Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot P43159 (CATE_RABIT)

Last modified July 28, 2009. Version 67. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Cathepsin E
    EC=3.4.23.34
Gene names
Name: CTSE
OrganismOryctolagus cuniculus (Rabbit)
Taxonomic identifier9986 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus

Protein attributes

Sequence length396 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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. 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.

Catalytic activity

Similar to cathepsin D, but slightly broader specificity.

Subunit structure

Homodimer; disulfide-linked By similarity.

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.

Post-translational modification

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

Sequence similarities

Belongs to the peptidase A1 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Potential
Propeptide20 – 5334Activation peptide By similarity
PRO_0000025978
Chain54 – 396343Cathepsin E
PRO_0000025979

Sites

Active site961 By similarity
Active site2811 By similarity

Amino acid modifications

Glycosylation901N-linked (GlcNAc...) Potential
Disulfide bond60Interchain Probable
Disulfide bond109 ↔ 114 By similarity
Disulfide bond272 ↔ 276 By similarity
Disulfide bond314 ↔ 351 By similarity

Sequences

Sequence LengthMass (Da)Tools
P43159-1 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: E5D84FE48DC760A4

FASTA39642,679
        10         20         30         40         50         60 
MKTLPLLLLL LLDLGQAQGT LDRVPLRRQP SLRKKLRAQG QLSEFWKAHK VDMVQYTETC 

        70         80         90        100        110        120 
TMEQSANEPL INYLDMEYFG TISIGSPPQN FTVIFDTVSS NLWVPSVYCT SPACQMHPQF 

       130        140        150        160        170        180 
RPSQSNTYSE VGTPFSIAYG TGSLTGIIGA DQVSVQGLTV VGQQFGESVK EPGQTFVNAE 

       190        200        210        220        230        240 
FDGILGLGYP SLAAGGVTPV FDNMMAQNLV SLPMFSVYMS SNPEGGSGSE LTFGGYDSSH 

       250        260        270        280        290        300 
FSGSLNWVPV TKQGYWQIAL DEIQVGGSPM FCPEGCQAIV DTGTSLITGP SDKIIQLQAA 

       310        320        330        340        350        360 
IGATPMDGEY AVECENLNIM PDVTFVINGV PYTLSATAYT LPDFVDGMQF CGSGFQGLDI 

       370        380        390 
QPPAGPLWIL GDVFIRQFYS VFDRGSNRVG LAPAVP 

« Hide

References

[1]"Rabbit procathepsin E and cathepsin E. Nucleotide sequence of cDNA, hydrolytic specificity for biologically active peptides and gene expression during development."
Kageyama T.
Eur. J. Biochem. 216:717-728(1993) [PubMed: 8404890] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Japanese white.

Cross-references

Sequence databases

L08418 mRNA. Translation: AAC37308.1.
PIRS36865.
RefSeqNP_001075713.1.
UniGeneOcu.2222

3D structure databases

HSSPHSSP built from PDB template 4CMS based on UniProtKB P00794.
SMRP43159. Positions 68-395.
ModBaseSearch...

Protein family/group databases

MEROPSA01.010.

Genome annotation databases

EnsemblENSOCUT00000001857; ENSOCUP00000001598; ENSOCUG00000001856; Oryctolagus cuniculus. [Genome view]
GeneID100009063.

Phylogenomic databases

HOVERGENP43159.

Enzyme and pathway databases

BRENDA3.4.23.34. 255.

Family and domain databases

InterProIPR001461. Peptidase_A1.
IPR001969. Peptidase_aspartic_AS.
IPR009007. Peptidase_aspartic_catalytic.
IPR012848. Propep_A1.
[Graphical view]
Gene3DG3DSA:2.40.70.10. Pept_Aspartc_cat. 2 hits.
PANTHERPTHR13683. Peptidase_A1. 1 hit.
PfamPF07966. A1_Propeptide. 1 hit.
PF00026. Asp. 1 hit.
[Graphical view]
PRINTSPR00792. PEPSIN.
PROSITEPS00141. ASP_PROTEASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

PMAP-CutDBP43159.

Entry information

Entry nameCATE_RABIT
AccessionPrimary (citable) accession number: P43159
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: July 28, 2009
This is version 67 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents