ID   CATD_PIG                Reviewed;         345 AA.
AC   P00795;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1990, sequence version 2.
DT   04-NOV-2008, entry version 73.
DE   RecName: Full=Cathepsin D;
DE            EC=3.4.23.5;
DE   Contains:
DE     RecName: Full=Cathepsin D light chain;
DE   Contains:
DE     RecName: Full=Cathepsin D heavy chain;
DE   Flags: Precursor;
GN   Name=CTSD;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;
OC   Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   PROTEIN SEQUENCE OF 1-98.
RC   TISSUE=Spleen;
RX   MEDLINE=83213348; PubMed=6406481;
RA   Takahashi T., Tang J.;
RT   "Amino acid sequence of porcine spleen cathepsin D light chain.";
RL   J. Biol. Chem. 258:6435-6443(1983).
RN   [2]
RP   PROTEIN SEQUENCE OF 104-345.
RC   TISSUE=Spleen;
RX   MEDLINE=84222027; PubMed=6587385;
RA   Shewale J.G., Tang J.;
RT   "Amino acid sequence of porcine spleen cathepsin D.";
RL   Proc. Natl. Acad. Sci. U.S.A. 81:3703-3707(1984).
RN   [3]
RP   NUCLEOTIDE SEQUENCE OF 74-148.
RX   MEDLINE=89034127; PubMed=3182800;
RA   Yonezawa S., Takahashi T., Wang X., Wong R.N.S., Hartsuck J.A.,
RA   Tang J.;
RT   "Structures at the proteolytic processing region of cathepsin D.";
RL   J. Biol. Chem. 263:16504-16511(1988).
RN   [4]
RP   STRUCTURE OF CARBOHYDRATES.
RX   MEDLINE=84152787; PubMed=6422853; DOI=10.1016/0003-9861(84)90128-0;
RA   Nakao Y., Kozutsumi Y., Kawasaki T., Yamashina I., van Halbeek H.,
RA   Vliegenthart J.F.G.;
RT   "Oligosaccharides on cathepsin D from porcine spleen.";
RL   Arch. Biochem. Biophys. 229:43-54(1984).
CC   -!- FUNCTION: Acid protease active in intracellular protein breakdown.
CC   -!- CATALYTIC ACTIVITY: Specificity similar to, but narrower than,
CC       that of pepsin A. Does not cleave the 4-Gln-|-His-5 bond in B
CC       chain of insulin.
CC   -!- SUBUNIT: Consists of a light chain and a heavy chain.
CC   -!- SUBCELLULAR LOCATION: Lysosome. Melanosome (By similarity).
CC   -!- SIMILARITY: Belongs to the peptidase A1 family.
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DR   PIR; A92425; KHPGD.
DR   HSSP; P07339; 1LYB.
DR   SMR; P00795; 105-345.
DR   HOVERGEN; P00795; -.
DR   GO; GO:0005764; C:lysosome; IEA:UniProtKB-KW.
DR   GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR   InterPro; IPR001969; Pept_Asp_AS.
DR   InterPro; IPR009007; Pept_Aspartc_cat.
DR   InterPro; IPR001461; Peptidase_A1.
DR   Gene3D; G3DSA:2.40.70.10; Pept_Aspartc_cat; 2.
DR   PANTHER; PTHR13683; Peptidase_A1; 1.
DR   Pfam; PF00026; Asp; 1.
DR   PRINTS; PR00792; PEPSIN.
DR   PROSITE; PS00141; ASP_PROTEASE; 2.
PE   1: Evidence at protein level;
KW   Aspartyl protease; Direct protein sequencing; Glycoprotein; Hydrolase;
KW   Lysosome; Protease; Zymogen.
FT   CHAIN         1     98       Cathepsin D light chain.
FT                                /FTId=PRO_0000025955.
FT   PROPEP       99    103
FT                                /FTId=PRO_0000025956.
FT   CHAIN       104    345       Cathepsin D heavy chain.
FT                                /FTId=PRO_0000025957.
FT   ACT_SITE     33     33
FT   ACT_SITE    230    230
FT   CARBOHYD     70     70       N-linked (GlcNAc...).
FT   CARBOHYD    198    198       N-linked (GlcNAc...).
FT   DISULFID     46     53
FT   DISULFID    221    225
FT   DISULFID    264    301
FT   VARIANT     234    234       S -> K.
FT   VARIANT     247    247       G -> Q.
FT   CONFLICT     89     89       Missing (in Ref. 1; AA sequence).
FT   CONFLICT     97     97       C -> S (in Ref. 1; AA sequence).
SQ   SEQUENCE   345 AA;  37295 MW;  B3E72C11787F14E2 CRC64;
     GPIPEVLKNY MDAQYYGEIG IGTPPQCFTV VFDTGSSNLW VPSIHCKLLD IACWIHHKYN
     SGKSSTYVKN GTTFAIHYGS GSLSGYLSSQ DTVSVPCNSA LSGVGGIKVE RQTFGEATKQ
     PGLTFIAAKF DGILGMAYPR ISVNNVVPVF DNLMQQKLVD KDIFSFYLNR DPGAQPGGEL
     MLGGIDSKYY KGSLDYHNVT RKAYWQIHMN QVAVGSSLTL CKGGCEAIVD TGTSLIVGQP
     EEVRELGKAI GAVPLIQGEY MIPCEKVPSL PDVTVTLGGK KYKLSSENYT LKVSQAGQTI
     CLSGFMGMDI PPPGGPLWIL GDVFIGRYYT VFDRDLNRVG LAEAA
//