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P70269 (CATE_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 120. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cathepsin E

EC=3.4.23.34
Gene names
Name:Ctse
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length397 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 By similarity
Propeptide21 – 5939Activation peptide By similarity
PRO_0000025976
Chain60 – 397338Cathepsin E
PRO_0000025977

Sites

Active site971 By similarity
Active site2821 By similarity

Amino acid modifications

Glycosylation911N-linked (GlcNAc...) Potential
Glycosylation3231N-linked (GlcNAc...) Potential
Disulfide bond61Interchain Probable
Disulfide bond110 ↔ 115 By similarity
Disulfide bond273 ↔ 277 By similarity

Experimental info

Sequence conflict2971Q → H in CAA66056. Ref.1
Sequence conflict2971Q → H in CAJ18460. Ref.5
Sequence conflict2971Q → H in AAH05432. Ref.7
Sequence conflict3471E → D in CAA66056. Ref.1
Sequence conflict3471E → D in CAA71859. Ref.2
Sequence conflict3471E → D in CAJ18460. Ref.5
Sequence conflict3471E → D in AAH05432. Ref.7

Sequences

Sequence LengthMass (Da)Tools
P70269 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: DF6AEFD5F78B3747

FASTA39742,938
        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 

« Hide

References

« Hide '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] [Europe PMC] [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] [Europe PMC] [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. expand/collapse author list , 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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 expand/collapse EMBL AC list , 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.
CCDSCCDS15271.1.
RefSeqNP_031825.2. NM_007799.3.
UniGeneMm.230249.

3D structure databases

ProteinModelPortalP70269.
SMRP70269. Positions 22-396.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000112235.

Chemistry

ChEMBLCHEMBL1681627.

Protein family/group databases

MEROPSA01.010.

PTM databases

PhosphoSiteP70269.

Proteomic databases

PaxDbP70269.
PRIDEP70269.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000073350; ENSMUSP00000073072; ENSMUSG00000004552.
GeneID13034.
KEGGmmu:13034.
UCSCuc007cnn.2. mouse.

Organism-specific databases

CTD1510.
MGIMGI:107361. Ctse.

Phylogenomic databases

eggNOGNOG248684.
GeneTreeENSGT00710000106265.
HOGENOMHOG000197681.
HOVERGENHBG000482.
InParanoidQ3UKT5.
KOK01382.
OMATVMFCSE.
OrthoDBEOG7HQN88.
TreeFamTF314990.

Gene expression databases

ArrayExpressP70269.
BgeeP70269.
CleanExMM_CTSE.
GenevestigatorP70269.

Family and domain databases

Gene3D2.40.70.10. 2 hits.
InterProIPR001461. Aspartic_peptidase.
IPR001969. Aspartic_peptidase_AS.
IPR012848. Aspartic_peptidase_N.
IPR021109. Peptidase_aspartic_dom.
[Graphical view]
PANTHERPTHR13683. PTHR13683. 1 hit.
PfamPF07966. A1_Propeptide. 1 hit.
PF00026. Asp. 1 hit.
[Graphical view]
PRINTSPR00792. PEPSIN.
SUPFAMSSF50630. SSF50630. 1 hit.
PROSITEPS00141. ASP_PROTEASE. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio282912.
PMAP-CutDBP70269.
PROP70269.
SOURCESearch...

Entry information

Entry nameCATE_MOUSE
AccessionPrimary (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: July 9, 2014
This is version 120 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot