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Cathepsin E (EC 3.4.23.34)

 CATE_MOUSE              Reviewed;         397 AA.
P70269; O35647; Q3UKT5; Q4FK00;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 2.
22-NOV-2017, entry version 145.
RecName: Full=Cathepsin E;
EC=3.4.23.34;
Flags: Precursor;
Name=Ctse;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND CATALYTIC ACTIVITY.
STRAIN=BALB/cJ; TISSUE=Spleen;
PubMed=9180269; DOI=10.1016/S0014-5793(97)00388-8;
Tatnell P.J., Lees W.E., Kay J.;
"Cloning, expression and characterisation of murine procathepsin E.";
FEBS Lett. 408:62-66(1997).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=129/SvJ;
PubMed=9602058; DOI=10.1016/S0167-4781(98)00028-1;
Tatnell P.J., Roth W., Deussing J., Peters C., Kay J.;
"Mouse procathepsin E gene: molecular organisation and chromosomal
localisation.";
Biochim. Biophys. Acta 1398:57-66(1998).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
STRAIN=129/SvJ; TISSUE=Gastric mucosa;
Yonezawa S., Masaki S., Hanai A., Ono T., Sonta S., Hirai H.,
Ichinose M., Miki K., Takahashi K., Kageyama T.;
"Cathepsin E gene in mouse.";
Biomed. Res. 19:327-334(1998).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Inner ear, Liver, and Spleen;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Ebert L., Muenstermann E., Schatten R., Henze S., Bohn E.,
Mollenhauer J., Wiemann S., Schick M., Korn B.;
"Cloning of mouse full open reading frames in Gateway(R) system entry
vector (pDONR201).";
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N; TISSUE=Mammary gland;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=1601038; DOI=10.1002/eji.1830220626;
Bennett K., Levine T., Ellis J.S., Peanasky R.J., Samloff I.M.,
Kay J., Chain B.M.;
"Antigen processing for presentation by class II major
histocompatibility complex requires cleavage by cathepsin E.";
Eur. J. Immunol. 22:1519-1524(1992).
[9]
GLYCOSYLATION.
PubMed=7983070;
Finley E.M., Kornfeld S.;
"Subcellular localization and targeting of cathepsin E.";
J. Biol. Chem. 269:31259-31266(1994).
[10]
TISSUE SPECIFICITY.
PubMed=11322887; DOI=10.1046/j.1432-1327.2001.02159.x;
Cook M., Caswell R.C., Richards R.J., Kay J., Tatnell P.J.;
"Regulation of human and mouse procathepsin E gene expression.";
Eur. J. Biochem. 268:2658-2668(2001).
[11]
FUNCTION.
PubMed=11719510; DOI=10.1074/jbc.M108382200;
Nishioku T., Hashimoto K., Yamashita K., Liou S.-Y., Kagamiishi Y.,
Maegawa H., Katsube N., Peters C., von Figura K., Saftig P.,
Katunuma N., Yamamoto K., Nakanishi H.;
"Involvement of cathepsin E in exogenous antigen processing in primary
cultured murine microglia.";
J. Biol. Chem. 277:4816-4822(2002).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Spleen;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- 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.
{ECO:0000269|PubMed:11719510, ECO:0000269|PubMed:1601038}.
-!- CATALYTIC ACTIVITY: Similar to cathepsin D, but slightly broader
specificity. {ECO:0000269|PubMed:9180269}.
-!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Endosome {ECO:0000269|PubMed:1601038}.
Note=The proenzyme is localized to the endoplasmic reticulum and
Golgi apparatus, while the mature enzyme is localized to the
endosome.
-!- TISSUE SPECIFICITY: Expressed abundantly in the stomach, Clara
cells and alveolar macrophages of the lung, brain microglia,
spleen and activated B-lymphocytes. Not expressed in resting B-
lymphocytes. {ECO:0000269|PubMed:11322887, ECO:0000269|Ref.3}.
-!- PTM: Glycosylated. The nature of the carbohydrate chain varies
between cell types. In fibroblasts, the proenzyme contains a high
mannose-type oligosaccharide, while the mature enzyme contains a
complex-type oligosaccharide. {ECO:0000269|PubMed:7983070}.
-!- SIMILARITY: Belongs to the peptidase A1 family. {ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; X97399; CAA66056.1; -; mRNA.
EMBL; Y10928; CAA71859.1; -; Genomic_DNA.
EMBL; AJ009840; CAA08880.2; -; Genomic_DNA.
EMBL; AJ009841; CAA08880.2; JOINED; Genomic_DNA.
EMBL; AJ009842; CAA08880.2; JOINED; Genomic_DNA.
EMBL; AJ009843; CAA08880.2; JOINED; Genomic_DNA.
EMBL; AJ009844; CAA08880.2; JOINED; Genomic_DNA.
EMBL; AJ009845; CAA08880.2; JOINED; Genomic_DNA.
EMBL; AJ009846; CAA08880.2; JOINED; Genomic_DNA.
EMBL; AJ009847; CAA08880.2; JOINED; Genomic_DNA.
EMBL; AJ009848; CAA08880.2; JOINED; Genomic_DNA.
EMBL; AK143581; BAE25449.1; -; mRNA.
EMBL; AK145875; BAE26716.1; -; mRNA.
EMBL; AK157907; BAE34257.1; -; mRNA.
EMBL; AK165271; BAE38113.1; -; mRNA.
EMBL; CT010252; CAJ18460.1; -; mRNA.
EMBL; CH466520; EDL39705.1; -; Genomic_DNA.
EMBL; BC005432; AAH05432.1; -; mRNA.
CCDS; CCDS15271.1; -.
RefSeq; NP_031825.2; NM_007799.3.
UniGene; Mm.230249; -.
ProteinModelPortal; P70269; -.
SMR; P70269; -.
STRING; 10090.ENSMUSP00000073072; -.
BindingDB; P70269; -.
ChEMBL; CHEMBL1681627; -.
MEROPS; A01.010; -.
PhosphoSitePlus; P70269; -.
SwissPalm; P70269; -.
MaxQB; P70269; -.
PaxDb; P70269; -.
PRIDE; P70269; -.
Ensembl; ENSMUST00000073350; ENSMUSP00000073072; ENSMUSG00000004552.
GeneID; 13034; -.
KEGG; mmu:13034; -.
UCSC; uc007cnn.2; mouse.
CTD; 1510; -.
MGI; MGI:107361; Ctse.
eggNOG; KOG1339; Eukaryota.
eggNOG; ENOG410XNV7; LUCA.
GeneTree; ENSGT00760000118929; -.
HOGENOM; HOG000197681; -.
HOVERGEN; HBG000482; -.
InParanoid; P70269; -.
KO; K01382; -.
OMA; KEPGQTF; -.
OrthoDB; EOG091G0JP7; -.
TreeFam; TF314990; -.
BRENDA; 3.4.23.34; 3474.
PMAP-CutDB; P70269; -.
PRO; PR:P70269; -.
Proteomes; UP000000589; Chromosome 1.
Bgee; ENSMUSG00000004552; -.
CleanEx; MM_CTSE; -.
ExpressionAtlas; P70269; baseline and differential.
Genevisible; P70269; MM.
GO; GO:0005768; C:endosome; IDA:UniProtKB.
GO; GO:0070062; C:extracellular exosome; ISO:MGI.
GO; GO:0004190; F:aspartic-type endopeptidase activity; IDA:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IDA:MGI.
GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; IDA:UniProtKB.
GO; GO:0016540; P:protein autoprocessing; IEA:Ensembl.
GO; GO:0030163; P:protein catabolic process; IBA:GO_Central.
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;
Disulfide bond; Endosome; Glycoprotein; Hydrolase; Protease;
Reference proteome; Signal; Zymogen.
SIGNAL 1 20 {ECO:0000250}.
PROPEP 21 59 Activation peptide. {ECO:0000250}.
/FTId=PRO_0000025976.
CHAIN 60 397 Cathepsin E.
/FTId=PRO_0000025977.
DOMAIN 79 393 Peptidase A1. {ECO:0000255|PROSITE-
ProRule:PRU01103}.
ACT_SITE 97 97 {ECO:0000255|PROSITE-ProRule:PRU10094}.
ACT_SITE 282 282 {ECO:0000255|PROSITE-ProRule:PRU10094}.
CARBOHYD 91 91 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 323 323 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 61 61 Interchain. {ECO:0000305}.
DISULFID 110 115 {ECO:0000250}.
DISULFID 273 277 {ECO:0000250}.
CONFLICT 297 297 Q -> H (in Ref. 1; CAA66056, 5; CAJ18460
and 7; AAH05432). {ECO:0000305}.
CONFLICT 347 347 E -> D (in Ref. 1; CAA66056, 2; CAA71859,
5; CAJ18460 and 7; AAH05432).
{ECO:0000305}.
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


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