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Reviewed, UniProtKB/Swiss-Prot Q28944 (CATL1_PIG)

Last modified September 1, 2009. Version 66. 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 L1
    EC=3.4.22.15
Cleaved into the following 2 chains:
    1- Recommended name:
            Cathepsin L1 heavy chain
    2- Recommended name:
            Cathepsin L1 light chain
Gene names
Name: CTSL1
Synonyms: CTSL
OrganismSus scrofa (Pig)
Taxonomic identifier9823 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus

Protein attributes

Sequence length334 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level.

General annotation (Comments)

Function

Important for the overall degradation of proteins in lysosomes.

Catalytic activity

Specificity close to that of papain. As compared to cathepsin B, cathepsin L exhibits higher activity toward protein substrates, but has little activity on Z-Arg-Arg-NHMec, and no peptidyl-dipeptidase activity.

Subunit structure

Dimer of a heavy and a light chain linked by disulfide bonds.

Subcellular location

Lysosome.

Sequence similarities

Belongs to the peptidase C1 family.

Ontologies

Keywords
   Cellular componentLysosome
   DomainSignal
   Molecular functionHydrolase
Protease
Thiol protease
   PTMDisulfide bond
Glycoprotein
Zymogen
Gene Ontology (GO)
   Biological processproteolysis

Inferred from electronic annotation. Source: InterPro

   Cellular componentlysosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functioncysteine-type endopeptidase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1717 Potential
Propeptide18 – 117100Activation peptide
PRO_0000026252
Chain118 – 289172Cathepsin L1 heavy chain
PRO_0000026253
Propeptide290 – 2912 By similarity
PRO_0000026254
Chain292 – 33443Cathepsin L1 light chain
PRO_0000026255

Sites

Active site1381 By similarity
Active site2771 By similarity
Active site3011 By similarity

Amino acid modifications

Glycosylation2221N-linked (GlcNAc...) Potential
Glycosylation2921N-linked (GlcNAc...) Potential
Disulfide bond135 ↔ 178 By similarity
Disulfide bond169 ↔ 212 By similarity
Disulfide bond270 ↔ 323Interchain (between heavy and light chains) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q28944-1 [UniParc].

Last modified November 1, 1997. Version 1.
Checksum: 51DBA79ACCF2CE53

FASTA33437,178
        10         20         30         40         50         60 
MKPSLFLTAL CLGIASAAPK LDQNLDADWY KWKATHGRLY GMNEEGWRRA VWEKNMKMIE 

        70         80         90        100        110        120 
LHNQEYSQGK HGFSMAMNAF GDMTNEEFRQ VMNGFQNQKH KKGKVFHESL VLEVPKSVDW 

       130        140        150        160        170        180 
REKGYVTAVK NQGQCGSCWA FSATGALEGQ MFRKTGKLVS LSEQNLVDCS RPQGNQGCNG 

       190        200        210        220        230        240 
GLMDNAFQYV KDNGGLDTEE SYPYLGRETN SCTYKPECSA ANDTGFVDIP QREKALMKAV 

       250        260        270        280        290        300 
ATVGPISVAI DAGHSSFQFY KSGIYYDPDC SSKDLDHGVL VVGYGFEGTD SNSSKFWIVK 

       310        320        330 
NSWGPEWGWN GYVKMAKDQN NHCGISTAAS YPTV 

« Hide

References

[1]"Direct evidence for the elevated synthesis and secretion of procathepsin L in the distal caput epididymis of boar."
Okamura N., Tamba M., Uchiyama Y., Sugita Y., Dacheux F., Syntin P., Dacheux J.-L.
Biochim. Biophys. Acta 1245:221-226(1995) [PubMed: 7492581] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Epididymis.
[2]"Characterization and comparative mapping of the porcine CTSL gene indicates a novel synteny between HSA9q21-->q22 and SSC10q11-->q12."
Spoetter A., Droegemueller C., Kuiper H., Brenig B., Leeb T., Distl O.
Cytogenet. Cell Genet. 95:92-96(2001) [PubMed: 11978977] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases

D37917 mRNA. Translation: BAA07140.1.
AJ315771 Genomic DNA. Translation: CAC44793.1.
PIRA58195.
RefSeqNP_999057.1.
UniGeneSsc.54036

3D structure databases

HSSPHSSP built from PDB template 1ICF based on UniProtKB P07711.
SMRQ28944. Positions 21-334.
ModBaseSearch...

Protein family/group databases

MEROPSC01.032.

Genome annotation databases

GeneID396926.
KEGGssc:396926.

Organism-specific databases

CTD396926.

Phylogenomic databases

HOVERGENQ28944.

Enzyme and pathway databases

BRENDA3.4.22.15. 249.

Family and domain databases

InterProIPR000169. Pept_cys_AS.
IPR013128. Peptidase_C1A.
IPR000668. Peptidase_C1A_C.
IPR013201. Prot_inhib_I29.
[Graphical view]
PANTHERPTHR12411. Peptidase_C1A. 1 hit.
PfamPF08246. Inhibitor_I29. 1 hit.
PF00112. Peptidase_C1. 1 hit.
[Graphical view]
PRINTSPR00705. PAPAIN.
ProDomPD000158. Peptidase_C1. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00645. Pept_C1. 1 hit.
[Graphical view]
PROSITEPS00640. THIOL_PROTEASE_ASN. 1 hit.
PS00139. THIOL_PROTEASE_CYS. 1 hit.
PS00639. THIOL_PROTEASE_HIS. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCATL1_PIG
AccessionPrimary (citable) accession number: Q28944
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: September 1, 2009
This is version 66 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