG
GAGCACGTGGAGCCAGGCCCCCGATGGCCCGACGTGGCCCGGCCGCCCTTCAACCCCCAC
GGGGGTGCAGAGCCCGGGGCGGACAGCGCAGAGGGCGACGTGGGGGATGGGGATGGGGAC
TTTGGGGCCGGGGTCAACAAGGACGGGGGCAGCCGCGTGGTGGTGCAGATGGAGGAGGTG
GCACGGACGGTGAACGTGGTGATGGTGCTGGTGCCACTGCTGCTGCTGCTCTGCGTCCTG
GGCCTCACCTACGCGCTGGTGCAGATGCAGCGCAAGGGTGCGCCACGTGTCCTGCTTTAC
TGCAAGCGCTCGCTGCAGGAGTGGGTCTGA
Protein Properties
Number of Residues 669
Molecular Weight 75806.4
Theoretical pI 7.49
Pfam Domain Function
Signals
  • 1-41
Transmembrane Regions
  • 626-646
Protein Sequence
>Matrix metalloproteinase-15
MGSDPSAPGRPGWTGSLLGDREEAARPRLLPLLLVLLGCLGLGVAAEDAEVHAENWLRLY
GYLPQPSRHMSTMRSAQILASALAEMQRFYGIPVTGVLDEETKEWMKRPRCGVPDQFGVR
VKANLRRRRKRYALTGRKWNNHHLTFSIQNYTEKLGWYHSMEAVRRAFRVWEQATPLVFQ
EVPYEDIRLRRQKEADIMVLFASGFHGDSSPFDGTGGFLAHAYFPGPGLGGDTHFDADEP
WTFSSTDLHGNNLFLVAVHELGHALGLEHSSNPNAIMAPFYQWKDVDNFKLPEDDLRGIQ
QLYGTPDGQPQPTQPLPTVTPRRPGRPDHRPPRPPQPPPPGGKPERPPKPGPPVQPRATE
RPDQYGPNICDGDFDTVAMLRGEMFVFKGRWFWRVRHNRVLDNYPMPIGHFWRGLPGDIS
AAYERQDGRFVFFKGDRYWLFREANLEPGYPQPLTSYGLGIPYDRIDTAIWWEPTGHTFF
FQEDRYWRFNEETQRGDPGYPKPISVWQGIPASPKGAFLSNDAAYTYFYKGTKYWKFDNE
RLRMEPGYPKSILRDFMGCQEHVEPGPRWPDVARPPFNPHGGAEPGADSAEGDVGDGDGD
FGAGVNKDGGSRVVVQMEEVARTVNVVMVLVPLLLLLCVLGLTYALVQMQRKGAPRVLLY
CKRSLQEWV
GenBank ID Protein 963056
UniProtKB/Swiss-Prot ID P51511
UniProtKB/Swiss-Prot Entry Name MMP15_HUMAN
PDB IDs Not Available
GenBank Gene ID Z48482
GeneCard ID MMP15
GenAtlas ID MMP15
HGNC ID HGNC:7161
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. Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. doi: 10.1016/j.molcel.2008.07.007. [PubMed:18691976 ]
  3. Sjoblom T, Jones S, Wood LD, Parsons DW, Lin J, Barber TD, Mandelker D, Leary RJ, Ptak J, Silliman N, Szabo S, Buckhaults P, Farrell C, Meeh P, Markowitz SD, Willis J, Dawson D, Willson JK, Gazdar AF, Hartigan J, Wu L, Liu C, Parmigiani G, Park BH, Bachman KE, Papadopoulos N, Vogelstein B, Kinzler KW, Velculescu VE: The consensus coding sequences of human breast and colorectal cancers. Science. 2006 Oct 13;314(5797):268-74. Epub 2006 Sep 7. [PubMed:16959974 ]
  4. Will H, Hinzmann B: cDNA sequence and mRNA tissue distribution of a novel human matrix metalloproteinase with a potential transmembrane segment. Eur J Biochem. 1995 Aug 1;231(3):602-8. [PubMed:7649159 ]
  5. Sato H, Tanaka M, Takino T, Inoue M, Seiki M: Assignment of the human genes for membrane-type-1, -2, and -3 matrix metalloproteinases (MMP14, MMP15, and MMP16) to 14q12.2, 16q12.2-q21, and 8q21, respectively, by in situ hybridization. Genomics. 1997 Feb 1;39(3):412-3. [PubMed:9119382 ]
  6. d'Ortho MP, Will H, Atkinson S, Butler G, Messent A, Gavrilovic J, Smith B, Timpl R, Zardi L, Murphy G: Membrane-type matrix metalloproteinases 1 and 2 exhibit broad-spectrum proteolytic capacities comparable to many matrix metalloproteinases. Eur J Biochem. 1997 Dec 15;250(3):751-7. [PubMed:9461298 ]