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Entry version 121 (02 Dec 2020)
Sequence version 1 (01 Mar 2001)
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Protein

Procathepsin L

Gene

CTSL

Organism
Canis lupus familiaris (Dog) (Canis familiaris)
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 transcript 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 (By similarity). 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. 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 (By similarity). 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 similarity

<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.By similarity 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 (By similarity). 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. Inhibited by amantadine (By similarity).By similarity

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 sitei138By similarity1
Active sitei277By similarity1
Active sitei300By similarity1

<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

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-CFA-1442490, Collagen degradation
R-CFA-1474228, Degradation of the extracellular matrix
R-CFA-1592389, Activation of Matrix Metalloproteinases
R-CFA-1679131, Trafficking and processing of endosomal TLR
R-CFA-2022090, Assembly of collagen fibrils and other multimeric structures
R-CFA-2132295, MHC class II antigen presentation
R-CFA-8939242, RUNX1 regulates transcription of genes involved in differentiation of keratinocytes

Protein family/group databases

MEROPS protease database

More...
MEROPSi
C01.032

<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 L (EC:3.4.22.15)
Alternative name(s):
Cathepsin L1
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:CTSL
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>OrganismiCanis lupus familiaris (Dog) (Canis familiaris)
<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 identifieri9615 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraCaniformiaCanidaeCanis
<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
  • UP000002254 <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> Componentsi: Chromosome 1, Chromosome X

<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

Keywords - Cellular componenti

Cell membrane, Cytoplasmic vesicle, Lysosome, Membrane, Secreted

<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_000002624018 – 117Activation peptideBy similarityAdd BLAST100
<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_0000450785118 – 333Cathepsin LBy similarityAdd BLAST216
ChainiPRO_0000026241118 – 289Cathepsin L heavy chainAdd BLAST172
PropeptideiPRO_0000026242290 – 291By similarity2
ChainiPRO_0000026243292 – 333Cathepsin L light chainAdd 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 ↔ 178By similarity
Disulfide bondi169 ↔ 212By similarity
<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>Glycosylationi222N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi270 ↔ 322Interchain (between heavy and light chains)By similarity

<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 (By similarity).By similarity

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 autolysisBy similarity2
Sitei107 – 108Cleavage; by autolysisBy similarity2
Sitei112 – 113Cleavage; by autolysisBy similarity2
Sitei113 – 114Cleavage; by autolysisBy similarity2

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

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

More...
PaxDbi
Q9GL24

PRoteomics IDEntifications database

More...
PRIDEi
Q9GL24

<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
ENSCAFG00000001149, Expressed in thymus and 50 other tissues

<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

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
9612.ENSCAFP00000040898

<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

3D structure databases

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

More...
SMRi
Q9GL24

Database of comparative protein structure models

More...
ModBasei
Search...

<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

More...
eggNOGi
KOG1543, Eukaryota

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000154367

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_012184_1_2_1

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q9GL24

Identification of Orthologs from Complete Genome Data

More...
OMAi
CSHPQGN

Database of Orthologous Groups

More...
OrthoDBi
1275401at2759

TreeFam database of animal gene trees

More...
TreeFami
TF313739

Family and domain databases

Conserved Domains Database

More...
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>Sequencei

<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.

Q9GL24-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MNPSLFLTAL CLGIASAAPK FDQSLNAQWY QWKATHRRLY GMNEEGWRRA
60 70 80 90 100
VWEKNMKMIE LHNREYSQGK HGFTMAMNAF GDMTNEEFRQ VMNGFQNQKH
110 120 130 140 150
KKGKMFQEPL FAEIPKSVDW REKGYVTPVK NQGQCGSCWA FSATGALEGQ
160 170 180 190 200
MFRKTGKLVS LSEQNLVDCS RAQGNEGCNG GLMDNAFRYV KDNGGLDSEE
210 220 230 240 250
SYPYLGRDTE TCNYKPECSA ANDTGFVDLP QREKALMKAV ATLGPISVAI
260 270 280 290 300
DAGHQSFQFY KSGIYFDPDC SSKDLDHGVL VVGYGFEGTD SNNKFWIVKN
310 320 330
SWGPEWGWNG YVKMAKDQNN HCGIATAASY PTV
Length:333
Mass (Da):37,383
Last modified:March 1, 2001 - v1
<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:i033096E72B791D1F
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
AJ279008 mRNA Translation: CAC08809.1

NCBI Reference Sequences

More...
RefSeqi
XP_005615836.1, XM_005615779.1
XP_005615837.1, XM_005615780.1
XP_005615838.1, XM_005615781.1

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSCAFT00000001770; ENSCAFP00000001630; ENSCAFG00000001149
ENSCAFT00000023837; ENSCAFP00000040898; ENSCAFG00000015024
ENSCAFT00030008770; ENSCAFP00030007712; ENSCAFG00030004769
ENSCAFT00030025598; ENSCAFP00030022351; ENSCAFG00030013828
ENSCAFT00040006653; ENSCAFP00040005759; ENSCAFG00040003499
ENSCAFT00040033001; ENSCAFP00040028714; ENSCAFG00040017888

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
102156614

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
cfa:102156614

<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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ279008 mRNA Translation: CAC08809.1
RefSeqiXP_005615836.1, XM_005615779.1
XP_005615837.1, XM_005615780.1
XP_005615838.1, XM_005615781.1

3D structure databases

SMRiQ9GL24
ModBaseiSearch...

Protein-protein interaction databases

STRINGi9612.ENSCAFP00000040898

Protein family/group databases

MEROPSiC01.032

Proteomic databases

PaxDbiQ9GL24
PRIDEiQ9GL24

Genome annotation databases

EnsembliENSCAFT00000001770; ENSCAFP00000001630; ENSCAFG00000001149
ENSCAFT00000023837; ENSCAFP00000040898; ENSCAFG00000015024
ENSCAFT00030008770; ENSCAFP00030007712; ENSCAFG00030004769
ENSCAFT00030025598; ENSCAFP00030022351; ENSCAFG00030013828
ENSCAFT00040006653; ENSCAFP00040005759; ENSCAFG00040003499
ENSCAFT00040033001; ENSCAFP00040028714; ENSCAFG00040017888
GeneIDi102156614
KEGGicfa:102156614

Phylogenomic databases

eggNOGiKOG1543, Eukaryota
GeneTreeiENSGT00940000154367
HOGENOMiCLU_012184_1_2_1
InParanoidiQ9GL24
OMAiCSHPQGN
OrthoDBi1275401at2759
TreeFamiTF313739

Enzyme and pathway databases

ReactomeiR-CFA-1442490, Collagen degradation
R-CFA-1474228, Degradation of the extracellular matrix
R-CFA-1592389, Activation of Matrix Metalloproteinases
R-CFA-1679131, Trafficking and processing of endosomal TLR
R-CFA-2022090, Assembly of collagen fibrils and other multimeric structures
R-CFA-2132295, MHC class II antigen presentation
R-CFA-8939242, RUNX1 regulates transcription of genes involved in differentiation of keratinocytes

Gene expression databases

BgeeiENSCAFG00000001149, Expressed in thymus and 50 other tissues

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

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
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_CANLF
<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: Q9GL24
<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 26, 2005
Last sequence update: March 1, 2001
Last modified: December 2, 2020
This is version 121 of the entry and version 1 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

<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

Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families
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