ID A0A091FQK7_9AVES Unreviewed; 396 AA.
AC A0A091FQK7;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=Cathepsin D {ECO:0000256|ARBA:ARBA00015582};
DE EC=3.4.23.5 {ECO:0000256|ARBA:ARBA00011930};
DE Flags: Fragment;
GN ORFNames=N303_00182 {ECO:0000313|EMBL:KFO71893.1};
OS Cuculus canorus (common cuckoo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Cuculiformes; Cuculidae; Cuculus.
OX NCBI_TaxID=55661 {ECO:0000313|EMBL:KFO71893.1, ECO:0000313|Proteomes:UP000053760};
RN [1] {ECO:0000313|EMBL:KFO71893.1, ECO:0000313|Proteomes:UP000053760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N303 {ECO:0000313|EMBL:KFO71893.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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 EMBL; KL447290; KFO71893.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091FQK7; -.
DR STRING; 55661.A0A091FQK7; -.
DR MEROPS; A01.009; -.
DR Proteomes; UP000053760; Unassembled WGS sequence.
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; 3.
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; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR PANTHER; PTHR47966:SF42; CATHEPSIN D; 1.
DR Pfam; PF07966; A1_Propeptide; 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|ARBA:ARBA00023157,
KW 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:UP000053760};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..396
FT /note="Cathepsin D"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001873414"
FT DOMAIN 78..395
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 96
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 283
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT CARBOHYD 133
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000256|PIRSR:PIRSR633144-3"
FT CARBOHYD 251
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000256|PIRSR:PIRSR633144-3"
FT DISULFID 109..116
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT DISULFID 274..278
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT DISULFID 317..354
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT NON_TER 396
FT /evidence="ECO:0000313|EMBL:KFO71893.1"
SQ SEQUENCE 396 AA; 43177 MW; 7D27142D261970EE CRC64;
MRPRGLLLLL LLGLAEPCAA IIRIPLTKFP SMRRVLNEVG SEIPDMNALT QLLKFKLGFA
DVSEPTPEIL KNYMDAQYYG EIGIGTPPQK FTVVFDTGSS NLWVPSVHCH LLDIACLLHH
KYDASKSSTY VENGTEFAIH YGTGSLSGFL SQDTVTLGNL KIKNQIFGEA VKQPGITFIA
AKFDGILGMA FPRISVDKVT PFFDNIMEQK LIEKNIFSFY LNRDPAAQPG GELLLGGTDP
KYYTGDFSWV NVTRKAYWQV HMDAVDVANG LTLCKGGCEA IVDTGTSLIT GPTKEVKELQ
TAIGAKPLIK GQYVIPCDKV SSLPVVTLTL GGKPYQLTGE QYVFKVSVQG ETICLSGFSG
LDVPPPGGPL WILGDVFIGP YYTVFDRDND SVGFAK
//
