[1]	PROTEIN SEQUENCE OF 1-98. TISSUE=Spleen; PubMed=6406481 [NCBI, ExPASy, EBI, Israel, Japan] Takahashi T., Tang J.; "Amino acid sequence of porcine spleen cathepsin D light chain."; J. Biol. Chem. 258:6435-6443(1983).
[2]	PROTEIN SEQUENCE OF 104-345. TISSUE=Spleen; PubMed=6587385 [NCBI, ExPASy, EBI, Israel, Japan] Shewale J.G., Tang J.; "Amino acid sequence of porcine spleen cathepsin D."; Proc. Natl. Acad. Sci. U.S.A. 81:3703-3707(1984).
[3]	NUCLEOTIDE SEQUENCE OF 74-148. PubMed=3182800 [NCBI, ExPASy, EBI, Israel, Japan] Yonezawa S., Takahashi T., Wang X., Wong R.N.S., Hartsuck J.A., Tang J.; "Structures at the proteolytic processing region of cathepsin D."; J. Biol. Chem. 263:16504-16511(1988).
[4]	STRUCTURE OF CARBOHYDRATES. DOI=10.1016/0003-9861(84)90128-0; PubMed=6422853 [NCBI, ExPASy, EBI, Israel, Japan] Nakao Y., Kozutsumi Y., Kawasaki T., Yamashina I., van Halbeek H., Vliegenthart J.F.G.; "Oligosaccharides on cathepsin D from porcine spleen."; Arch. Biochem. Biophys. 229:43-54(1984).

Comments

FUNCTION: Acid protease active in intracellular protein breakdown.
CATALYTIC ACTIVITY: Specificity similar to, but narrower than, that of pepsin A. Does not cleave the 4-Gln-|-His-5 bond in B chain of insulin.
SUBUNIT: Consists of a light chain and a heavy chain.
SUBCELLULAR LOCATION: Lysosome. Melanosome (By similarity).
SIMILARITY: Belongs to the peptidase A1 family [view classification].

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

PIR

A92425; KHPGD.

3D structure databases

HSSP

P07339; 1LYB. [HSSP ENTRY / PDB]

SMR

P00795; 105-345.

ModBase

P00795.

Ontologies

GO:0005764;	Cellular component: lysosome (inferred from electronic annotation from UniProtKB-KW).
GO:0042470;	Cellular component: melanosome (inferred from electronic annotation from UniProtKB-SubCell).
GO:0004190;	Molecular function: aspartic-type endopeptidase activity (inferred from electronic annotation from InterPro).
GO:0006508;	Biological process: proteolysis (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR001969; Pept_Asp_AS.
IPR009007; Pept_Aspartc_cat.
IPR001461; Peptidase_A1.
Graphical view of domain structure.

Gene3D

G3DSA:2.40.70.10; Pept_Aspartc_cat; 2.

PANTHER

PTHR13683; Peptidase_A1; 1.

Pfam

PF00026; Asp; 1.
Pfam graphical view of domain structure.

PRINTS

PR00792; PEPSIN.

PROSITE

PS00141; ASP_PROTEASE; 2.

ProtoNet

P00795.

Phylogenomic databases

HOVERGEN

P00795; -.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Aspartyl protease; Direct protein sequencing; Glycoprotein; Hydrolase; Lysosome; Protease; Zymogen.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 98`	`98`	`Cathepsin D light chain.`	`PRO_0000025955`
`PROPEP`	`99 103`	`5`		`PRO_0000025956`
`CHAIN`	`104 345`	`242`	`Cathepsin D heavy chain.`	`PRO_0000025957`
`ACT_SITE`	`33 33`
`ACT_SITE`	`230 230`
`CARBOHYD`	`70 70`		`N-linked (GlcNAc...).`
`CARBOHYD`	`198 198`		`N-linked (GlcNAc...).`
`DISULFID`	`46 53`
`DISULFID`	`221 225`
`DISULFID`	`264 301`
`VARIANT`	`234 234`	`1`	`S -> K.`
`VARIANT`	`247 247`	`1`	`G -> Q.`
`CONFLICT`	`89 89`		`Missing (in Ref. 1; AA sequence).`
`CONFLICT`	`97 97`		`C -> S (in Ref. 1; AA sequence).`

Sequence information

Length: 345 AA [This is the length of the unprocessed precursor]

Molecular weight: 37295 Da [This is the MW of the unprocessed precursor]

CRC64: B3E72C11787F14E2 [This is a checksum on the sequence]

        10         20         30         40         50         60 
GPIPEVLKNY MDAQYYGEIG IGTPPQCFTV VFDTGSSNLW VPSIHCKLLD IACWIHHKYN 

        70         80         90        100        110        120 
SGKSSTYVKN GTTFAIHYGS GSLSGYLSSQ DTVSVPCNSA LSGVGGIKVE RQTFGEATKQ 

       130        140        150        160        170        180 
PGLTFIAAKF DGILGMAYPR ISVNNVVPVF DNLMQQKLVD KDIFSFYLNR DPGAQPGGEL 

       190        200        210        220        230        240 
MLGGIDSKYY KGSLDYHNVT RKAYWQIHMN QVAVGSSLTL CKGGCEAIVD TGTSLIVGQP 

       250        260        270        280        290        300 
EEVRELGKAI GAVPLIQGEY MIPCEKVPSL PDVTVTLGGK KYKLSSENYT LKVSQAGQTI 

       310        320        330        340 
CLSGFMGMDI PPPGGPLWIL GDVFIGRYYT VFDRDLNRVG LAEAA

P00795 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools