ID   CATE_RABIT              Reviewed;         396 AA.
AC   P43159;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   25-MAY-2022, entry version 120.
DE   RecName: Full=Cathepsin E;
DE            EC=3.4.23.34;
DE   Flags: Precursor;
GN   Name=CTSE;
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Japanese white;
RX   PubMed=8404890; DOI=10.1111/j.1432-1033.1993.tb18191.x;
RA   Kageyama T.;
RT   "Rabbit procathepsin E and cathepsin E. Nucleotide sequence of cDNA,
RT   hydrolytic specificity for biologically active peptides and gene expression
RT   during development.";
RL   Eur. J. Biochem. 216:717-728(1993).
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. May play a role in activation-induced lymphocyte
CC       depletion in the thymus, and in neuronal degeneration and glial cell
CC       activation in the brain (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Similar to cathepsin D, but slightly broader specificity.;
CC         EC=3.4.23.34;
CC   -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000250}.
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   -!- PTM: Glycosylated. The nature of the carbohydrate chain varies between
CC       cell types (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase A1 family. {ECO:0000305}.
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DR   EMBL; L08418; AAC37308.1; -; mRNA.
DR   PIR; S36865; S36865.
DR   RefSeq; NP_001075713.1; NM_001082244.1.
DR   AlphaFoldDB; P43159; -.
DR   SMR; P43159; -.
DR   STRING; 9986.ENSOCUP00000001598; -.
DR   MEROPS; A01.010; -.
DR   GeneID; 100009063; -.
DR   KEGG; ocu:100009063; -.
DR   CTD; 1510; -.
DR   eggNOG; KOG1339; Eukaryota.
DR   InParanoid; P43159; -.
DR   Proteomes; UP000001811; Unplaced.
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:0016540; P:protein autoprocessing; IEA:InterPro.
DR   Gene3D; 2.40.70.10; -; 2.
DR   InterPro; IPR001461; Aspartic_peptidase_A1.
DR   InterPro; IPR001969; Aspartic_peptidase_AS.
DR   InterPro; IPR012848; Aspartic_peptidase_N.
DR   InterPro; IPR033145; Cathepsin_E.
DR   InterPro; IPR033121; PEPTIDASE_A1.
DR   InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR   PANTHER; PTHR47966; PTHR47966; 1.
DR   PANTHER; PTHR47966:SF26; PTHR47966:SF26; 1.
DR   Pfam; PF07966; A1_Propeptide; 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; Autocatalytic cleavage; Disulfide bond; Endosome;
KW   Glycoprotein; Hydrolase; Protease; Reference proteome; Signal; Zymogen.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   PROPEP          20..53
FT                   /note="Activation peptide"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000025978"
FT   CHAIN           54..396
FT                   /note="Cathepsin E"
FT                   /id="PRO_0000025979"
FT   DOMAIN          78..392
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT   ACT_SITE        96
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT   ACT_SITE        281
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT   CARBOHYD        90
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        60
FT                   /note="Interchain"
FT                   /evidence="ECO:0000305"
FT   DISULFID        109..114
FT                   /evidence="ECO:0000250"
FT   DISULFID        272..276
FT                   /evidence="ECO:0000250"
FT   DISULFID        314..351
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   396 AA;  42679 MW;  E5D84FE48DC760A4 CRC64;
     MKTLPLLLLL LLDLGQAQGT LDRVPLRRQP SLRKKLRAQG QLSEFWKAHK VDMVQYTETC
     TMEQSANEPL INYLDMEYFG TISIGSPPQN FTVIFDTVSS NLWVPSVYCT SPACQMHPQF
     RPSQSNTYSE VGTPFSIAYG TGSLTGIIGA DQVSVQGLTV VGQQFGESVK EPGQTFVNAE
     FDGILGLGYP SLAAGGVTPV FDNMMAQNLV SLPMFSVYMS SNPEGGSGSE LTFGGYDSSH
     FSGSLNWVPV TKQGYWQIAL DEIQVGGSPM FCPEGCQAIV DTGTSLITGP SDKIIQLQAA
     IGATPMDGEY AVECENLNIM PDVTFVINGV PYTLSATAYT LPDFVDGMQF CGSGFQGLDI
     QPPAGPLWIL GDVFIRQFYS VFDRGSNRVG LAPAVP