ID C1LCB6_SCHJA Unreviewed; 429 AA.
AC C1LCB6;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=Cathepsin D (Lysosomal aspartyl protease) {ECO:0000313|EMBL:CAX72344.1};
DE EC=3.4.23.5 {ECO:0000313|EMBL:CAX72344.1};
GN Name=ctsd {ECO:0000313|EMBL:CAX72344.1};
OS Schistosoma japonicum (Blood fluke).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma.
OX NCBI_TaxID=6182 {ECO:0000313|EMBL:CAX72344.1};
RN [1] {ECO:0000313|EMBL:CAX72344.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Anhui {ECO:0000313|EMBL:CAX72344.1};
RX DOI=10.1038/nature08140;
RA Liu F., Zhou Y., Wang Z.Q., Lu G., Zheng H., Brindley P.J., McManus D.P.,
RA Blair D., Zhang Q.H., Zhong Y., Wang S., Han Z.G., Chen Z.;
RT "The Schistosoma japonicum genome reveals features of host-parasite
RT interplay.";
RL Nature 460:345-351(2009).
RN [2] {ECO:0000313|EMBL:CAX72344.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Anhui {ECO:0000313|EMBL:CAX72344.1};
RA Gang L.;
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase A1 family.
CC {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
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DR EMBL; FN316613; CAX72344.1; -; mRNA.
DR AlphaFoldDB; C1LCB6; -.
DR MEROPS; A01.009; -.
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; IPR012848; Aspartic_peptidase_N.
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:SF51; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 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 2: Evidence at transcript level;
KW Aspartyl protease {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 Protease {ECO:0000256|RuleBase:RU000454, ECO:0000313|EMBL:CAX72344.1}.
FT DOMAIN 66..380
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 84
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 270
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT DISULFID 97..104
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT DISULFID 261..265
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT DISULFID 304..341
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ SEQUENCE 429 AA; 47378 MW; 64CFD8B65C19E3AE CRC64;
MLHLLLLLHL VSSEVVRVPL YPLKSARRSL IEFETSLENV QKVWFSRFSN VEPRPEYLKN
YLDAQYYGDI TIGTPPQTFS VVFDTGSSNL WVPSKHCSYF DIACLLHRKY DSSKSTTYVP
NGTDFSIRYG TGSLSGFLST DSLQLGSLGV KGQTFGEATK QPGLVFVMAK FDGILGMAYP
SLAVGGVTPV FVNMIKQGVV DSPVFSFYLS RNITNVLGGE LMIGGIDDKY YTGEINYVNL
TEKSYWLFKM DNLTISDLSI CTDGCQAIAD TGTSMIAGPT DEVKQINQKL GATHLPGGIY
TVSCDVINNL PSIDFVINGK HMTLEPTDYI MKVSKLGSEI CLTGFIGMDL PRKKLWILGD
VFIGKFYTIF DMGKNRVGFA KAVKPDSSYH HPKVYSPMLR LFPAQSIPKV APKSPNGVFA
FSKLLHDAN
//
