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disintegrin and metalloproteinase domain-containing protein 17 isoform 2 [Homo sapiens]
ZnMc_TACE_like and ADAM17_MPD domain-containing protein( domain architecture ID 10857782)
protein containing domains ZnMc_TACE_like, DISIN, and ADAM17_MPD
List of domain hits
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Name | Accession | Description | Interval | E-value | |||||
ZnMc_TACE_like | cd04270 | Zinc-dependent metalloprotease; TACE_like subfamily. TACE, the tumor-necrosis factor-alpha ... |
3-257 | 3.23e-154 | |||||
Zinc-dependent metalloprotease; TACE_like subfamily. TACE, the tumor-necrosis factor-alpha converting enzyme, releases soluble TNF-alpha from transmembrane pro-TNF-alpha. : Pssm-ID: 239798 [Multi-domain] Cd Length: 244 Bit Score: 442.58 E-value: 3.23e-154
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ADAM17_MPD | pfam16698 | Membrane-proximal domain, switch, for ADAM17; ADAM17_MPD is the membrane-proximal domain of a ... |
361-422 | 3.02e-31 | |||||
Membrane-proximal domain, switch, for ADAM17; ADAM17_MPD is the membrane-proximal domain of a family of disintegrin and metalloproteinase domain-containing protein 17 found in metazoan species. ADAM17 is a major sheddase that is responsible for the regulation of a wide range of biological processes, such as cellular differentiation, regeneration, and cancer progression. This MPD region acts as the sheddase switch. PDI or protein-disulfide isomerase interacts with ADAM17 and to down-regulate its enzymatic activity. The interaction is directly with the MPD, the region of dimerization and substrate recognition, where it catalyzes an isomerization of disulfide bridges within the thioredoxin motif CXXC. this isomerization results in a major structural change between an active, open state and an inactive, closed state of the MPD. This change is thought to act as a molecular switch, allowing a global reorientation of the extracellular domains in ADAM17 and regulating its shedding activity. : Pssm-ID: 465239 Cd Length: 62 Bit Score: 115.52 E-value: 3.02e-31
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DISIN | smart00050 | Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ... |
264-340 | 1.53e-22 | |||||
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to integrin receptors. They contain a 'RGD' sequence, identical to the recognition site of many adhesion proteins. Molecules containing both disintegrin and metalloprotease domains are known as ADAMs. : Pssm-ID: 214490 Cd Length: 75 Bit Score: 91.60 E-value: 1.53e-22
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Name | Accession | Description | Interval | E-value | |||||
ZnMc_TACE_like | cd04270 | Zinc-dependent metalloprotease; TACE_like subfamily. TACE, the tumor-necrosis factor-alpha ... |
3-257 | 3.23e-154 | |||||
Zinc-dependent metalloprotease; TACE_like subfamily. TACE, the tumor-necrosis factor-alpha converting enzyme, releases soluble TNF-alpha from transmembrane pro-TNF-alpha. Pssm-ID: 239798 [Multi-domain] Cd Length: 244 Bit Score: 442.58 E-value: 3.23e-154
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ADAM17_MPD | pfam16698 | Membrane-proximal domain, switch, for ADAM17; ADAM17_MPD is the membrane-proximal domain of a ... |
361-422 | 3.02e-31 | |||||
Membrane-proximal domain, switch, for ADAM17; ADAM17_MPD is the membrane-proximal domain of a family of disintegrin and metalloproteinase domain-containing protein 17 found in metazoan species. ADAM17 is a major sheddase that is responsible for the regulation of a wide range of biological processes, such as cellular differentiation, regeneration, and cancer progression. This MPD region acts as the sheddase switch. PDI or protein-disulfide isomerase interacts with ADAM17 and to down-regulate its enzymatic activity. The interaction is directly with the MPD, the region of dimerization and substrate recognition, where it catalyzes an isomerization of disulfide bridges within the thioredoxin motif CXXC. this isomerization results in a major structural change between an active, open state and an inactive, closed state of the MPD. This change is thought to act as a molecular switch, allowing a global reorientation of the extracellular domains in ADAM17 and regulating its shedding activity. Pssm-ID: 465239 Cd Length: 62 Bit Score: 115.52 E-value: 3.02e-31
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Reprolysin_2 | pfam13574 | Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ... |
26-238 | 8.69e-31 | |||||
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the characteriztic binding motif HExxGHxxGxxH of Reprolysin-like peptidases of family M12B. Pssm-ID: 372637 Cd Length: 193 Bit Score: 118.89 E-value: 8.69e-31
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ADAM17_MPD | cd14246 | Membrane-proximal domain of a disintegrin and metalloprotease 17 (ADAM17); ADAM17 is a ... |
360-422 | 1.20e-23 | |||||
Membrane-proximal domain of a disintegrin and metalloprotease 17 (ADAM17); ADAM17 is a multi-domain protein that acts as a sheddase; is involved in the cleavage and release of the soluble ectodomain of tumor necrosis factor alpha from the cell surface and in the trans-Golgi network, as well as in the release of various other targets such as cytokines and cell adhesion molecules. This links ADAM17 to a variety of biological processes, including cellular differentiation and the progression of cancer. It was shown that the enzymatic activity of ADAM17 is regulated via a protein-disulfide isomerase (PDI). Specifically, the disulfide bridges within a CxxC motif of the membrane-proximal domain (MPD) are isomerized by PDI; the conversion triggers a conformational change between a closed and an opened form of the MPD, which may constitute a molecular switch that triggers the shedding activity of ADAM17. Pssm-ID: 271205 Cd Length: 60 Bit Score: 93.98 E-value: 1.20e-23
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DISIN | smart00050 | Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ... |
264-340 | 1.53e-22 | |||||
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to integrin receptors. They contain a 'RGD' sequence, identical to the recognition site of many adhesion proteins. Molecules containing both disintegrin and metalloprotease domains are known as ADAMs. Pssm-ID: 214490 Cd Length: 75 Bit Score: 91.60 E-value: 1.53e-22
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Disintegrin | pfam00200 | Disintegrin; |
264-338 | 6.26e-20 | |||||
Disintegrin; Pssm-ID: 459709 Cd Length: 74 Bit Score: 83.83 E-value: 6.26e-20
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myxo_disulf_rpt | TIGR02232 | Myxococcus cysteine-rich repeat; This model represents a sequence region shared between ... |
258-294 | 4.14e-03 | |||||
Myxococcus cysteine-rich repeat; This model represents a sequence region shared between several proteins of Myxococcus xanthus DK 1622 and some eukaryotic proteins that include human pappalysin-1 (SP|Q13219). The region of about 40 amino acids contains several conserved Cys residues presumed to form disulfide bonds. The region appears in up to 13 repeats in Myxococcus. Pssm-ID: 200169 [Multi-domain] Cd Length: 38 Bit Score: 35.43 E-value: 4.14e-03
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Name | Accession | Description | Interval | E-value | |||||
ZnMc_TACE_like | cd04270 | Zinc-dependent metalloprotease; TACE_like subfamily. TACE, the tumor-necrosis factor-alpha ... |
3-257 | 3.23e-154 | |||||
Zinc-dependent metalloprotease; TACE_like subfamily. TACE, the tumor-necrosis factor-alpha converting enzyme, releases soluble TNF-alpha from transmembrane pro-TNF-alpha. Pssm-ID: 239798 [Multi-domain] Cd Length: 244 Bit Score: 442.58 E-value: 3.23e-154
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ZnMc_ADAM_like | cd04267 | Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ... |
3-243 | 2.62e-60 | |||||
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ADAM family of metalloproteases contains proteolytic domains from snake venoms, proteases from the mammalian reproductive tract, and the tumor necrosis factor alpha convertase, TACE. ADAMs (A Disintegrin And Metalloprotease) are glycoproteins, which play roles in cell signaling, cell fusion, and cell-cell interactions. Pssm-ID: 239795 Cd Length: 192 Bit Score: 198.80 E-value: 2.62e-60
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ADAM17_MPD | pfam16698 | Membrane-proximal domain, switch, for ADAM17; ADAM17_MPD is the membrane-proximal domain of a ... |
361-422 | 3.02e-31 | |||||
Membrane-proximal domain, switch, for ADAM17; ADAM17_MPD is the membrane-proximal domain of a family of disintegrin and metalloproteinase domain-containing protein 17 found in metazoan species. ADAM17 is a major sheddase that is responsible for the regulation of a wide range of biological processes, such as cellular differentiation, regeneration, and cancer progression. This MPD region acts as the sheddase switch. PDI or protein-disulfide isomerase interacts with ADAM17 and to down-regulate its enzymatic activity. The interaction is directly with the MPD, the region of dimerization and substrate recognition, where it catalyzes an isomerization of disulfide bridges within the thioredoxin motif CXXC. this isomerization results in a major structural change between an active, open state and an inactive, closed state of the MPD. This change is thought to act as a molecular switch, allowing a global reorientation of the extracellular domains in ADAM17 and regulating its shedding activity. Pssm-ID: 465239 Cd Length: 62 Bit Score: 115.52 E-value: 3.02e-31
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Reprolysin_2 | pfam13574 | Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ... |
26-238 | 8.69e-31 | |||||
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the characteriztic binding motif HExxGHxxGxxH of Reprolysin-like peptidases of family M12B. Pssm-ID: 372637 Cd Length: 193 Bit Score: 118.89 E-value: 8.69e-31
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ZnMc | cd00203 | Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ... |
3-242 | 1.73e-28 | |||||
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major branches, the astacin-like proteases and the adamalysin/reprolysin-like proteases. Both branches have wide phylogenetic distribution, and contain sub-families, which are involved in vertebrate development and disease. Pssm-ID: 238124 [Multi-domain] Cd Length: 167 Bit Score: 111.46 E-value: 1.73e-28
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Reprolysin_5 | pfam13688 | Metallo-peptidase family M12; |
3-231 | 6.94e-27 | |||||
Metallo-peptidase family M12; Pssm-ID: 372673 Cd Length: 191 Bit Score: 107.89 E-value: 6.94e-27
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ADAM17_MPD | cd14246 | Membrane-proximal domain of a disintegrin and metalloprotease 17 (ADAM17); ADAM17 is a ... |
360-422 | 1.20e-23 | |||||
Membrane-proximal domain of a disintegrin and metalloprotease 17 (ADAM17); ADAM17 is a multi-domain protein that acts as a sheddase; is involved in the cleavage and release of the soluble ectodomain of tumor necrosis factor alpha from the cell surface and in the trans-Golgi network, as well as in the release of various other targets such as cytokines and cell adhesion molecules. This links ADAM17 to a variety of biological processes, including cellular differentiation and the progression of cancer. It was shown that the enzymatic activity of ADAM17 is regulated via a protein-disulfide isomerase (PDI). Specifically, the disulfide bridges within a CxxC motif of the membrane-proximal domain (MPD) are isomerized by PDI; the conversion triggers a conformational change between a closed and an opened form of the MPD, which may constitute a molecular switch that triggers the shedding activity of ADAM17. Pssm-ID: 271205 Cd Length: 60 Bit Score: 93.98 E-value: 1.20e-23
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DISIN | smart00050 | Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ... |
264-340 | 1.53e-22 | |||||
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to integrin receptors. They contain a 'RGD' sequence, identical to the recognition site of many adhesion proteins. Molecules containing both disintegrin and metalloprotease domains are known as ADAMs. Pssm-ID: 214490 Cd Length: 75 Bit Score: 91.60 E-value: 1.53e-22
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Disintegrin | pfam00200 | Disintegrin; |
264-338 | 6.26e-20 | |||||
Disintegrin; Pssm-ID: 459709 Cd Length: 74 Bit Score: 83.83 E-value: 6.26e-20
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ZnMc_adamalysin_II_like | cd04269 | Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ... |
6-249 | 2.08e-19 | |||||
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom zinc endopeptidase. This subfamily contains other snake venom metalloproteinases, as well as membrane-anchored metalloproteases belonging to the ADAM family. ADAMs (A Disintegrin And Metalloprotease) are glycoproteins, which play roles in cell signaling, cell fusion, and cell-cell interactions. Pssm-ID: 239797 [Multi-domain] Cd Length: 194 Bit Score: 86.52 E-value: 2.08e-19
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ZnMc_ADAMTS_like | cd04273 | Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ... |
7-249 | 2.24e-13 | |||||
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) are glycoproteins, which play roles in cell signaling, cell fusion, and cell-cell interactions. This particular subfamily represents domain architectures that combine ADAM-like metalloproteinases with thrombospondin type-1 repeats. ADAMTS (a disintegrin and metalloproteinase with thrombospondin motifs) proteinases are inhibited by TIMPs (tissue inhibitors of metalloproteinases), and they play roles in coagulation, angiogenesis, development and progression of arthritis. They hydrolyze the von Willebrand factor precursor and various components of the extracellular matrix. Pssm-ID: 239801 Cd Length: 207 Bit Score: 69.19 E-value: 2.24e-13
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Reprolysin | pfam01421 | Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ... |
7-253 | 9.08e-12 | |||||
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that cleave peptides. These proteases require zinc for catalysis. Members of this family are also known as adamalysins. Most members of this family are snake venom endopeptidases, but there are also some mammalian proteins such as Swiss:P78325, and fertilin. Fertilin and closely related proteins appear to not have some active site residues and may not be active enzymes. Pssm-ID: 426256 [Multi-domain] Cd Length: 200 Bit Score: 64.63 E-value: 9.08e-12
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Reprolysin_3 | pfam13582 | Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ... |
83-196 | 7.08e-10 | |||||
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the characteriztic binding motif HExxGHxxGxxH of Reprolysin-like peptidases of family M12B. Pssm-ID: 463926 [Multi-domain] Cd Length: 122 Bit Score: 56.99 E-value: 7.08e-10
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ZnMc_salivary_gland_MPs | cd04272 | Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary ... |
6-251 | 1.56e-06 | |||||
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary glands of arthropods. Pssm-ID: 239800 Cd Length: 220 Bit Score: 49.27 E-value: 1.56e-06
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ZnMc_ADAM_fungal | cd04271 | Zinc-dependent metalloprotease, ADAM_fungal subgroup. The adamalysin_like or ADAM (A ... |
181-245 | 3.16e-06 | |||||
Zinc-dependent metalloprotease, ADAM_fungal subgroup. The adamalysin_like or ADAM (A Disintegrin And Metalloprotease) family of metalloproteases are integral membrane proteases acting on a variety of extracellular targets. They are involved in shedding soluble peptides or proteins from the cell surface. This subfamily contains fungal ADAMs, whose precise function has yet to be determined. Pssm-ID: 239799 [Multi-domain] Cd Length: 228 Bit Score: 48.57 E-value: 3.16e-06
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Reprolysin_4 | pfam13583 | Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ... |
114-248 | 1.09e-03 | |||||
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the characteriztic binding motif HExxGHxxGxxH of Reprolysin-like peptidases of family M12B. Pssm-ID: 404471 Cd Length: 203 Bit Score: 40.68 E-value: 1.09e-03
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myxo_disulf_rpt | TIGR02232 | Myxococcus cysteine-rich repeat; This model represents a sequence region shared between ... |
258-294 | 4.14e-03 | |||||
Myxococcus cysteine-rich repeat; This model represents a sequence region shared between several proteins of Myxococcus xanthus DK 1622 and some eukaryotic proteins that include human pappalysin-1 (SP|Q13219). The region of about 40 amino acids contains several conserved Cys residues presumed to form disulfide bonds. The region appears in up to 13 repeats in Myxococcus. Pssm-ID: 200169 [Multi-domain] Cd Length: 38 Bit Score: 35.43 E-value: 4.14e-03
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ZnMc_MMP_like | cd04268 | Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ... |
118-225 | 6.70e-03 | |||||
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix metalloproteinases (MMPs), serralysins, and the astacin_like family of proteases. Pssm-ID: 239796 [Multi-domain] Cd Length: 165 Bit Score: 37.86 E-value: 6.70e-03
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Blast search parameters | ||||
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