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Reviewed, UniProtKB/Swiss-Prot Q9GKL8 (CATL1_CERAE)

Last modified June 16, 2009. Version 35. 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
Alternative name(s):
    Major excreted protein
      Short name=MEP
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
OrganismCercopithecus aethiops (Green monkey) (Grivet)
Taxonomic identifier9534 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniCercopithecidaeCercopithecinaeChlorocebus

Protein attributes

Sequence length333 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Important for the overall degradation of proteins in lysosomes By similarity.

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 By similarity.

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 – 11396Activation peptide By similarity
PRO_0000287866
Chain114 – 288175Cathepsin L1 heavy chain
PRO_0000287867
Propeptide289 – 2913 By similarity
PRO_0000287868
Chain292 – 33342Cathepsin L1 light chain
PRO_0000287869

Sites

Active site1381 By similarity
Active site2761 By similarity
Active site3001 By similarity

Amino acid modifications

Glycosylation2211N-linked (GlcNAc...)
Disulfide bond135 ↔ 178 By similarity
Disulfide bond169 ↔ 211 By similarity
Disulfide bond269 ↔ 322Interchain (between heavy and light chains) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9GKL8-1 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: F6CB37EF18A36E59

FASTA33337,430
        10         20         30         40         50         60 
MNPTFILAAL CLGIASATLT FNHSLEAQWT KWKAMHNRLY GMNEEGWRRA VWEKNMKMIE 

        70         80         90        100        110        120 
LHNQEYSQGK HSFTMAMNTF GDMTSEEFRQ VMNGFQNRKP RKGKVFQEPL FYEAPRSVDW 

       130        140        150        160        170        180 
REKGYVTPVK NQGQCGSCWA FSATGALEGQ MFRKTGKLVS LSEQNLVDCS GPQGNEGCNG 

       190        200        210        220        230        240 
GLMDYAFQYV ADNGGLDSEE SYPYEATEES CKYNPEYSVA NDTGFVDIPK QEKALMKAVA 

       250        260        270        280        290        300 
TVGPISVAID AGHESFMFYK EGIYFEPDCS SEDMDHGVLV VGYGFESTES DNSKYWLVKN 

       310        320        330 
SWGEEWGMGG YIKMAKDRRN HCGIASAASY PTV 

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References

[1]"Molecular cloning of a cDNA encoding a nuclear localizing cathepsin L-like cysteine protease, SPase."
Nishinaka T., Huynh T., Cheng C.-H., Chiu R.
Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Kidney.

Cross-references

Sequence databases

AF201700 mRNA. Translation: AAG35605.1.

3D structure databases

HSSPHSSP built from PDB template 1ICF based on UniProtKB P07711.
SMRQ9GKL8. Positions 18-333.
ModBaseSearch...

Protein family/group databases

MEROPSC01.032.
I29.001.

Phylogenomic databases

HOVERGENQ9GKL8.

Enzyme and pathway databases

BRENDA3.4.22.15. 2052.

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_CERAE
AccessionPrimary (citable) accession number: Q9GKL8
Entry history
Integrated into UniProtKB/Swiss-Prot: May 15, 2007
Last sequence update: March 1, 2001
Last modified: June 16, 2009
This is version 35 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