CATE_MOUSE
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 03-AUG-2022, entry version 170.
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, Clara cells
CC and alveolar macrophages of the lung, brain microglia, spleen and
CC activated 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}.
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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 GlyGen; P70269; 2 sites.
DR PhosphoSitePlus; P70269; -.
DR SwissPalm; P70269; -.
DR MaxQB; P70269; -.
DR PaxDb; P70269; -.
DR PRIDE; P70269; -.
DR ProteomicsDB; 265539; -.
DR Antibodypedia; 1957; 310 antibodies from 30 providers.
DR DNASU; 13034; -.
DR Ensembl; ENSMUST00000073350; ENSMUSP00000073072; ENSMUSG00000004552.
DR GeneID; 13034; -.
DR KEGG; mmu:13034; -.
DR UCSC; uc007cnn.2; mouse.
DR CTD; 1510; -.
DR MGI; MGI:107361; Ctse.
DR VEuPathDB; HostDB:ENSMUSG00000004552; -.
DR eggNOG; KOG1339; Eukaryota.
DR GeneTree; ENSGT00940000161300; -.
DR InParanoid; P70269; -.
DR OMA; GVECANL; -.
DR OrthoDB; 1619495at2759; -.
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 74 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 160 other tissues.
DR ExpressionAtlas; P70269; baseline and differential.
DR Genevisible; P70269; MM.
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; 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; 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
