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Q805F3

- CATEA_XENLA

UniProt

Q805F3 - CATEA_XENLA

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Protein
Cathepsin E-A
Gene
ctse-a, ce1
Organism
Xenopus laevis (African clawed frog)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

May have a role in immune function. Probably involved in the processing of antigenic peptides during MHC class II-mediated antigen presentation By similarity.By similarity

Catalytic activityi

Similar to cathepsin D, but slightly broader specificity.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei92 – 921 By similarityBy similarity
Active sitei277 – 2771 By similarityBy similarity

GO - Molecular functioni

  1. aspartic-type endopeptidase activity Source: UniProtKB

GO - Biological processi

  1. antigen processing and presentation of exogenous peptide antigen via MHC class II Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Aspartyl protease, Hydrolase, Protease

Protein family/group databases

MEROPSiA01.010.

Names & Taxonomyi

Protein namesi
Recommended name:
Cathepsin E-A (EC:3.4.23.34)
Gene namesi
Name:ctse-a
Synonyms:ce1
OrganismiXenopus laevis (African clawed frog)
Taxonomic identifieri8355 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

Organism-specific databases

XenbaseiXB-GENE-947868. ctse.

Subcellular locationi

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.

GO - Cellular componenti

  1. endosome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Endosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 16161 Publication
Add
BLAST
Propeptidei17 – 5236Activation peptide1 Publication
PRO_0000025984Add
BLAST
Chaini53 – 397345Cathepsin E-A1 Publication
PRO_0000025985Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi86 – 861N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi105 ↔ 110 By similarityBy similarity
Glycosylationi130 – 1301N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi268 ↔ 272 By similarityBy similarity
Disulfide bondi310 ↔ 344 By similarityBy similarity

Post-translational modificationi

Glycosylated. Contains high mannose-type oligosaccharide.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Expressioni

Tissue specificityi

Expressed predominantly in the larval foregut and the anterior and posterior adult stomach.1 Publication

Developmental stagei

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.1 Publication

Interactioni

Subunit structurei

Homodimer; disulfide-linked.1 Publication

Structurei

3D structure databases

ProteinModelPortaliQ805F3.
SMRiQ805F3. Positions 64-388.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase A1 family.

Keywords - Domaini

Signal

Phylogenomic databases

HOVERGENiHBG000482.
KOiK01382.

Family and domain databases

Gene3Di2.40.70.10. 2 hits.
InterProiIPR001461. Aspartic_peptidase.
IPR001969. Aspartic_peptidase_AS.
IPR012848. Aspartic_peptidase_N.
IPR018222. Nuclear_transport_factor_2_euk.
IPR021109. Peptidase_aspartic_dom.
[Graphical view]
PANTHERiPTHR13683. PTHR13683. 1 hit.
PfamiPF07966. A1_Propeptide. 1 hit.
PF00026. Asp. 1 hit.
[Graphical view]
PRINTSiPR00792. PEPSIN.
SUPFAMiSSF50630. SSF50630. 1 hit.
PROSITEiPS00141. ASP_PROTEASE. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q805F3-1 [UniParc]FASTAAdd to Basket

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MRQILVLLLF ATLVYGLIRV PLKRQKSIRK TLKEKGKLSH IWTQQGIDMV    50
QYTDSCSNDQ APSEPLINYM DVEYFGEISV GTPPQNFTVI FDTGSSNLWV 100
PSVYCISQAC AQHDRFQPQL SSTYESNGNN FSLQYGTGSL SGVIGIDAVT 150
VEGILVQNQQ FGESVSEPGS TFVDAEFDGI LGLGYPSIAV GDCTPVFDNM 200
IAQNLVELPM FSVYMSRNPN SAVGGELVFG GFDASRFSGQ LNWVPVTNQG 250
YWQIQLDNVQ INGEVLFCSG GCQAIVDTGT SLITGPSSDI VQLQNIIGAS 300
AANGDYEVDC SVLNEMPTVT FTINGIGYQM TPQQYTLQDG GGVCSSGFQG 350
LDIPPPAGPL WILGDVFIGQ YYSVFDRGNN RVGLAPVVPY PPLKNGV 397
Length:397
Mass (Da):42,907
Last modified:June 1, 2003 - v1
Checksum:i3DA99B6866E84611
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB080684 mRNA. Translation: BAC57453.1.
RefSeqiNP_001079043.1. NM_001085574.1.
UniGeneiXl.35410.

Genome annotation databases

GeneIDi373572.
KEGGixla:373572.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB080684 mRNA. Translation: BAC57453.1 .
RefSeqi NP_001079043.1. NM_001085574.1.
UniGenei Xl.35410.

3D structure databases

ProteinModelPortali Q805F3.
SMRi Q805F3. Positions 64-388.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

MEROPSi A01.010.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 373572.
KEGGi xla:373572.

Organism-specific databases

CTDi 373572.
Xenbasei XB-GENE-947868. ctse.

Phylogenomic databases

HOVERGENi HBG000482.
KOi K01382.

Family and domain databases

Gene3Di 2.40.70.10. 2 hits.
InterProi IPR001461. Aspartic_peptidase.
IPR001969. Aspartic_peptidase_AS.
IPR012848. Aspartic_peptidase_N.
IPR018222. Nuclear_transport_factor_2_euk.
IPR021109. Peptidase_aspartic_dom.
[Graphical view ]
PANTHERi PTHR13683. PTHR13683. 1 hit.
Pfami PF07966. A1_Propeptide. 1 hit.
PF00026. Asp. 1 hit.
[Graphical view ]
PRINTSi PR00792. PEPSIN.
SUPFAMi SSF50630. SSF50630. 1 hit.
PROSITEi PS00141. ASP_PROTEASE. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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.

Entry informationi

Entry nameiCATEA_XENLA
AccessioniPrimary (citable) accession number: Q805F3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: June 1, 2003
Last modified: May 14, 2014
This is version 61 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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