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Protein

Cathepsin L1

Gene

CTSL

Organism
Homo sapiens (Human)
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)DescriptionActionsGraphical viewLength
Active sitei1381
Active sitei2761
Active sitei3001

GO - Molecular functioni

  • collagen binding Source: BHF-UCL
  • cysteine-type endopeptidase activity Source: UniProtKB
  • cysteine-type peptidase activity Source: UniProtKB
  • fibronectin binding Source: BHF-UCL
  • histone binding Source: BHF-UCL
  • proteoglycan binding Source: BHF-UCL
  • serine-type endopeptidase activity Source: Reactome
  • serpin family protein binding Source: UniProtKB

GO - Biological processi

  • adaptive immune response Source: UniProtKB
  • antigen processing and presentation Source: UniProtKB
  • antigen processing and presentation of exogenous peptide antigen via MHC class II Source: Reactome
  • cellular response to thyroid hormone stimulus Source: UniProtKB
  • collagen catabolic process Source: BHF-UCL
  • extracellular matrix disassembly Source: Reactome
  • macrophage apoptotic process Source: BHF-UCL
  • proteolysis Source: UniProtKB
  • proteolysis involved in cellular protein catabolic process Source: BHF-UCL
  • toll-like receptor signaling pathway Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Thiol protease

Enzyme and pathway databases

BioCyciZFISH:HS05942-MONOMER.
BRENDAi3.4.22.15. 2681.
ReactomeiR-HSA-1236977. Endosomal/Vacuolar pathway.
R-HSA-1442490. Collagen degradation.
R-HSA-1474228. Degradation of the extracellular matrix.
R-HSA-1679131. Trafficking and processing of endosomal TLR.
R-HSA-2022090. Assembly of collagen fibrils and other multimeric structures.
R-HSA-2132295. MHC class II antigen presentation.

Protein family/group databases

MEROPSiI29.001.

Names & Taxonomyi

Protein namesi
Recommended name:
Cathepsin L1 (EC:3.4.22.15)
Alternative name(s):
Cathepsin L
Major excreted protein
Short name:
MEP
Cleaved into the following 2 chains:
Gene namesi
Name:CTSL
Synonyms:CTSL1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 9

Organism-specific databases

HGNCiHGNC:2537. CTSL.

Subcellular locationi

GO - Cellular componenti

  • endolysosome lumen Source: Reactome
  • extracellular exosome Source: UniProtKB
  • extracellular region Source: UniProtKB
  • extracellular space Source: BHF-UCL
  • lysosomal lumen Source: Reactome
  • lysosome Source: UniProtKB
  • nucleus Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Lysosome

Pathology & Biotechi

Organism-specific databases

DisGeNETi1514.
OpenTargetsiENSG00000135047.
PharmGKBiPA162382890.

Chemistry databases

ChEMBLiCHEMBL3837.
GuidetoPHARMACOLOGYi2351.

Polymorphism and mutation databases

BioMutaiCTSL.
DMDMi115741.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 17By similarityAdd BLAST17
PropeptideiPRO_000002624418 – 113Activation peptideAdd BLAST96
ChainiPRO_0000026245114 – 288Cathepsin L1 heavy chainAdd BLAST175
PropeptideiPRO_0000026246289 – 2913
ChainiPRO_0000026247292 – 333Cathepsin L1 light chainAdd BLAST42

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi135 ↔ 178
Disulfide bondi169 ↔ 211
Glycosylationi221N-linked (GlcNAc...)3 Publications1
Disulfide bondi269 ↔ 322Interchain (between heavy and light chains)

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

EPDiP07711.
MaxQBiP07711.
PaxDbiP07711.
PeptideAtlasiP07711.
PRIDEiP07711.
TopDownProteomicsiP07711.

PTM databases

iPTMnetiP07711.
PhosphoSitePlusiP07711.

Miscellaneous databases

PMAP-CutDBP07711.

Expressioni

Gene expression databases

BgeeiENSG00000135047.
CleanExiHS_CTSL1.
ExpressionAtlasiP07711. baseline and differential.
GenevisibleiP07711. HS.

Organism-specific databases

HPAiCAB000459.

Interactioni

Subunit structurei

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

Binary interactionsi

WithEntry#Exp.IntActNotes
SGTAO437653EBI-1220160,EBI-347996
srp-6G5EFH42EBI-1220160,EBI-1549936From a different organism.

GO - Molecular functioni

  • collagen binding Source: BHF-UCL
  • fibronectin binding Source: BHF-UCL
  • histone binding Source: BHF-UCL
  • serpin family protein binding Source: UniProtKB

Protein-protein interaction databases

BioGridi107894. 23 interactors.
IntActiP07711. 14 interactors.
MINTiMINT-3005764.
STRINGi9606.ENSP00000345344.

Chemistry databases

BindingDBiP07711.

Structurei

Secondary structure

1333
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi23 – 25Combined sources3
Helixi26 – 35Combined sources10
Helixi44 – 67Combined sources24
Beta strandi72 – 75Combined sources4
Turni79 – 82Combined sources4
Helixi85 – 92Combined sources8
Beta strandi103 – 105Combined sources3
Helixi120 – 123Combined sources4
Beta strandi134 – 136Combined sources3
Helixi138 – 155Combined sources18
Helixi163 – 169Combined sources7
Turni171 – 174Combined sources4
Helixi177 – 179Combined sources3
Helixi183 – 193Combined sources11
Beta strandi196 – 198Combined sources3
Turni199 – 201Combined sources3
Helixi215 – 217Combined sources3
Beta strandi218 – 220Combined sources3
Beta strandi223 – 227Combined sources5
Helixi232 – 241Combined sources10
Beta strandi245 – 249Combined sources5
Helixi254 – 257Combined sources4
Beta strandi261 – 264Combined sources4
Beta strandi271 – 273Combined sources3
Beta strandi276 – 285Combined sources10
Beta strandi289 – 291Combined sources3
Beta strandi294 – 299Combined sources6
Beta strandi304 – 306Combined sources3
Beta strandi311 – 315Combined sources5
Beta strandi317 – 320Combined sources4
Helixi321 – 323Combined sources3
Turni324 – 326Combined sources3
Beta strandi329 – 332Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1CJLX-ray2.20A22-333[»]
1CS8X-ray1.80A19-333[»]
1ICFX-ray2.00A/C114-288[»]
B/D292-333[»]
1MHWX-ray1.90A/B114-288[»]
C/D292-333[»]
2NQDX-ray1.75B113-333[»]
2VHSX-ray1.50A/B/C/D114-285[»]
A/B/C/D294-333[»]
2XU1X-ray1.45A/B/C/D114-333[»]
2XU3X-ray0.90A114-333[»]
2XU4X-ray1.12A114-333[»]
2XU5X-ray1.60A114-333[»]
2YJ2X-ray1.15A114-333[»]
2YJ8X-ray1.30A114-333[»]
2YJ9X-ray1.35A114-333[»]
2YJBX-ray1.40A114-333[»]
2YJCX-ray1.14A114-333[»]
3BC3X-ray2.20A/B114-333[»]
3H89X-ray2.50A/B/C/D/E/F114-333[»]
3H8BX-ray1.80A/B/C/D/E/F114-333[»]
3H8CX-ray2.50A/B114-333[»]
3HHAX-ray1.27A/B/C/D114-333[»]
3HWNX-ray2.33A/B/C/D76-333[»]
3IV2X-ray2.20A/B114-333[»]
3K24X-ray2.50A/B114-333[»]
3KSEX-ray1.71A/B/C114-333[»]
3OF8X-ray2.20A113-333[»]
3OF9X-ray1.76A113-333[»]
4AXLX-ray1.92A114-333[»]
4AXMX-ray2.80A/B/F/I/L/O114-333[»]
5F02X-ray1.43A114-333[»]
5I4HX-ray1.42A113-218[»]
B222-333[»]
ProteinModelPortaliP07711.
SMRiP07711.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP07711.

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.
InParanoidiP07711.
KOiK01365.
OMAiLARDESC.
OrthoDBiEOG091G0AKT.
PhylomeDBiP07711.
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.

P07711-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNPTLILAAF CLGIASATLT FDHSLEAQWT KWKAMHNRLY GMNEEGWRRA
60 70 80 90 100
VWEKNMKMIE LHNQEYREGK HSFTMAMNAF GDMTSEEFRQ VMNGFQNRKP
110 120 130 140 150
RKGKVFQEPL FYEAPRSVDW REKGYVTPVK NQGQCGSCWA FSATGALEGQ
160 170 180 190 200
MFRKTGRLIS LSEQNLVDCS GPQGNEGCNG GLMDYAFQYV QDNGGLDSEE
210 220 230 240 250
SYPYEATEES CKYNPKYSVA NDTGFVDIPK QEKALMKAVA TVGPISVAID
260 270 280 290 300
AGHESFLFYK EGIYFEPDCS SEDMDHGVLV VGYGFESTES DNNKYWLVKN
310 320 330
SWGEEWGMGG YVKMAKDRRN HCGIASAASY PTV
Length:333
Mass (Da):37,564
Last modified:October 1, 1989 - v2
Checksum:i8CD17D00EF859D85
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti56M → V in AAH12612 (PubMed:15489334).Curated1
Sequence conflicti268D → N AA sequence (PubMed:3342889).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X12451 mRNA. Translation: CAA30981.1.
M20496 mRNA. Translation: AAA66974.1.
CR457053 mRNA. Translation: CAG33334.1.
BX537395 mRNA. Translation: CAD97637.1.
AL160279 Genomic DNA. Translation: CAI16308.1.
BC012612 mRNA. Translation: AAH12612.1.
X05256 mRNA. Translation: CAA28877.1.
CCDSiCCDS6675.1.
PIRiS01002. KHHUL.
RefSeqiNP_001244900.1. NM_001257971.1.
NP_001244901.1. NM_001257972.1.
NP_001903.1. NM_001912.4.
NP_666023.1. NM_145918.2.
XP_005251773.1. XM_005251716.3.
UniGeneiHs.731507.

Genome annotation databases

EnsembliENST00000340342; ENSP00000365061; ENSG00000135047.
ENST00000343150; ENSP00000345344; ENSG00000135047.
GeneIDi1514.
KEGGihsa:1514.
UCSCiuc004aph.4. human.

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X12451 mRNA. Translation: CAA30981.1.
M20496 mRNA. Translation: AAA66974.1.
CR457053 mRNA. Translation: CAG33334.1.
BX537395 mRNA. Translation: CAD97637.1.
AL160279 Genomic DNA. Translation: CAI16308.1.
BC012612 mRNA. Translation: AAH12612.1.
X05256 mRNA. Translation: CAA28877.1.
CCDSiCCDS6675.1.
PIRiS01002. KHHUL.
RefSeqiNP_001244900.1. NM_001257971.1.
NP_001244901.1. NM_001257972.1.
NP_001903.1. NM_001912.4.
NP_666023.1. NM_145918.2.
XP_005251773.1. XM_005251716.3.
UniGeneiHs.731507.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1CJLX-ray2.20A22-333[»]
1CS8X-ray1.80A19-333[»]
1ICFX-ray2.00A/C114-288[»]
B/D292-333[»]
1MHWX-ray1.90A/B114-288[»]
C/D292-333[»]
2NQDX-ray1.75B113-333[»]
2VHSX-ray1.50A/B/C/D114-285[»]
A/B/C/D294-333[»]
2XU1X-ray1.45A/B/C/D114-333[»]
2XU3X-ray0.90A114-333[»]
2XU4X-ray1.12A114-333[»]
2XU5X-ray1.60A114-333[»]
2YJ2X-ray1.15A114-333[»]
2YJ8X-ray1.30A114-333[»]
2YJ9X-ray1.35A114-333[»]
2YJBX-ray1.40A114-333[»]
2YJCX-ray1.14A114-333[»]
3BC3X-ray2.20A/B114-333[»]
3H89X-ray2.50A/B/C/D/E/F114-333[»]
3H8BX-ray1.80A/B/C/D/E/F114-333[»]
3H8CX-ray2.50A/B114-333[»]
3HHAX-ray1.27A/B/C/D114-333[»]
3HWNX-ray2.33A/B/C/D76-333[»]
3IV2X-ray2.20A/B114-333[»]
3K24X-ray2.50A/B114-333[»]
3KSEX-ray1.71A/B/C114-333[»]
3OF8X-ray2.20A113-333[»]
3OF9X-ray1.76A113-333[»]
4AXLX-ray1.92A114-333[»]
4AXMX-ray2.80A/B/F/I/L/O114-333[»]
5F02X-ray1.43A114-333[»]
5I4HX-ray1.42A113-218[»]
B222-333[»]
ProteinModelPortaliP07711.
SMRiP07711.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107894. 23 interactors.
IntActiP07711. 14 interactors.
MINTiMINT-3005764.
STRINGi9606.ENSP00000345344.

Chemistry databases

BindingDBiP07711.
ChEMBLiCHEMBL3837.
GuidetoPHARMACOLOGYi2351.

Protein family/group databases

MEROPSiI29.001.

PTM databases

iPTMnetiP07711.
PhosphoSitePlusiP07711.

Polymorphism and mutation databases

BioMutaiCTSL.
DMDMi115741.

Proteomic databases

EPDiP07711.
MaxQBiP07711.
PaxDbiP07711.
PeptideAtlasiP07711.
PRIDEiP07711.
TopDownProteomicsiP07711.

Protocols and materials databases

DNASUi1514.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000340342; ENSP00000365061; ENSG00000135047.
ENST00000343150; ENSP00000345344; ENSG00000135047.
GeneIDi1514.
KEGGihsa:1514.
UCSCiuc004aph.4. human.

Organism-specific databases

CTDi1514.
DisGeNETi1514.
GeneCardsiCTSL.
H-InvDBHIX0058839.
HIX0170314.
HGNCiHGNC:2537. CTSL.
HPAiCAB000459.
MIMi116880. gene.
neXtProtiNX_P07711.
OpenTargetsiENSG00000135047.
PharmGKBiPA162382890.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1543. Eukaryota.
COG4870. LUCA.
GeneTreeiENSGT00760000118871.
HOGENOMiHOG000230774.
HOVERGENiHBG011513.
InParanoidiP07711.
KOiK01365.
OMAiLARDESC.
OrthoDBiEOG091G0AKT.
PhylomeDBiP07711.
TreeFamiTF313739.

Enzyme and pathway databases

BioCyciZFISH:HS05942-MONOMER.
BRENDAi3.4.22.15. 2681.
ReactomeiR-HSA-1236977. Endosomal/Vacuolar pathway.
R-HSA-1442490. Collagen degradation.
R-HSA-1474228. Degradation of the extracellular matrix.
R-HSA-1679131. Trafficking and processing of endosomal TLR.
R-HSA-2022090. Assembly of collagen fibrils and other multimeric structures.
R-HSA-2132295. MHC class II antigen presentation.

Miscellaneous databases

EvolutionaryTraceiP07711.
GeneWikiiCathepsin_L1.
GenomeRNAii1514.
PMAP-CutDBP07711.
PROiP07711.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000135047.
CleanExiHS_CTSL1.
ExpressionAtlasiP07711. baseline and differential.
GenevisibleiP07711. HS.

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...

Entry informationi

Entry nameiCATL1_HUMAN
AccessioniPrimary (citable) accession number: P07711
Secondary accession number(s): Q6IAV1, Q96QJ0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: October 1, 1989
Last modified: November 2, 2016
This is version 191 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 9
    Human chromosome 9: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. Peptidase families
    Classification of peptidase families and list of entries
  5. 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.