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Q800A0 (CATE_LITCT) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 55. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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
Synonyms:CE
OrganismLithobates catesbeiana (American bullfrog) (Rana catesbeiana)
Taxonomic identifier8400 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraNeobatrachiaRanoideaRanidaeRanaAquarana

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 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1616 Ref.1
Propeptide17 – 4933Activation peptide Ref.1
PRO_0000025982
Chain50 – 397348Cathepsin E Ref.1
PRO_0000025983

Sites

Active site921 By similarity UniProtKB P00790
Active site2771 By similarity UniProtKB P00790

Amino acid modifications

Glycosylation1391N-linked (GlcNAc...) Potential
Disulfide bond105 ↔ 110 By similarity UniProtKB P00790
Disulfide bond268 ↔ 272 By similarity UniProtKB P00790
Disulfide bond310 ↔ 344 By similarity UniProtKB P00790

Sequences

Sequence LengthMass (Da)Tools
Q800A0 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 4F2D59D7F50F06B4

FASTA39743,307
        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 

« Hide

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] [Europe PMC] [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

ProteinModelPortalQ800A0.
SMRQ800A0. Positions 64-388.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSA01.010.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG000482.

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...

Entry information

Entry nameCATE_LITCT
AccessionPrimary (citable) accession number: Q800A0
Entry history
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: June 1, 2003
Last modified: May 14, 2014
This is version 55 of the entry and version 1 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