ID   CATE_MOUSE              Reviewed;         397 AA.
AC   P70269; O35647; Q3UKT5; Q4FK00;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 2.
DT   27-MAR-2024, entry version 178.
DE   RecName: Full=Cathepsin E;
DE            EC=3.4.23.34;
DE   Flags: Precursor;
GN   Name=Ctse;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND CATALYTIC ACTIVITY.
RC   STRAIN=BALB/cJ; TISSUE=Spleen;
RX   PubMed=9180269; DOI=10.1016/s0014-5793(97)00388-8;
RA   Tatnell P.J., Lees W.E., Kay J.;
RT   "Cloning, expression and characterisation of murine procathepsin E.";
RL   FEBS Lett. 408:62-66(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=129/SvJ;
RX   PubMed=9602058; DOI=10.1016/s0167-4781(98)00028-1;
RA   Tatnell P.J., Roth W., Deussing J., Peters C., Kay J.;
RT   "Mouse procathepsin E gene: molecular organisation and chromosomal
RT   localisation.";
RL   Biochim. Biophys. Acta 1398:57-66(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RC   STRAIN=129/SvJ; TISSUE=Gastric mucosa;
RA   Yonezawa S., Masaki S., Hanai A., Ono T., Sonta S., Hirai H., Ichinose M.,
RA   Miki K., Takahashi K., Kageyama T.;
RT   "Cathepsin E gene in mouse.";
RL   Biomed. Res. 19:327-334(1998).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Inner ear, Liver, and Spleen;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Ebert L., Muenstermann E., Schatten R., Henze S., Bohn E., Mollenhauer J.,
RA   Wiemann S., Schick M., Korn B.;
RT   "Cloning of mouse full open reading frames in Gateway(R) system entry
RT   vector (pDONR201).";
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [8]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=1601038; DOI=10.1002/eji.1830220626;
RA   Bennett K., Levine T., Ellis J.S., Peanasky R.J., Samloff I.M., Kay J.,
RA   Chain B.M.;
RT   "Antigen processing for presentation by class II major histocompatibility
RT   complex requires cleavage by cathepsin E.";
RL   Eur. J. Immunol. 22:1519-1524(1992).
RN   [9]
RP   GLYCOSYLATION.
RX   PubMed=7983070; DOI=10.1016/s0021-9258(18)47417-0;
RA   Finley E.M., Kornfeld S.;
RT   "Subcellular localization and targeting of cathepsin E.";
RL   J. Biol. Chem. 269:31259-31266(1994).
RN   [10]
RP   TISSUE SPECIFICITY.
RX   PubMed=11322887; DOI=10.1046/j.1432-1327.2001.02159.x;
RA   Cook M., Caswell R.C., Richards R.J., Kay J., Tatnell P.J.;
RT   "Regulation of human and mouse procathepsin E gene expression.";
RL   Eur. J. Biochem. 268:2658-2668(2001).
RN   [11]
RP   FUNCTION.
RX   PubMed=11719510; DOI=10.1074/jbc.m108382200;
RA   Nishioku T., Hashimoto K., Yamashita K., Liou S.-Y., Kagamiishi Y.,
RA   Maegawa H., Katsube N., Peters C., von Figura K., Saftig P., Katunuma N.,
RA   Yamamoto K., Nakanishi H.;
RT   "Involvement of cathepsin E in exogenous antigen processing in primary
RT   cultured murine microglia.";
RL   J. Biol. Chem. 277:4816-4822(2002).
RN   [12]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Spleen;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
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. {ECO:0000269|PubMed:11719510,
CC       ECO:0000269|PubMed:1601038}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Similar to cathepsin D, but slightly broader specificity.;
CC         EC=3.4.23.34; Evidence={ECO:0000269|PubMed:9180269};
CC   -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Endosome {ECO:0000269|PubMed:1601038}. Note=The
CC       proenzyme is localized to the endoplasmic reticulum and Golgi
CC       apparatus, while the mature enzyme is localized to the endosome.
CC   -!- TISSUE SPECIFICITY: Expressed abundantly in the stomach, club cells and
CC       alveolar macrophages of the lung, brain microglia, spleen and activated
CC       B-lymphocytes. Not expressed in resting B-lymphocytes.
CC       {ECO:0000269|PubMed:11322887, ECO:0000269|Ref.3}.
CC   -!- PTM: Glycosylated. The nature of the carbohydrate chain varies between
CC       cell types. In fibroblasts, the proenzyme contains a high mannose-type
CC       oligosaccharide, while the mature enzyme contains a complex-type
CC       oligosaccharide. {ECO:0000269|PubMed:7983070}.
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; X97399; CAA66056.1; -; mRNA.
DR   EMBL; Y10928; CAA71859.1; -; Genomic_DNA.
DR   EMBL; AJ009840; CAA08880.2; -; Genomic_DNA.
DR   EMBL; AJ009841; CAA08880.2; JOINED; Genomic_DNA.
DR   EMBL; AJ009842; CAA08880.2; JOINED; Genomic_DNA.
DR   EMBL; AJ009843; CAA08880.2; JOINED; Genomic_DNA.
DR   EMBL; AJ009844; CAA08880.2; JOINED; Genomic_DNA.
DR   EMBL; AJ009845; CAA08880.2; JOINED; Genomic_DNA.
DR   EMBL; AJ009846; CAA08880.2; JOINED; Genomic_DNA.
DR   EMBL; AJ009847; CAA08880.2; JOINED; Genomic_DNA.
DR   EMBL; AJ009848; CAA08880.2; JOINED; Genomic_DNA.
DR   EMBL; AK143581; BAE25449.1; -; mRNA.
DR   EMBL; AK145875; BAE26716.1; -; mRNA.
DR   EMBL; AK157907; BAE34257.1; -; mRNA.
DR   EMBL; AK165271; BAE38113.1; -; mRNA.
DR   EMBL; CT010252; CAJ18460.1; -; mRNA.
DR   EMBL; CH466520; EDL39705.1; -; Genomic_DNA.
DR   EMBL; BC005432; AAH05432.1; -; mRNA.
DR   CCDS; CCDS15271.1; -.
DR   RefSeq; NP_031825.2; NM_007799.3.
DR   AlphaFoldDB; P70269; -.
DR   SMR; P70269; -.
DR   STRING; 10090.ENSMUSP00000073072; -.
DR   BindingDB; P70269; -.
DR   ChEMBL; CHEMBL1681627; -.
DR   MEROPS; A01.010; -.
DR   GlyCosmos; P70269; 2 sites, No reported glycans.
DR   GlyGen; P70269; 2 sites.
DR   PhosphoSitePlus; P70269; -.
DR   SwissPalm; P70269; -.
DR   MaxQB; P70269; -.
DR   PaxDb; 10090-ENSMUSP00000073072; -.
DR   ProteomicsDB; 265539; -.
DR   Antibodypedia; 1957; 331 antibodies from 30 providers.
DR   DNASU; 13034; -.
DR   Ensembl; ENSMUST00000073350.13; ENSMUSP00000073072.7; ENSMUSG00000004552.17.
DR   GeneID; 13034; -.
DR   KEGG; mmu:13034; -.
DR   UCSC; uc007cnn.2; mouse.
DR   AGR; MGI:107361; -.
DR   CTD; 1510; -.
DR   MGI; MGI:107361; Ctse.
DR   VEuPathDB; HostDB:ENSMUSG00000004552; -.
DR   eggNOG; KOG1339; Eukaryota.
DR   GeneTree; ENSGT00940000161300; -.
DR   InParanoid; P70269; -.
DR   OMA; YGVECAN; -.
DR   OrthoDB; 1120702at2759; -.
DR   PhylomeDB; P70269; -.
DR   TreeFam; TF314990; -.
DR   BRENDA; 3.4.23.34; 3474.
DR   Reactome; R-MMU-2132295; MHC class II antigen presentation.
DR   BioGRID-ORCS; 13034; 4 hits in 79 CRISPR screens.
DR   ChiTaRS; Ctse; mouse.
DR   PRO; PR:P70269; -.
DR   Proteomes; UP000000589; Chromosome 1.
DR   RNAct; P70269; Protein.
DR   Bgee; ENSMUSG00000004552; Expressed in epithelium of stomach and 161 other cell types or tissues.
DR   ExpressionAtlas; P70269; baseline and differential.
DR   GO; GO:0005768; C:endosome; IDA:UniProtKB.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IDA:UniProtKB.
DR   GO; GO:0042802; F:identical protein binding; IPI:MGI.
DR   GO; GO:0008233; F:peptidase activity; ISO:MGI.
DR   GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; IDA:UniProtKB.
DR   GO; GO:0016540; P:protein autoprocessing; ISO:MGI.
DR   GO; GO:0006508; P:proteolysis; ISO:MGI.
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.
DR   Genevisible; P70269; MM.
PE   1: Evidence at protein level;
KW   Aspartyl protease; Autocatalytic cleavage; Disulfide bond; Endosome;
KW   Glycoprotein; Hydrolase; Protease; Reference proteome; Signal; Zymogen.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000250"
FT   PROPEP          21..59
FT                   /note="Activation peptide"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000025976"
FT   CHAIN           60..397
FT                   /note="Cathepsin E"
FT                   /id="PRO_0000025977"
FT   DOMAIN          79..393
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT   ACT_SITE        97
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT   ACT_SITE        282
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT   CARBOHYD        91
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        323
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        61
FT                   /note="Interchain"
FT                   /evidence="ECO:0000305"
FT   DISULFID        110..115
FT                   /evidence="ECO:0000250"
FT   DISULFID        273..277
FT                   /evidence="ECO:0000250"
FT   CONFLICT        297
FT                   /note="Q -> H (in Ref. 1; CAA66056, 5; CAJ18460 and 7;
FT                   AAH05432)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        347
FT                   /note="E -> D (in Ref. 1; CAA66056, 2; CAA71859, 5;
FT                   CAJ18460 and 7; AAH05432)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   397 AA;  42938 MW;  DF6AEFD5F78B3747 CRC64;
     MKPLLVLLLL LLLDLAQAQG ALHRVPLRRH QSLRKKLRAQ GQLSEFWRSH NLDMTRLSES
     CNVYSSVNEP LINYLDMEYF GTISIGTPPQ NFTVIFDTGS SNLWVPSVYC TSPACKAHPV
     FHPSQSDTYT EVGNHFSIQY GTGSLTGIIG ADQVSVEGLT VDGQQFGESV KEPGQTFVNA
     EFDGILGLGY PSLAAGGVTP VFDNMMAQNL VALPMFSVYL SSDPQGGSGS ELTFGGYDPS
     HFSGSLNWIP VTKQAYWQIA LDGIQVGDTV MFCSEGCQAI VDTGTSLITG PPDKIKQLQE
     AIGATPIDGE YAVDCATLDT MPNVTFLINE VSYTLNPTDY ILPDLVEGMQ FCGSGFQGLD
     IPPPAGPLWI LGDVFIRQFY SVFDRGNNQV GLAPAVP
//