P70269 (CATE_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Cathepsin E
EC=3.4.23.34

Gene names

Name:

Ctse

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	397 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

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. Ref.8 Ref.11
Catalytic activity	Similar to cathepsin D, but slightly broader specificity. Ref.1
Subunit structure	Homodimer; disulfide-linked By similarity.
Subcellular location	Endosome. Note: The proenzyme is localized to the endoplasmic reticulum and Golgi apparatus, while the mature enzyme is localized to the endosome. Ref.8
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. Ref.3 Ref.10
Post-translational modification	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. Ref.9
Sequence similarities	Belongs to the peptidase A1 family.

Ontologies

Keywords
Cellular component	Endosome
Domain	Signal
Molecular function	Aspartyl protease Hydrolase Protease
PTM	Autocatalytic cleavage Disulfide bond Glycoprotein Zymogen
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	antigen processing and presentation of exogenous peptide antigen via MHC class II Inferred from direct assay Ref.11. Source: UniProtKB proteolysis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	endosome Inferred from direct assay Ref.8. Source: UniProtKB
Molecular function	aspartic-type endopeptidase activity Inferred from direct assay Ref.1. Source: UniProtKB protein homodimerization activity Inferred from direct assay. Source: MGI
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 20	20	By similarity
	Propeptide	21 – 59	39	Activation peptide By similarity		PRO_0000025976
	Chain	60 – 397	338	Cathepsin E		PRO_0000025977
Sites
	Active site	97	1	By similarity
	Active site	282	1	By similarity
Amino acid modifications
	Glycosylation	91	1	N-linked (GlcNAc...) Potential
	Glycosylation	323	1	N-linked (GlcNAc...) Potential
	Disulfide bond	61		Interchain Probable
	Disulfide bond	110 ↔ 115		By similarity
	Disulfide bond	273 ↔ 277		By similarity
Experimental info
	Sequence conflict	297	1	Q → H in CAA66056. Ref.1
	Sequence conflict	297	1	Q → H in CAJ18460. Ref.5
	Sequence conflict	297	1	Q → H in AAH05432. Ref.7
	Sequence conflict	347	1	E → D in CAA66056. Ref.1
	Sequence conflict	347	1	E → D in CAA71859. Ref.2
	Sequence conflict	347	1	E → D in CAJ18460. Ref.5
	Sequence conflict	347	1	E → D in AAH05432. Ref.7

Sequences

	Sequence		Length	Mass (Da)
	P70269 [UniParc]. Last modified July 27, 2011. Version 2. Checksum: DF6AEFD5F78B3747	FASTA	397	42,938
	10 20 30 40 50 60 MKPLLVLLLL LLLDLAQAQG ALHRVPLRRH QSLRKKLRAQ GQLSEFWRSH NLDMTRLSES 70 80 90 100 110 120 CNVYSSVNEP LINYLDMEYF GTISIGTPPQ NFTVIFDTGS SNLWVPSVYC TSPACKAHPV 130 140 150 160 170 180 FHPSQSDTYT EVGNHFSIQY GTGSLTGIIG ADQVSVEGLT VDGQQFGESV KEPGQTFVNA 190 200 210 220 230 240 EFDGILGLGY PSLAAGGVTP VFDNMMAQNL VALPMFSVYL SSDPQGGSGS ELTFGGYDPS 250 260 270 280 290 300 HFSGSLNWIP VTKQAYWQIA LDGIQVGDTV MFCSEGCQAI VDTGTSLITG PPDKIKQLQE 310 320 330 340 350 360 AIGATPIDGE YAVDCATLDT MPNVTFLINE VSYTLNPTDY ILPDLVEGMQ FCGSGFQGLD 370 380 390 IPPPAGPLWI LGDVFIRQFY SVFDRGNNQV GLAPAVP

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning, expression and characterisation of murine procathepsin E." Tatnell P.J., Lees W.E., Kay J. FEBS Lett. 408:62-66(1997) [PubMed: 9180269] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY. Strain: BALB/c. Tissue: Spleen.
[2]	"Mouse procathepsin E gene: molecular organisation and chromosomal localisation." Tatnell P.J., Roth W., Deussing J., Peters C., Kay J. Biochim. Biophys. Acta 1398:57-66(1998) [PubMed: 9602058] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 129/SvJ.
[3]	"Cathepsin E gene in mouse." Yonezawa S., Masaki S., Hanai A., Ono T., Sonta S., Hirai H., Ichinose M., Miki K., Takahashi K., Kageyama T. Biomed. Res. 19:327-334(1998) Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY. Strain: 129/SvJ. Tissue: Gastric mucosa.
[4]	"The transcriptional landscape of the mammalian genome." 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. Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Inner ear, Liver and Spleen.
[5]	"Cloning of mouse full open reading frames in Gateway(R) system entry vector (pDONR201)." Ebert L., Muenstermann E., Schatten R., Henze S., Bohn E., Mollenhauer J., Wiemann S., Schick M., Korn B. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[6]	Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: FVB/N. Tissue: Mammary gland.
[8]	"Antigen processing for presentation by class II major histocompatibility complex requires cleavage by cathepsin E." Bennett K., Levine T., Ellis J.S., Peanasky R.J., Samloff I.M., Kay J., Chain B.M. Eur. J. Immunol. 22:1519-1524(1992) [PubMed: 1601038] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[9]	"Subcellular localization and targeting of cathepsin E." Finley E.M., Kornfeld S. J. Biol. Chem. 269:31259-31266(1994) [PubMed: 7983070] [Abstract] Cited for: GLYCOSYLATION.
[10]	"Regulation of human and mouse procathepsin E gene expression." Cook M., Caswell R.C., Richards R.J., Kay J., Tatnell P.J. Eur. J. Biochem. 268:2658-2668(2001) [PubMed: 11322887] [Abstract] Cited for: TISSUE SPECIFICITY.
[11]	"Involvement of cathepsin E in exogenous antigen processing in primary cultured murine microglia." 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. J. Biol. Chem. 277:4816-4822(2002) [PubMed: 11719510] [Abstract] Cited for: FUNCTION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X97399 mRNA. Translation: CAA66056.1. Y10928 Genomic DNA. Translation: CAA71859.1. AJ009840 , AJ009841, AJ009842, AJ009843, AJ009844, AJ009845, AJ009846, AJ009847, AJ009848 Genomic DNA. Translation: CAA08880.2. AK143581 mRNA. Translation: BAE25449.1. AK145875 mRNA. Translation: BAE26716.1. AK157907 mRNA. Translation: BAE34257.1. AK165271 mRNA. Translation: BAE38113.1. CT010252 mRNA. Translation: CAJ18460.1. CH466520 Genomic DNA. Translation: EDL39705.1. BC005432 mRNA. Translation: AAH05432.1.
IPI	IPI00137542.
RefSeq	NP_031825.2. NM_007799.3.
UniGene	Mm.230249.
3D structure databases
ProteinModelPortal	P70269.
SMR	P70269. Positions 22-396.
ModBase	Search...
Protein-protein interaction databases
STRING	P70269.
Protein family/group databases
MEROPS	A01.010.
Proteomic databases
PRIDE	P70269.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000073350; ENSMUSP00000073072; ENSMUSG00000004552.
GeneID	13034.
KEGG	mmu:13034.
Organism-specific databases
CTD	1510.
MGI	MGI:107361. Ctse.
Phylogenomic databases
eggNOG	roNOG13270.
HOGENOM	HBG590923.
HOVERGEN	HBG000482.
InParanoid	P70269.
OrthoDB	EOG4Z8XWJ.
PhylomeDB	P70269.
Gene expression databases
ArrayExpress	P70269.
Bgee	P70269.
CleanEx	MM_CTSE.
Genevestigator	P70269.
GermOnline	ENSMUSG00000004552. Mus musculus.
Family and domain databases
InterPro	IPR001461. Peptidase_A1. IPR021109. Peptidase_aspartic. IPR001969. Peptidase_aspartic_AS. IPR009007. Peptidase_aspartic_catalytic. IPR012848. Propep_A1. [Graphical view]
Gene3D	G3DSA:2.40.70.10. Pept_Aspartc_cat. 2 hits.
KO	K01382.
PANTHER	PTHR13683. Peptidase_A1. 1 hit.
Pfam	PF07966. A1_Propeptide. 1 hit. PF00026. Asp. 1 hit. [Graphical view]
PRINTS	PR00792. PEPSIN.
SUPFAM	SSF50630. Pept_Aspartic. 1 hit.
PROSITE	PS00141. ASP_PROTEASE. 2 hits. [Graphical view]
ProtoNet	Search...
Other
PMAP-CutDB	P70269.
SOURCE	Search...

Entry information

Entry name

CATE_MOUSE

Accession

Primary (citable) accession number: P70269
Secondary accession number(s): O35647, Q3UKT5, Q4FK00

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	July 27, 2011
Last modified:	November 16, 2011
This is version 99 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program