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Reviewed, UniProtKB/Swiss-Prot P25975 (CATL1_BOVIN)

Last modified November 3, 2009. Version 84. 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
OrganismBos taurus (Bovine)
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length334 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.

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
   Technical termDirect protein sequencing
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_0000026236
Chain118 – 289172Cathepsin L1 heavy chain
PRO_0000026237
Propeptide290 – 2912
PRO_0000026238
Chain292 – 33443Cathepsin L1 light chain
PRO_0000026239

Sites

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

Amino acid modifications

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

Experimental info

Sequence conflict721G → A in CAA62870. Ref.1
Sequence conflict1161K → W Ref.4
Sequence conflict1161K → W Ref.5
Sequence conflict2721S → C in CAA62870. Ref.1
Sequence conflict3051P → G Ref.4
Sequence conflict3051P → G Ref.5
Sequence conflict3101N → G Ref.4
Sequence conflict3101N → G Ref.5

Sequences

Sequence LengthMass (Da)Tools
P25975-1 [UniParc].

Last modified May 30, 2006. Version 3.
Checksum: ECA5D7415DDECFC9

FASTA33437,347
        10         20         30         40         50         60 
MNPSFFLTVL CLGVASAAPK LDPNLDAHWH QWKATHRRLY GMNEEEWRRA VWEKNKKIID 

        70         80         90        100        110        120 
LHNQEYSEGK HGFRMAMNAF GDMTNEEFRQ VMNGFQNQKH KKGKLFHEPL LVDVPKSVDW 

       130        140        150        160        170        180 
TKKGYVTPVK NQGQCGSCWA FSATGALEGQ MFRKTGKLVS LSEQNLVDCS RAQGNQGCNG 

       190        200        210        220        230        240 
GLMDNAFQYI KDNGGLDSEE SYPYLATDTN SCNYKPECSA ANDTGFVDIP QREKALMKAV 

       250        260        270        280        290        300 
ATVGPISVAI DAGHTSFQFY KSGIYYDPDC SSKDLDHGVL VVGYGFEGTD SNNNKFWIVK 

       310        320        330 
NSWGPEWGWN GYVKMAKDQN NHCGIATAAS YPTV 

« Hide

References

« Hide 'large scale' references
[1]Voelkel H., Schultz J.E., Kurz U.
Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Retinal pigment epithelium.
[2]NIH - Mammalian Gene Collection (MGC) project
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Crossbred X Angus.
Tissue: Ileum.
[3]"Bos taurus cathepsin L gene."
Miyashita N.
Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-301.
[4]"The complete amino acid sequence of bovine cathepsin S and a partial sequence of bovine cathepsin L."
Ritonja A., Colic A., Dolenc I., Ogrinc T., Podobnik M., Turk V.
FEBS Lett. 283:329-331(1991) [PubMed: 2044774] [Abstract]
Cited for: PROTEIN SEQUENCE OF 114-132 AND 293-311.
[5]"Bovine cathepsins S and L: isolation and amino acid sequences."
Dolenc I., Ritonja A., Colic A., Podobnik M., Ogrinc T., Turk V.
Biol. Chem. Hoppe-Seyler 373:407-412(1992) [PubMed: 1515067] [Abstract]
Cited for: PROTEIN SEQUENCE OF 114-132 AND 293-311.
Tissue: Kidney.

Cross-references

Sequence databases

X91755 mRNA. Translation: CAA62870.1.
BC102312 mRNA. Translation: AAI02313.1.
AB017648 Genomic DNA. Translation: BAA33398.1.
IPIIPI00687440.
PIRS15845.
RefSeqNP_776457.1.
UniGeneBt.3987

3D structure databases

HSSPHSSP built from PDB template 1FH0 based on UniProtKB O60911.
SMRP25975. Positions 21-334.
ModBaseSearch...

Protein-protein interaction databases

STRINGP25975.

Genome annotation databases

EnsemblENSBTAT00000022710; ENSBTAP00000022710; ENSBTAG00000017077; Bos taurus. [Genome view]
ENSBTAT00000036427; ENSBTAP00000036285; ENSBTAG00000017077; Bos taurus. [Genome view]
GeneID281108.
KEGGbta:281108.

Organism-specific databases

CTD281108.

Phylogenomic databases

HOVERGENP25975.
OMARMERNIK.

Enzyme and pathway databases

BRENDA3.4.22.15. 251.

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...

Other Resources

BindingDBP25975.

Entry information

Entry nameCATL1_BOVIN
AccessionPrimary (citable) accession number: P25975
Secondary accession number(s): O77502, Q3T0P2
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: May 30, 2006
Last modified: November 3, 2009
This is version 84 of the entry and version 3 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