Refining structural and functional predictions for secretasome components by comparative sequence analysis.
Comparative sequence analysis of presenilins reveals the conserved transmembrane domain shared with leukocyte antigen CD47, possibly involved in signal transduction. Sensitive techniques of multiple sequence alignment extend the earlier observation of the aminopeptidase homology domain in nicastrin to suggest that this protein may be a catalytically active component of secretasome involved in proteolysis or co-proteolysis of presenilin or beta-amyloid.
Mushegian
Arcady
A
Stowers Institute for Medical Research, Kansas City, Missouri, USA. arm@stowers-institute.org
D000595:Amino Acid Sequence; D053829:Amyloid Precursor Protein Secretases; D015703:Antigens, CD / Q000737:chemistry; D051928:CD47 Antigen; D002352:Carrier Proteins / Q000737:chemistry; D020134:Catalytic Domain; D017124:Conserved Sequence; D005544:Forecasting; D006801:Humans; D008562:Membrane Glycoproteins / Q000737:chemistry* / Q000502:physiology*; D008565:Membrane Proteins / Q000737:chemistry* / Q000502:physiology*; D008969:Molecular Sequence Data; D010447:Peptide Hydrolases / Q000737:chemistry; D053764:Presenilin-1; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D016415:Sequence Alignment; D020539:Sequence Analysis, Protein; D013329:Structure-Activity Relationship
D015703:Antigens, CD; D051928:CD47 Antigen; C497894:CD47 protein, human; D002352:Carrier Proteins; D008562:Membrane Glycoproteins; D008565:Membrane Proteins; C508853:PSEN1 protein, human; D053764:Presenilin-1; C413604:nicastrin protein; D053829:Amyloid Precursor Protein Secretases; D010447:Peptide Hydrolases