ID   CATE_AQUCT              Reviewed;         397 AA.
AC   Q800A0;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   24-JAN-2024, entry version 78.
DE   RecName: Full=Cathepsin E;
DE            EC=3.4.23.34;
DE   Flags: Precursor;
GN   Name=CTSE; Synonyms=CE;
OS   Aquarana catesbeiana (American bullfrog) (Rana catesbeiana).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Neobatrachia; Ranoidea; Ranidae; Rana; Aquarana.
OX   NCBI_TaxID=8400 {ECO:0000312|EMBL:BAC75398.1};
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 17-42 AND 50-69, TISSUE
RP   SPECIFICITY, AND GLYCOSYLATION.
RC   TISSUE=Stomach {ECO:0000312|EMBL:BAC75398.1};
RX   PubMed=12892756; DOI=10.1016/s1096-4959(03)00142-8;
RA   Inokuchi T., Ikuzawa M., Mineta T., Yasumasu S., Kobayashi K.;
RT   "Molecular cloning of preprocathepsin E cDNA from the stomach of bullfrog
RT   Rana catesbeiana.";
RL   Comp. Biochem. Physiol. 135B:647-655(2003).
CC   -!- FUNCTION: May have a role in immune function. Probably involved in the
CC       processing of antigenic peptides during MHC class II-mediated antigen
CC       presentation (By similarity). {ECO:0000250|UniProtKB:P14091}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Similar to cathepsin D, but slightly broader specificity.;
CC         EC=3.4.23.34; Evidence={ECO:0000250|UniProtKB:Q805F3};
CC   -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000250|UniProtKB:Q805F3}.
CC   -!- SUBCELLULAR LOCATION: Endosome {ECO:0000250}. Note=The proenzyme is
CC       localized to the endoplasmic reticulum and Golgi apparatus, while the
CC       mature enzyme is localized to the endosome. {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Found in the larval foregut and adult stomach.
CC       {ECO:0000269|PubMed:12892756}.
CC   -!- PTM: Glycosylated. Contains high mannose-type oligosaccharide.
CC       {ECO:0000269|PubMed:12892756}.
CC   -!- SIMILARITY: Belongs to the peptidase A1 family. {ECO:0000305}.
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; AB093036; BAC75398.1; -; mRNA.
DR   AlphaFoldDB; Q800A0; -.
DR   SMR; Q800A0; -.
DR   MEROPS; A01.010; -.
DR   GlyCosmos; Q800A0; 1 site, No reported glycans.
DR   GO; GO:0005768; C:endosome; ISS:UniProtKB.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; ISS:UniProtKB.
DR   GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; ISS:UniProtKB.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 6.10.140.60; -; 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:SF26; CATHEPSIN E; 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   1: Evidence at protein level;
KW   Aspartyl protease; Direct protein sequencing; Disulfide bond; Endosome;
KW   Glycoprotein; Hydrolase; Protease; Signal; Zymogen.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000269|PubMed:12892756"
FT   PROPEP          17..49
FT                   /note="Activation peptide"
FT                   /evidence="ECO:0000269|PubMed:12892756"
FT                   /id="PRO_0000025982"
FT   CHAIN           50..397
FT                   /note="Cathepsin E"
FT                   /evidence="ECO:0000269|PubMed:12892756"
FT                   /id="PRO_0000025983"
FT   DOMAIN          74..385
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT   ACT_SITE        92
FT                   /evidence="ECO:0000250|UniProtKB:P00790,
FT                   ECO:0000255|PROSITE-ProRule:PRU10094"
FT   ACT_SITE        277
FT                   /evidence="ECO:0000250|UniProtKB:P00790,
FT                   ECO:0000255|PROSITE-ProRule:PRU10094"
FT   CARBOHYD        139
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000305"
FT   DISULFID        105..110
FT                   /evidence="ECO:0000250|UniProtKB:P00790"
FT   DISULFID        268..272
FT                   /evidence="ECO:0000250|UniProtKB:P00790"
FT   DISULFID        310..344
FT                   /evidence="ECO:0000250|UniProtKB:P00790"
SQ   SEQUENCE   397 AA;  43307 MW;  4F2D59D7F50F06B4 CRC64;
     MKQFLVVLLI LSFVHGIIRV PLKRQKSMRK ILKEKGKLSH LWTKQGNEFL QLSDSCSSPE
     TASEPLMNYL DVEYFGQISI GTPPQQFTVI FDTGSSNLWV PSIYCTSQAC TKHNRYRPSE
     STTYVSNGEA FFIQYGTGNL TGILGIDQVT VQGITVQSQT FAESVSEPGS TFQDSNFDGI
     LGLAYPNLAV DNCIPVFDNM IAQNLVELPL FGVYMNRDPN SADGGELVLG GFDTSRFSGQ
     LNWVPITVQG YWQIQVDSIQ VAGQVIFCSD GCQAIVDTGT SLITGPSGDI EQLQNYIGVT
     NTNGEYGVSC STLSLMPSVT FTINGLDYSL TPEQYMLEDG GGYCSSGFQG LDISPPSGPL
     WILGDVFIGQ YYSVFDRGNN RVGFAPVVFY ETTTNGA
//