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©) 1990 Oxford University Press
7184 Nucleic Acids Research, Vol. 18, No. 23
Nucleotide sequence of cathepsin D
cDNA encoding
a
mouse
J.F.Diedrich, K.A.Staskus, E.F.Retzel and A.T.Haase* Department of Microbiology, University of Minnesota, Minneapolis, MN 55455, USA Submitted June 13, 1990
We report the nucleotide sequence of mouse cathepsin D mRNA derived from clones in a XgtlO cDNA library constructed from C57BL/6J mouse brain. Cathepsin D is a lysosomal aspartyl protease, and this cDNA was isolated while screening for upregulated genes in scrapie (manuscript in preparation). The sequence is 1893 bp and contains an open reading frame of 1230 bp with an initiation codon at nucleotide position 7 and a termination codon at 1237. The predicted amino acid sequence (410 aa) shows 81 % similarity with the human kidney cathepsin D (1) and 82% with the porcine spleen cathepsin D (2, 3). ActiveME T
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L
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site aspartyl residues and the presumed polyadenylation signal within the 3' untranslated region are underlined.
REFERENCES
1. Faust,P.L., Kornfeld,S. and Chirgwin,J.M. (1985) Proc. Natl Acad. Sci. USA 82, 4910-4914. 2. Shewale,J.G. and Tang,J. (1984) Proc. Natl. Acad. Sci. USA 81, 3703 -3707. 3. Erickson,A.H., Conner,G.E. and Blobel,G. (1981) J. Biol. Chem. 256, 11224-11231.
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Note added in proof. Since the acceptance of this manuscript we have become aware of results by Grusby et al. (Nucl. Acids Res., vol. 18, p. 4008, 1990) concerning the cloning of a mouse cathepsin D cDNA. Their sequence shows one nucleotide difference (position 1681, A to T) in the 3' untranslated region when compared to the sequence given here. This sequence was accepted July 16, 1990. * To whom correspondence should be addressed
©) 1990 Oxford University Press
7184 Nucleic Acids Research, Vol. 18, No. 23
Nucleotide sequence of cathepsin D
cDNA encoding
a
mouse
J.F.Diedrich, K.A.Staskus, E.F.Retzel and A.T.Haase* Department of Microbiology, University of Minnesota, Minneapolis, MN 55455, USA Submitted June 13, 1990
We report the nucleotide sequence of mouse cathepsin D mRNA derived from clones in a XgtlO cDNA library constructed from C57BL/6J mouse brain. Cathepsin D is a lysosomal aspartyl protease, and this cDNA was isolated while screening for upregulated genes in scrapie (manuscript in preparation). The sequence is 1893 bp and contains an open reading frame of 1230 bp with an initiation codon at nucleotide position 7 and a termination codon at 1237. The predicted amino acid sequence (410 aa) shows 81 % similarity with the human kidney cathepsin D (1) and 82% with the porcine spleen cathepsin D (2, 3). ActiveME T
P
C
L
V
L
L
I
S
LL A
L
site aspartyl residues and the presumed polyadenylation signal within the 3' untranslated region are underlined.
REFERENCES
1. Faust,P.L., Kornfeld,S. and Chirgwin,J.M. (1985) Proc. Natl Acad. Sci. USA 82, 4910-4914. 2. Shewale,J.G. and Tang,J. (1984) Proc. Natl. Acad. Sci. USA 81, 3703 -3707. 3. Erickson,A.H., Conner,G.E. and Blobel,G. (1981) J. Biol. Chem. 256, 11224-11231.
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EMBL accession no. X53337
960 Q
1080 R
D
OOCAG'-CAITTTTMTAC&TTTOACGAGC 1200
*
_ GCACCASCccAcCTCCICCTCCCZCCA
1320
CTCACJCASACTCAQCSC'CGCTACTGTCSOSGCCTT__TCTOTCCTCACCCSTGCCTCkLTCTOCCCCTCl!COT 1440 TC 1560 COCCTCCOCTCCTC&;=X GT=CTAAGGGCCAROC^CC = c
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S
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GSCCCCTGTA=ArAA
STTGCOCTTfCr __==
1680 1800 1893
Note added in proof. Since the acceptance of this manuscript we have become aware of results by Grusby et al. (Nucl. Acids Res., vol. 18, p. 4008, 1990) concerning the cloning of a mouse cathepsin D cDNA. Their sequence shows one nucleotide difference (position 1681, A to T) in the 3' untranslated region when compared to the sequence given here. This sequence was accepted July 16, 1990. * To whom correspondence should be addressed
