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Q805F3 (CATEA_XENLA) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 60. 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-A

EC=3.4.23.34
Gene names
Name:ctse-a
Synonyms:ce1
OrganismXenopus laevis (African clawed frog)
Taxonomic identifier8355 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

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. Ref.1

Subunit structure

Homodimer; disulfide-linked. Ref.1

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 larval foregut and the anterior and posterior adult stomach. Ref.1

Developmental stage

Expression levels are high in surface mucous cells and manicotto gland cells of the foregut epithelium of pro-metamorphic tadpoles. During metamorphosis, expression levels decrease markedly in larval epithelial cells but are high 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. 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 – 5236Activation peptide Ref.1
PRO_0000025984
Chain53 – 397345Cathepsin E-A Ref.1
PRO_0000025985

Sites

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

Amino acid modifications

Glycosylation861N-linked (GlcNAc...) Potential
Glycosylation1301N-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
Q805F3 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 3DA99B6866E84611

FASTA39742,907
        10         20         30         40         50         60 
MRQILVLLLF ATLVYGLIRV PLKRQKSIRK TLKEKGKLSH IWTQQGIDMV QYTDSCSNDQ 

        70         80         90        100        110        120 
APSEPLINYM DVEYFGEISV GTPPQNFTVI FDTGSSNLWV PSVYCISQAC AQHDRFQPQL 

       130        140        150        160        170        180 
SSTYESNGNN FSLQYGTGSL SGVIGIDAVT VEGILVQNQQ FGESVSEPGS TFVDAEFDGI 

       190        200        210        220        230        240 
LGLGYPSIAV GDCTPVFDNM IAQNLVELPM FSVYMSRNPN SAVGGELVFG GFDASRFSGQ 

       250        260        270        280        290        300 
LNWVPVTNQG YWQIQLDNVQ INGEVLFCSG GCQAIVDTGT SLITGPSSDI VQLQNIIGAS 

       310        320        330        340        350        360 
AANGDYEVDC SVLNEMPTVT FTINGIGYQM TPQQYTLQDG GGVCSSGFQG LDIPPPAGPL 

       370        380        390 
WILGDVFIGQ YYSVFDRGNN RVGLAPVVPY PPLKNGV 

« Hide

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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 17-25 AND 53-59, CATALYTIC ACTIVITY, SUBUNIT, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, GLYCOSYLATION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB080684 mRNA. Translation: BAC57453.1.
RefSeqNP_001079043.1. NM_001085574.1.
UniGeneXl.35410.

3D structure databases

ProteinModelPortalQ805F3.
SMRQ805F3. Positions 64-388.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSA01.010.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID373572.
KEGGxla:373572.

Organism-specific databases

CTD373572.
XenbaseXB-GENE-947868. ctse.

Phylogenomic databases

HOVERGENHBG000482.
KOK01382.

Family and domain databases

Gene3D2.40.70.10. 2 hits.
InterProIPR001461. Aspartic_peptidase.
IPR001969. Aspartic_peptidase_AS.
IPR012848. Aspartic_peptidase_N.
IPR018222. Nuclear_transport_factor_2_euk.
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 nameCATEA_XENLA
AccessionPrimary (citable) accession number: Q805F3
Entry history
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: June 1, 2003
Last modified: October 16, 2013
This is version 60 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