Matrix metalloproteinase-15

Details

Name
Matrix metalloproteinase-15
Synonyms
  • 3.4.24.-
  • Membrane-type matrix metalloproteinase 2
  • Membrane-type-2 matrix metalloproteinase
  • MMP-15
  • MT-MMP 2
  • MT2-MMP
  • MT2MMP
  • MTMMP2
  • SMCP-2
Gene Name
MMP15
Organism
Humans
Amino acid sequence
>lcl|BSEQ0007094|Matrix metalloproteinase-15
MGSDPSAPGRPGWTGSLLGDREEAARPRLLPLLLVLLGCLGLGVAAEDAEVHAENWLRLY
GYLPQPSRHMSTMRSAQILASALAEMQRFYGIPVTGVLDEETKEWMKRPRCGVPDQFGVR
VKANLRRRRKRYALTGRKWNNHHLTFSIQNYTEKLGWYHSMEAVRRAFRVWEQATPLVFQ
EVPYEDIRLRRQKEADIMVLFASGFHGDSSPFDGTGGFLAHAYFPGPGLGGDTHFDADEP
WTFSSTDLHGNNLFLVAVHELGHALGLEHSSNPNAIMAPFYQWKDVDNFKLPEDDLRGIQ
QLYGTPDGQPQPTQPLPTVTPRRPGRPDHRPPRPPQPPPPGGKPERPPKPGPPVQPRATE
RPDQYGPNICDGDFDTVAMLRGEMFVFKGRWFWRVRHNRVLDNYPMPIGHFWRGLPGDIS
AAYERQDGRFVFFKGDRYWLFREANLEPGYPQPLTSYGLGIPYDRIDTAIWWEPTGHTFF
FQEDRYWRFNEETQRGDPGYPKPISVWQGIPASPKGAFLSNDAAYTYFYKGTKYWKFDNE
RLRMEPGYPKSILRDFMGCQEHVEPGPRWPDVARPPFNPHGGAEPGADSAEGDVGDGDGD
FGAGVNKDGGSRVVVQMEEVARTVNVVMVLVPLLLLLCVLGLTYALVQMQRKGAPRVLLY
CKRSLQEWV
Number of residues
669
Molecular Weight
75806.45
Theoretical pI
7.49
GO Classification
Functions
calcium ion binding / enzyme activator activity / metalloendopeptidase activity / zinc ion binding
Processes
cellular protein modification process / collagen catabolic process / endodermal cell differentiation / extracellular matrix disassembly / extracellular matrix organization / positive regulation of catalytic activity / response to estradiol
Components
extracellular matrix / integral component of plasma membrane / plasma membrane
General Function
Zinc ion binding
Specific Function
Endopeptidase that degrades various components of the extracellular matrix. May activate progelatinase A.
Pfam Domain Function
Transmembrane Regions
626-646
Cellular Location
Membrane
Gene sequence
>lcl|BSEQ0020708|Matrix metalloproteinase-15 (MMP15)
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
Chromosome Location
16
Locus
16q13-q21
External Identifiers
ResourceLink
UniProtKB IDP51511
UniProtKB Entry NameMMP15_HUMAN
GenBank Protein ID963056
GenBank Gene IDZ48482
HGNC IDHGNC:7161
General References
  1. 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. [Article]
  2. 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]
  3. 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. [Article]
  4. 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. [Article]
  5. 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. [Article]
  6. Bian Y, Song C, Cheng K, Dong M, Wang F, Huang J, Sun D, Wang L, Ye M, Zou H: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. J Proteomics. 2014 Jan 16;96:253-62. doi: 10.1016/j.jprot.2013.11.014. Epub 2013 Nov 22. [Article]
  7. 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. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB00786MarimastatinvestigationalyesinhibitorDetails