Reviewed, UniProtKB/Swiss-Prot Q800A0 (CATE_RANCA)

Names and origin

Protein names

Recommended name:
    Cathepsin E
    EC=3.4.23.34

Gene names

Name:	CTSE
Synonyms:	CE

Organism

Rana catesbeiana (Bull frog)

Taxonomic identifier

8400 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Amphibia › Batrachia › Anura › Neobatrachia › Ranoidea › Ranidae › Raninae › Rana › Aquarana

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 By similarity. UniProtKB P14091
Catalytic activity	Similar to cathepsin D, but slightly broader specificity. UniProtKB Q805F3
Subunit structure	Homodimer; disulfide-linked By similarity. UniProtKB Q805F3
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.
Tissue specificity	Found in the larval foregut and adult stomach. Ref.1
Post-translational modification	Glycosylated. Contains high mannose-type oligosaccharide. Ref.1
Sequence similarities	Belongs to the peptidase A1 family.

Ontologies

Keywords
Cellular component	Endosome
Domain	Signal
Molecular function	Aspartyl protease Hydrolase Protease
PTM	Disulfide bond Glycoprotein Zymogen
Technical term	Direct protein sequencing
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: InterPro
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 – 16	16	Ref.1
	Propeptide	17 – 49	33	Activation peptide Ref.1		PRO_0000025982
	Chain	50 – 397	348	Cathepsin E Ref.1		PRO_0000025983
Sites
	Active site	92	1	By similarity UniProtKB P00790
	Active site	277	1	By similarity UniProtKB P00790
Amino acid modifications
	Glycosylation	139	1	N-linked (GlcNAc...) Potential
	Disulfide bond	105 ↔ 110		By similarity UniProtKB P00790
	Disulfide bond	268 ↔ 272		By similarity UniProtKB P00790
	Disulfide bond	310 ↔ 344		By similarity UniProtKB P00790

Sequences

	Sequence		Length	Mass (Da)
	Q800A0-1 [UniParc]. Last modified June 1, 2003. Version 1. Checksum: 4F2D59D7F50F06B4	FASTA	397	43,307
	10 20 30 40 50 60 MKQFLVVLLI LSFVHGIIRV PLKRQKSMRK ILKEKGKLSH LWTKQGNEFL QLSDSCSSPE 70 80 90 100 110 120 TASEPLMNYL DVEYFGQISI GTPPQQFTVI FDTGSSNLWV PSIYCTSQAC TKHNRYRPSE 130 140 150 160 170 180 STTYVSNGEA FFIQYGTGNL TGILGIDQVT VQGITVQSQT FAESVSEPGS TFQDSNFDGI 190 200 210 220 230 240 LGLAYPNLAV DNCIPVFDNM IAQNLVELPL FGVYMNRDPN SADGGELVLG GFDTSRFSGQ 250 260 270 280 290 300 LNWVPITVQG YWQIQVDSIQ VAGQVIFCSD GCQAIVDTGT SLITGPSGDI EQLQNYIGVT 310 320 330 340 350 360 NTNGEYGVSC STLSLMPSVT FTINGLDYSL TPEQYMLEDG GGYCSSGFQG LDISPPSGPL 370 380 390 WILGDVFIGQ YYSVFDRGNN RVGFAPVVFY ETTTNGA

References

[1]

"Molecular cloning of preprocathepsin E cDNA from the stomach of bullfrog Rana catesbeiana." Inokuchi T., Ikuzawa M., Mineta T., Yasumasu S., Kobayashi K. Comp. Biochem. Physiol. 135B:647-655(2003) [PubMed: 12892756] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 17-42 AND 50-69, TISSUE SPECIFICITY, GLYCOSYLATION. Tissue: Stomach.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB093036 mRNA. Translation: BAC75398.1.
3D structure databases
SMR	Q800A0. Positions 19-388.
ModBase	Search...
Protein family/group databases
MEROPS	A01.010.
Phylogenomic databases
HOVERGEN	Q800A0.
Enzyme and pathway databases
BRENDA	3.4.23.34. 829.
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. 1 hit.
PANTHER	PTHR13683. Peptidase_A1. 1 hit.
Pfam	PF07966. A1_Propeptide. 1 hit. PF00026. Asp. 1 hit. [Graphical view]
PRINTS	PR00792. PEPSIN.
PROSITE	PS00141. ASP_PROTEASE. 2 hits. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CATE_RANCA

Accession

Primary (citable) accession number: Q800A0

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 13, 2004
Last sequence update:	June 1, 2003
Last modified:	February 9, 2010
This is version 38 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)