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Cathepsin D (EC 3.4.23.5)

 CATD_CANLF              Reviewed;         410 AA.
Q4LAL9;
10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
02-AUG-2005, sequence version 1.
22-NOV-2017, entry version 90.
RecName: Full=Cathepsin D;
EC=3.4.23.5;
Flags: Precursor;
Name=CTSD;
Canis lupus familiaris (Dog) (Canis familiaris).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae;
Canis.
NCBI_TaxID=9615;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT THR-254.
STRAIN=Beagle; TISSUE=Lung;
PubMed=16293139; DOI=10.1111/j.1365-2052.2005.01375.x;
Woehlke A., Distl O., Droegemueller C.;
"The canine CTSD gene as a candidate for late-onset neuronal ceroid
lipofuscinosis.";
Anim. Genet. 36:530-532(2005).
-!- 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.
{ECO:0000250|UniProtKB:P07339}.
-!- 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. Interacts
with ADAM30; this leads to activation of CTSD.
{ECO:0000250|UniProtKB:P07339}.
-!- SUBCELLULAR LOCATION: Lysosome. Melanosome {ECO:0000250}.
Secreted, extracellular space {ECO:0000250}.
-!- PTM: N- and O-glycosylated. {ECO:0000250|UniProtKB:P07339}.
-!- PTM: Undergoes proteolytic cleavage and activation by ADAM30.
{ECO:0000250|UniProtKB:P07339}.
-!- SIMILARITY: Belongs to the peptidase A1 family. {ECO:0000305}.
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EMBL; AM048627; CAJ14973.1; -; mRNA.
RefSeq; NP_001020792.1; NM_001025621.1.
UniGene; Cfa.17547; -.
ProteinModelPortal; Q4LAL9; -.
SMR; Q4LAL9; -.
STRING; 9615.ENSCAFP00000014791; -.
MEROPS; A01.009; -.
PaxDb; Q4LAL9; -.
PRIDE; Q4LAL9; -.
Ensembl; ENSCAFT00000015991; ENSCAFP00000014791; ENSCAFG00000010052.
GeneID; 483662; -.
KEGG; cfa:483662; -.
CTD; 1509; -.
eggNOG; KOG1339; Eukaryota.
eggNOG; ENOG410XNV7; LUCA.
GeneTree; ENSGT00760000118929; -.
HOGENOM; HOG000197681; -.
HOVERGEN; HBG000482; -.
InParanoid; Q4LAL9; -.
KO; K01379; -.
OMA; WNGQYTV; -.
OrthoDB; EOG091G0JP7; -.
TreeFam; TF314990; -.
Reactome; R-CFA-1442490; Collagen degradation.
Reactome; R-CFA-2132295; MHC class II antigen presentation.
Reactome; R-CFA-6798695; Neutrophil degranulation.
Proteomes; UP000002254; Chromosome 18.
Bgee; ENSCAFG00000010052; -.
GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
GO; GO:0004190; F:aspartic-type endopeptidase activity; IBA:GO_Central.
GO; GO:0006914; P:autophagy; IBA:GO_Central.
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; IPR033144; Cathepsin_D.
InterPro; IPR033121; PEPTIDASE_A1.
InterPro; IPR021109; Peptidase_aspartic_dom_sf.
PANTHER; PTHR13683; PTHR13683; 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.
2: Evidence at transcript level;
Aspartyl protease; Complete proteome; Disulfide bond; Glycoprotein;
Hydrolase; Lysosome; Polymorphism; Protease; Reference proteome;
Secreted; Signal; Zymogen.
SIGNAL 1 18 {ECO:0000250}.
PROPEP 19 64 Activation peptide. {ECO:0000250}.
/FTId=PRO_0000045434.
CHAIN 65 410 Cathepsin D.
/FTId=PRO_0000045435.
DOMAIN 79 405 Peptidase A1. {ECO:0000255|PROSITE-
ProRule:PRU01103}.
ACT_SITE 97 97 {ECO:0000255|PROSITE-ProRule:PRU10094}.
ACT_SITE 293 293 {ECO:0000255|PROSITE-ProRule:PRU10094}.
CARBOHYD 134 134 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 261 261 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 91 160 {ECO:0000250}.
DISULFID 110 117 {ECO:0000250}.
DISULFID 284 288 {ECO:0000250}.
DISULFID 327 364 {ECO:0000250}.
VARIANT 254 254 K -> T. {ECO:0000269|PubMed:16293139}.
SEQUENCE 410 AA; 44320 MW; 1E97B7C15BAAF9CD CRC64;
MQPPSLLLLV LGLLAAPAAA LVRIPLHKFT SVRRTMTELG GPVEDLIAKG PISKYAQGAP
AVTGGPIPEM LRNYMDAQYY GEIGIGTPPQ CFTVVFDTGS SNLWVPSIHC KLLDIACWIH
HKYNSGKSST YVKNGTSFDI HYGSGSLSGY LSQDTVSVPC KSALSGLAGI KVERQTFGEA
TKQPGITFIA AKFDGILGMA YPRISVNNVL PVFDNLMQQK LVEKNIFSFY LNRDPNAQPG
GELMLGGTDS KYYKGPLSYL NVTRKAYWQV HMEQVDVGSS LTLCKGGCEA IVDTGTSLIV
GPVDEVRELQ KAIGAVPLIQ GEYMIPCEKV STLPDVTLKL GGKLYKLSSE DYTLKVSQGG
KTICLSGFMG MDIPPPGGPL WILGDVFIGC YYTVFDRDQN RVGLAQATRL


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