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Conserved domains on  [gi|4507515|ref|NP_003247|]
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metalloproteinase inhibitor 4 precursor [Homo sapiens]

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 ...
 30-213 3.52e-114

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: 323.99  E-value: 3.52e-114
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507515   30 CSCAPAHPQQHICHSALVIRAKISSEKVVPASADPADTEKMLRYEIKQIKMFKGFEKVKDVQYIYTPFDSSLCGVKLEAN 109
Cdd:cd03585   1 CSCAPVHPQQAFCNSDIVIRAKIVGEKEVDSGNDYGNPIKRIQYEIKQIKMFKGFDKDKDIQYIYTPASSSLCGVKLDVN 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507515  110 SQKQYLLTGQVLsDGKVFIHLCNYIEPWEDLSLVQRESLNHHYHLNCGCQITTCYTVPCTISAPNECLWTDWLLERKLYG 189
Cdd:cd03585  81 GKKEYLISGKVE-GGKVHITLCDFVEPWDSLSLTQKKGLNHRYQMGCECKITPCYTIPCFVSSPNECLWTDWLSEKSING 159

                       170       180
                ....*....|....*....|....
gi 4507515  190 YQAQHYVCMKHVDGTCSWYRGHLP 213
Cdd:cd03585 160 HQAKHYACIKRSDGSCSWYRGGAP 183
 
Name Accession Description Interval E-value
NTR_TIMP cd03585
NTR domain, TIMP subfamily; TIMPs, or tissue inibitors of metalloproteases, are essential ...
 30-213 3.52e-114

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: 323.99  E-value: 3.52e-114
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507515   30 CSCAPAHPQQHICHSALVIRAKISSEKVVPASADPADTEKMLRYEIKQIKMFKGFEKVKDVQYIYTPFDSSLCGVKLEAN 109
Cdd:cd03585   1 CSCAPVHPQQAFCNSDIVIRAKIVGEKEVDSGNDYGNPIKRIQYEIKQIKMFKGFDKDKDIQYIYTPASSSLCGVKLDVN 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507515  110 SQKQYLLTGQVLsDGKVFIHLCNYIEPWEDLSLVQRESLNHHYHLNCGCQITTCYTVPCTISAPNECLWTDWLLERKLYG 189
Cdd:cd03585  81 GKKEYLISGKVE-GGKVHITLCDFVEPWDSLSLTQKKGLNHRYQMGCECKITPCYTIPCFVSSPNECLWTDWLSEKSING 159

                       170       180
                ....*....|....*....|....
gi 4507515  190 YQAQHYVCMKHVDGTCSWYRGHLP 213
Cdd:cd03585 160 HQAKHYACIKRSDGSCSWYRGGAP 183
NTR smart00206
Tissue inhibitor of metalloproteinase family; Form complexes with metalloproteinases, such as ...
 30-207 2.22e-104

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


Pssm-ID: 128502  Cd Length: 172  Bit Score: 298.61  E-value: 2.22e-104
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507515      30 CSCAPAHPQQHICHSALVIRAKISSEKVVPASAdpadtEKMLRYEIKQIKMFKGFEKVKDVQYIYTPFDSSLCGVKLEAN 109
Cdd:smart00206   1 CSCSPPHPQTAFCNSDLVIRAKFVGKKEVNEGN-----TLYQRYEIKQTKMFKGFDKLGDIRFIYTPASESLCGYKLESQ 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507515     110 SQKQYLLTGQVLsDGKVFIHLCNYIEPWEDLSLVQRESLNHHYHLNCGCQITTCYTVPCTISAPNECLWTDWLLERKLYG 189
Cdd:smart00206  76 NKEEYLIAGRLE-DGKMHITLCSFVVPWDSLSLAQRKGLNKRYHAGCECKIFPCYSIPCKLSSDTECLWTDQLLEGSEKG 154

                          170
                   ....*....|....*...
gi 4507515     190 YQAQHYVCMKHVDGTCSW 207
Cdd:smart00206 155 YQSKHYACIPREPGLCTW 172
TIMP pfam00965
Tissue inhibitor of metalloproteinase; Members of this family are common in extracellular ...
 28-207 4.03e-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: 265.46  E-value: 4.03e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507515     28 EACSCAPAHPQQHICHSALVIRAKISSEKVVPASADPADTE-KMLRYEIKQIKMFKGFEKV---KDVQYIYTPFDSSLCG 103
Cdd:pfam00965   1 EACSCSPSHPQQAFCNADVVIRAKVVGEKEVKTGNDMYGPPiKNIVYEIKQIKMFKGPQLVgkaADIQAVYTPPSSSLCG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507515    104 VKLEANSqKQYLLTGQVLSDGKVFIHLCNYIEPWEDLSLVQRESLNHHYHLNCGCQITTCYTVPCTISAPNECLWTDWLL 183
Cdd:pfam00965  81 VTLELNG-KEYLIAGKLVSDGKLHVTLCNFVEPWETLTLAQRRGLNQRYGMGCDCKITPCSSIPCSLSSPGECLWTDWVL 159

                         170       180
                  ....*....|....*....|....
gi 4507515    184 ERKLYGYQAQHYVCMKHVDGTCSW 207
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 ...
 30-213 3.52e-114

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: 323.99  E-value: 3.52e-114
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507515   30 CSCAPAHPQQHICHSALVIRAKISSEKVVPASADPADTEKMLRYEIKQIKMFKGFEKVKDVQYIYTPFDSSLCGVKLEAN 109
Cdd:cd03585   1 CSCAPVHPQQAFCNSDIVIRAKIVGEKEVDSGNDYGNPIKRIQYEIKQIKMFKGFDKDKDIQYIYTPASSSLCGVKLDVN 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507515  110 SQKQYLLTGQVLsDGKVFIHLCNYIEPWEDLSLVQRESLNHHYHLNCGCQITTCYTVPCTISAPNECLWTDWLLERKLYG 189
Cdd:cd03585  81 GKKEYLISGKVE-GGKVHITLCDFVEPWDSLSLTQKKGLNHRYQMGCECKITPCYTIPCFVSSPNECLWTDWLSEKSING 159

                       170       180
                ....*....|....*....|....
gi 4507515  190 YQAQHYVCMKHVDGTCSWYRGHLP 213
Cdd:cd03585 160 HQAKHYACIKRSDGSCSWYRGGAP 183
NTR smart00206
Tissue inhibitor of metalloproteinase family; Form complexes with metalloproteinases, such as ...
 30-207 2.22e-104

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


Pssm-ID: 128502  Cd Length: 172  Bit Score: 298.61  E-value: 2.22e-104
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507515      30 CSCAPAHPQQHICHSALVIRAKISSEKVVPASAdpadtEKMLRYEIKQIKMFKGFEKVKDVQYIYTPFDSSLCGVKLEAN 109
Cdd:smart00206   1 CSCSPPHPQTAFCNSDLVIRAKFVGKKEVNEGN-----TLYQRYEIKQTKMFKGFDKLGDIRFIYTPASESLCGYKLESQ 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507515     110 SQKQYLLTGQVLsDGKVFIHLCNYIEPWEDLSLVQRESLNHHYHLNCGCQITTCYTVPCTISAPNECLWTDWLLERKLYG 189
Cdd:smart00206  76 NKEEYLIAGRLE-DGKMHITLCSFVVPWDSLSLAQRKGLNKRYHAGCECKIFPCYSIPCKLSSDTECLWTDQLLEGSEKG 154

                          170
                   ....*....|....*...
gi 4507515     190 YQAQHYVCMKHVDGTCSW 207
Cdd:smart00206 155 YQSKHYACIPREPGLCTW 172
TIMP pfam00965
Tissue inhibitor of metalloproteinase; Members of this family are common in extracellular ...
 28-207 4.03e-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: 265.46  E-value: 4.03e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507515     28 EACSCAPAHPQQHICHSALVIRAKISSEKVVPASADPADTE-KMLRYEIKQIKMFKGFEKV---KDVQYIYTPFDSSLCG 103
Cdd:pfam00965   1 EACSCSPSHPQQAFCNADVVIRAKVVGEKEVKTGNDMYGPPiKNIVYEIKQIKMFKGPQLVgkaADIQAVYTPPSSSLCG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507515    104 VKLEANSqKQYLLTGQVLSDGKVFIHLCNYIEPWEDLSLVQRESLNHHYHLNCGCQITTCYTVPCTISAPNECLWTDWLL 183
Cdd:pfam00965  81 VTLELNG-KEYLIAGKLVSDGKLHVTLCNFVEPWETLTLAQRRGLNQRYGMGCDCKITPCSSIPCSLSSPGECLWTDWVL 159

                         170       180
                  ....*....|....*....|....
gi 4507515    184 ERKLYGYQAQHYVCMKHVDGTCSW 207
Cdd:pfam00965 160 EKDVNGCQAKHYACIKRSDGSCAW 183
NTR_TIMP_like cd03577
NTR domain, TIMP-like subfamily; TIMPs, or tissue inibitors of metalloproteases, are essential ...
 30-152 2.01e-30

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: 108.60  E-value: 2.01e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507515   30 CSCAPAHPQQHICHSALVIRAKISSEKVVpasadpaDTEKMLRYEIKQIKMFKGFEKVKDVQYIYTPFDSSLCGVKLEan 109
Cdd:cd03577   1 CSCMPQHPQEKYCQADFVIKVKVLKKKLD-------GAGLNIRYTIEIKKVYKGSEKSLLPITIYTPSDDSACGIPLL-- 71

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 4507515  110 SQKQYLLTGQVlSDGKVFIHLCNYIEPWEDLSLVQRESLNHHY 152
Cdd:cd03577  72 EGKEYLIAGKV-EDGALHTTLCDGVAPWDDLTKEQKRGLKGLY 113
NTR_like cd03523
NTR_like domain; a beta barrel with an oligosaccharide/oligonucleotide-binding fold found in ...
 39-150 1.71e-16

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: 72.12  E-value: 1.71e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507515   39 QHICHSALVIRAKISSEKVVPASadpadtekmLRYEIKQIKMFKGFEKVKDVQYIYTPFDSSLCGVK-LEANSQKQYLLT 117
Cdd:cd03523   1 KAFCKSDYVVRAKIKEIKEENDD---------VKYEVKIIKIYKTGKAKADKADLRFYYTAPACCPChPILNPGREYLIM 71

                        90       100       110
                ....*....|....*....|....*....|....
gi 4507515  118 GQV-LSDGKVFIHLCNYIEPWEDLSLVQRESLNH 150
Cdd:cd03523  72 GKEeDSQGGLVLDPLSFVEPWSPLSLRQDRRLRE 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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