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Identification
HMDB Protein ID HMDBP07805
Secondary Accession Numbers
  • 13514
Name Matrix metalloproteinase-16
Synonyms
  1. MMP-16
  2. MMP-X2
  3. MT-MMP 3
  4. MT3-MMP
  5. MT3MMP
  6. MTMMP3
  7. Membrane-type matrix metalloproteinase 3
  8. Membrane-type-3 matrix metalloproteinase
Gene Name MMP16
Protein Type Unknown
Biological Properties
General Function Involved in metalloendopeptidase activity
Specific Function Endopeptidase that degrades various components of the extracellular matrix, such as collagen type III and fibronectin. Activates progelatinase A. Involved in the matrix remodeling of blood vessels. Isoform short cleaves fibronectin and also collagen type III, but at lower rate. It has no effect on type I, II, IV and V collagen. However, upon interaction with CSPG4, it may be involved in degradation and invasion of type I collagen by melanoma cells
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. extracellular space
  2. extracellular matrix
  3. Cell surface
  4. Isoform Short:Secreted
Gene Properties
Chromosome Location Chromosome:8
Locus 8q21.3
SNPs MMP16
Gene Sequence
>1824 bp
ATGATCTTACTCACATTCAGCACTGGAAGACGGTTGGATTTCGTGCATCATTCGGGGGTG
TTTTTCTTGCAAACCTTGCTTTGGATTTTATGTGCTACAGTCTGCGGAACGGAGCAGTAT
TTCAATGTGGAGGTTTGGTTACAAAAGTACGGCTACCTTCCACCGACTGACCCCAGAATG
TCAGTGCTGCGCTCTGCAGAGACCATGCAGTCTGCCCTAGCTGCCATGCAGCAGTTCTAT
GGCATTAACATGACAGGAAAAGTGGACAGAAACACAATTGACTGGATGAAGAAGCCCCGA
TGCGGTGTACCTGACCAGACAAGAGGTAGCTCCAAATTTCATATTCGTCGAAAGCGATAT
GCATTGACAGGACAGAAATGGCAGCACAAGCACATCACTTACAGTATAAAGAACGTAACT
CCAAAAGTAGGAGACCCTGAGACTCGTAAAGCTATTCGCCGTGCCTTTGATGTGTGGCAG
AATGTAACTCCTCTGACATTTGAAGAAGTTCCCTACAGTGAATTAGAAAATGGCAAACGT
GATGTGGATATAACCATTATTTTTGCATCTGGTTTCCATGGGGACAGCTCTCCCTTTGAT
GGAGAGGGAGGATTTTTGGCACATGCCTACTTCCCTGGACCAGGAATTGGAGGAGATACC
CATTTTGACTCAGATGAGCCATGGACACTAGGAAATCCTAATCATGATGGAAATGACTTA
TTTCTTGTAGCAGTCCATGAACTGGGACATGCTCTGGGATTGGAGCATTCCAATGACCCC
ACTGCCATCATGGCTCCATTTTACCAGTACATGGAAACAGACAACTTCAAACTACCTAAT
GATGATTTACAGGGCATCCAGAAAATATATGGTCCACCTGACAAGATTCCTCCACCTACA
AGACCTCTACCGACAGTGCCCCCACACCGCTCTATTCCTCCGGCTGACCCAAGGAAAAAT
GACAGGCCAAAACCTCCTCGGCCTCCAACCGGCAGACCCTCCTATCCCGGAGCCAAACCC
AACATCTGTGATGGGAACTTTAACACTCTAGCTATTCTTCGTCGTGAGATGTTTGTTTTC
AAGGACCAGTGGTTTTGGCGAGTGAGAAACAACAGGGTGATGGATGGATACCCAATGCAA
ATTACTTACTTCTGGCGGGGCTTGCCTCCTAGTATCGATGCAGTTTATGAAAATAGCGAC
GGGAATTTTGTGTTCTTTAAAGGTAACAAATATTGGGTGTTCAAGGATACAACTCTTCAA
CCTGGTTACCCTCATGACTTGATAACCCTTGGAAGTGGAATTCCCCCTCATGGTATTGAT
TCAGCCATTTGGTGGGAGGACGTCGGGAAAACCTATTTCTTCAAGGGAGACAGATATTGG
AGATATAGTGAAGAAATGAAAACAATGGACCCTGGCTATCCCAAGCCAATCACAGTCTGG
AAAGGGATCCCTGAATCTCCTCAGGGAGCATTTGTACACAAAGAAAATGGCTTTACGTAT
TTCTACAAAGGAAAGGAGTATTGGAAATTCAACAACCAGATACTCAAGGTAGAACCTGGA
CATCCAAGATCCATCCTCAAGGATTTTATGGGCTGTGATGGACCAACAGACAGAGTTAAA
GAAGGACACAGCCCACCAGATGATGTAGACATTGTCATCAAACTGGACAACACAGCCAGC
ACTGTGAAAGCCATAGCTATTGTCATTCCCTGCATCTTGGCCTTATGCCTCCTTGTATTG
GTTTACACTGTGTTCCAGTTCAAGAGGAAAGGAACACCCCGCCACATACTGTACTGTAAA
CGCTCTATGCAAGAGTGGGTGTGA
Protein Properties
Number of Residues 607
Molecular Weight 69521.0
Theoretical pI 8.74
Pfam Domain Function
Signals
  • 1-31
Transmembrane Regions
  • 565-585
Protein Sequence
>Matrix metalloproteinase-16
MILLTFSTGRRLDFVHHSGVFFLQTLLWILCATVCGTEQYFNVEVWLQKYGYLPPTDPRM
SVLRSAETMQSALAAMQQFYGINMTGKVDRNTIDWMKKPRCGVPDQTRGSSKFHIRRKRY
ALTGQKWQHKHITYSIKNVTPKVGDPETRKAIRRAFDVWQNVTPLTFEEVPYSELENGKR
DVDITIIFASGFHGDSSPFDGEGGFLAHAYFPGPGIGGDTHFDSDEPWTLGNPNHDGNDL
FLVAVHELGHALGLEHSNDPTAIMAPFYQYMETDNFKLPNDDLQGIQKIYGPPDKIPPPT
RPLPTVPPHRSIPPADPRKNDRPKPPRPPTGRPSYPGAKPNICDGNFNTLAILRREMFVF
KDQWFWRVRNNRVMDGYPMQITYFWRGLPPSIDAVYENSDGNFVFFKGNKYWVFKDTTLQ
PGYPHDLITLGSGIPPHGIDSAIWWEDVGKTYFFKGDRYWRYSEEMKTMDPGYPKPITVW
KGIPESPQGAFVHKENGFTYFYKGKEYWKFNNQILKVEPGYPRSILKDFMGCDGPTDRVK
EGHSPPDDVDIVIKLDNTASTVKAIAIVIPCILALCLLVLVYTVFQFKRKGTPRHILYCK
RSMQEWV
GenBank ID Protein 2662306
UniProtKB/Swiss-Prot ID P51512
UniProtKB/Swiss-Prot Entry Name MMP16_HUMAN
PDB IDs
GenBank Gene ID AB009303
GeneCard ID MMP16
GenAtlas ID MMP16
HGNC ID HGNC:7162
References
General References
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  3. Rikova K, Guo A, Zeng Q, Possemato A, Yu J, Haack H, Nardone J, Lee K, Reeves C, Li Y, Hu Y, Tan Z, Stokes M, Sullivan L, Mitchell J, Wetzel R, Macneill J, Ren JM, Yuan J, Bakalarski CE, Villen J, Kornhauser JM, Smith B, Li D, Zhou X, Gygi SP, Gu TL, Polakiewicz RD, Rush J, Comb MJ: Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer. Cell. 2007 Dec 14;131(6):1190-203. [PubMed:18083107 ]
  4. Takino T, Sato H, Shinagawa A, Seiki M: Identification of the second membrane-type matrix metalloproteinase (MT-MMP-2) gene from a human placenta cDNA library. MT-MMPs form a unique membrane-type subclass in the MMP family. J Biol Chem. 1995 Sep 29;270(39):23013-20. [PubMed:7559440 ]
  5. Matsumoto S, Katoh M, Saito S, Watanabe T, Masuho Y: Identification of soluble type of membrane-type matrix metalloproteinase-3 formed by alternatively spliced mRNA. Biochim Biophys Acta. 1997 Nov 1;1354(2):159-70. [PubMed:9396633 ]
  6. Shofuda K, Yasumitsu H, Nishihashi A, Miki K, Miyazaki K: Expression of three membrane-type matrix metalloproteinases (MT-MMPs) in rat vascular smooth muscle cells and characterization of MT3-MMPs with and without transmembrane domain. J Biol Chem. 1997 Apr 11;272(15):9749-54. [PubMed:9092507 ]
  7. Iida J, Pei D, Kang T, Simpson MA, Herlyn M, Furcht LT, McCarthy JB: Melanoma chondroitin sulfate proteoglycan regulates matrix metalloproteinase-dependent human melanoma invasion into type I collagen. J Biol Chem. 2001 Jun 1;276(22):18786-94. Epub 2001 Mar 6. [PubMed:11278606 ]