CTSL
entrez
1514
canonical
uniprot
P07711
canonical
ensembl
ENSG00000135047
resolver
ensp
ENSP00000340470
resolver
ensp
ENSP00000345344
resolver
ensp
ENSP00000502968
resolver
ensp
ENSP00000503298
resolver
ensp
ENSP00000503439
resolver
ensp
ENSP00000504313
resolver
ensp
ENSP00000504473
resolver
ensp
ENSP00000668918
resolver
ensp
ENSP00000692693
resolver
enst
ENST00000342020
resolver
genesymbol
CTSL
resolver
genesymbol_syn
CTSL1
resolver
hgnc
HGNC:2537
resolver
uniprot
Q5T8F0
resolver
uniprot
Q6IAV1
resolver
uniprot
Q96QJ0
resolver
uniprot
Q9HBQ7
resolver
uniprot_entry
CATL1_HUMAN
resolver
uniprot_entry
Q5T8F0_HUMAN
resolver
uniprot_entry
Q9HBQ7_HUMAN
resolver
uniprot_sec
Q6IAV1
resolver
uniprot_sec
Q96QJ0
resolver
activity_regulation
ACTIVITY REGULATION: Inhibited by the propeptide produced by autocleavage (PubMed:9468501). Long isoform of CD74/Ii chain stabilizes the conformation of mature CTSL by binding to its active site and serving as a chaperone to help maintain a pool of mature enzyme in endocytic compartments and extracellular space of APCs. IFNG enhances the conversion into the CTSL mature and active form (By similarity). Inhibited by CST6. Inhibited by the glycopeptide antibiotic teicoplanin (PubMed:26953343). Inhibited by amantadine (PubMed:32361028). {ECO:0000250|UniProtKB:P06797, ECO:0000269|PubMed:26953343, ECO:0000269|PubMed:30425301, ECO:0000269|PubMed:32361028, ECO:0000269|PubMed:9468501}.
uniprot
proteins
amino_acid_sequence
MNPTLILAAFCLGIASATLTFDHSLEAQWTKWKAMHNRLYGMNEEGWRRAVWEKNMKMIELHNQEYREGKHSFTMAMNAFGDMTSEEFRQVMNGFQNRKPRKGKVFQEPLFYEAPRSVDWREKGYVTPVKNQGQCGSCWAFSATGALEGQMFRKTGRLISLSEQNLVDCSGPQGNEGCNGGLMDYAFQYVQDNGGLDSEESYPYEATEESCKYNPKYSVANDTGFVDIPKQEKALMKAVATVGPISVAIDAGHESFLFYKEGIYFEPDCSSEDMDHGVLVVGYGFESTESDNNKYWLVKNSWGEEWGMGGYVKMAKDRRNHCGIASAASYPTV
uniprot
proteins
ec_number
3.4.22.15
uniprot
proteins
function
FUNCTION: Thiol protease important for the overall degradation of proteins in lysosomes (Probable). Plays a critical for normal cellular functions such as general protein turnover, antigen processing and bone remodeling. Involved in the solubilization of cross-linked TG/thyroglobulin and in the subsequent release of thyroid hormone thyroxine (T4) by limited proteolysis of TG/thyroglobulin in the thyroid follicle lumen (By similarity). In neuroendocrine chromaffin cells secretory vesicles, catalyzes the prohormone proenkephalin processing to the active enkephalin peptide neurotransmitter (By similarity). In thymus, regulates CD4(+) T cell positive selection by generating the major histocompatibility complex class II (MHCII) bound peptide ligands presented by cortical thymic epithelial cells. Also mediates invariant chain processing in cortical thymic epithelial cells (By similarity). Major elastin-degrading enzyme at neutral pH. Accumulates as a mature and active enzyme in the extracellular space of antigen presenting cells (APCs) to regulate degradation of the extracellular matrix in the course of inflammation (By similarity). Secreted form generates endostatin from COL18A1 (PubMed:10716919). Critical for cardiac morphology and function. Plays an important role in hair follicle morphogenesis and cycling, as well as epidermal differentiation (By similarity). Required for maximal stimulation of steroidogenesis by TIMP1 (By similarity). {ECO:0000250|UniProtKB:P06797, ECO:0000250|UniProtKB:P07154, ECO:0000250|UniProtKB:P25975, ECO:0000269|PubMed:10716919, ECO:0000305}.; FUNCTION: (Microbial infection) In cells lacking TMPRSS2 expression, facilitates human coronaviruses SARS-CoV and SARS-CoV-2 infections via a slow acid-activated route with the proteolysis of coronavirus spike (S) glycoproteins in lysosome for entry into host cell (PubMed:16339146, PubMed:18562523, PubMed:32142651, PubMed:32221306, PubMed:37990007). Proteolysis within lysosomes is sufficient to activate membrane fusion by coronaviruses SARS-CoV and EMC (HCoV-EMC) S as well as Zaire ebolavirus glycoproteins (PubMed:16081529, PubMed:18562523, PubMed:26953343). {ECO:0000269|PubMed:16081529, ECO:0000269|PubMed:16339146, ECO:0000269|PubMed:18562523, ECO:0000269|PubMed:26953343, ECO:0000269|PubMed:32142651, ECO:0000269|PubMed:32221306, ECO:0000269|PubMed:32855215, ECO:0000269|PubMed:37990007}.; FUNCTION: [Isoform 2]: Functions in the regulation of cell cycle progression through proteolytic processing of the CUX1 transcription factor (PubMed:15099520). Translation initiation at downstream start sites allows the synthesis of isoforms that are devoid of a signal peptide and localize to the nucleus where they cleave the CUX1 transcription factor and modify its DNA binding properties (PubMed:15099520). {ECO:0000269|PubMed:15099520}.
uniprot
proteins
mass_dalton
37564
uniprot
proteins
mutagenesis
MUTAGEN 138; /note="C->S: Catalytically inactive. Unable to autocleave procathepsin L."; /evidence="ECO:0000269|PubMed:9468501
uniprot
proteins
post_translational_modification
PTM: During export along the endocytic pathway, pro-CTSL undergoes several proteolytic cleavages to generate the CTSL single-chain and two-chain mature forms, composed of a heavy chain linked to a light chain by disulfide bonds (By similarity). Autocleavage; produces the single-chain CTSL after cleavage of the propeptide. The cleavage can be intermolecular (PubMed:9468501). {ECO:0000250|UniProtKB:P06797, ECO:0000269|PubMed:9468501}.
uniprot
proteins
protein_family
Peptidase C1 family
uniprot
proteins
pubmed
10716919
uniprot
proteins
pubmed
12754519
uniprot
proteins
pubmed
15099520
uniprot
proteins
pubmed
15164053
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16081529
uniprot
proteins
pubmed
16335952
uniprot
proteins
pubmed
16339146
uniprot
proteins
pubmed
17974005
uniprot
proteins
pubmed
18562523
uniprot
proteins
pubmed
19159218
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
22905912
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
26953343
uniprot
proteins
pubmed
2835398
uniprot
proteins
pubmed
30425301
uniprot
proteins
pubmed
32142651
uniprot
proteins
pubmed
32221306
uniprot
proteins
pubmed
32361028
uniprot
proteins
pubmed
32855215
uniprot
proteins
pubmed
3342889
uniprot
proteins
pubmed
34159616
uniprot
proteins
pubmed
3421948
uniprot
proteins
pubmed
3545185
uniprot
proteins
pubmed
3550705
uniprot
proteins
pubmed
37990007
uniprot
proteins
pubmed
8896443
uniprot
proteins
pubmed
9141479
uniprot
proteins
pubmed
9468501
uniprot
proteins
sequence_length
333
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Lysosome {ECO:0000250|UniProtKB:P06797}. Apical cell membrane {ECO:0000250|UniProtKB:P06797}; Peripheral membrane protein {ECO:0000250|UniProtKB:P06797}; Extracellular side {ECO:0000250|UniProtKB:P06797}. Cytoplasmic vesicle, secretory vesicle, chromaffin granule {ECO:0000250|UniProtKB:P25975}. Secreted, extracellular space {ECO:0000250|UniProtKB:P06797}. Secreted {ECO:0000250|UniProtKB:P06797}. Note=Localizes to the apical membrane of thyroid epithelial cells. Released at extracellular space by activated dendritic cells and macrophages. {ECO:0000250|UniProtKB:P06797}.; SUBCELLULAR LOCATION: [Isoform 2]: Nucleus {ECO:0000269|PubMed:15099520}. Note=Translation initiation at downstream start sites allows the synthesis of isoforms that are devoid of a signal peptide and do not transit through the endoplasmic reticulum to localize to the nucleus (PubMed:15099520). Nuclear location varies during the cell cycle, with higher levels during S phase (PubMed:15099520). {ECO:0000269|PubMed:15099520}.
uniprot
proteins