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Conserved domains on  [gi|31543867|ref|NP_035724|]
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metalloproteinase inhibitor 2 precursor [Mus musculus]

Protein Classification

NTR_TIMP domain-containing protein( domain architecture ID 10132426)

NTR_TIMP domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
NTR_TIMP cd03585
NTR domain, TIMP subfamily; TIMPs, or tissue inibitors of metalloproteases, are essential ...
 27-209 3.04e-121

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: 341.32  E-value: 3.04e-121
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543867  27 CSCSPVHPQQAFCNADVVIRAKAVSEKEVDSGNDiYGNPIKRIQYEIKQIKMFKGPD--KDIEFIYTAPSSAVCGVSLDV 104
Cdd:cd03585   1 CSCAPVHPQQAFCNSDIVIRAKIVGEKEVDSGND-YGNPIKRIQYEIKQIKMFKGFDkdKDIQYIYTPASSSLCGVKLDV 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543867 105 GGKKEYLIAGKAEgDGKMHITLCDFIVPWDTLSITQKKSLNHRYQMGCECKITRCPMIPCYISSPDECLWMDWVTEKSIN 184
Cdd:cd03585  80 NGKKEYLISGKVE-GGKVHITLCDFVEPWDSLSLTQKKGLNHRYQMGCECKITPCYTIPCFVSSPNECLWTDWLSEKSIN 158

                       170       180
                ....*....|....*....|....*
gi 31543867 185 GHQAKFFACIKRSDGSCAWYRGAAP 209
Cdd:cd03585 159 GHQAKHYACIKRSDGSCSWYRGGAP 183
 
Name Accession Description Interval E-value
NTR_TIMP cd03585
NTR domain, TIMP subfamily; TIMPs, or tissue inibitors of metalloproteases, are essential ...
 27-209 3.04e-121

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: 341.32  E-value: 3.04e-121
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543867  27 CSCSPVHPQQAFCNADVVIRAKAVSEKEVDSGNDiYGNPIKRIQYEIKQIKMFKGPD--KDIEFIYTAPSSAVCGVSLDV 104
Cdd:cd03585   1 CSCAPVHPQQAFCNSDIVIRAKIVGEKEVDSGND-YGNPIKRIQYEIKQIKMFKGFDkdKDIQYIYTPASSSLCGVKLDV 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543867 105 GGKKEYLIAGKAEgDGKMHITLCDFIVPWDTLSITQKKSLNHRYQMGCECKITRCPMIPCYISSPDECLWMDWVTEKSIN 184
Cdd:cd03585  80 NGKKEYLISGKVE-GGKVHITLCDFVEPWDSLSLTQKKGLNHRYQMGCECKITPCYTIPCFVSSPNECLWTDWLSEKSIN 158

                       170       180
                ....*....|....*....|....*
gi 31543867 185 GHQAKFFACIKRSDGSCAWYRGAAP 209
Cdd:cd03585 159 GHQAKHYACIKRSDGSCSWYRGGAP 183
NTR smart00206
Tissue inhibitor of metalloproteinase family; Form complexes with metalloproteinases, such as ...
 27-203 7.14e-113

Tissue inhibitor of metalloproteinase family; Form complexes with metalloproteinases, such as collagenases, and irreversibly inactivate them.


Pssm-ID: 128502  Cd Length: 172  Bit Score: 319.80  E-value: 7.14e-113
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543867     27 CSCSPVHPQQAFCNADVVIRAKAVSEKEVDSGndiygnPIKRIQYEIKQIKMFKGPDK--DIEFIYTAPSSAVCGVSLDV 104
Cdd:smart00206   1 CSCSPPHPQTAFCNSDLVIRAKFVGKKEVNEG------NTLYQRYEIKQTKMFKGFDKlgDIRFIYTPASESLCGYKLES 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543867    105 GGKKEYLIAGKAEgDGKMHITLCDFIVPWDTLSITQKKSLNHRYQMGCECKITRCPMIPCYISSPDECLWMDWVTEKSIN 184
Cdd:smart00206  75 QNKEEYLIAGRLE-DGKMHITLCSFVVPWDSLSLAQRKGLNKRYHAGCECKIFPCYSIPCKLSSDTECLWTDQLLEGSEK 153

                          170
                   ....*....|....*....
gi 31543867    185 GHQAKFFACIKRSDGSCAW 203
Cdd:smart00206 154 GYQSKHYACIPREPGLCTW 172
TIMP pfam00965
Tissue inhibitor of metalloproteinase; Members of this family are common in extracellular ...
 25-203 9.56e-107

Tissue inhibitor of metalloproteinase; Members of this family are common in extracellular regions of vertebrate species


Pssm-ID: 460012  Cd Length: 183  Bit Score: 304.75  E-value: 9.56e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543867    25 DACSCSPVHPQQAFCNADVVIRAKAVSEKEVDSGNDIYGNPIKRIQYEIKQIKMFKGPDK-----DIEFIYTAPSSAVCG 99
Cdd:pfam00965   1 EACSCSPSHPQQAFCNADVVIRAKVVGEKEVKTGNDMYGPPIKNIVYEIKQIKMFKGPQLvgkaaDIQAVYTPPSSSLCG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543867   100 VSLDVGGKkEYLIAGKAEGDGKMHITLCDFIVPWDTLSITQKKSLNHRYQMGCECKITRCPMIPCYISSPDECLWMDWVT 179
Cdd:pfam00965  81 VTLELNGK-EYLIAGKLVSDGKLHVTLCNFVEPWETLTLAQRRGLNQRYGMGCDCKITPCSSIPCSLSSPGECLWTDWVL 159

                         170       180
                  ....*....|....*....|....
gi 31543867   180 EKSINGHQAKFFACIKRSDGSCAW 203
Cdd:pfam00965 160 EKDVNGCQAKHYACIKRSDGSCAW 183
 
Name Accession Description Interval E-value
NTR_TIMP cd03585
NTR domain, TIMP subfamily; TIMPs, or tissue inibitors of metalloproteases, are essential ...
 27-209 3.04e-121

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: 341.32  E-value: 3.04e-121
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543867  27 CSCSPVHPQQAFCNADVVIRAKAVSEKEVDSGNDiYGNPIKRIQYEIKQIKMFKGPD--KDIEFIYTAPSSAVCGVSLDV 104
Cdd:cd03585   1 CSCAPVHPQQAFCNSDIVIRAKIVGEKEVDSGND-YGNPIKRIQYEIKQIKMFKGFDkdKDIQYIYTPASSSLCGVKLDV 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543867 105 GGKKEYLIAGKAEgDGKMHITLCDFIVPWDTLSITQKKSLNHRYQMGCECKITRCPMIPCYISSPDECLWMDWVTEKSIN 184
Cdd:cd03585  80 NGKKEYLISGKVE-GGKVHITLCDFVEPWDSLSLTQKKGLNHRYQMGCECKITPCYTIPCFVSSPNECLWTDWLSEKSIN 158

                       170       180
                ....*....|....*....|....*
gi 31543867 185 GHQAKFFACIKRSDGSCAWYRGAAP 209
Cdd:cd03585 159 GHQAKHYACIKRSDGSCSWYRGGAP 183
NTR smart00206
Tissue inhibitor of metalloproteinase family; Form complexes with metalloproteinases, such as ...
 27-203 7.14e-113

Tissue inhibitor of metalloproteinase family; Form complexes with metalloproteinases, such as collagenases, and irreversibly inactivate them.


Pssm-ID: 128502  Cd Length: 172  Bit Score: 319.80  E-value: 7.14e-113
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543867     27 CSCSPVHPQQAFCNADVVIRAKAVSEKEVDSGndiygnPIKRIQYEIKQIKMFKGPDK--DIEFIYTAPSSAVCGVSLDV 104
Cdd:smart00206   1 CSCSPPHPQTAFCNSDLVIRAKFVGKKEVNEG------NTLYQRYEIKQTKMFKGFDKlgDIRFIYTPASESLCGYKLES 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543867    105 GGKKEYLIAGKAEgDGKMHITLCDFIVPWDTLSITQKKSLNHRYQMGCECKITRCPMIPCYISSPDECLWMDWVTEKSIN 184
Cdd:smart00206  75 QNKEEYLIAGRLE-DGKMHITLCSFVVPWDSLSLAQRKGLNKRYHAGCECKIFPCYSIPCKLSSDTECLWTDQLLEGSEK 153

                          170
                   ....*....|....*....
gi 31543867    185 GHQAKFFACIKRSDGSCAW 203
Cdd:smart00206 154 GYQSKHYACIPREPGLCTW 172
TIMP pfam00965
Tissue inhibitor of metalloproteinase; Members of this family are common in extracellular ...
 25-203 9.56e-107

Tissue inhibitor of metalloproteinase; Members of this family are common in extracellular regions of vertebrate species


Pssm-ID: 460012  Cd Length: 183  Bit Score: 304.75  E-value: 9.56e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543867    25 DACSCSPVHPQQAFCNADVVIRAKAVSEKEVDSGNDIYGNPIKRIQYEIKQIKMFKGPDK-----DIEFIYTAPSSAVCG 99
Cdd:pfam00965   1 EACSCSPSHPQQAFCNADVVIRAKVVGEKEVKTGNDMYGPPIKNIVYEIKQIKMFKGPQLvgkaaDIQAVYTPPSSSLCG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543867   100 VSLDVGGKkEYLIAGKAEGDGKMHITLCDFIVPWDTLSITQKKSLNHRYQMGCECKITRCPMIPCYISSPDECLWMDWVT 179
Cdd:pfam00965  81 VTLELNGK-EYLIAGKLVSDGKLHVTLCNFVEPWETLTLAQRRGLNQRYGMGCDCKITPCSSIPCSLSSPGECLWTDWVL 159

                         170       180
                  ....*....|....*....|....
gi 31543867   180 EKSINGHQAKFFACIKRSDGSCAW 203
Cdd:pfam00965 160 EKDVNGCQAKHYACIKRSDGSCAW 183
NTR_TIMP_like cd03577
NTR domain, TIMP-like subfamily; TIMPs, or tissue inibitors of metalloproteases, are essential ...
 27-151 3.59e-42

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: 138.65  E-value: 3.59e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543867  27 CSCSPVHPQQAFCNADVVIRAKAVSEKEVDSGNdiygnpikRIQYEIKQIKMFKGPDKD--IEFIYTAPSSAVCGVSLDV 104
Cdd:cd03577   1 CSCMPQHPQEKYCQADFVIKVKVLKKKLDGAGL--------NIRYTIEIKKVYKGSEKSllPITIYTPSDDSACGIPLLE 72

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 31543867 105 GgkKEYLIAGKAEgDGKMHITLCDFIVPWDTLSITQKKSLNHRYQMG 151
Cdd:cd03577  73 G--KEYLIAGKVE-DGALHTTLCDGVAPWDDLTKEQKRGLKGLYKKG 116
NTR_like cd03523
NTR_like domain; a beta barrel with an oligosaccharide/oligonucleotide-binding fold found in ...
 36-146 3.32e-28

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: 102.55  E-value: 3.32e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543867  36 QAFCNADVVIRAKAVSEKEVDsgndiygnpiKRIQYEIKQIKMFKGPD-----KDIEFIYTAPSSAVCgvSLDVGGKKEY 110
Cdd:cd03523   1 KAFCKSDYVVRAKIKEIKEEN----------DDVKYEVKIIKIYKTGKakadkADLRFYYTAPACCPC--HPILNPGREY 68

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 31543867 111 LIAGKAEGD-GKMHITLCDFIVPWDTLSITQKKSLNH 146
Cdd:cd03523  69 LIMGKEEDSqGGLVLDPLSFVEPWSPLSLRQDRRLRE 105
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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