The primary structure of mouse saposin.
The primary structure of mouse sphingolipid activator protein (saposin) was determined by cDNA sequencing. The amino acid sequence predicted by the cDNA sequence revealed that mouse saposin was highly homologous to human saposin and also to rat sertoli cell glycoprotein. Mouse saposin also has four functional domains, which are structurally similar to each other, and each domain has cysteines, prolines, and a potential glycosylation site at an almost identical position. An amino acid comparison between human and mouse saposins revealed that the similarity was approximately 70%, and human saposin lacks thirty-one amino acids between domains C and D. Heterogeneities of mRNA were found in both the coding and noncoding regions.
Tsuda
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M
Department of Pediatrics, Nihon University, School of Medicine, Tokyo, Japan.
Sakiyama
T
T
Endo
H
H
Kitagawa
T
T
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D003001:Cloning, Molecular; D004247:DNA / Q000235:genetics* / Q000302:isolation & purification; D015723:Gene Library; D006023:Glycoproteins / Q000737:chemistry / Q000235:genetics*; D006801:Humans; D008099:Liver / Q000378:metabolism*; D008297:Male; D051379:Mice; D008969:Molecular Sequence Data; D012333:RNA, Messenger / Q000235:genetics; D051381:Rats; D015183:Restriction Mapping; D049231:Saposins; D012689:Sequence Homology, Nucleic Acid; D012708:Sertoli Cells / Q000378:metabolism; D049128:Sphingolipid Activator Proteins
D006023:Glycoproteins; C483345:PSAP protein, human; C483344:Psap protein, mouse; C483347:Psap protein, rat; D012333:RNA, Messenger; D049231:Saposins; D049128:Sphingolipid Activator Proteins; D004247:DNA