*nlm.life
			PubMed Journals: Proc Natl Acad Sci U S A

  Source:		PMID: 3927292


    		Proc Natl Acad Sci U S A. 1985 Aug;82(15):4910-4.
     
			Cloning and sequence analysis of cDNA for
			human cathepsin D.

			Faust PL, Kornfeld S, Chirgwin JM.

			An 1110-base-pair cDNA clone for human cathepsin
			D was obtained by screening a lambda gt10
			human hepatoma G2 cDNA library with a human
			renin exon 3 genomic fragment. Poly(A)+
			RNA blot analysis with this cathepsin D
			clone demonstrated a message length of about
			2.2 kilobases. The partial clone was used
			to screen a size-selected human kidney cDNA
			library, from which two cathepsin D recombinant
			plasmids with inserts of about 2200 and
			2150 base pairs were obtained. The nucleotide
			sequences of these clones and of the lambda
			gt10 clone were determined. The amino acid
			sequence predicted from the cDNA sequence
			shows that human cathepsin D consists of
			412 amino acids with 20 and 44 amino acids
			in a pre- and a prosegment, respectively.
			The mature protein region shows 87% amino
			acid identity with porcine cathepsin D but
			differs in having nine additional amino
			acids. Two of these are at the COOH terminus;
			the other seven are positioned between the
			previously determined junction for the light
			and heavy chains of porcine cathepsin D.
			A high degree of sequence homology was observed
			between human cathepsin D and other aspartyl
			proteases, suggesting a conservation of
			three-dimensional structure in this family
			of proteins.

			PMCID: PMC390467 PMID: 3927292 [Indexed
			for MEDLINE]

     			                         Tweet       Print