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Entry version 223 (02 Dec 2020)
Sequence version 2 (01 Oct 1989)
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Protein

Procathepsin L

Gene

CTSL

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

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).By similarityCurated1 Publication
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).1 Publication
(Microbial infection) Facilitates human coronaviruses SARS-CoV and SARS-CoV-2 infections via proteolysis of coronavirus spike (S) glycoproteins in lysosome for entry into host cell (PubMed:32142651, PubMed:32221306, PubMed:16339146, PubMed:18562523). 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:26953343, PubMed:18562523).6 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>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.1 Publication EC:3.4.22.15

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

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).By similarity4 Publications

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>pH dependencei

Optimum pH is 5.5, also active at pH 7.0 with CUX1 as substrate.4 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei1381 Publication1
Active sitei2761
Active sitei3001

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionHydrolase, Protease, Thiol protease

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
3.4.22.15, 2681

Pathway Commons web resource for biological pathway data

More...
PathwayCommonsi
P07711

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-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
R-HSA-9678110, Attachment and Entry

SIGNOR Signaling Network Open Resource

More...
SIGNORi
P07711

Protein family/group databases

MEROPS protease database

More...
MEROPSi
I29.001

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Procathepsin LCurated (EC:3.4.22.151 Publication)
Alternative name(s):
Cathepsin L1Curated
Major excreted protein
Short name:
MEP
Cleaved into the following 3 chains:
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:CTSLImported
Synonyms:CTSL1
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 9

Organism-specific databases

Eukaryotic Pathogen and Host Database Resources

More...
EuPathDBi
HostDB:ENSG00000135047.14

Human Gene Nomenclature Database

More...
HGNCi
HGNC:2537, CTSL

Online Mendelian Inheritance in Man (OMIM)

More...
MIMi
116880, gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_P07711

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>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 & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell membrane, Cytoplasmic vesicle, Lysosome, Membrane, Nucleus, Secreted

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi138C → S: Catalytically inactive. Unable to autocleave procathepsin L. 1 Publication1

Organism-specific databases

DisGeNET

More...
DisGeNETi
1514

Open Targets

More...
OpenTargetsi
ENSG00000135047

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...
PharmGKBi
PA162382890

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...
Pharosi
P07711, Tchem

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL3837

Drug and drug target database

More...
DrugBanki
DB07477, Felbinac
DB12010, Fostamatinib
DB03661, L-cysteic acid
DB14962, Trastuzumab deruxtecan

DrugCentral

More...
DrugCentrali
P07711

IUPHAR/BPS Guide to PHARMACOLOGY

More...
GuidetoPHARMACOLOGYi
2351

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
CTSL

Domain mapping of disease mutations (DMDM)

More...
DMDMi
115741

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 17By similarityAdd BLAST17
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section describes a propeptide, which is a part of a protein that is cleaved during maturation or activation. Once cleaved, a propeptide generally has no independent biological function.<p><a href='/help/propep' target='_top'>More...</a></p>PropeptideiPRO_000002624418 – 113Activation peptide1 PublicationAdd BLAST96
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_0000450791114 – 333Cathepsin L1 PublicationAdd BLAST220
ChainiPRO_0000026245114 – 288Cathepsin L heavy chainAdd BLAST175
PropeptideiPRO_0000026246289 – 2913
ChainiPRO_0000026247292 – 333Cathepsin L light chain1 PublicationAdd BLAST42

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi135 ↔ 178
Disulfide bondi169 ↔ 211
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi221N-linked (GlcNAc...) asparagine3 Publications1
Disulfide bondi269 ↔ 322Interchain (between heavy and light chains)

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

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).By similarity1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei106 – 107Cleavage; by autolysis1 Publication2
Sitei107 – 108Cleavage; by autolysis1 Publication2
Sitei112 – 113Cleavage; by autolysis1 Publication2
Sitei113 – 114Cleavage; by autolysis1 Publication2

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
P07711

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
P07711

MassIVE - Mass Spectrometry Interactive Virtual Environment

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MassIVEi
P07711

MaxQB - The MaxQuant DataBase

More...
MaxQBi
P07711

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
P07711

PeptideAtlas

More...
PeptideAtlasi
P07711

PRoteomics IDEntifications database

More...
PRIDEi
P07711

ProteomicsDB: a multi-organism proteome resource

More...
ProteomicsDBi
52023

Consortium for Top Down Proteomics

More...
TopDownProteomicsi
P07711-1

PTM databases

GlyConnect protein glycosylation platform

More...
GlyConnecti
1081, 12 N-Linked glycans (1 site)

GlyGen: Computational and Informatics Resources for Glycoscience

More...
GlyGeni
P07711, 1 site, 1 N-linked glycan (1 site)

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P07711

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...
PhosphoSitePlusi
P07711

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSG00000135047, Expressed in layer of synovial tissue and 248 other tissues

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
P07711, baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
P07711, HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
ENSG00000135047, Tissue enhanced (placenta)

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

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

Interacts with Long isoform of CD74/Ii chain; the interaction stabilizes the conformation of mature CTSL.

By similarity

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Hide details

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

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BioGRIDi
107894, 27 interactors

Protein interaction database and analysis system

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IntActi
P07711, 22 interactors

Molecular INTeraction database

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MINTi
P07711

STRING: functional protein association networks

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STRINGi
9606.ENSP00000345344

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
P07711

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...
RNActi
P07711, protein

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1333
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
P07711

Database of comparative protein structure models

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ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P07711

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the peptidase C1 family.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG1543, Eukaryota

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000154367

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
CLU_012184_1_2_1

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P07711

Identification of Orthologs from Complete Genome Data

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OMAi
GQHYRKS

Database of Orthologous Groups

More...
OrthoDBi
1275401at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P07711

TreeFam database of animal gene trees

More...
TreeFami
TF313739

Family and domain databases

Conserved Domains Database

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CDDi
cd02248, Peptidase_C1A, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR038765, Papain-like_cys_pep_sf
IPR025661, Pept_asp_AS
IPR000169, Pept_cys_AS
IPR025660, Pept_his_AS
IPR000668, Peptidase_C1A_C
IPR039417, Peptidase_C1A_papain-like
IPR013201, Prot_inhib_I29

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF08246, Inhibitor_I29, 1 hit
PF00112, Peptidase_C1, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00705, PAPAIN

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00848, Inhibitor_I29, 1 hit
SM00645, Pept_C1, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF54001, SSF54001, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00640, THIOL_PROTEASE_ASN, 1 hit
PS00139, THIOL_PROTEASE_CYS, 1 hit
PS00639, THIOL_PROTEASE_HIS, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 <p>This subsection of the 'Sequence' section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform. This section is only present in reviewed entries, i.e. in UniProtKB/Swiss-Prot.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative initiation. AlignAdd to basket

This entry has 2 described isoforms and 1 potential isoform that is computationally mapped.Show allAlign All

Isoform 1 (identifier: P07711-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« 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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i8CD17D00EF859D85
GO
Isoform 2 (identifier: P07711-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-55: Missing.

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Length:278
Mass (Da):31,173
Checksum:iC5AF8867424808FF
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
Q5T8F0Q5T8F0_HUMAN
Procathepsin L
CTSL
225Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti56M → V in AAH12612 (PubMed:15489334).Curated1
Sequence conflicti268D → N AA sequence (PubMed:3342889).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0607201 – 55Missing in isoform 2. Add BLAST55

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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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

The Consensus CDS (CCDS) project

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CCDSi
CCDS6675.1

Protein sequence database of the Protein Information Resource

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PIRi
S01002, KHHUL

NCBI Reference Sequences

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RefSeqi
NP_001244900.1, NM_001257971.1 [P07711-1]
NP_001244901.1, NM_001257972.1 [P07711-1]
NP_001903.1, NM_001912.4 [P07711-1]
NP_666023.1, NM_145918.2 [P07711-1]
XP_005251773.1, XM_005251716.3

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENST00000340342; ENSP00000365061; ENSG00000135047
ENST00000343150; ENSP00000345344; ENSG00000135047

Database of genes from NCBI RefSeq genomes

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GeneIDi
1514

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
hsa:1514

UCSC genome browser

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UCSCi
uc004aph.4, human [P07711-1]

Keywords - Coding sequence diversityi

Alternative initiation

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross%5Freferences%5Fsection">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>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 No translation available.
BC012612 mRNA Translation: AAH12612.1
X05256 mRNA Translation: CAA28877.1
CCDSiCCDS6675.1
PIRiS01002, KHHUL
RefSeqiNP_001244900.1, NM_001257971.1 [P07711-1]
NP_001244901.1, NM_001257972.1 [P07711-1]
NP_001903.1, NM_001912.4 [P07711-1]
NP_666023.1, NM_145918.2 [P07711-1]
XP_005251773.1, XM_005251716.3

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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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[»]
6JD0X-ray1.80A18-333[»]
6JD8X-ray1.46A18-333[»]
SMRiP07711
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi107894, 27 interactors
IntActiP07711, 22 interactors
MINTiP07711
STRINGi9606.ENSP00000345344

Chemistry databases

BindingDBiP07711
ChEMBLiCHEMBL3837
DrugBankiDB07477, Felbinac
DB12010, Fostamatinib
DB03661, L-cysteic acid
DB14962, Trastuzumab deruxtecan
DrugCentraliP07711
GuidetoPHARMACOLOGYi2351

Protein family/group databases

MEROPSiI29.001

PTM databases

GlyConnecti1081, 12 N-Linked glycans (1 site)
GlyGeniP07711, 1 site, 1 N-linked glycan (1 site)
iPTMnetiP07711
PhosphoSitePlusiP07711

Polymorphism and mutation databases

BioMutaiCTSL
DMDMi115741

Proteomic databases

EPDiP07711
jPOSTiP07711
MassIVEiP07711
MaxQBiP07711
PaxDbiP07711
PeptideAtlasiP07711
PRIDEiP07711
ProteomicsDBi52023
TopDownProteomicsiP07711-1

Protocols and materials databases

ABCD curated depository of sequenced antibodies

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ABCDi
P07711, 1 sequenced antibody

Antibodypedia a portal for validated antibodies

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Antibodypediai
4374, 609 antibodies

The DNASU plasmid repository

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DNASUi
1514

Genome annotation databases

EnsembliENST00000340342; ENSP00000365061; ENSG00000135047
ENST00000343150; ENSP00000345344; ENSG00000135047
GeneIDi1514
KEGGihsa:1514
UCSCiuc004aph.4, human [P07711-1]

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
1514
DisGeNETi1514
EuPathDBiHostDB:ENSG00000135047.14

GeneCards: human genes, protein and diseases

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GeneCardsi
CTSL
HGNCiHGNC:2537, CTSL
HPAiENSG00000135047, Tissue enhanced (placenta)
MIMi116880, gene
neXtProtiNX_P07711
OpenTargetsiENSG00000135047
PharmGKBiPA162382890

GenAtlas: human gene database

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GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG1543, Eukaryota
GeneTreeiENSGT00940000154367
HOGENOMiCLU_012184_1_2_1
InParanoidiP07711
OMAiGQHYRKS
OrthoDBi1275401at2759
PhylomeDBiP07711
TreeFamiTF313739

Enzyme and pathway databases

BRENDAi3.4.22.15, 2681
PathwayCommonsiP07711
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
R-HSA-9678110, Attachment and Entry
SIGNORiP07711

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

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BioGRID-ORCSi
1514, 7 hits in 840 CRISPR screens

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

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ChiTaRSi
CTSL, human
EvolutionaryTraceiP07711

The Gene Wiki collection of pages on human genes and proteins

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GeneWikii
Cathepsin_L1

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

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GenomeRNAii
1514
PharosiP07711, Tchem

Protein Ontology

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PROi
PR:P07711
RNActiP07711, protein

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
Search...

Gene expression databases

BgeeiENSG00000135047, Expressed in layer of synovial tissue and 248 other tissues
ExpressionAtlasiP07711, baseline and differential
GenevisibleiP07711, HS

Family and domain databases

CDDicd02248, Peptidase_C1A, 1 hit
InterProiView protein in InterPro
IPR038765, Papain-like_cys_pep_sf
IPR025661, Pept_asp_AS
IPR000169, Pept_cys_AS
IPR025660, Pept_his_AS
IPR000668, Peptidase_C1A_C
IPR039417, Peptidase_C1A_papain-like
IPR013201, Prot_inhib_I29
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

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiCATL1_HUMAN
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P07711
Secondary accession number(s): Q6IAV1, Q96QJ0
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: October 1, 1989
Last modified: December 2, 2020
This is version 223 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>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.

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, 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. SIMILARITY comments
    Index of protein domains and families
  5. Peptidase families
    Classification of peptidase families and list of entries
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