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Protein

Cathepsin L1

Gene

CTSL

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -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
  • regulation of keratinocyte differentiation Source: Reactome

Keywordsi

Molecular functionHydrolase, Protease, Thiol protease

Enzyme and pathway databases

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
R-HSA-8939242 RUNX1 regulates transcription of genes involved in differentiation of keratinocytes

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

EuPathDBiHostDB:ENSG00000135047.14
HGNCiHGNC:2537 CTSL
MIMi116880 gene
neXtProtiNX_P07711

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Lysosome

Pathology & Biotechi

Organism-specific databases

DisGeNETi1514
OpenTargetsiENSG00000135047
PharmGKBiPA162382890

Chemistry databases

ChEMBLiCHEMBL3837
DrugBankiDB07477 BIPHENYL-4-YL-ACETALDEHYDE
DB03661 Cysteinesulfonic Acid
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...) asparagine3 Publications1
Disulfide bondi269 ↔ 322Interchain (between heavy and light chains)

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

EPDiP07711
MaxQBiP07711
PaxDbiP07711
PeptideAtlasiP07711
PRIDEiP07711
ProteomicsDBi52023
TopDownProteomicsiP07711

PTM databases

iPTMnetiP07711
PhosphoSitePlusiP07711

Miscellaneous databases

PMAP-CutDBiP07711

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

Show more details

GO - Molecular functioni

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

Protein-protein interaction databases

BioGridi107894, 24 interactors
IntActiP07711, 14 interactors
MINTiP07711
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
Beta strandi116 – 119Combined sources4
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/D114-333[»]
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[»]
5MAEX-ray1.00A114-333[»]
5MAJX-ray1.00A114-333[»]
5MQYX-ray1.13A114-333[»]
6EZPX-ray1.37A114-333[»]
6EZXX-ray2.34A/B114-333[»]
6F06X-ray2.02A/B114-333[»]
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
GeneTreeiENSGT00900000140823
HOGENOMiHOG000230774
HOVERGENiHBG011513
InParanoidiP07711
KOiK01365
OMAiQHYRKSG
OrthoDBiEOG091G0AKT
PhylomeDBiP07711
TreeFamiTF313739

Family and domain databases

InterProiView protein in InterPro
IPR038765 Papain_like_cys_pep_sf
IPR025661 Pept_asp_AS
IPR000169 Pept_cys_AS
IPR025660 Pept_his_AS
IPR013128 Peptidase_C1A
IPR000668 Peptidase_C1A_C
IPR013201 Prot_inhib_I29
PANTHERiPTHR12411 PTHR12411, 1 hit
PfamiView protein in Pfam
PF08246 Inhibitor_I29, 1 hit
PF00112 Peptidase_C1, 1 hit
PRINTSiPR00705 PAPAIN
SMARTiView protein in SMART
SM00848 Inhibitor_I29, 1 hit
SM00645 Pept_C1, 1 hit
SUPFAMiSSF54001 SSF54001, 1 hit
PROSITEiView protein in PROSITE
PS00640 THIOL_PROTEASE_ASN, 1 hit
PS00139 THIOL_PROTEASE_CYS, 1 hit
PS00639 THIOL_PROTEASE_HIS, 1 hit

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 No translation available.
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

Similar proteinsi

Entry informationi

Entry nameiCATL1_HUMAN
AccessioniPrimary (citable) accession number: P07711
Secondary accession number(s): Q6IAV1, Q96QJ0
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: October 1, 1989
Last modified: June 20, 2018
This is version 204 of the entry and version 2 of the sequence. See 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

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