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 L1

Gene

CTSL

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Important for the overall degradation of proteins in lysosomes.

Catalytic activityi

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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei138 – 1381By similarity
Active sitei277 – 2771By similarity
Active sitei301 – 3011By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Thiol protease

Protein family/group databases

MEROPSiI29.010.

Names & Taxonomyi

Protein namesi
Recommended name:
Cathepsin L1 (EC:3.4.22.15)
Alternative name(s):
Cathepsin L
Cleaved into the following 2 chains:
Gene namesi
Name:CTSL
Synonyms:CTSL1
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 8

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Lysosome

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL2113.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1717By similarityAdd
BLAST
Propeptidei18 – 117100Activation peptidePRO_0000026236Add
BLAST
Chaini118 – 289172Cathepsin L1 heavy chainPRO_0000026237Add
BLAST
Propeptidei290 – 2912PRO_0000026238
Chaini292 – 33443Cathepsin L1 light chainPRO_0000026239Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi135 ↔ 178By similarity
Disulfide bondi169 ↔ 212By similarity
Glycosylationi222 – 2221N-linked (GlcNAc...)Sequence analysis
Disulfide bondi270 ↔ 323Interchain (between heavy and light chains)By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

PaxDbiP25975.
PRIDEiP25975.

Expressioni

Gene expression databases

ExpressionAtlasiP25975. baseline and differential.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000022710.

Chemistry

BindingDBiP25975.

Structurei

3D structure databases

ProteinModelPortaliP25975.
SMRiP25975. Positions 21-334.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase C1 family.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG1543. Eukaryota.
COG4870. LUCA.
GeneTreeiENSGT00760000118871.
HOGENOMiHOG000230774.
HOVERGENiHBG011513.
InParanoidiP25975.
KOiK01365.
OMAiSKFWIVK.
OrthoDBiEOG786H3P.
TreeFamiTF313739.

Family and domain databases

InterProiIPR025661. Pept_asp_AS.
IPR000169. Pept_cys_AS.
IPR025660. Pept_his_AS.
IPR013128. Peptidase_C1A.
IPR000668. Peptidase_C1A_C.
IPR013201. Prot_inhib_I29.
[Graphical view]
PANTHERiPTHR12411. PTHR12411. 1 hit.
PfamiPF08246. Inhibitor_I29. 1 hit.
PF00112. Peptidase_C1. 1 hit.
[Graphical view]
PRINTSiPR00705. PAPAIN.
SMARTiSM00848. Inhibitor_I29. 1 hit.
SM00645. Pept_C1. 1 hit.
[Graphical view]
PROSITEiPS00640. THIOL_PROTEASE_ASN. 1 hit.
PS00139. THIOL_PROTEASE_CYS. 1 hit.
PS00639. THIOL_PROTEASE_HIS. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P25975-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNPSFFLTVL CLGVASAAPK LDPNLDAHWH QWKATHRRLY GMNEEEWRRA
60 70 80 90 100
VWEKNKKIID LHNQEYSEGK HGFRMAMNAF GDMTNEEFRQ VMNGFQNQKH
110 120 130 140 150
KKGKLFHEPL LVDVPKSVDW TKKGYVTPVK NQGQCGSCWA FSATGALEGQ
160 170 180 190 200
MFRKTGKLVS LSEQNLVDCS RAQGNQGCNG GLMDNAFQYI KDNGGLDSEE
210 220 230 240 250
SYPYLATDTN SCNYKPECSA ANDTGFVDIP QREKALMKAV ATVGPISVAI
260 270 280 290 300
DAGHTSFQFY KSGIYYDPDC SSKDLDHGVL VVGYGFEGTD SNNNKFWIVK
310 320 330
NSWGPEWGWN GYVKMAKDQN NHCGIATAAS YPTV
Length:334
Mass (Da):37,347
Last modified:May 30, 2006 - v3
Checksum:iECA5D7415DDECFC9
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti72 – 721G → A in CAA62870 (Ref. 1) Curated
Sequence conflicti116 – 1161K → W AA sequence (PubMed:2044774).Curated
Sequence conflicti116 – 1161K → W AA sequence (PubMed:1515067).Curated
Sequence conflicti272 – 2721S → C in CAA62870 (Ref. 1) Curated
Sequence conflicti305 – 3051P → G AA sequence (PubMed:2044774).Curated
Sequence conflicti305 – 3051P → G AA sequence (PubMed:1515067).Curated
Sequence conflicti310 – 3101N → G AA sequence (PubMed:2044774).Curated
Sequence conflicti310 – 3101N → G AA sequence (PubMed:1515067).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X91755 mRNA. Translation: CAA62870.1.
BC102312 mRNA. Translation: AAI02313.1.
AB017648 Genomic DNA. Translation: BAA33398.1.
PIRiS15845.
RefSeqiNP_776457.1. NM_174032.2.
UniGeneiBt.3987.

Genome annotation databases

EnsembliENSBTAT00000022710; ENSBTAP00000022710; ENSBTAG00000017077.
ENSBTAT00000036427; ENSBTAP00000036285; ENSBTAG00000017077.
GeneIDi281108.
KEGGibta:281108.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X91755 mRNA. Translation: CAA62870.1.
BC102312 mRNA. Translation: AAI02313.1.
AB017648 Genomic DNA. Translation: BAA33398.1.
PIRiS15845.
RefSeqiNP_776457.1. NM_174032.2.
UniGeneiBt.3987.

3D structure databases

ProteinModelPortaliP25975.
SMRiP25975. Positions 21-334.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000022710.

Chemistry

BindingDBiP25975.
ChEMBLiCHEMBL2113.

Protein family/group databases

MEROPSiI29.010.

Proteomic databases

PaxDbiP25975.
PRIDEiP25975.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000022710; ENSBTAP00000022710; ENSBTAG00000017077.
ENSBTAT00000036427; ENSBTAP00000036285; ENSBTAG00000017077.
GeneIDi281108.
KEGGibta:281108.

Organism-specific databases

CTDi1515.

Phylogenomic databases

eggNOGiKOG1543. Eukaryota.
COG4870. LUCA.
GeneTreeiENSGT00760000118871.
HOGENOMiHOG000230774.
HOVERGENiHBG011513.
InParanoidiP25975.
KOiK01365.
OMAiSKFWIVK.
OrthoDBiEOG786H3P.
TreeFamiTF313739.

Miscellaneous databases

PROiP25975.

Gene expression databases

ExpressionAtlasiP25975. baseline and differential.

Family and domain databases

InterProiIPR025661. Pept_asp_AS.
IPR000169. Pept_cys_AS.
IPR025660. Pept_his_AS.
IPR013128. Peptidase_C1A.
IPR000668. Peptidase_C1A_C.
IPR013201. Prot_inhib_I29.
[Graphical view]
PANTHERiPTHR12411. PTHR12411. 1 hit.
PfamiPF08246. Inhibitor_I29. 1 hit.
PF00112. Peptidase_C1. 1 hit.
[Graphical view]
PRINTSiPR00705. PAPAIN.
SMARTiSM00848. Inhibitor_I29. 1 hit.
SM00645. Pept_C1. 1 hit.
[Graphical view]
PROSITEiPS00640. THIOL_PROTEASE_ASN. 1 hit.
PS00139. THIOL_PROTEASE_CYS. 1 hit.
PS00639. THIOL_PROTEASE_HIS. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 114-132 AND 293-311.
    Tissue: Kidney.

Entry informationi

Entry nameiCATL1_BOVIN
AccessioniPrimary (citable) accession number: P25975
Secondary accession number(s): O77502, Q3T0P2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: May 30, 2006
Last modified: June 8, 2016
This is version 133 of the entry and version 3 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.