Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Cathepsin E

Gene

CTSE

Organism
Cavia porcellus (Guinea pig)
Status
Reviewed-Annotation score: Annotation score: 4 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. May play a role in activation-induced lymphocyte depletion in the thymus, and in neuronal degeneration and glial cell activation in the brain (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 – 921PROSITE-ProRule annotation
Active sitei276 – 2761PROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Aspartyl protease, Hydrolase, Protease

Protein family/group databases

MEROPSiA01.010.

Names & Taxonomyi

Protein namesi
Recommended name:
Cathepsin E (EC:3.4.23.34)
Gene namesi
Name:CTSE
OrganismiCavia porcellus (Guinea pig)
Taxonomic identifieri10141 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaHystricognathiCaviidaeCavia
Proteomesi
  • UP000005447 Componenti: Unassembled WGS sequence

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

Complete GO annotation...

Keywords - Cellular componenti

Endosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 19191 PublicationAdd
BLAST
Propeptidei20 – 5334Activation peptideSequence analysisPRO_0000025972Add
BLAST
Chaini54 – 391338Cathepsin EPRO_0000025973Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi56 – 56InterchainCurated
Glycosylationi86 – 861N-linked (GlcNAc...)Sequence analysis
Disulfide bondi105 ↔ 110By similarity
Disulfide bondi267 ↔ 271By similarity
Disulfide bondi309 ↔ 346By similarity

Post-translational modificationi

Glycosylated. The nature of the carbohydrate chain varies between cell types (By similarity).By similarity

Keywords - PTMi

Autocatalytic cleavage, Disulfide bond, Glycoprotein, Zymogen

Miscellaneous databases

PMAP-CutDBP25796.

Expressioni

Tissue specificityi

Expressed abundantly in the surface and foveolar epithelial cells of the fundic and pyloric stomach mucosa, and at very low levels in the spleen.2 Publications

Interactioni

Subunit structurei

Homodimer; disulfide-linked.1 Publication

Protein-protein interaction databases

STRINGi10141.ENSCPOP00000008547.

Structurei

3D structure databases

ProteinModelPortaliP25796.
SMRiP25796. Positions 64-390.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini74 – 387314Peptidase A1PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the peptidase A1 family.Curated
Contains 1 peptidase A1 domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG1339. Eukaryota.
ENOG410XNV7. LUCA.
GeneTreeiENSGT00760000118929.
HOGENOMiHOG000197681.
HOVERGENiHBG000482.
InParanoidiP25796.
OMAiGEYAMEC.
OrthoDBiEOG7HQN88.
TreeFamiTF314990.

Family and domain databases

Gene3Di2.40.70.10. 2 hits.
InterProiIPR001461. Aspartic_peptidase_A1.
IPR001969. Aspartic_peptidase_AS.
IPR012848. Aspartic_peptidase_N.
IPR033145. Cathepsin_E.
IPR033121. PEPTIDASE_A1.
IPR021109. Peptidase_aspartic_dom.
[Graphical view]
PANTHERiPTHR13683. PTHR13683. 1 hit.
PTHR13683:SF81. PTHR13683:SF81. 1 hit.
PfamiPF07966. A1_Propeptide. 1 hit.
PF00026. Asp. 1 hit.
[Graphical view]
PRINTSiPR00792. PEPSIN.
SUPFAMiSSF50630. SSF50630. 1 hit.
PROSITEiPS00141. ASP_PROTEASE. 2 hits.
PS51767. PEPTIDASE_A1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P25796-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKTFLLLLLV LLELGQAPGA LHRVPLSRRE SLRKKLRAQG QLTELWKSQN
60 70 80 90 100
LNMDQCSTIQ SANEPLINYL DMEYFGTISI GSPPQNFTVI FDTGSSNLWV
110 120 130 140 150
PSVYCTSPAC QTHPVFHPSL SSTYREVGNS FSIQYGTGSL TGIIGADQVS
160 170 180 190 200
VEGLTVVGQQ FGESVQEPGK TFVHAEFDGI LGLGYPSLAA GGVTPVFDNM
210 220 230 240 250
MAQNLVALPM FSVYMSSNPG GSGSELTFGG YDPSHFSGSL NWVPVTKQAY
260 270 280 290 300
WQIALDGIQV GDSVMFCSEG CQAIVDTGTS LITGPPGKIK QLQEALGATY
310 320 330 340 350
VDEGYSVQCA NLNMMLDVTF IINGVPYTLN PTAYTLLDFV DGMQVCSTGF
360 370 380 390
EGLEIQPPAG PLWILGDVFI RQFYAVFDRG NNRVGLAPAV P
Length:391
Mass (Da):42,132
Last modified:May 1, 1992 - v1
Checksum:i78D216BF8CFCDABD
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M88653 mRNA. Translation: AAA37052.1.
S80547 mRNA. Translation: AAB35844.1.
PIRiA43356.
RefSeqiNP_001166408.1. NM_001172937.1.

Genome annotation databases

EnsembliENSCPOT00000009609; ENSCPOP00000008547; ENSCPOG00000009523.
GeneIDi100135509.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M88653 mRNA. Translation: AAA37052.1.
S80547 mRNA. Translation: AAB35844.1.
PIRiA43356.
RefSeqiNP_001166408.1. NM_001172937.1.

3D structure databases

ProteinModelPortaliP25796.
SMRiP25796. Positions 64-390.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10141.ENSCPOP00000008547.

Protein family/group databases

MEROPSiA01.010.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSCPOT00000009609; ENSCPOP00000008547; ENSCPOG00000009523.
GeneIDi100135509.

Organism-specific databases

CTDi1510.

Phylogenomic databases

eggNOGiKOG1339. Eukaryota.
ENOG410XNV7. LUCA.
GeneTreeiENSGT00760000118929.
HOGENOMiHOG000197681.
HOVERGENiHBG000482.
InParanoidiP25796.
OMAiGEYAMEC.
OrthoDBiEOG7HQN88.
TreeFamiTF314990.

Miscellaneous databases

PMAP-CutDBP25796.

Family and domain databases

Gene3Di2.40.70.10. 2 hits.
InterProiIPR001461. Aspartic_peptidase_A1.
IPR001969. Aspartic_peptidase_AS.
IPR012848. Aspartic_peptidase_N.
IPR033145. Cathepsin_E.
IPR033121. PEPTIDASE_A1.
IPR021109. Peptidase_aspartic_dom.
[Graphical view]
PANTHERiPTHR13683. PTHR13683. 1 hit.
PTHR13683:SF81. PTHR13683:SF81. 1 hit.
PfamiPF07966. A1_Propeptide. 1 hit.
PF00026. Asp. 1 hit.
[Graphical view]
PRINTSiPR00792. PEPSIN.
SUPFAMiSSF50630. SSF50630. 1 hit.
PROSITEiPS00141. ASP_PROTEASE. 2 hits.
PS51767. PEPTIDASE_A1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Gastric procathepsin E and progastricsin from guinea pig. Purification, molecular cloning of cDNAs, and characterization of enzymatic properties, with special reference to procathepsin E."
    Kageyama T., Ichinose M., Tsukada S., Miki K., Kurokawa K., Koiwai O., Tanji M., Yakabe E., Athauda S.B., Takahashi K.
    J. Biol. Chem. 267:16450-16459(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 20-48, CATALYTIC ACTIVITY, SUBUNIT, TISSUE SPECIFICITY.
  2. "Isolation, characterization, and structure of procathepsin E and cathepsin E from the gastric mucosa of guinea pig."
    Kageyama T., Ichinose M., Miki K., Moriyama A., Yonezawa S., Tanji M., Athauda S.B., Takahashi K.
    Adv. Exp. Med. Biol. 362:211-221(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Gastric mucosa.
  3. Cited for: TISSUE SPECIFICITY.

Entry informationi

Entry nameiCATE_CAVPO
AccessioniPrimary (citable) accession number: P25796
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: May 1, 1992
Last modified: May 11, 2016
This is version 112 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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.