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metalloproteinase inhibitor 3 precursor [Homo sapiens]
NTR_TIMP domain-containing protein( domain architecture ID 10132426)
NTR_TIMP domain-containing protein
List of domain hits
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Name | Accession | Description | Interval | E-value | ||||
NTR_TIMP | cd03585 | NTR domain, TIMP subfamily; TIMPs, or tissue inibitors of metalloproteases, are essential ... |
24-200 | 5.12e-118 | ||||
NTR domain, TIMP subfamily; TIMPs, or tissue inibitors of metalloproteases, are essential regulators of extracellular matrix turnover and remodeling. They form complexes with matrix metalloproteases (MMPs) and inactivate them irreversibly by non-covalently binding their active zinc-binding sites. The levels of activated membrane-type MMPs, MMPs, and free TIMPs determine the balance between matrix degradation and matrix formation or stabilization. Consequently, TIMPs play roles in processes that require the remodeling and degradation of connective tissue, such as development, morphogenesis, wound healing, as well as in various diseases and pathological states such as tumor cell metastasis, arthritis, and artherosclerosis. Most TIMPs bind to a variety of MMPs. TIMP-1 and TIMP-2 appear to be multifunctional proteins with diverse biological action. They may exhibit growth factor-like activity and can inhibit angiogenesis. TIMP-3 has been implicated in apoptosis. : Pssm-ID: 239640 Cd Length: 183 Bit Score: 332.85 E-value: 5.12e-118
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Name | Accession | Description | Interval | E-value | ||||
NTR_TIMP | cd03585 | NTR domain, TIMP subfamily; TIMPs, or tissue inibitors of metalloproteases, are essential ... |
24-200 | 5.12e-118 | ||||
NTR domain, TIMP subfamily; TIMPs, or tissue inibitors of metalloproteases, are essential regulators of extracellular matrix turnover and remodeling. They form complexes with matrix metalloproteases (MMPs) and inactivate them irreversibly by non-covalently binding their active zinc-binding sites. The levels of activated membrane-type MMPs, MMPs, and free TIMPs determine the balance between matrix degradation and matrix formation or stabilization. Consequently, TIMPs play roles in processes that require the remodeling and degradation of connective tissue, such as development, morphogenesis, wound healing, as well as in various diseases and pathological states such as tumor cell metastasis, arthritis, and artherosclerosis. Most TIMPs bind to a variety of MMPs. TIMP-1 and TIMP-2 appear to be multifunctional proteins with diverse biological action. They may exhibit growth factor-like activity and can inhibit angiogenesis. TIMP-3 has been implicated in apoptosis. Pssm-ID: 239640 Cd Length: 183 Bit Score: 332.85 E-value: 5.12e-118
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NTR | smart00206 | Tissue inhibitor of metalloproteinase family; Form complexes with metalloproteinases, such as ... |
24-194 | 5.65e-111 | ||||
Tissue inhibitor of metalloproteinase family; Form complexes with metalloproteinases, such as collagenases, and irreversibly inactivate them. Pssm-ID: 128502 Cd Length: 172 Bit Score: 314.79 E-value: 5.65e-111
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TIMP | pfam00965 | Tissue inhibitor of metalloproteinase; Members of this family are common in extracellular ... |
22-194 | 6.36e-91 | ||||
Tissue inhibitor of metalloproteinase; Members of this family are common in extracellular regions of vertebrate species Pssm-ID: 460012 Cd Length: 183 Bit Score: 264.31 E-value: 6.36e-91
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Name | Accession | Description | Interval | E-value | ||||
NTR_TIMP | cd03585 | NTR domain, TIMP subfamily; TIMPs, or tissue inibitors of metalloproteases, are essential ... |
24-200 | 5.12e-118 | ||||
NTR domain, TIMP subfamily; TIMPs, or tissue inibitors of metalloproteases, are essential regulators of extracellular matrix turnover and remodeling. They form complexes with matrix metalloproteases (MMPs) and inactivate them irreversibly by non-covalently binding their active zinc-binding sites. The levels of activated membrane-type MMPs, MMPs, and free TIMPs determine the balance between matrix degradation and matrix formation or stabilization. Consequently, TIMPs play roles in processes that require the remodeling and degradation of connective tissue, such as development, morphogenesis, wound healing, as well as in various diseases and pathological states such as tumor cell metastasis, arthritis, and artherosclerosis. Most TIMPs bind to a variety of MMPs. TIMP-1 and TIMP-2 appear to be multifunctional proteins with diverse biological action. They may exhibit growth factor-like activity and can inhibit angiogenesis. TIMP-3 has been implicated in apoptosis. Pssm-ID: 239640 Cd Length: 183 Bit Score: 332.85 E-value: 5.12e-118
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NTR | smart00206 | Tissue inhibitor of metalloproteinase family; Form complexes with metalloproteinases, such as ... |
24-194 | 5.65e-111 | ||||
Tissue inhibitor of metalloproteinase family; Form complexes with metalloproteinases, such as collagenases, and irreversibly inactivate them. Pssm-ID: 128502 Cd Length: 172 Bit Score: 314.79 E-value: 5.65e-111
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TIMP | pfam00965 | Tissue inhibitor of metalloproteinase; Members of this family are common in extracellular ... |
22-194 | 6.36e-91 | ||||
Tissue inhibitor of metalloproteinase; Members of this family are common in extracellular regions of vertebrate species Pssm-ID: 460012 Cd Length: 183 Bit Score: 264.31 E-value: 6.36e-91
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NTR_TIMP_like | cd03577 | NTR domain, TIMP-like subfamily; TIMPs, or tissue inibitors of metalloproteases, are essential ... |
24-139 | 9.40e-35 | ||||
NTR domain, TIMP-like subfamily; TIMPs, or tissue inibitors of metalloproteases, are essential regulators of extracellular matrix turnover and remodeling. They form complexes with matrix metalloproteases (MMPs) and inactivate them irreversibly by non-covalently binding their active zinc-binding sites. This group contains domains similar to the TIMP NTR domain, which binds MMPs. Members of this group may or may not function as MMP inhibitors. Pssm-ID: 239632 Cd Length: 116 Bit Score: 119.39 E-value: 9.40e-35
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NTR_like | cd03523 | NTR_like domain; a beta barrel with an oligosaccharide/oligonucleotide-binding fold found in ... |
34-136 | 2.81e-14 | ||||
NTR_like domain; a beta barrel with an oligosaccharide/oligonucleotide-binding fold found in netrins, complement proteins, tissue inhibitors of metalloproteases (TIMP), and procollagen C-proteinase enhancers (PCOLCE), amongst others. In netrins, the domain plays a role in controlling axon branching in neural development, while the common function of these modules in TIMPs appears to be binding to metzincins. A subset of this family is also known as the C345C domain because it occurs as a C-terminal domain in complement C3, C4 and C5. In C5, the domain interacts with various partners during the formation of the membrane attack complex. Pssm-ID: 239600 Cd Length: 105 Bit Score: 65.95 E-value: 2.81e-14
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Blast search parameters | ||||
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