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Cathepsin E (EC 3.4.23.34)

 CATE_CAVPO              Reviewed;         391 AA.
P25796;
01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
01-MAY-1992, sequence version 1.
22-NOV-2017, entry version 121.
RecName: Full=Cathepsin E;
EC=3.4.23.34;
Flags: Precursor;
Name=CTSE;
Cavia porcellus (Guinea pig).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia;
Hystricomorpha; Caviidae; Cavia.
NCBI_TaxID=10141;
[1]
NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 20-48, CATALYTIC
ACTIVITY, SUBUNIT, AND TISSUE SPECIFICITY.
PubMed=1644829;
Kageyama T., Ichinose M., Tsukada S., Miki K., Kurokawa K., Koiwai O.,
Tanji M., Yakabe E., Athauda S.B., Takahashi K.;
"Gastric procathepsin E and progastricsin from guinea pig.
Purification, molecular cloning of cDNAs, and characterization of
enzymatic properties, with special reference to procathepsin E.";
J. Biol. Chem. 267:16450-16459(1992).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Gastric mucosa;
PubMed=8540321;
Kageyama T., Ichinose M., Miki K., Moriyama A., Yonezawa S., Tanji M.,
Athauda S.B., Takahashi K.;
"Isolation, characterization, and structure of procathepsin E and
cathepsin E from the gastric mucosa of guinea pig.";
Adv. Exp. Med. Biol. 362:211-221(1995).
[3]
TISSUE SPECIFICITY.
PubMed=1417816; DOI=10.1016/0006-291X(92)90458-W;
Tsukada S., Ichinose M., Miki K., Tatematsu M., Yonezawa S.,
Matsushima M., Kakei N., Fukamachi H., Yasugi S., Kurokawa K.,
Kageyama T., Takahashi K.;
"Tissue- and cell-specific control of guinea pig cathepsin E gene
expression.";
Biochem. Biophys. Res. Commun. 187:1401-1408(1992).
-!- FUNCTION: May have a role in immune function. Probably involved in
the processing of antigenic peptides during MHC class II-mediated
antigen presentation. May play a role in activation-induced
lymphocyte depletion in the thymus, and in neuronal degeneration
and glial cell activation in the brain (By similarity).
{ECO:0000250}.
-!- CATALYTIC ACTIVITY: Similar to cathepsin D, but slightly broader
specificity. {ECO:0000269|PubMed:1644829}.
-!- SUBUNIT: Homodimer; disulfide-linked.
{ECO:0000269|PubMed:1644829}.
-!- SUBCELLULAR LOCATION: Endosome {ECO:0000250}. Note=The proenzyme
is localized to the endoplasmic reticulum and Golgi apparatus,
while the mature enzyme is localized to the endosome.
{ECO:0000250}.
-!- TISSUE SPECIFICITY: Expressed abundantly in the surface and
foveolar epithelial cells of the fundic and pyloric stomach
mucosa, and at very low levels in the spleen.
{ECO:0000269|PubMed:1417816, ECO:0000269|PubMed:1644829}.
-!- PTM: Glycosylated. The nature of the carbohydrate chain varies
between cell types (By similarity). {ECO:0000250}.
-!- SIMILARITY: Belongs to the peptidase A1 family. {ECO:0000305}.
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EMBL; M88653; AAA37052.1; -; mRNA.
EMBL; S80547; AAB35844.1; -; mRNA.
PIR; A43356; A43356.
RefSeq; NP_001166408.1; NM_001172937.1.
ProteinModelPortal; P25796; -.
SMR; P25796; -.
STRING; 10141.ENSCPOP00000008547; -.
MEROPS; A01.010; -.
Ensembl; ENSCPOT00000009609; ENSCPOP00000008547; ENSCPOG00000009523.
GeneID; 100135509; -.
CTD; 1510; -.
eggNOG; KOG1339; Eukaryota.
eggNOG; ENOG410XNV7; LUCA.
GeneTree; ENSGT00760000118929; -.
HOGENOM; HOG000197681; -.
HOVERGEN; HBG000482; -.
InParanoid; P25796; -.
OMA; KEPGQTF; -.
OrthoDB; EOG091G0JP7; -.
TreeFam; TF314990; -.
PMAP-CutDB; P25796; -.
Proteomes; UP000005447; Unassembled WGS sequence.
Bgee; ENSCPOG00000009523; -.
GO; GO:0005768; C:endosome; ISS:UniProtKB.
GO; GO:0070062; C:extracellular exosome; IEA:Ensembl.
GO; GO:0004190; F:aspartic-type endopeptidase activity; ISS:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; ISS:UniProtKB.
GO; GO:0016540; P:protein autoprocessing; IEA:InterPro.
Gene3D; 2.40.70.10; -; 2.
InterPro; IPR001461; Aspartic_peptidase_A1.
InterPro; IPR001969; Aspartic_peptidase_AS.
InterPro; IPR012848; Aspartic_peptidase_N.
InterPro; IPR033145; Cathepsin_E.
InterPro; IPR033121; PEPTIDASE_A1.
InterPro; IPR021109; Peptidase_aspartic_dom_sf.
PANTHER; PTHR13683; PTHR13683; 1.
PANTHER; PTHR13683:SF81; PTHR13683:SF81; 1.
Pfam; PF07966; A1_Propeptide; 1.
Pfam; PF00026; Asp; 1.
PRINTS; PR00792; PEPSIN.
SUPFAM; SSF50630; SSF50630; 1.
PROSITE; PS00141; ASP_PROTEASE; 2.
PROSITE; PS51767; PEPTIDASE_A1; 1.
1: Evidence at protein level;
Aspartyl protease; Autocatalytic cleavage; Complete proteome;
Direct protein sequencing; Disulfide bond; Endosome; Glycoprotein;
Hydrolase; Protease; Reference proteome; Signal; Zymogen.
SIGNAL 1 19 {ECO:0000269|PubMed:1644829}.
PROPEP 20 53 Activation peptide. {ECO:0000255}.
/FTId=PRO_0000025972.
CHAIN 54 391 Cathepsin E.
/FTId=PRO_0000025973.
DOMAIN 74 387 Peptidase A1. {ECO:0000255|PROSITE-
ProRule:PRU01103}.
ACT_SITE 92 92 {ECO:0000255|PROSITE-ProRule:PRU10094}.
ACT_SITE 276 276 {ECO:0000255|PROSITE-ProRule:PRU10094}.
CARBOHYD 86 86 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 56 56 Interchain. {ECO:0000305}.
DISULFID 105 110 {ECO:0000250}.
DISULFID 267 271 {ECO:0000250}.
DISULFID 309 346 {ECO:0000250}.
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


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