ID Q8AY88_CTEID Unreviewed; 203 AA.
AC Q8AY88;
DT 01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2003, sequence version 1.
DT 27-MAR-2024, entry version 81.
DE RecName: Full=Cathepsin D {ECO:0000256|ARBA:ARBA00015582};
DE EC=3.4.23.5 {ECO:0000256|ARBA:ARBA00011930};
DE Flags: Fragment;
OS Ctenopharyngodon idella (Grass carp) (Leuciscus idella).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Xenocyprididae; Xenocypridinae; Ctenopharyngodon.
OX NCBI_TaxID=7959 {ECO:0000313|EMBL:AAN62917.1};
RN [1] {ECO:0000313|EMBL:AAN62917.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Brain {ECO:0000313|EMBL:AAN62917.1};
RA Jiang Y.H., Zhang Z.P., Wang Y.L., Yang M.M., Kwong R.Y.C., Randall D.,
RA Wu R.S.S., Wong A.O.L.;
RT "Novel genes involved in GH auto-regulation in Chinese grass carp.";
RL Submitted (SEP-2002) 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; AF544968; AAN62917.1; -; mRNA.
DR AlphaFoldDB; Q8AY88; -.
DR MEROPS; A01.009; -.
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 Gene3D; 2.40.70.10; Acid Proteases; 1.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR001969; Aspartic_peptidase_AS.
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; 1.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 2: Evidence at transcript level;
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}.
FT DOMAIN 1..198
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT DISULFID 77..81
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT DISULFID 120..157
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AAN62917.1"
SQ SEQUENCE 203 AA; 22180 MW; A151D1D85AF0D45A CRC64;
GVPPVFDMMM SQKKVEKNIF SFYLNRNPDT QPGGELLLGG TDPKYYTGDF NYVDISRQAY
WQIHMDGMSI GSELTLCKGG CEAIVDTGTS LITGPATEIK ALQKAIGAIP LIQGEYMVDC
KKVPTLPTIS FVLGGKTYSL TGEQYILKES QAGQEICLSG FMGLDIPPPA GPLWILGDVF
IGQYYTVFDR ENNRVGFAKA AQQ
//
