ID A0A099ZCD4_TINGU Unreviewed; 321 AA.
AC A0A099ZCD4;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Cathepsin D {ECO:0000256|ARBA:ARBA00015582};
DE EC=3.4.23.5 {ECO:0000256|ARBA:ARBA00011930};
DE Flags: Fragment;
GN ORFNames=N309_11683 {ECO:0000313|EMBL:KGL79397.1};
OS Tinamus guttatus (White-throated tinamou).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Palaeognathae; Tinamiformes; Tinamidae; Tinamus.
OX NCBI_TaxID=94827 {ECO:0000313|EMBL:KGL79397.1, ECO:0000313|Proteomes:UP000053641};
RN [1] {ECO:0000313|EMBL:KGL79397.1, ECO:0000313|Proteomes:UP000053641}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N309 {ECO:0000313|EMBL:KGL79397.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (JUN-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; KL892049; KGL79397.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A099ZCD4; -.
DR STRING; 94827.A0A099ZCD4; -.
DR MEROPS; A01.009; -.
DR Proteomes; UP000053641; 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 Gene3D; 2.60.40.1960; -; 1.
DR Gene3D; 2.40.70.10; Acid Proteases; 2.
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; 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:UP000053641}.
FT DOMAIN 5..320
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 23
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 208
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT DISULFID 199..203
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KGL79397.1"
FT NON_TER 321
FT /evidence="ECO:0000313|EMBL:KGL79397.1"
SQ SEQUENCE 321 AA; 34759 MW; 1366A67BD073D504 CRC64;
LQAQYYGEIG IGTPPQKVTV VFDTGSPHLW GPAPHLLDIA CLLHHKYDAS KSSTYVKNGT
EFAIHYGTGS LSGYLSQDTV TLGDLEIKNQ IFGEAVKQPG ITFIAAKFDG ILGMAFPKIS
VDKVTPFFDN IMQQKLIEKN IFSFYLNRDP TAQPGGELLL GGTDPKYYSG DFSWVNVTRK
AYWQVHMDAV DVANGLTLCK GGCEAIVDTG TSLITGPTKE VKELQKAIGA KPLIKGEYVI
PCEKVSSLPV ITLTLGGKPY QLTGEQYVFK VSAQGETICL SGFSGLDVPP PGGPLWILGD
VFIGPYYTVF DRDNDSVGFA K
//
