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Cathepsin D (EC 3.4.23.5) [Cleaved into: Cathepsin D light chain; Cathepsin D heavy chain]

 CATD_HUMAN              Reviewed;         412 AA.
P07339; Q6IB57;
01-APR-1988, integrated into UniProtKB/Swiss-Prot.
01-APR-1988, sequence version 1.
27-SEP-2017, entry version 206.
RecName: Full=Cathepsin D;
EC=3.4.23.5;
Contains:
RecName: Full=Cathepsin D light chain;
Contains:
RecName: Full=Cathepsin D heavy chain;
Flags: Precursor;
Name=CTSD; Synonyms=CPSD;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3927292; DOI=10.1073/pnas.82.15.4910;
Faust P.L., Kornfeld S., Chirgwin J.M.;
"Cloning and sequence analysis of cDNA for human cathepsin D.";
Proc. Natl. Acad. Sci. U.S.A. 82:4910-4914(1985).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3588310; DOI=10.1093/nar/15.9.3773;
Westley B.R., May F.E.B.;
"Oestrogen regulates cathepsin D mRNA levels in oestrogen responsive
human breast cancer cells.";
Nucleic Acids Res. 15:3773-3786(1987).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2069717; DOI=10.1089/dna.1991.10.423;
Redecker B., Heckendorf B., Grosch H.W., Mersmann G., Hasilik A.;
"Molecular organization of the human cathepsin D gene.";
DNA Cell Biol. 10:423-431(1991).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Kidney;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-22.
PubMed=8262386; DOI=10.1016/0378-1119(93)90107-E;
May F.E., Smith D.J., Westley B.R.;
"The human cathepsin D-encoding gene is transcribed from an estrogen-
regulated and a constitutive start point.";
Gene 134:277-282(1993).
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-22.
PubMed=7935485; DOI=10.1210/mend.8.6.7935485;
Augereau P., Miralles F., Cavailles V., Gaudelet C., Parker M.,
Rochefort H.;
"Characterization of the proximal estrogen-responsive element of human
cathepsin D gene.";
Mol. Endocrinol. 8:693-703(1994).
[9]
PROTEIN SEQUENCE OF 170-180.
TISSUE=Liver;
Hochstrasser D.F., Frutiger S., Paquet N., Bairoch A., Ravier F.,
Pasquali C., Sanchez J.-C., Tissot J.-D., Bjellqvist B., Vargas R.,
Appel R.D., Hughes G.J.;
Submitted (JUN-1992) to UniProtKB.
[10]
PROTEIN SEQUENCE OF 154-162 AND 169-180, SUBUNIT, AND TISSUE
SPECIFICITY.
PubMed=1426530; DOI=10.1016/0020-711X(92)90076-D;
Kobayashi T., Honke K., Gasa S., Fujii T., Maguchi S., Miyazaki T.,
Makita A.;
"Proteolytic processing sites producing the mature form of human
cathepsin D.";
Int. J. Biochem. 24:1487-1491(1992).
[11]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
TISSUE=Melanoma;
PubMed=12643545; DOI=10.1021/pr025562r;
Basrur V., Yang F., Kushimoto T., Higashimoto Y., Yasumoto K.,
Valencia J., Muller J., Vieira W.D., Watabe H., Shabanowitz J.,
Hearing V.J., Hunt D.F., Appella E.;
"Proteomic analysis of early melanosomes: identification of novel
melanosomal proteins.";
J. Proteome Res. 2:69-79(2003).
[12]
GLYCOSYLATION AT ASN-263.
PubMed=12754519; DOI=10.1038/nbt827;
Zhang H., Li X.-J., Martin D.B., Aebersold R.;
"Identification and quantification of N-linked glycoproteins using
hydrazide chemistry, stable isotope labeling and mass spectrometry.";
Nat. Biotechnol. 21:660-666(2003).
[13]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-263.
TISSUE=Plasma;
PubMed=16335952; DOI=10.1021/pr0502065;
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,
Moore R.J., Smith R.D.;
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
hydrazide chemistry, and mass spectrometry.";
J. Proteome Res. 4:2070-2080(2005).
[14]
INVOLVEMENT IN CLN10, AND VARIANT ARG-282.
PubMed=16670177; DOI=10.1093/brain/awl107;
Siintola E., Partanen S., Stromme P., Haapanen A., Haltia M.,
Maehlen J., Lehesjoki A.E., Tyynela J.;
"Cathepsin D deficiency underlies congenital human neuronal ceroid-
lipofuscinosis.";
Brain 129:1438-1445(2006).
[15]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
TISSUE=Melanoma;
PubMed=17081065; DOI=10.1021/pr060363j;
Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H.,
Mangini N.J., Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R.,
Yamagishi S., Shabanowitz J., Hearing V.J., Wu C., Appella E.,
Hunt D.F.;
"Proteomic and bioinformatic characterization of the biogenesis and
function of melanosomes.";
J. Proteome Res. 5:3135-3144(2006).
[16]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-263.
TISSUE=Platelet;
PubMed=16263699; DOI=10.1074/mcp.M500324-MCP200;
Lewandrowski U., Moebius J., Walter U., Sickmann A.;
"Elucidation of N-glycosylation sites on human platelet proteins: a
glycoproteomic approach.";
Mol. Cell. Proteomics 5:226-233(2006).
[17]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-134 AND ASN-263.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of
multiple enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
[18]
TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
PubMed=20551380; DOI=10.1074/mcp.M110.001693;
Didangelos A., Yin X., Mandal K., Baumert M., Jahangiri M., Mayr M.;
"Proteomics characterization of extracellular space components in the
human aorta.";
Mol. Cell. Proteomics 9:2048-2062(2010).
[19]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[20]
GLYCOSYLATION AT THR-63, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=23234360; DOI=10.1021/pr300963h;
Halim A., Ruetschi U., Larson G., Nilsson J.;
"LC-MS/MS characterization of O-glycosylation sites and glycan
structures of human cerebrospinal fluid glycoproteins.";
J. Proteome Res. 12:573-584(2013).
[21]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[22]
INTERACTION WITH ADAM30, IDENTIFICATION BY MASS SPECTROMETRY, AND
CLEAVAGE.
PubMed=27333034; DOI=10.1016/j.ebiom.2016.06.002;
Letronne F., Laumet G., Ayral A.M., Chapuis J., Demiautte F., Laga M.,
Vandenberghe M.E., Malmanche N., Leroux F., Eysert F., Sottejeau Y.,
Chami L., Flaig A., Bauer C., Dourlen P., Lesaffre M., Delay C.,
Huot L., Dumont J., Werkmeister E., Lafont F., Mendes T.,
Hansmannel F., Dermaut B., Deprez B., Herard A.S., Dhenain M.,
Souedet N., Pasquier F., Tulasne D., Berr C., Hauw J.J., Lemoine Y.,
Amouyel P., Mann D., Deprez R., Checler F., Hot D., Delzescaux T.,
Gevaert K., Lambert J.C.;
"ADAM30 Downregulates APP-Linked Defects Through Cathepsin D
Activation in Alzheimer's Disease.";
EBioMedicine 9:278-292(2016).
[23]
X-RAY CRYSTALLOGRAPHY (3 ANGSTROMS).
TISSUE=Spleen;
PubMed=8467789;
Metcalf P., Fusek M.;
"Two crystal structures for cathepsin D: the lysosomal targeting
signal and active site.";
EMBO J. 12:1293-1302(1993).
[24]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), AND SUBUNIT.
TISSUE=Liver;
PubMed=8393577; DOI=10.1073/pnas.90.14.6796;
Baldwin E.T., Bhat T.N., Gulnik S., Hosur M.V., Sowder R.C. II,
Cachau R.E., Collins J., Silva A.M., Erickson J.W.;
"Crystal structures of native and inhibited forms of human cathepsin
D: implications for lysosomal targeting and drug design.";
Proc. Natl. Acad. Sci. U.S.A. 90:6796-6800(1993).
[25]
VARIANT VAL-58.
PubMed=10716266;
DOI=10.1002/1531-8249(200003)47:3<399::AID-ANA22>3.3.CO;2-X;
Papassotiropoulos A., Bagli M., Kurz A., Kornhuber J., Forstl H.,
Maier W., Pauls J., Lautenschlager N., Heun R.;
"A genetic variation of cathepsin D is a major risk factor for
Alzheimer's disease.";
Ann. Neurol. 47:399-403(2000).
[26]
VARIANTS CLN10 ILE-229 AND CYS-383.
PubMed=16685649; DOI=10.1086/504159;
Steinfeld R., Reinhardt K., Schreiber K., Hillebrand M., Kraetzner R.,
Bruck W., Saftig P., Gartner J.;
"Cathepsin D deficiency is associated with a human neurodegenerative
disorder.";
Am. J. Hum. Genet. 78:988-998(2006).
[27]
VARIANT CLN10 ILE-229.
PubMed=21990111; DOI=10.1002/humu.21624;
Kousi M., Lehesjoki A.E., Mole S.E.;
"Update of the mutation spectrum and clinical correlations of over 360
mutations in eight genes that underlie the neuronal ceroid
lipofuscinoses.";
Hum. Mutat. 33:42-63(2012).
-!- FUNCTION: Acid protease active in intracellular protein breakdown.
Plays a role in APP processing following cleavage and activation
by ADAM30 which leads to APP degradation (PubMed:27333034).
Involved in the pathogenesis of several diseases such as breast
cancer and possibly Alzheimer disease.
{ECO:0000269|PubMed:27333034}.
-!- 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
(PubMed:8393577, PubMed:1426530). Interacts with ADAM30; this
leads to activation of CTSD (PubMed:27333034).
{ECO:0000269|PubMed:1426530, ECO:0000269|PubMed:27333034,
ECO:0000269|PubMed:8393577}.
-!- INTERACTION:
P05067:APP; NbExp=2; IntAct=EBI-2115097, EBI-77613;
-!- SUBCELLULAR LOCATION: Lysosome. Melanosome. Secreted,
extracellular space. Note=Identified by mass spectrometry in
melanosome fractions from stage I to stage IV. In aortic samples,
detected as an extracellular protein loosely bound to the matrix
(PubMed:20551380). {ECO:0000269|PubMed:20551380}.
-!- TISSUE SPECIFICITY: Expressed in the aorta extrcellular space (at
protein level) (PubMed:20551380). Expressed in liver (at protein
level) (PubMed:1426530). {ECO:0000269|PubMed:1426530,
ECO:0000269|PubMed:20551380}.
-!- PTM: N- and O-glycosylated. {ECO:0000269|PubMed:12754519,
ECO:0000269|PubMed:16263699, ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:23234360}.
-!- PTM: Undergoes proteolytic cleavage and activation by ADAM30.
{ECO:0000269|PubMed:27333034}.
-!- PTM: As well as the major heavy chain which starts at Leu-169, 2
minor forms starting at Gly-170 and Gly-171 have been identified
(PubMed:1426530). An additional form starting at Ala-168 has also
been identified (PubMed:27333034). {ECO:0000269|PubMed:1426530,
ECO:0000269|PubMed:27333034}.
-!- POLYMORPHISM: The Val-58 allele is significantly overrepresented
in demented patients (11.8%) compared with non-demented controls
(4.9%). Carriers of the Val-58 allele have a 3.1-fold increased
risk for developing AD than non-carriers.
-!- DISEASE: Ceroid lipofuscinosis, neuronal, 10 (CLN10) [MIM:610127]:
A form of neuronal ceroid lipofuscinosis with onset at birth or
early childhood. Neuronal ceroid lipofuscinoses are progressive
neurodegenerative, lysosomal storage diseases characterized by
intracellular accumulation of autofluorescent liposomal material,
and clinically by seizures, dementia, visual loss, and/or cerebral
atrophy. {ECO:0000269|PubMed:16670177,
ECO:0000269|PubMed:16685649, ECO:0000269|PubMed:21990111}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- SIMILARITY: Belongs to the peptidase A1 family. {ECO:0000305}.
-!- WEB RESOURCE: Name=NCL CTSD; Note=Neural Ceroid Lipofuscinoses
mutation db;
URL="http://www.ucl.ac.uk/ncl/catD.shtml";
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EMBL; M11233; AAB59529.1; -; mRNA.
EMBL; X05344; CAA28955.1; -; mRNA.
EMBL; M63138; AAA51922.1; -; Genomic_DNA.
EMBL; M63134; AAA51922.1; JOINED; Genomic_DNA.
EMBL; M63135; AAA51922.1; JOINED; Genomic_DNA.
EMBL; M63136; AAA51922.1; JOINED; Genomic_DNA.
EMBL; M63137; AAA51922.1; JOINED; Genomic_DNA.
EMBL; CR456947; CAG33228.1; -; mRNA.
EMBL; BT006910; AAP35556.1; -; mRNA.
EMBL; BT020155; AAV38957.1; -; mRNA.
EMBL; BC016320; AAH16320.1; -; mRNA.
EMBL; L12980; AAA16314.1; -; Genomic_DNA.
EMBL; S74689; AAD14156.1; -; Genomic_DNA.
EMBL; S52557; AAD13868.1; -; Genomic_DNA.
CCDS; CCDS7725.1; -.
PIR; A25771; KHHUD.
RefSeq; NP_001900.1; NM_001909.4.
UniGene; Hs.654447; -.
PDB; 1LYA; X-ray; 2.50 A; A/C=65-161, B/D=170-410.
PDB; 1LYB; X-ray; 2.50 A; A/C=65-161, B/D=170-410.
PDB; 1LYW; X-ray; 2.50 A; A/C/E/G=65-161, B/D/F/H=170-410.
PDB; 4OBZ; X-ray; 2.90 A; A/C=60-162, B/D=170-412.
PDB; 4OC6; X-ray; 2.64 A; A=60-162, B=170-412.
PDB; 4OD9; X-ray; 1.90 A; A/C=60-162, B/D=170-412.
PDBsum; 1LYA; -.
PDBsum; 1LYB; -.
PDBsum; 1LYW; -.
PDBsum; 4OBZ; -.
PDBsum; 4OC6; -.
PDBsum; 4OD9; -.
ProteinModelPortal; P07339; -.
SMR; P07339; -.
BioGrid; 107889; 46.
DIP; DIP-43906N; -.
IntAct; P07339; 21.
MINT; MINT-3005628; -.
STRING; 9606.ENSP00000236671; -.
BindingDB; P07339; -.
ChEMBL; CHEMBL2581; -.
DrugBank; DB03028; 1h-Benoximidazole-2-Carboxylic Acid.
DrugBank; DB07542; 5-AMINO-6-CYCLOHEXYL-4-HYDROXY-2-ISOBUTYL-HEXANOIC ACID.
DrugBank; DB00030; Insulin Human.
DrugBank; DB00071; Insulin Pork.
DrugBank; DB03096; N-Aminoethylmorpholine.
DrugBank; DB02216; S-Methylcysteine.
GuidetoPHARMACOLOGY; 2345; -.
MEROPS; A01.009; -.
iPTMnet; P07339; -.
PhosphoSitePlus; P07339; -.
SwissPalm; P07339; -.
BioMuta; CTSD; -.
DMDM; 115717; -.
DOSAC-COBS-2DPAGE; P07339; -.
REPRODUCTION-2DPAGE; IPI00011229; -.
SWISS-2DPAGE; P07339; -.
UCD-2DPAGE; P07339; -.
EPD; P07339; -.
PaxDb; P07339; -.
PeptideAtlas; P07339; -.
PRIDE; P07339; -.
TopDownProteomics; P07339; -.
DNASU; 1509; -.
Ensembl; ENST00000236671; ENSP00000236671; ENSG00000117984.
GeneID; 1509; -.
KEGG; hsa:1509; -.
CTD; 1509; -.
DisGeNET; 1509; -.
EuPathDB; HostDB:ENSG00000117984.12; -.
GeneCards; CTSD; -.
GeneReviews; CTSD; -.
H-InvDB; HIX0009359; -.
HGNC; HGNC:2529; CTSD.
HPA; CAB000109; -.
HPA; HPA003001; -.
MalaCards; CTSD; -.
MIM; 116840; gene.
MIM; 610127; phenotype.
neXtProt; NX_P07339; -.
OpenTargets; ENSG00000117984; -.
Orphanet; 228337; CLN10 disease.
PharmGKB; PA27029; -.
eggNOG; KOG1339; Eukaryota.
eggNOG; ENOG410XNV7; LUCA.
GeneTree; ENSGT00760000118929; -.
HOGENOM; HOG000197681; -.
HOVERGEN; HBG000482; -.
InParanoid; P07339; -.
KO; K01379; -.
OMA; WNGQYTV; -.
OrthoDB; EOG091G0JP7; -.
PhylomeDB; P07339; -.
TreeFam; TF314990; -.
BioCyc; MetaCyc:HS04183-MONOMER; -.
BRENDA; 3.4.23.5; 2681.
Reactome; R-HSA-1442490; Collagen degradation.
Reactome; R-HSA-2022377; Metabolism of Angiotensinogen to Angiotensins.
Reactome; R-HSA-2132295; MHC class II antigen presentation.
Reactome; R-HSA-6798695; Neutrophil degranulation.
EvolutionaryTrace; P07339; -.
GeneWiki; Cathepsin_D; -.
GenomeRNAi; 1509; -.
PMAP-CutDB; P07339; -.
PRO; PR:P07339; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000117984; -.
CleanEx; HS_CTSD; -.
ExpressionAtlas; P07339; baseline and differential.
Genevisible; P07339; HS.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:1904813; C:ficolin-1-rich granule lumen; TAS:Reactome.
GO; GO:0043202; C:lysosomal lumen; TAS:Reactome.
GO; GO:0005764; C:lysosome; IDA:UniProtKB.
GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
GO; GO:0045121; C:membrane raft; IDA:UniProtKB.
GO; GO:0035580; C:specific granule lumen; TAS:Reactome.
GO; GO:1904724; C:tertiary granule lumen; TAS:Reactome.
GO; GO:0004190; F:aspartic-type endopeptidase activity; IBA:GO_Central.
GO; GO:0004197; F:cysteine-type endopeptidase activity; TAS:Reactome.
GO; GO:0004252; F:serine-type endopeptidase activity; TAS:Reactome.
GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; TAS:Reactome.
GO; GO:0006914; P:autophagy; IBA:GO_Central.
GO; GO:0030574; P:collagen catabolic process; TAS:Reactome.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
GO; GO:0030163; P:protein catabolic process; IBA:GO_Central.
GO; GO:0006508; P:proteolysis; IBA:GO_Central.
CDD; cd05490; Cathepsin_D2; 1.
Gene3D; 2.40.70.10; -; 2.
InterPro; IPR001461; Aspartic_peptidase_A1.
InterPro; IPR001969; Aspartic_peptidase_AS.
InterPro; IPR012848; Aspartic_peptidase_N.
InterPro; IPR033736; Cathepsin_chordata.
InterPro; IPR033144; Cathepsin_D.
InterPro; IPR033121; PEPTIDASE_A1.
InterPro; IPR021109; Peptidase_aspartic_dom.
PANTHER; PTHR13683; PTHR13683; 1.
PANTHER; PTHR13683:SF487; PTHR13683:SF487; 1.
Pfam; PF07966; A1_Propeptide; 1.
Pfam; PF00026; Asp; 1.
PRINTS; PR00792; PEPSIN.
SUPFAM; SSF50630; SSF50630; 1.
PROSITE; PS00141; ASP_PROTEASE; 2.
PROSITE; PS51767; PEPTIDASE_A1; 1.
1: Evidence at protein level;
3D-structure; Alzheimer disease; Aspartyl protease; Complete proteome;
Direct protein sequencing; Disease mutation; Disulfide bond;
Glycoprotein; Hydrolase; Lysosome; Neurodegeneration;
Neuronal ceroid lipofuscinosis; Polymorphism; Protease;
Reference proteome; Secreted; Signal; Zymogen.
SIGNAL 1 20 {ECO:0000255}.
PROPEP 21 64 Activation peptide.
/FTId=PRO_0000025949.
CHAIN 65 412 Cathepsin D.
/FTId=PRO_0000025950.
CHAIN 65 162 Cathepsin D light chain.
{ECO:0000305|PubMed:1426530}.
/FTId=PRO_0000025951.
CHAIN 169 412 Cathepsin D heavy chain.
{ECO:0000305|PubMed:1426530}.
/FTId=PRO_0000025952.
DOMAIN 79 407 Peptidase A1. {ECO:0000255|PROSITE-
ProRule:PRU01103}.
ACT_SITE 97 97 {ECO:0000255|PROSITE-ProRule:PRU10094,
ECO:0000269|PubMed:8393577}.
ACT_SITE 295 295 {ECO:0000255|PROSITE-ProRule:PRU10094,
ECO:0000269|PubMed:8393577}.
CARBOHYD 63 63 O-linked (GalNAc...) threonine.
{ECO:0000269|PubMed:23234360}.
CARBOHYD 134 134 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218}.
CARBOHYD 263 263 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:12754519,
ECO:0000269|PubMed:16263699,
ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:19159218,
ECO:0000269|PubMed:8393577}.
DISULFID 91 160 {ECO:0000269|PubMed:8393577}.
DISULFID 110 117 {ECO:0000269|PubMed:8393577}.
DISULFID 286 290 {ECO:0000269|PubMed:8393577}.
DISULFID 329 366
VARIANT 58 58 A -> V (associated with increased risk
for AD; possibly influences secretion and
intracellular maturation; dbSNP:rs17571).
{ECO:0000269|PubMed:10716266}.
/FTId=VAR_011621.
VARIANT 229 229 F -> I (in CLN10; dbSNP:rs121912789).
{ECO:0000269|PubMed:16685649,
ECO:0000269|PubMed:21990111}.
/FTId=VAR_029362.
VARIANT 282 282 G -> R (in dbSNP:rs147278302).
{ECO:0000269|PubMed:16670177}.
/FTId=VAR_058490.
VARIANT 383 383 W -> C (in CLN10; dbSNP:rs121912790).
{ECO:0000269|PubMed:16685649}.
/FTId=VAR_029363.
STRAND 67 74 {ECO:0000244|PDB:4OD9}.
TURN 75 77 {ECO:0000244|PDB:4OD9}.
STRAND 78 85 {ECO:0000244|PDB:4OD9}.
TURN 86 89 {ECO:0000244|PDB:4OD9}.
STRAND 90 97 {ECO:0000244|PDB:4OD9}.
STRAND 103 107 {ECO:0000244|PDB:4OD9}.
HELIX 115 118 {ECO:0000244|PDB:4OD9}.
HELIX 125 127 {ECO:0000244|PDB:4OD9}.
STRAND 132 141 {ECO:0000244|PDB:4OD9}.
STRAND 146 159 {ECO:0000244|PDB:4OD9}.
STRAND 172 184 {ECO:0000244|PDB:4OD9}.
HELIX 189 192 {ECO:0000244|PDB:4OD9}.
STRAND 194 200 {ECO:0000244|PDB:4OD9}.
HELIX 204 206 {ECO:0000244|PDB:4OD9}.
HELIX 208 210 {ECO:0000244|PDB:4OD9}.
HELIX 214 220 {ECO:0000244|PDB:4OD9}.
STRAND 224 226 {ECO:0000244|PDB:4OD9}.
STRAND 228 233 {ECO:0000244|PDB:4OD9}.
STRAND 236 238 {ECO:0000244|PDB:1LYW}.
STRAND 239 249 {ECO:0000244|PDB:4OD9}.
HELIX 252 254 {ECO:0000244|PDB:4OD9}.
STRAND 255 263 {ECO:0000244|PDB:4OD9}.
TURN 267 270 {ECO:0000244|PDB:4OD9}.
STRAND 271 274 {ECO:0000244|PDB:4OD9}.
STRAND 276 279 {ECO:0000244|PDB:4OD9}.
TURN 280 282 {ECO:0000244|PDB:1LYW}.
STRAND 284 286 {ECO:0000244|PDB:4OD9}.
STRAND 290 294 {ECO:0000244|PDB:4OD9}.
STRAND 299 303 {ECO:0000244|PDB:4OD9}.
HELIX 305 314 {ECO:0000244|PDB:4OD9}.
STRAND 318 321 {ECO:0000244|PDB:1LYA}.
STRAND 325 327 {ECO:0000244|PDB:4OD9}.
HELIX 329 334 {ECO:0000244|PDB:4OD9}.
STRAND 338 342 {ECO:0000244|PDB:4OD9}.
STRAND 345 349 {ECO:0000244|PDB:4OD9}.
HELIX 351 354 {ECO:0000244|PDB:4OD9}.
STRAND 355 360 {ECO:0000244|PDB:4OD9}.
STRAND 363 372 {ECO:0000244|PDB:4OD9}.
TURN 377 379 {ECO:0000244|PDB:4OD9}.
STRAND 383 385 {ECO:0000244|PDB:4OD9}.
HELIX 387 392 {ECO:0000244|PDB:4OD9}.
STRAND 393 398 {ECO:0000244|PDB:4OD9}.
TURN 399 402 {ECO:0000244|PDB:4OD9}.
STRAND 403 409 {ECO:0000244|PDB:4OD9}.
SEQUENCE 412 AA; 44552 MW; 903FB8412E0CF0B0 CRC64;
MQPSSLLPLA LCLLAAPASA LVRIPLHKFT SIRRTMSEVG GSVEDLIAKG PVSKYSQAVP
AVTEGPIPEV LKNYMDAQYY GEIGIGTPPQ CFTVVFDTGS SNLWVPSIHC KLLDIACWIH
HKYNSDKSST YVKNGTSFDI HYGSGSLSGY LSQDTVSVPC QSASSASALG GVKVERQVFG
EATKQPGITF IAAKFDGILG MAYPRISVNN VLPVFDNLMQ QKLVDQNIFS FYLSRDPDAQ
PGGELMLGGT DSKYYKGSLS YLNVTRKAYW QVHLDQVEVA SGLTLCKEGC EAIVDTGTSL
MVGPVDEVRE LQKAIGAVPL IQGEYMIPCE KVSTLPAITL KLGGKGYKLS PEDYTLKVSQ
AGKTLCLSGF MGMDIPPPSG PLWILGDVFI GRYYTVFDRD NNRVGFAEAA RL


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