ID I3KEQ5_ORENI Unreviewed; 379 AA.
AC I3KEQ5;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 2.
DT 27-MAR-2024, entry version 71.
DE RecName: Full=Cathepsin D {ECO:0000256|ARBA:ARBA00015582};
DE EC=3.4.23.5 {ECO:0000256|ARBA:ARBA00011930};
GN Name=ctsd {ECO:0000313|Ensembl:ENSONIP00000019600.2};
OS Oreochromis niloticus (Nile tilapia) (Tilapia nilotica).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Oreochromini; Oreochromis.
OX NCBI_TaxID=8128 {ECO:0000313|Ensembl:ENSONIP00000019600.2, ECO:0000313|Proteomes:UP000005207};
RN [1] {ECO:0000313|Proteomes:UP000005207}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Broad Institute Genome Assembly Team;
RG Broad Institute Sequencing Platform;
RA Di Palma F., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Oreochromis niloticus (Nile Tilapia).";
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSONIP00000019600.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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; Evidence={ECO:0000256|ARBA:ARBA00000585};
CC -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000256|ARBA:ARBA00004371}.
CC -!- SIMILARITY: Belongs to the peptidase A1 family.
CC {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
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DR AlphaFoldDB; I3KEQ5; -.
DR STRING; 8128.ENSONIP00000059874; -.
DR MEROPS; A01.009; -.
DR Ensembl; ENSONIT00000019617.2; ENSONIP00000019600.2; ENSONIG00000015575.2.
DR eggNOG; KOG1339; Eukaryota.
DR GeneTree; ENSGT00940000155733; -.
DR HOGENOM; CLU_013253_3_3_1; -.
DR TreeFam; TF314990; -.
DR Proteomes; UP000005207; Linkage group LG1.
DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd05490; Cathepsin_D2; 1.
DR Gene3D; 2.40.70.10; Acid Proteases; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR001969; Aspartic_peptidase_AS.
DR InterPro; IPR033144; Cathepsin_D.
DR InterPro; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR PANTHER; PTHR47966; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR PANTHER; PTHR47966:SF42; CATHEPSIN D; 1.
DR Pfam; PF00026; Asp; 1.
DR PRINTS; PR00792; PEPSIN.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR PROSITE; PS00141; ASP_PROTEASE; 2.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 3: Inferred from homology;
KW Aspartyl protease {ECO:0000256|ARBA:ARBA00022750,
KW ECO:0000256|RuleBase:RU000454};
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR601461-2};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000454};
KW Lysosome {ECO:0000256|ARBA:ARBA00023228};
KW Protease {ECO:0000256|RuleBase:RU000454};
KW Reference proteome {ECO:0000313|Proteomes:UP000005207}.
FT DOMAIN 59..376
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 77
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 264
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT DISULFID 90..97
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT DISULFID 255..259
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT DISULFID 298..335
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ SEQUENCE 379 AA; 41289 MW; CB15F135F5434AFB CRC64;
LRVGIPLKKF RSIRRELTDS GKGIEELVAD KHSLKYNFGF PSSNGPTPET LKNYLDAQYY
GEITLGTPPQ KFTVVFDTGS SNLWVPSVHC SFFDIACWLH HKYNSAKSST YVKNGTSFAI
QYGSGSLSGY LSQDTCSIGD ISVEKQIFGE AIKQPGVAFI AAKFDGILGM AYPSISVDGV
VPVFDNMMNQ KKVEKNVFSF YLNRNPDTEP GGELLLGGTD PKYYDGDFHY ANISRQAYWQ
VHMDGMTVGS QLSLCKGGCE AIVDTGTSLI TGPAAEVKAL QKAIGAIPLI QGEYLVNCSK
IPSLPVITFN VGGQSYTLTG EQYVLQESQA GKTICLSGFM GLDIPPPAGP LWILGDVFIG
QYYTVFDRDN NRVGFAKSK
//
