Reviewed, UniProtKB/Swiss-Prot P00795 (CATD_PIG)

Names and origin

Protein names

Recommended name:
    Cathepsin D
    EC=3.4.23.5
Cleaved into the following 2 chains:
    1- Recommended name:
            Cathepsin D light chain
    2- Recommended name:
            Cathepsin D heavy chain

Gene names

Name:

CTSD

Organism

Sus scrofa (Pig)

Taxonomic identifier

9823 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Suina › Suidae › Sus

Protein attributes

Sequence length	345 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (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 structure	Consists of a light chain and a heavy chain.
Subcellular location	Lysosome. Melanosome By similarity.
Sequence similarities	Belongs to the peptidase A1 family.

Ontologies

Keywords
Cellular component	Lysosome
Molecular function	Aspartyl protease Hydrolase Protease
PTM	Disulfide bond Glycoprotein Zymogen
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	proteolysis Inferred from electronic annotation. Source: InterPro
Cellular component	lysosome Inferred from electronic annotation. Source: UniProtKB-SubCell melanosome Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	aspartic-type endopeptidase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 98	98	Cathepsin D light chain		PRO_0000025955
	Propeptide	99 – 103	5	Ref.2		PRO_0000025956
	Chain	104 – 345	242	Cathepsin D heavy chain		PRO_0000025957
Sites
	Active site	33	1
	Active site	230	1
Amino acid modifications
	Glycosylation	70	1	N-linked (GlcNAc...)
	Glycosylation	198	1	N-linked (GlcNAc...)
	Disulfide bond	46 ↔ 53
	Disulfide bond	221 ↔ 225
	Disulfide bond	264 ↔ 301
Natural variations
	Natural variant	234	1	S → K
	Natural variant	247	1	G → Q
Experimental info
	Sequence conflict	89	1	Missing AA sequence Ref.1
	Sequence conflict	97	1	C → S AA sequence Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P00795-1 [UniParc]. Last modified November 1, 1990. Version 2. Checksum: B3E72C11787F14E2	FASTA	345	37,295
	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

References

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

Cross-references

Sequence databases
PIR	KHPGD. A92425.
3D structure databases
HSSP	HSSP built from PDB template 1LYB based on UniProtKB P07339.
SMR	P00795. Positions 105-345.
ModBase	Search...
Phylogenomic databases
HOVERGEN	P00795.
Enzyme and pathway databases
BRENDA	3.4.23.5. 249.
Family and domain databases
InterPro	IPR001461. Peptidase_A1. IPR001969. Peptidase_aspartic_AS. IPR009007. Peptidase_aspartic_catalytic. [Graphical view]
Gene3D	G3DSA:2.40.70.10. Pept_Aspartc_cat. 2 hits.
PANTHER	PTHR13683. Peptidase_A1. 1 hit.
Pfam	PF00026. Asp. 1 hit. [Graphical view]
PRINTS	PR00792. PEPSIN.
PROSITE	PS00141. ASP_PROTEASE. 2 hits. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CATD_PIG

Accession

Primary (citable) accession number: P00795

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	November 1, 1990
Last modified:	June 16, 2009
This is version 78 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)