ID   CATE_CAVPO              Reviewed;         391 AA.
AC   P25796;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1992, sequence version 1.
DT   03-AUG-2022, entry version 138.
DE   RecName: Full=Cathepsin E;
DE            EC=3.4.23.34;
DE   Flags: Precursor;
GN   Name=CTSE;
OS   Cavia porcellus (Guinea pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC   Cavia.
OX   NCBI_TaxID=10141;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 20-48, CATALYTIC ACTIVITY,
RP   SUBUNIT, AND TISSUE SPECIFICITY.
RX   PubMed=1644829; DOI=10.1016/s0021-9258(18)42024-8;
RA   Kageyama T., Ichinose M., Tsukada S., Miki K., Kurokawa K., Koiwai O.,
RA   Tanji M., Yakabe E., Athauda S.B., Takahashi K.;
RT   "Gastric procathepsin E and progastricsin from guinea pig. Purification,
RT   molecular cloning of cDNAs, and characterization of enzymatic properties,
RT   with special reference to procathepsin E.";
RL   J. Biol. Chem. 267:16450-16459(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Gastric mucosa;
RX   PubMed=8540321; DOI=10.1007/978-1-4615-1871-6_25;
RA   Kageyama T., Ichinose M., Miki K., Moriyama A., Yonezawa S., Tanji M.,
RA   Athauda S.B., Takahashi K.;
RT   "Isolation, characterization, and structure of procathepsin E and cathepsin
RT   E from the gastric mucosa of guinea pig.";
RL   Adv. Exp. Med. Biol. 362:211-221(1995).
RN   [3]
RP   TISSUE SPECIFICITY.
RX   PubMed=1417816; DOI=10.1016/0006-291x(92)90458-w;
RA   Tsukada S., Ichinose M., Miki K., Tatematsu M., Yonezawa S., Matsushima M.,
RA   Kakei N., Fukamachi H., Yasugi S., Kurokawa K., Kageyama T., Takahashi K.;
RT   "Tissue- and cell-specific control of guinea pig cathepsin E gene
RT   expression.";
RL   Biochem. Biophys. Res. Commun. 187:1401-1408(1992).
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; Evidence={ECO:0000269|PubMed:1644829};
CC   -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000269|PubMed:1644829}.
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: Expressed abundantly in the surface and foveolar
CC       epithelial cells of the fundic and pyloric stomach mucosa, and at very
CC       low levels in the spleen. {ECO:0000269|PubMed:1417816,
CC       ECO:0000269|PubMed:1644829}.
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; M88653; AAA37052.1; -; mRNA.
DR   EMBL; S80547; AAB35844.1; -; mRNA.
DR   PIR; A43356; A43356.
DR   RefSeq; NP_001166408.1; NM_001172937.1.
DR   AlphaFoldDB; P25796; -.
DR   SMR; P25796; -.
DR   STRING; 10141.ENSCPOP00000008547; -.
DR   MEROPS; A01.010; -.
DR   Ensembl; ENSCPOT00000009609; ENSCPOP00000008547; ENSCPOG00000009523.
DR   GeneID; 100135509; -.
DR   KEGG; cpoc:100135509; -.
DR   CTD; 1510; -.
DR   eggNOG; KOG1339; Eukaryota.
DR   GeneTree; ENSGT00940000161300; -.
DR   HOGENOM; CLU_013253_3_0_1; -.
DR   InParanoid; P25796; -.
DR   OMA; GVECANL; -.
DR   OrthoDB; 1619495at2759; -.
DR   TreeFam; TF314990; -.
DR   Proteomes; UP000005447; Unassembled WGS sequence.
DR   Bgee; ENSCPOG00000009523; Expressed in zone of skin and 3 other tissues.
DR   GO; GO:0005768; C:endosome; ISS:UniProtKB.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; ISS:UniProtKB.
DR   GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
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; 2.
DR   PROSITE; PS51767; PEPTIDASE_A1; 1.
PE   1: Evidence at protein level;
KW   Aspartyl protease; Autocatalytic cleavage; Direct protein sequencing;
KW   Disulfide bond; Endosome; Glycoprotein; Hydrolase; Protease;
KW   Reference proteome; Signal; Zymogen.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000269|PubMed:1644829"
FT   PROPEP          20..53
FT                   /note="Activation peptide"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000025972"
FT   CHAIN           54..391
FT                   /note="Cathepsin E"
FT                   /id="PRO_0000025973"
FT   DOMAIN          74..387
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT   ACT_SITE        92
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT   ACT_SITE        276
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT   CARBOHYD        86
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        56
FT                   /note="Interchain"
FT                   /evidence="ECO:0000305"
FT   DISULFID        105..110
FT                   /evidence="ECO:0000250"
FT   DISULFID        267..271
FT                   /evidence="ECO:0000250"
FT   DISULFID        309..346
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   391 AA;  42132 MW;  78D216BF8CFCDABD CRC64;
     MKTFLLLLLV LLELGQAPGA LHRVPLSRRE SLRKKLRAQG QLTELWKSQN LNMDQCSTIQ
     SANEPLINYL DMEYFGTISI GSPPQNFTVI FDTGSSNLWV PSVYCTSPAC QTHPVFHPSL
     SSTYREVGNS FSIQYGTGSL TGIIGADQVS VEGLTVVGQQ FGESVQEPGK TFVHAEFDGI
     LGLGYPSLAA GGVTPVFDNM MAQNLVALPM FSVYMSSNPG GSGSELTFGG YDPSHFSGSL
     NWVPVTKQAY WQIALDGIQV GDSVMFCSEG CQAIVDTGTS LITGPPGKIK QLQEALGATY
     VDEGYSVQCA NLNMMLDVTF IINGVPYTLN PTAYTLLDFV DGMQVCSTGF EGLEIQPPAG
     PLWILGDVFI RQFYAVFDRG NNRVGLAPAV P