ID Q5C141_SCHJA Unreviewed; 262 AA. AC Q5C141; DT 12-APR-2005, integrated into UniProtKB/TrEMBL. DT 12-APR-2005, sequence version 1. DT 15-FEB-2017, entry version 59. DE SubName: Full=Cathepsin D (Lysosomal aspartyl protease) {ECO:0000313|EMBL:CAX72341.1}; DE EC=3.4.23.5 {ECO:0000313|EMBL:CAX72341.1}; DE SubName: Full=Putative uncharacterized protein {ECO:0000313|EMBL:AAX26634.1}; GN Name=ctsd {ECO:0000313|EMBL:CAX72341.1}; OS Schistosoma japonicum (Blood fluke). OC Eukaryota; Metazoa; Platyhelminthes; Trematoda; Digenea; Strigeidida; OC Schistosomatoidea; Schistosomatidae; Schistosoma. OX NCBI_TaxID=6182 {ECO:0000313|EMBL:AAX26634.1}; RN [1] {ECO:0000313|EMBL:AAX26634.1} RP NUCLEOTIDE SEQUENCE. RA Han Z.; RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:AAX26634.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=16617374; DOI=10.1371/journal.ppat.0020029; RA Liu F., Lu J., Hu W., Wang S.Y., Cui S.J., Chi M., Yan Q., Wang X.R., RA Song H.D., Xu X.N., Wang J.J., Zhang X.L., Zhang X., Wang Z.Q., RA Xue C.L., Brindley P.J., McManus D.P., Yang P.Y., Feng Z., Chen Z., RA Han Z.G.; RT "New perspectives on host-parasite interplay by comparative RT transcriptomic and proteomic analyses of Schistosoma japonicum."; RL PLoS Pathog. 2:268-281(2006). RN [3] {ECO:0000313|EMBL:CAX72341.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Anhui {ECO:0000313|EMBL:CAX72341.1}; RX DOI=10.1038/nature08140; RA Liu F., Zhou Y., Wang Z.Q., Lu G., Zheng H., Brindley P.J., RA McManus D.P., Blair D., Zhang Q.H., Zhong Y., Wang S., Han Z.G., RA Chen Z.; RT "The Schistosoma japonicum genome reveals features of host-parasite RT interplay."; RL Nature 460:345-351(2009). RN [4] {ECO:0000313|EMBL:CAX72341.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Anhui {ECO:0000313|EMBL:CAX72341.1}; RA Gang L.; RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the peptidase A1 family. CC {ECO:0000256|PROSITE-ProRule:PRU01103, CC ECO:0000256|RuleBase:RU000454, ECO:0000256|SAAS:SAAS00670156}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01103}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AY810745; AAX26634.1; -; mRNA. DR EMBL; FN316610; CAX72341.1; -; mRNA. DR MEROPS; A01.009; -. DR GO; GO:0005764; C:lysosome; IEA:InterPro. DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW. DR Gene3D; 2.40.70.10; -; 1. 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. DR PANTHER; PTHR13683; PTHR13683; 1. DR PANTHER; PTHR13683:SF487; PTHR13683:SF487; 1. DR Pfam; PF00026; Asp; 1. DR PRINTS; PR00792; PEPSIN. DR SUPFAM; SSF50630; SSF50630; 1. DR PROSITE; PS00141; ASP_PROTEASE; 1. DR PROSITE; PS51767; PEPTIDASE_A1; 1. PE 2: Evidence at transcript level; KW Aspartyl protease {ECO:0000256|RuleBase:RU000454, KW ECO:0000256|SAAS:SAAS00629219}; KW Hydrolase {ECO:0000256|RuleBase:RU000454, KW ECO:0000256|SAAS:SAAS00629231, ECO:0000313|EMBL:CAX72341.1}; KW Protease {ECO:0000256|RuleBase:RU000454, KW ECO:0000256|SAAS:SAAS00629201, ECO:0000313|EMBL:CAX72341.1}. FT DOMAIN 1 213 Peptidase A1. {ECO:0000259|PROSITE: FT PS51767}. SQ SEQUENCE 262 AA; 28687 MW; B83065B5693118A1 CRC64; MAKFDGILGM AYPSLAVGGV TPVFVNMIKQ GVVDSPVFSF YLSRNITNVL GGELMIGGID DKYYTGEINY VNLTEKSYWL FKMDNLTISD LSICTDGCQA IADTGTSMIA GPTDEVKQIN QKLGATHLPG GIYTVSCDVI NNLPSIDFVI NGKHMTLEPT DYIMKVSKLG SEICLTGFIG MDLPRKKLWI LGDVFIGKFY TIFDMGKNRV GFAKAVKPDS SYHHTKVYSP MLRLFPAQSI PKVAPKSPNG VFAFSKLLHD AN //