P43159 (CATE_RABIT) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Cathepsin E
EC=3.4.23.34

Gene names

Name:

CTSE

Organism

Oryctolagus cuniculus (Rabbit) [Reference proteome]

Taxonomic identifier

9986 [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 › Lagomorpha › Leporidae › Oryctolagus

Protein attributes

Sequence length	396 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript 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.
Subunit structure	Homodimer; disulfide-linked By similarity.
Subcellular location	Endosome By similarity. Note: The proenzyme is localized to the endoplasmic reticulum and Golgi apparatus, while the mature enzyme is localized to the endosome By similarity.
Post-translational modification	Glycosylated. The nature of the carbohydrate chain varies between cell types By similarity.
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 sequence or structural similarity. Source: UniProtKB proteolysis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	endosome Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	aspartic-type endopeptidase activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 19	19	Potential
	Propeptide	20 – 53	34	Activation peptide By similarity		PRO_0000025978
	Chain	54 – 396	343	Cathepsin E		PRO_0000025979
Sites
	Active site	96	1	By similarity
	Active site	281	1	By similarity
Amino acid modifications
	Glycosylation	90	1	N-linked (GlcNAc...) Potential
	Disulfide bond	60		Interchain Probable
	Disulfide bond	109 ↔ 114		By similarity
	Disulfide bond	272 ↔ 276		By similarity
	Disulfide bond	314 ↔ 351		By similarity

Sequences

	Sequence		Length	Mass (Da)
	P43159 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: E5D84FE48DC760A4	FASTA	396	42,679
	10 20 30 40 50 60 MKTLPLLLLL LLDLGQAQGT LDRVPLRRQP SLRKKLRAQG QLSEFWKAHK VDMVQYTETC 70 80 90 100 110 120 TMEQSANEPL INYLDMEYFG TISIGSPPQN FTVIFDTVSS NLWVPSVYCT SPACQMHPQF 130 140 150 160 170 180 RPSQSNTYSE VGTPFSIAYG TGSLTGIIGA DQVSVQGLTV VGQQFGESVK EPGQTFVNAE 190 200 210 220 230 240 FDGILGLGYP SLAAGGVTPV FDNMMAQNLV SLPMFSVYMS SNPEGGSGSE LTFGGYDSSH 250 260 270 280 290 300 FSGSLNWVPV TKQGYWQIAL DEIQVGGSPM FCPEGCQAIV DTGTSLITGP SDKIIQLQAA 310 320 330 340 350 360 IGATPMDGEY AVECENLNIM PDVTFVINGV PYTLSATAYT LPDFVDGMQF CGSGFQGLDI 370 380 390 QPPAGPLWIL GDVFIRQFYS VFDRGSNRVG LAPAVP

References

[1]

"Rabbit procathepsin E and cathepsin E. Nucleotide sequence of cDNA, hydrolytic specificity for biologically active peptides and gene expression during development." Kageyama T. Eur. J. Biochem. 216:717-728(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: Japanese white.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L08418 mRNA. Translation: AAC37308.1.
PIR	S36865.
RefSeq	NP_001075713.1. NM_001082244.1.
UniGene	Ocu.2222.
3D structure databases
ProteinModelPortal	P43159.
SMR	P43159. Positions 68-395.
ModBase	Search...
Protein-protein interaction databases
STRING	9986.ENSOCUP00000001598.
Protein family/group databases
MEROPS	A01.010.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	100009063.
Organism-specific databases
CTD	1510.
Phylogenomic databases
eggNOG	NOG248684.
HOGENOM	HOG000197681.
HOVERGEN	HBG000482.
OrthoDB	EOG4Z8XWJ.
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. 1 hit. [Graphical view]
ProtoNet	Search...
Other
PMAP-CutDB	P43159.

Entry information

Entry name

CATE_RABIT

Accession

Primary (citable) accession number: P43159

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	April 3, 2013
This is version 89 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program