ID L5KQK6_PTEAL Unreviewed; 375 AA.
AC L5KQK6;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=Cathepsin D {ECO:0000256|ARBA:ARBA00015582};
DE EC=3.4.23.5 {ECO:0000256|ARBA:ARBA00011930};
GN ORFNames=PAL_GLEAN10011195 {ECO:0000313|EMBL:ELK13201.1};
OS Pteropus alecto (Black flying fox).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Megachiroptera; Pteropodidae;
OC Pteropodinae; Pteropus.
OX NCBI_TaxID=9402 {ECO:0000313|EMBL:ELK13201.1, ECO:0000313|Proteomes:UP000010552};
RN [1] {ECO:0000313|Proteomes:UP000010552}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23258410; DOI=10.1126/science.1230835;
RA Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X.,
RA Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., Zhou P.,
RA Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., Sun X.,
RA Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., Wang L.F.,
RA Wang J.;
RT "Comparative analysis of bat genomes provides insight into the evolution of
RT flight and immunity.";
RL Science 339:456-460(2013).
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; KB030625; ELK13201.1; -; Genomic_DNA.
DR RefSeq; XP_015444394.1; XM_015588908.1.
DR AlphaFoldDB; L5KQK6; -.
DR STRING; 9402.L5KQK6; -.
DR MEROPS; A01.009; -.
DR GeneID; 102888325; -.
DR KEGG; pale:102888325; -.
DR CTD; 1509; -.
DR eggNOG; KOG1339; Eukaryota.
DR InParanoid; L5KQK6; -.
DR OrthoDB; 1120702at2759; -.
DR Proteomes; UP000010552; 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; 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:UP000010552}.
FT DOMAIN 44..370
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 62
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 258
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT CARBOHYD 99
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000256|PIRSR:PIRSR633144-3"
FT CARBOHYD 226
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000256|PIRSR:PIRSR633144-3"
FT DISULFID 56..125
FT /evidence="ECO:0000256|PIRSR:PIRSR633144-2"
FT DISULFID 75..82
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT DISULFID 249..253
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT DISULFID 292..329
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ SEQUENCE 375 AA; 40470 MW; 946D17EA0D6AD36B CRC64;
MSEMGGPVED LIAKGPISKY AQGAPAVSGG PIPEMLKNYM DAQYYGEIGI GTPPQCFTVV
FDTGSSNLWV PSIHCKLLDI ACWIHHKYNS GKSSTYVRNG TAFDIHYGSG SLSGYLSQDT
VSVPCKSAPS PPSSVKVERQ IFGEATKQPG ITFIAAKFDG ILGMAYPRIS VNNVLPVFDN
LMQQKLVDKN IFSFYLNRDP NAQPGGELML GGTDSKYYTG SLSYLNVTRK AYWQVHMEQV
DVGNSLTLCK AGCEAIVDTG TSLVVGPVEE VRALQKAIGA VPLIQGEYMI PCEKVSSLPE
VTLKLGGKGY KLGAEDYTLK VSQGGKTICL SGFMGMDIPP PGGPLWILGD VFIGRYYTVF
DRDENRVGLA EATRV
//
