PREDICTED: amyloid-like protein 2 isoform X2 [Nanorana parkeri]
Protein Classification
List of domain hits
| Name | Accession | Description | Interval | E-value | ||||
| APP_E2 | pfam12925 | E2 domain of amyloid precursor protein; The E2 domain is the largest of the conserved domains ... |
297-479 | 1.71e-91 | ||||
E2 domain of amyloid precursor protein; The E2 domain is the largest of the conserved domains of the amyloid precursor protein. The structure of E2 consists of two coiled-coil sub-structures connected through a continuous helix, and bears an unexpected resemblance to the spectrin family of protein structures.E 2 can reversibly dimerize in solution, and the dimerization occurs along the longest dimension of the molecule in an antiparallel orientation, which enables the N-terminal substructure of one monomer to pack against the C-terminal substructure of a second monomer. The high degree of conservation of residues at the putative dimer interface suggests that the E2 dimer observed in the crystal could be physiologically relevant. Heparin sulfate proteoglycans, the putative ligands for the precursor present in extracellular matrix, bind to E2 at a conserved and positively charged site near the dimer interface. : Pssm-ID: 463752 Cd Length: 190 Bit Score: 282.31 E-value: 1.71e-91
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| A4_EXTRA super family | cl30964 | amyloid A4; amyloid A4 precursor of Alzheimers disease |
36-195 | 1.94e-85 | ||||
amyloid A4; amyloid A4 precursor of Alzheimers disease The actual alignment was detected with superfamily member smart00006: Pssm-ID: 128326 [Multi-domain] Cd Length: 165 Bit Score: 265.52 E-value: 1.94e-85
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| JMTM_Notch_APP super family | cl41775 | juxtamembrane and transmembrane (JMTM) domain found in Notch and APP family proteins; The ... |
605-682 | 2.99e-49 | ||||
juxtamembrane and transmembrane (JMTM) domain found in Notch and APP family proteins; The substrates of gamma-secretase include amyloid precursor protein (APP) and the Notch receptor. APP, also called APPI, or Alzheimer disease amyloid protein (ABPP), or amyloid precursor protein, or amyloid-beta A4 protein, or cerebral vascular amyloid peptide (CVAP), or PreA4, or protease nexin-II (PN-II), functions as a cell surface receptor and performs physiological functions on the surface of neurons relevant to neurite growth, neuronal adhesion and axonogenesis. Notch proteins are a family of type-1 transmembrane proteins that form a core component of the Notch signaling pathway. They operate in a variety of different tissues and play a role in a variety of developmental processes by controlling cell fate decisions. Successive cleavage of the APP carboxyl-terminal fragment generates amyloid-beta (Abeta) peptides of varying lengths. Accumulation of Abeta peptides such as Abeta42 and Abeta43 leads to formation of amyloid plaques in the brain, a hallmark of Alzheimer's disease. Notch cleavage is involved in cell-fate determination during development and neurogenesis. The model corresponds to the juxtamembrane and transmembrane (JMTM) domain found in Notch and APP family proteins. It comprises a transmembrane helix (TM) with adjacent juxtamembrane (JM) regions. The JMTM domain is likely to be recognized by gamma-secretase in a similar fashion to both Notch and APP family proteins. The actual alignment was detected with superfamily member cd21709: Pssm-ID: 425406 Cd Length: 81 Bit Score: 166.64 E-value: 2.99e-49
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| Name | Accession | Description | Interval | E-value | ||||
| APP_E2 | pfam12925 | E2 domain of amyloid precursor protein; The E2 domain is the largest of the conserved domains ... |
297-479 | 1.71e-91 | ||||
E2 domain of amyloid precursor protein; The E2 domain is the largest of the conserved domains of the amyloid precursor protein. The structure of E2 consists of two coiled-coil sub-structures connected through a continuous helix, and bears an unexpected resemblance to the spectrin family of protein structures.E 2 can reversibly dimerize in solution, and the dimerization occurs along the longest dimension of the molecule in an antiparallel orientation, which enables the N-terminal substructure of one monomer to pack against the C-terminal substructure of a second monomer. The high degree of conservation of residues at the putative dimer interface suggests that the E2 dimer observed in the crystal could be physiologically relevant. Heparin sulfate proteoglycans, the putative ligands for the precursor present in extracellular matrix, bind to E2 at a conserved and positively charged site near the dimer interface. Pssm-ID: 463752 Cd Length: 190 Bit Score: 282.31 E-value: 1.71e-91
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| A4_EXTRA | smart00006 | amyloid A4; amyloid A4 precursor of Alzheimers disease |
36-195 | 1.94e-85 | ||||
amyloid A4; amyloid A4 precursor of Alzheimers disease Pssm-ID: 128326 [Multi-domain] Cd Length: 165 Bit Score: 265.52 E-value: 1.94e-85
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| APP_N | pfam02177 | Amyloid A4 N-terminal heparin-binding; This N-terminal domain of APP, amyloid precursor ... |
38-138 | 8.15e-51 | ||||
Amyloid A4 N-terminal heparin-binding; This N-terminal domain of APP, amyloid precursor protein, is the heparin-binding domain of the protein. this region is also responsible for stimulation of neurite outgrowth. The structure reveals both a highly charged basic surface that may interact with glycosaminoglycans in the brain and an abutting hydrophobic surface that is proposed to play an important functional role such as in dimerization or ligand-binding. Structural similarities with cysteine-rich growth factors, taken together with its known growth-promoting properties, suggest the APP N-terminal domain could function as a growth factor in vivo. Pssm-ID: 460474 Cd Length: 100 Bit Score: 171.72 E-value: 8.15e-51
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| JMTM_APLP2 | cd21709 | juxtamembrane and transmembrane (JMTM) domain found in amyloid-like protein 2 (APLP-2) and ... |
605-682 | 2.99e-49 | ||||
juxtamembrane and transmembrane (JMTM) domain found in amyloid-like protein 2 (APLP-2) and similar proteins; Amyloid-like protein 2 (APLP-2), also called amyloid protein homolog (APPH), or CDEI box-binding protein (CDEBP), may play a role in the regulation of hemostasis. Its soluble form may have inhibitory properties towards coagulation factors. APLP-2 may bind to the DNA 5'-GTCACATG-3'(CDEI box). It inhibits trypsin, chymotrypsin, plasmin, factor XIA, and plasma and glandular kallikrein. This model corresponds to juxtamembrane and transmembrane (JMTM) domain of APLP-2, which consists of the intact transmembrane (TM) domain with adjacent N-terminal juxtamembrane (JM) region. Pssm-ID: 411992 Cd Length: 81 Bit Score: 166.64 E-value: 2.99e-49
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| APP_amyloid | pfam10515 | Beta-amyloid precursor protein C-terminus; This is the amyloid, C-terminal, protein of the ... |
631-681 | 6.62e-25 | ||||
Beta-amyloid precursor protein C-terminus; This is the amyloid, C-terminal, protein of the beta-Amyloid precursor protein (APP) which is a conserved and ubiquitous transmembrane glycoprotein strongly implicated in the pathogenesis of Alzheimer's disease but whose normal biological function is unknown. The C-terminal 100 residues are released and aggregate into amyloid deposits which are strongly implicated in the pathology of Alzheimer's disease plaque-formation. The domain is associated with family A4_EXTRA, pfam02177, further towards the N-terminus. Pssm-ID: 463129 Cd Length: 52 Bit Score: 97.79 E-value: 6.62e-25
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| SMC_prok_A | TIGR02169 | chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
320-527 | 8.87e-04 | ||||
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins] Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 42.75 E-value: 8.87e-04
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| Name | Accession | Description | Interval | E-value | ||||
| APP_E2 | pfam12925 | E2 domain of amyloid precursor protein; The E2 domain is the largest of the conserved domains ... |
297-479 | 1.71e-91 | ||||
E2 domain of amyloid precursor protein; The E2 domain is the largest of the conserved domains of the amyloid precursor protein. The structure of E2 consists of two coiled-coil sub-structures connected through a continuous helix, and bears an unexpected resemblance to the spectrin family of protein structures.E 2 can reversibly dimerize in solution, and the dimerization occurs along the longest dimension of the molecule in an antiparallel orientation, which enables the N-terminal substructure of one monomer to pack against the C-terminal substructure of a second monomer. The high degree of conservation of residues at the putative dimer interface suggests that the E2 dimer observed in the crystal could be physiologically relevant. Heparin sulfate proteoglycans, the putative ligands for the precursor present in extracellular matrix, bind to E2 at a conserved and positively charged site near the dimer interface. Pssm-ID: 463752 Cd Length: 190 Bit Score: 282.31 E-value: 1.71e-91
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| A4_EXTRA | smart00006 | amyloid A4; amyloid A4 precursor of Alzheimers disease |
36-195 | 1.94e-85 | ||||
amyloid A4; amyloid A4 precursor of Alzheimers disease Pssm-ID: 128326 [Multi-domain] Cd Length: 165 Bit Score: 265.52 E-value: 1.94e-85
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| APP_N | pfam02177 | Amyloid A4 N-terminal heparin-binding; This N-terminal domain of APP, amyloid precursor ... |
38-138 | 8.15e-51 | ||||
Amyloid A4 N-terminal heparin-binding; This N-terminal domain of APP, amyloid precursor protein, is the heparin-binding domain of the protein. this region is also responsible for stimulation of neurite outgrowth. The structure reveals both a highly charged basic surface that may interact with glycosaminoglycans in the brain and an abutting hydrophobic surface that is proposed to play an important functional role such as in dimerization or ligand-binding. Structural similarities with cysteine-rich growth factors, taken together with its known growth-promoting properties, suggest the APP N-terminal domain could function as a growth factor in vivo. Pssm-ID: 460474 Cd Length: 100 Bit Score: 171.72 E-value: 8.15e-51
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| JMTM_APLP2 | cd21709 | juxtamembrane and transmembrane (JMTM) domain found in amyloid-like protein 2 (APLP-2) and ... |
605-682 | 2.99e-49 | ||||
juxtamembrane and transmembrane (JMTM) domain found in amyloid-like protein 2 (APLP-2) and similar proteins; Amyloid-like protein 2 (APLP-2), also called amyloid protein homolog (APPH), or CDEI box-binding protein (CDEBP), may play a role in the regulation of hemostasis. Its soluble form may have inhibitory properties towards coagulation factors. APLP-2 may bind to the DNA 5'-GTCACATG-3'(CDEI box). It inhibits trypsin, chymotrypsin, plasmin, factor XIA, and plasma and glandular kallikrein. This model corresponds to juxtamembrane and transmembrane (JMTM) domain of APLP-2, which consists of the intact transmembrane (TM) domain with adjacent N-terminal juxtamembrane (JM) region. Pssm-ID: 411992 Cd Length: 81 Bit Score: 166.64 E-value: 2.99e-49
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| JMTM_APLP1 | cd21708 | juxtamembrane and transmembrane (JMTM) domain found in amyloid-like protein 1 (APLP-1) and ... |
599-682 | 3.05e-37 | ||||
juxtamembrane and transmembrane (JMTM) domain found in amyloid-like protein 1 (APLP-1) and similar proteins; Amyloid-like protein 1 (APLP-1), also called APLP, may play a role in postsynaptic function. It couples to JIP signal transduction through C-terminal binding. APLP-1 may interact with cellular G-protein signaling pathways. It can regulate neurite outgrowth through binding to components of the extracellular matrix such as heparin and collagen I. This model corresponds to the juxtamembrane and transmembrane (JMTM) domain of APLP-1, which consists of the intact transmembrane (TM) domain with adjacent N-terminal juxtamembrane (JM) region. Pssm-ID: 411991 Cd Length: 85 Bit Score: 133.80 E-value: 3.05e-37
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| APP_Cu_bd | pfam12924 | Copper-binding of amyloid precursor, CuBD; This short domain, part of the extra-cellular ... |
140-195 | 2.57e-30 | ||||
Copper-binding of amyloid precursor, CuBD; This short domain, part of the extra-cellular N-terminus of the amyloid precursor protein, APP, can bind both copper and zinc, CuBD. The structure of Cu2+-bound CuBD reveals that the metal ligands are His147, His151, Tyr168 and two water molecules, which are arranged in a square pyramidal geometry. The structure of Cu+-bound CuBD is almost identical to the Cu2+-bound structure except for the loss of one of the water ligands. The geometry of the site is unfavourable for Cu+, thus providing a mechanism by which CuBD could readily transfer Cu ions to other proteins. Pssm-ID: 463751 Cd Length: 56 Bit Score: 113.14 E-value: 2.57e-30
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| APP_amyloid | pfam10515 | Beta-amyloid precursor protein C-terminus; This is the amyloid, C-terminal, protein of the ... |
631-681 | 6.62e-25 | ||||
Beta-amyloid precursor protein C-terminus; This is the amyloid, C-terminal, protein of the beta-Amyloid precursor protein (APP) which is a conserved and ubiquitous transmembrane glycoprotein strongly implicated in the pathogenesis of Alzheimer's disease but whose normal biological function is unknown. The C-terminal 100 residues are released and aggregate into amyloid deposits which are strongly implicated in the pathology of Alzheimer's disease plaque-formation. The domain is associated with family A4_EXTRA, pfam02177, further towards the N-terminus. Pssm-ID: 463129 Cd Length: 52 Bit Score: 97.79 E-value: 6.62e-25
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| JMTM_APP_like | cd21699 | juxtamembrane and transmembrane (JMTM) domain found in the amyloid-beta precursor protein (APP) ... |
611-641 | 7.47e-07 | ||||
juxtamembrane and transmembrane (JMTM) domain found in the amyloid-beta precursor protein (APP) family; The amyloid-beta precursor protein (APP) family includes amyloid-like proteins APLP-1 and APLP-2. APP (also called ABPP, APPI, Alzheimer disease (AD) amyloid protein, amyloid precursor protein, amyloid-beta A4 protein, cerebral vascular amyloid peptide (CVAP), PreA4, or protease nexin-II (PN-II)) functions as a cell surface receptor and performs physiological functions on the surface of neurons relevant to neurite growth, neuronal adhesion and axonogenesis. Amyloid-beta peptides are lipophilic metal chelators with metal-reducing activity; they bind transient metals such as copper, zinc and iron. APLP-1, also called APLP, may play a role in postsynaptic function. It couples to JIP signal transduction through C-terminal binding. APLP-1 may interact with cellular G-protein signaling pathways. It can regulate neurite outgrowth through binding to components of the extracellular matrix such as heparin and collagen I. APLP-2 (also called amyloid protein homolog (APPH), or CDEI box-binding protein (CDEBP)) may play a role in the regulation of hemostasis. Its soluble form may have inhibitory properties towards coagulation factors. APLP-2 may bind to the DNA 5'-GTCACATG-3'(CDEI box). It inhibits trypsin, chymotrypsin, plasmin, factor XIA, and plasma and glandular kallikrein. This model corresponds to juxtamembrane and transmembrane (JMTM) domain of APP, which consists of the intact transmembrane (TM) domain with adjacent N-terminal juxtamembrane (JM) region. More than half of all familial APP mutations of Alzheimer's disease are seen in its JMTM domain region. Pssm-ID: 411982 Cd Length: 41 Bit Score: 46.12 E-value: 7.47e-07
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| SMC_prok_A | TIGR02169 | chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
320-527 | 8.87e-04 | ||||
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins] Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 42.75 E-value: 8.87e-04
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| JMTM_APP | cd21707 | juxtamembrane and transmembrane (JMTM) domain found in amyloid-beta precursor protein (APP) ... |
613-641 | 5.21e-03 | ||||
juxtamembrane and transmembrane (JMTM) domain found in amyloid-beta precursor protein (APP) and similar proteins; Amyloid-beta precursor protein (APP), also called APPI, ABPP, Alzheimer disease amyloid protein, amyloid precursor protein, amyloid-beta A4 protein, cerebral vascular amyloid peptide (CVAP), PreA4, or protease nexin-II (PN-II), functions as a cell surface receptor and performs physiological functions on the surface of neurons relevant to neurite growth, neuronal adhesion and axonogenesis. Amyloid-beta peptides are lipophilic metal chelators with metal-reducing activity; they bind transient metals such as copper, zinc and iron. This model corresponds to juxtamembrane and transmembrane (JMTM) domain of APP, which consists of the intact transmembrane (TM) domain with adjacent N-terminal juxtamembrane (JM) region. More than half of all familial APP mutations of Alzheimer's disease are seen in its JMTM domain region. Pssm-ID: 411990 Cd Length: 40 Bit Score: 35.31 E-value: 5.21e-03
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| Blast search parameters | ||||
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