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Conserved domains on  [gi|1877782180|pdb|6TI5|B]
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Chain B, Amyloid-beta precursor protein

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Beta-APP super family cl04111
Beta-amyloid peptide (beta-APP);
5-40 2.48e-13

Beta-amyloid peptide (beta-APP);


The actual alignment was detected with superfamily member pfam03494:

Pssm-ID: 427335  Cd Length: 39  Bit Score: 56.00  E-value: 2.48e-13
                         10        20        30
                 ....*....|....*....|....*....|....*.
6TI5_B         5 RHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV 40
Cdd:pfam03494  2 RQSAGYEVYHEKLVFLAEDMGSNKGAIIGLMVGGVV 37
 
Name Accession Description Interval E-value
Beta-APP pfam03494
Beta-amyloid peptide (beta-APP);
5-40 2.48e-13

Beta-amyloid peptide (beta-APP);


Pssm-ID: 427335  Cd Length: 39  Bit Score: 56.00  E-value: 2.48e-13
                         10        20        30
                 ....*....|....*....|....*....|....*.
6TI5_B         5 RHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV 40
Cdd:pfam03494  2 RQSAGYEVYHEKLVFLAEDMGSNKGAIIGLMVGGVV 37
JMTM_APP cd21707
juxtamembrane and transmembrane (JMTM) domain found in amyloid-beta precursor protein (APP) ...
 16-40 1.26e-07

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: 41.86  E-value: 1.26e-07
                       10        20
               ....*....|....*....|....*
6TI5_B      16 KLVFFAEDVGSNKGAIIGLMVGGVV 40
Cdd:cd21707  1 KLVFFAEDVGSNKGAIIGLMVGGVV 25
 
Name Accession Description Interval E-value
Beta-APP pfam03494
Beta-amyloid peptide (beta-APP);
5-40 2.48e-13

Beta-amyloid peptide (beta-APP);


Pssm-ID: 427335  Cd Length: 39  Bit Score: 56.00  E-value: 2.48e-13
                         10        20        30
                 ....*....|....*....|....*....|....*.
6TI5_B         5 RHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV 40
Cdd:pfam03494  2 RQSAGYEVYHEKLVFLAEDMGSNKGAIIGLMVGGVV 37
JMTM_APP cd21707
juxtamembrane and transmembrane (JMTM) domain found in amyloid-beta precursor protein (APP) ...
 16-40 1.26e-07

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: 41.86  E-value: 1.26e-07
                       10        20
               ....*....|....*....|....*
6TI5_B      16 KLVFFAEDVGSNKGAIIGLMVGGVV 40
Cdd:cd21707  1 KLVFFAEDVGSNKGAIIGLMVGGVV 25
JMTM_Notch_APP cd21700
juxtamembrane and transmembrane (JMTM) domain found in Notch and APP family proteins; The ...
 17-40 8.44e-03

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.


Pssm-ID: 411983  Cd Length: 41  Bit Score: 29.67  E-value: 8.44e-03
                       10        20
               ....*....|....*....|....
6TI5_B      17 LVFFAEDVGSNKGAIIGLMVGGVV 40
Cdd:cd21700  1 LPFFALDDGSGKGAIIGLLVGAVV 24
 
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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