Reviewed, UniProtKB/Swiss-Prot Q805F2 (CATEB_XENLA)

Names and origin

Protein names

Recommended name:
    Cathepsin E-B
    EC=3.4.23.34

Gene names

Name:	ctse-B
Synonyms:	ce2

Organism

Xenopus laevis (African clawed frog)

Taxonomic identifier

8355 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Amphibia › Batrachia › Anura › Mesobatrachia › Pipoidea › Pipidae › Xenopodinae › Xenopus › Xenopus

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 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 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	Expressed predominantly in the anterior and posterior adult stomach and at much lower levels in the larval foregut. Ref.1
Developmental stage	Expression levels are low in surface mucous cells and manicotto gland cells of the foregut epithelium of pro-metamorphic tadpoles. During metamorphosis, expression levels rise markedly in proliferating adult epithelial primordia. In the adult stomach, expression was strongest in oxynticopeptic cells, but was also detected at a lower level in surface mucose cells. Ref.1
Post-translational modification	Glycosylated. Contains high mannose-type oligosaccharide By similarity.
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
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	By similarity UniProtKB Q805F3
	Propeptide	17 – 49	33	Activation peptide By similarity UniProtKB Q805F3		PRO_0000025986
	Chain	50 – 397	348	Cathepsin E-B UniProtKB Q805F3		PRO_0000025987
Sites
	Active site	92	1	By similarity UniProtKB P00790
	Active site	277	1	By similarity UniProtKB P00790
Amino acid modifications
	Glycosylation	86	1	N-linked (GlcNAc...) Potential
	Glycosylation	130	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)
	Q805F2-1 [UniParc]. Last modified June 1, 2003. Version 1. Checksum: BF5CE987689046CC	FASTA	397	43,002
	10 20 30 40 50 60 MRQILVLLLF VTLVYGLIRV PLKRQKSIRK TPKEKGKLSH VWTQQGIDMV QYTDSCNNDQ 70 80 90 100 110 120 APSEPLINYM DVQYFGEISI GTPPQNFTVI FDTGSSNLWV PSVYCISPAC AQHNRFQPQL 130 140 150 160 170 180 SSTYESNGNN FSLQYGTGSL SGVIGIDSVT VEGILVQNQQ FGESVSEPGS TFVDASFDGI 190 200 210 220 230 240 LGLGYPSIAV GGCTPVFDNM IAQNLVELPM FSVYMSRDPN SPVGGELVFG GFDASRFSGQ 250 260 270 280 290 300 LNWVPVTNQG YWQIQLDNIQ INGEVVFCSG GCQAIVDTGT SMITGPSSDI VQLQSIIGAS 310 320 330 340 350 360 AANGDYEVDC TVLNKMPTMT FTINGIGYQM TPQQYTLQDD DGVCSSGFQG LDISPPAGPL 370 380 390 WILGDVFIGQ YYSVFDRGNN RVGLAPVVPY PPLMNGV

References

[1]

"Differential expression of two cathepsin Es during metamorphosis-associated remodeling of the larval to adult type epithelium in Xenopus stomach." Ikuzawa M., Yasumasu S., Inokuchi T., Kobayashi K., Nomura K., Iuchi I. J. Biochem. 134:385-394(2003) [PubMed: 14561724] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB080685 mRNA. Translation: BAC57454.1.
RefSeq	NP_001079044.1.
UniGene	Xl.23629
3D structure databases
SMR	Q805F2. Positions 64-388.
ModBase	Search...
Protein family/group databases
MEROPS	A01.010.
Genome annotation databases
GeneID	373573.
KEGG	xla:373573.
Organism-specific databases
CTD	373573.
Phylogenomic databases
HOVERGEN	Q805F2.
Enzyme and pathway databases
BRENDA	3.4.23.34. 648.
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

CATEB_XENLA

Accession

Primary (citable) accession number: Q805F2

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 13, 2004
Last sequence update:	June 1, 2003
Last modified:	February 9, 2010
This is version 42 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Xenopus annotation project