CATD_CANLF
ID CATD_CANLF Reviewed; 410 AA.
AC Q4LAL9;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2005, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Cathepsin D;
DE EC=3.4.23.5;
DE Flags: Precursor;
GN Name=CTSD;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT THR-254.
RC STRAIN=Beagle; TISSUE=Lung;
RX PubMed=16293139; DOI=10.1111/j.1365-2052.2005.01375.x;
RA Woehlke A., Distl O., Droegemueller C.;
RT "The canine CTSD gene as a candidate for late-onset neuronal ceroid
RT lipofuscinosis.";
RL Anim. Genet. 36:530-532(2005).
CC -!- FUNCTION: Acid protease active in intracellular protein breakdown.
CC Plays a role in APP processing following cleavage and activation by
CC ADAM30 which leads to APP degradation. {ECO:0000250|UniProtKB:P07339}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Specificity similar to, but narrower than, that of pepsin A.
CC Does not cleave the 4-Gln-|-His-5 bond in B chain of insulin.;
CC EC=3.4.23.5;
CC -!- SUBUNIT: Consists of a light chain and a heavy chain. Interacts with
CC ADAM30; this leads to activation of CTSD. Interacts with GRN;
CC stabilizes CTSD; increases its proteolytic activity (By similarity).
CC {ECO:0000250|UniProtKB:P07339, ECO:0000250|UniProtKB:P18242}.
CC -!- SUBCELLULAR LOCATION: Lysosome. Melanosome {ECO:0000250}. Secreted,
CC extracellular space {ECO:0000250}.
CC -!- PTM: N- and O-glycosylated. {ECO:0000250|UniProtKB:P07339}.
CC -!- PTM: Undergoes proteolytic cleavage and activation by ADAM30.
CC {ECO:0000250|UniProtKB:P07339}.
CC -!- SIMILARITY: Belongs to the peptidase A1 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AM048627; CAJ14973.1; -; mRNA.
DR RefSeq; NP_001020792.1; NM_001025621.1.
DR AlphaFoldDB; Q4LAL9; -.
DR SMR; Q4LAL9; -.
DR STRING; 9615.ENSCAFP00000014791; -.
DR MEROPS; A01.009; -.
DR PaxDb; Q4LAL9; -.
DR PRIDE; Q4LAL9; -.
DR Ensembl; ENSCAFT00040045867; ENSCAFP00040040020; ENSCAFG00040024588.
DR Ensembl; ENSCAFT00845017589; ENSCAFP00845013693; ENSCAFG00845009905.
DR GeneID; 483662; -.
DR KEGG; cfa:483662; -.
DR CTD; 1509; -.
DR VEuPathDB; HostDB:ENSCAFG00845009905; -.
DR eggNOG; KOG1339; Eukaryota.
DR GeneTree; ENSGT00940000155733; -.
DR HOGENOM; CLU_013253_3_1_1; -.
DR InParanoid; Q4LAL9; -.
DR OMA; DKSHYTG; -.
DR OrthoDB; 1619495at2759; -.
DR TreeFam; TF314990; -.
DR Reactome; R-CFA-2022377; Metabolism of Angiotensinogen to Angiotensins.
DR Reactome; R-CFA-2132295; MHC class II antigen presentation.
DR Reactome; R-CFA-6798695; Neutrophil degranulation.
DR Proteomes; UP000002254; Chromosome 18.
DR Bgee; ENSCAFG00000010052; Expressed in mucosa of urinary bladder and 44 other tissues.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005764; C:lysosome; ISS:UniProtKB.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0000045; P:autophagosome assembly; IEA:Ensembl.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR CDD; cd05490; Cathepsin_D2; 1.
DR Gene3D; 2.40.70.10; -; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR001969; Aspartic_peptidase_AS.
DR InterPro; IPR012848; Aspartic_peptidase_N.
DR InterPro; IPR033144; Cathepsin_D.
DR InterPro; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR PANTHER; PTHR47966; PTHR47966; 1.
DR Pfam; PF07966; A1_Propeptide; 1.
DR Pfam; PF00026; Asp; 1.
DR PRINTS; PR00792; PEPSIN.
DR SUPFAM; SSF50630; SSF50630; 1.
DR PROSITE; PS00141; ASP_PROTEASE; 2.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 2: Evidence at transcript level;
KW Aspartyl protease; Disulfide bond; Glycoprotein; Hydrolase; Lysosome;
KW Protease; Reference proteome; Secreted; Signal; Zymogen.
FT SIGNAL 1..18
FT /evidence="ECO:0000250"
FT PROPEP 19..64
FT /note="Activation peptide"
FT /evidence="ECO:0000250"
FT /id="PRO_0000045434"
FT CHAIN 65..410
FT /note="Cathepsin D"
FT /id="PRO_0000045435"
FT DOMAIN 79..405
FT /note="Peptidase A1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT ACT_SITE 97
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT ACT_SITE 293
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT CARBOHYD 134
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 261
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 91..160
FT /evidence="ECO:0000250"
FT DISULFID 110..117
FT /evidence="ECO:0000250"
FT DISULFID 284..288
FT /evidence="ECO:0000250"
FT DISULFID 327..364
FT /evidence="ECO:0000250"
FT VARIANT 254
FT /note="K -> T"
FT /evidence="ECO:0000269|PubMed:16293139"
SQ 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
