| Predicate | Object |
|---|---|
| rdf:type | |
| biopax3:comment |
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. COFACTOR: Binds 1 zinc ion per subunit (By similarity). COFACTOR: Calcium (By similarity). ENZYME REGULATION: TIMP-2 shows little inhibitory activity compared to TIMP-1. TIMP-1 seems to have less binding affinity than TIMP-2 for the short isoform. SUBUNIT: Interacts with CSPG4 through CSPG4 chondroitin sulfate glycosaminoglycan. SUBCELLULAR LOCATION: Isoform Long: Cell membrane; Single-pass type I membrane protein; Extracellular side (Potential). Note=Localized at the cell surface of melanoma cells. SUBCELLULAR LOCATION: Isoform Short: Secreted, extracellular space, extracellular matrix. Cell surface. Note=Localized at the cell surface of melanoma cells. ALTERNATIVE PRODUCTS: Event=Alternative splicing; Named isoforms=2; Name=Long; IsoId=P51512-1; Sequence=Displayed; Name=Short; Synonyms=SM3; IsoId=P51512-2; Sequence=VSP_005453, VSP_005454; TISSUE SPECIFICITY: Expressed in heart, brain, placenta, ovary and small intestine. Isoform Short is found in the ovary. DEVELOPMENTAL STAGE: Expressed in tissues undergoing reconstruction. Present in fetal tissues, especially in brain. Expression seems to decline with advanced development. DOMAIN: The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme. PTM: The precursor is cleaved by a furin endopeptidase (By similarity). SIMILARITY: Belongs to the peptidase M10A family. SIMILARITY: Contains 4 hemopexin-like domains. WEB RESOURCE: Name=NIEHS-SNPs; URL="http://egp.gs.washington.edu/data/mmp16/"; GENE SYNONYMS:MMP16 MMPX2. COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.,
SEQUENCE 607 AA; 69521 MW; 30D6247D9CB21663 CRC64;
|
| biopax3:xref |
urn:biopax:RelationshipXref:HGNC_HGNC:7162,
urn:biopax:RelationshipXref:NCBI GENE_4325,
urn:biopax:RelationshipXref:REFSEQ_NP_005932,
urn:biopax:UnificationXref:UNIPROT_B2RAN7,
urn:biopax:UnificationXref:UNIPROT_P51512,
urn:biopax:UnificationXref:UNIPROT_Q14824,
urn:biopax:UnificationXref:UNIPROT_Q52H48
|
| biopax3:displayName |
MMP16_HUMAN
|
| biopax3:name |
3.4.24.-,
MMP-16,
MMP-X2,
MMP16,
MT-MMP 3,
MT3-MMP,
MT3MMP,
MTMMP3,
Membrane-type matrix metalloproteinase 3,
Membrane-type-3 matrix metalloproteinase
|
| biopax3:entityFeature | |
| biopax3:organism | |
| biopax3:sequence |
MILLTFSTGRRLDFVHHSGVFFLQTLLWILCATVCGTEQYFNVEVWLQKYGYLPPTDPRMSVLRSAETMQSALAAMQQFYGINMTGKVDRNTIDWMKKPRCGVPDQTRGSSKFHIRRKRYALTGQKWQHKHITYSIKNVTPKVGDPETRKAIRRAFDVWQNVTPLTFEEVPYSELENGKRDVDITIIFASGFHGDSSPFDGEGGFLAHAYFPGPGIGGDTHFDSDEPWTLGNPNHDGNDLFLVAVHELGHALGLEHSNDPTAIMAPFYQYMETDNFKLPNDDLQGIQKIYGPPDKIPPPTRPLPTVPPHRSIPPADPRKNDRPKPPRPPTGRPSYPGAKPNICDGNFNTLAILRREMFVFKDQWFWRVRNNRVMDGYPMQITYFWRGLPPSIDAVYENSDGNFVFFKGNKYWVFKDTTLQPGYPHDLITLGSGIPPHGIDSAIWWEDVGKTYFFKGDRYWRYSEEMKTMDPGYPKPITVWKGIPESPQGAFVHKENGFTYFYKGKEYWKFNNQILKVEPGYPRSILKDFMGCDGPTDRVKEGHSPPDDVDIVIKLDNTASTVKAIAIVIPCILALCLLVLVYTVFQFKRKGTPRHILYCKRSMQEWV
|
| biopax3:standardName |
Matrix metalloproteinase-16
|