P16228 (CATE_RAT) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Cathepsin E
EC=3.4.23.34

Gene names

Name:

Ctse

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	398 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 By similarity.
Catalytic activity	Similar to cathepsin D, but slightly broader specificity. Ref.7
Subunit structure	Homodimer; disulfide-linked. Ref.9
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.6 Ref.9
Tissue specificity	Expressed abundantly in lymphocytes and macrophages of the thymus and spleen, and in the M cells of the intestine. In the brain, expression is limited to reactive microglial cells, the large pyrimidial neurons in the cerebral cortex, the CA1 and CA3 pyrimidial neurons of the hippocampus, the large neurons of the neostriatum, and the Purkinje neurons of the cerebellum. Ref.5 Ref.6 Ref.7 Ref.8 Ref.9
Developmental stage	Expression increases in all brain regions examined with age, and increases markedly in reactive microglial cells amd CA1 pyrimidial neurons following ischemic injury. In the thymus expression increased steadily up to 8 weeks of age before decreasing to a much lower level by 52 weeks. Expression levels in the spleen and stomach do not appear to vary with age. Ref.7
Post-translational modification	Glycosylated. The nature of the carbohydrate chain varies between cell types. In brain microglia, the proenzyme contains a high mannose-type oligosaccharide, while the mature enzyme contains a complex-type oligosaccharide. In stomach and spleen, the mature enzyme contains a high mannose-type oligosaccharide. In erythrocyte membranes, the mature enzyme contains a complex-type oligosaccharide. Ref.3 Ref.4 Ref.9
Miscellaneous	Administration of dexamethasone results in the conversion of the proenzyme to the mature form in thymocytes.
Sequence similarities	Belongs to the peptidase A1 family.

Ontologies

Keywords
Cellular component	Endosome
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Signal
Molecular function	Aspartyl protease Hydrolase Protease
PTM	Autocatalytic cleavage Disulfide bond Glycoprotein Zymogen
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	antigen processing and presentation of exogenous peptide antigen via MHC class II Inferred from direct assay Ref.6. Source: UniProtKB protein autoprocessing Inferred from mutant phenotype PubMed 16367762. Source: RGD proteolysis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	endosome Inferred from direct assay Ref.9. Source: UniProtKB
Molecular_function	aspartic-type endopeptidase activity Inferred from direct assay Ref.7. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P16228-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: P16228-2)

The sequence of this isoform differs from the canonical sequence as follows:
     312-344: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 21	21	By similarity
	Propeptide	22 – 58	37	Activation peptide		PRO_0000025980
	Chain	59 – 398	340	Cathepsin E		PRO_0000025981
Sites
	Active site	98	1	By similarity
	Active site	283	1	By similarity
Amino acid modifications
	Glycosylation	92	1	N-linked (GlcNAc...) Probable
	Disulfide bond	62		Interchain Probable
	Disulfide bond	111 ↔ 116		By similarity
	Disulfide bond	274 ↔ 278		By similarity
Natural variations
	Alternative sequence	312 – 344	33	Missing in isoform 2.		VSP_005224
	Natural variant	114	1	P → S. Ref.1
Experimental info
	Sequence conflict	55	1	M → V in AAH62002. Ref.2
	Sequence conflict	79	1	E → N AA sequence Ref.3
	Sequence conflict	83 – 84	2	TV → SR AA sequence Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified July 15, 1998. Version 3. Checksum: 25F123E67C46EB5F	FASTA	398	43,021
	10 20 30 40 50 60 MKPLFVLLLL LLLLDLAQAQ GVLHRVPLRR HQSLRKKLRA QGQLSDFWRS HNLDMIEFSE 70 80 90 100 110 120 SCNVDKGINE PLINYLDMEY FGTVSIGSPS QNFTVIFDTG SSNLWVPSVY CTSPACKAHP 130 140 150 160 170 180 VFHPSQSSTY MEVGNHFSIQ YGTGSLTGII GADQVSVEGL TVEGQQFGES VKEPGQTFVN 190 200 210 220 230 240 AEFDGILGLG YPSLAVGGVT PVFDNMMAQN LVALPMFSVY LSSDPQGGSG SELTFGGYDP 250 260 270 280 290 300 SHFSGSLNWI PVTKQGYWQI ALDGIQVGDT VMFCSEGCQA IVDTGTSLIT GPPKKIKQLQ 310 320 330 340 350 360 EAIGATPMDG EYAVDCATLN MMPNVTFLIN GVSYTLSPTA YILPDLVDGM QFCGSGFQGL 370 380 390 DIQPPAGPLW ILGDVFIRKF YSVFDRGNNQ VGLAPAVP
	Isoform 2 [UniParc]. Checksum: 7AED1AB6B6A447D7	FASTA	365	39,445
	10 20 30 40 50 60 MKPLFVLLLL LLLLDLAQAQ GVLHRVPLRR HQSLRKKLRA QGQLSDFWRS HNLDMIEFSE 70 80 90 100 110 120 SCNVDKGINE PLINYLDMEY FGTVSIGSPS QNFTVIFDTG SSNLWVPSVY CTSPACKAHP 130 140 150 160 170 180 VFHPSQSSTY MEVGNHFSIQ YGTGSLTGII GADQVSVEGL TVEGQQFGES VKEPGQTFVN 190 200 210 220 230 240 AEFDGILGLG YPSLAVGGVT PVFDNMMAQN LVALPMFSVY LSSDPQGGSG SELTFGGYDP 250 260 270 280 290 300 SHFSGSLNWI PVTKQGYWQI ALDGIQVGDT VMFCSEGCQA IVDTGTSLIT GPPKKIKQLQ 310 320 330 340 350 360 EAIGATPMDG EDLVDGMQFC GSGFQGLDIQ PPAGPLWILG DVFIRKFYSV FDRGNNQVGL APAVP

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Isolation and sequencing of two cDNA clones encoding rat spleen cathepsin E and analysis of the activation of purified procathepsin E." Okamoto K., Yu H., Misumi Y., Ikehara Y., Yamamoto K. Arch. Biochem. Biophys. 322:103-111(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), VARIANT SER-114. Tissue: Spleen.
[2]	"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] (ISOFORM 1). Tissue: Prostate.
[3]	"Structural studies of rat cathepsin E: amino-terminal structure and carbohydrate units of mature enzyme." Yonezawa S., Takahashi T., Ichinose M., Miki K., Tanaka J., Gasa S. Biochem. Biophys. Res. Commun. 166:1032-1038(1990) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 59-110, GLYCOSYLATION.
[4]	"Isolation and biochemical characterization of procathepsin E from human erythrocyte membranes." Takeda-Ezaki M., Yamamoto K. Arch. Biochem. Biophys. 304:352-358(1993) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION.
[5]	"Transient forebrain ischemia induces increased expression and specific localization of cathepsins E and D in rat hippocampus and neostriatum." Nakanishi H., Tsukuba T., Kondou T., Tanaka T., Yamamoto K. Exp. Neurol. 121:215-223(1993) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY.
[6]	"Cathepsin E in follicle associated epithelium of intestine and tonsils: localization to M cells and possible role in antigen processing." Finzi G., Cornaggia M., Capella C., Fiocca R., Bosi F., Solcia E., Samloff I.M. Histochemistry 99:201-211(1993) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[7]	"Age-related changes in activities and localizations of cathepsins D, E, B, and L in the rat brain tissues." Nakanishi H., Tominaga K., Amano T., Hirotsu I., Inoue T., Yamamoto K. Exp. Neurol. 126:119-128(1994) [PubMed] [Europe PMC] [Abstract] Cited for: CATALYTIC ACTIVITY, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
[8]	"Age-related and dexamethasone-induced changes in cathepsins E and D in rat thymic and splenic cells." Nishishita K., Sakai H., Sakai E., Kato Y., Yamamoto K. Arch. Biochem. Biophys. 333:349-358(1996) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY, DEXAMETHASONE ADMINISTRATION.
[9]	"Identification of cellular compartments involved in processing of cathepsin E in primary cultures of rat microglia." Sastradipura D.F., Nakanishi H., Tsukuba T., Nishishita K., Sakai H., Kato Y., Gotow T., Uchiyama Y., Yamamoto K. J. Neurochem. 70:2045-2056(1998) [PubMed] [Europe PMC] [Abstract] Cited for: SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, GLYCOSYLATION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	D38104 mRNA. Translation: BAA07285.1. D45187 mRNA. Translation: BAA08128.1. BC062002 mRNA. Translation: AAH62002.1.
IPI	IPI00211078. IPI00323987.
PIR	A34657. S66465. S66466.
RefSeq	NP_037070.1. NM_012938.1.
UniGene	Rn.92738.
3D structure databases
ProteinModelPortal	P16228.
SMR	P16228. Positions 70-397.
ModBase	Search...
Protein family/group databases
MEROPS	A01.010.
Proteomic databases
PRIDE	P16228.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSRNOT00000009241; ENSRNOP00000009242; ENSRNOG00000006963. ENSRNOT00000048391; ENSRNOP00000048353; ENSRNOG00000006963.
GeneID	25424.
KEGG	rno:25424.
UCSC	RGD:2446. rat.
Organism-specific databases
CTD	1510.
RGD	2446. Ctse.
Phylogenomic databases
eggNOG	NOG248684.
GeneTree	ENSGT00700000104165.
HOGENOM	HOG000197681.
HOVERGEN	HBG000482.
InParanoid	P16228.
KO	K01382.
OMA	GQLSEFW.
OrthoDB	EOG4Z8XWJ.
Gene expression databases
Genevestigator	P16228.
GermOnline	ENSRNOG00000006963. Rattus norvegicus.
Family and domain databases
Gene3D	2.40.70.10. 2 hits.
InterPro	IPR001461. Peptidase_A1. IPR021109. Peptidase_aspartic. IPR001969. Peptidase_aspartic_AS. IPR012848. Propep_A1. [Graphical view]
PANTHER	PTHR13683. PTHR13683. 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
NextBio	606595.

Entry information

Entry name

CATE_RAT

Accession

Primary (citable) accession number: P16228
Secondary accession number(s): Q63701

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1990
Last sequence update:	July 15, 1998
Last modified:	April 3, 2013
This is version 125 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program