Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Due to a server migration, the UniProt 'ID mapping', 'Peptide search' and 'community bibliography submission' tools will not be available on the 19th April 2021 during the morning (EST).

UniProtKB - Q585F3 (MCA2_TRYB2)

Entry version 94 (07 Apr 2021)
Sequence version 1 (10 May 2005)
Previous versions | rss
Add a publicationFeedback
Protein

Metacaspase-2

Gene

MCA2

Organism
Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
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

Cysteine protease that cleaves specifically after arginine or lysine residues.2 Publications

<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

Activated by Ca2+ (PubMed:18005666, PubMed:23506317, PubMed:28089596, PubMed:22529389). In response to calcium binding, the 280-loop, a disordered loop consisting of residues 269-275, undergoes a conformational change which stabilizes substrates in the active site (PubMed:22529389). The binding to the substrate triggers the release of the N-terminal region resulting in the activation of the enzyme (PubMed:22529389). Proteolytic cleavage is required for catalytic activity towards large protein substrates (PubMed:28089596).4 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 7.7.2 Publications

Temperature dependencei

Optimum temperature is 20-25 degrees Celsius.1 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>Sitei95Important for Arg/Lys-specific substrate specificity1 Publication1
<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 sitei158By similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi173CalciumCombined sources1 Publication1
Metal bindingi189CalciumCombined sources1 Publication1
Metal bindingi190CalciumCombined sources1 Publication1
Sitei211Important for Arg/Lys-specific substrate specificity1 Publication1
Active sitei2131 Publication1
Metal bindingi220CalciumCombined sources1 Publication1

<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

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<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
LigandCalcium, Metal-binding

Protein family/group databases

MEROPS protease database

More...MEROPSi		C14.044

<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:
Metacaspase-2Curated (EC:3.4.22.-4 Publications)
Alternative name(s):
TbMCA21 Publication
Cleaved into the following 2 chains:
Large subunit p20Curated
Small subunit p10Curated
<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:MCA21 Publication
ORF Names:Tb927.6.940Imported
<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>OrganismiTrypanosoma brucei brucei (strain 927/4 GUTat10.1)Imported
<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 identifieri185431 [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 lineageiEukaryota › Discoba › Euglenozoa › Kinetoplastea › Metakinetoplastina › Trypanosomatida › Trypanosomatidae › Trypanosoma ›
<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
  • UP000008524 <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 6

Organism-specific databases

Eukaryotic Pathogen, Vector and Host Database Resources

More...VEuPathDBi		TriTrypDB:Tb927.6.940

<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

Endosome

<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>Mutagenesisi31Y → A: Increases autoprocessing resulting in the degradation of the enzyme. 1 Publication1
Mutagenesisi55K → G: Loss of autoprocessing. Loss of catalytic activity towards large protein substrates, no effect on catalytic activity towards short oligopeptide substrates, reduces affinity of the high affinity Ca(2+) binding site, shifts optimum pH for activity towards basic pH; when associated with G-268. 2 Publications1
Mutagenesisi92C → A: Reduced autoprocessing and 50% loss of catalytic activity towards substrates. 1 Publication1
Mutagenesisi95D → A: Loss of autoprocessing and catalytic activity towards substrates. 1 Publication1
Mutagenesisi156S → A: 3-fold increase in catalytic activity towards substrates. 1 Publication1
Mutagenesisi189 – 190DD → AA: Loss of autoprocessing and catalytic activity towards substrates. 1 Publication2
Mutagenesisi211D → A: Loss of autoprocessing and catalytic activity towards substrates. 1 Publication1
Mutagenesisi212C → G: Severe loss of catalytic activity. 1 Publication1
Mutagenesisi213C → G: Complete loss of catalytic activity. 1 Publication1
Mutagenesisi268K → G: Loss of autoprocessing. Loss of catalytic activity towards large protein substrates, no effect on catalytic activity towards short oligopeptide substrates, reduces affinity of the high affinity Ca(2+) binding site, shift optimum pH for activity towards basic pH; when associated with G-55. 2 Publications1

<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 <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_00004512731 – 551 PublicationAdd BLAST55
<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_000045127456 – 347Metacaspase-2Add BLAST292
ChainiPRO_000045127556 – 268Large subunit p201 PublicationAdd BLAST213
ChainiPRO_0000451276269 – 347Small subunit p101 PublicationAdd BLAST79

<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

Auto-proteolytic cleavage of the propeptide after Lys-55 and between the large and small subunits after Lys-268 is required for catalytic activity towards large protein substrates but is dispensable towards small oligopeptide substrates (PubMed:18005666, PubMed:28089596, PubMed:22529389). After processing, the propeptide and the large and small subunits remain associated by non-covalent bonds (PubMed:18005666). In vivo, the unprocessed enzyme appears to be the predominant form (By similarity).By similarity3 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei55 – 56Cleavage; by autolysis1 Publication2
Sitei268Cleavage; by autolysis1 Publication1

Keywords - PTMi

Autocatalytic cleavage, Zymogen

<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

Monomer.

1 Publication

Protein-protein interaction databases

STRING: functional protein association networks

More...STRINGi		5691.AAZ11657

<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

1347
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

More...SMRi		Q585F3

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		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

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni1 – 70Regulates substrate access to the active site1 PublicationAdd BLAST70

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

There are 2 calcium binding sites with high and low affinity, respectively.1 Publication

<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 C14B family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG1546, Eukaryota

Identification of Orthologs from Complete Genome Data

More...OMAi		WAFISAI

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR029030, Caspase-like_dom_sf

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF52129, SSF52129, 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.

Q585F3-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MCSLITQLCD AGQLADYVGL GWLNAVSSQP YLVQALGLQP PPRRVDVDAA 
        60         70         80         90        100
FRDAKGLHGH QPWVATPLPG QTVRALFIGI NYYGTSAALS GCCNDVKQML 
       110        120        130        140        150
ATLQKKGLPI NEAVILVDED NFPGRTDQPT RDNIVRYMAW LVKDAKPGDV 
       160        170        180        190        200
LFFHYSGHGT QCKSRGDSDE KYDQCIAPVD FQKSGCIVDD DIHKLLFSRL 
       210        220        230        240        250
PEKVRLTAVF DCCHSGSIMD LPFTYVCSGG EQASGTPHMK RIREGNDVLG 
       260        270        280        290        300
DVMMISGCAD EQTSADVKNT ATFGTGSTGA GGAATQCITC MLMNNQSLSY 
       310        320        330        340 
GKLLIETRDM LKRKGFKQVP QLSASKAIDL DQTFSLTEMF SVDRSIQ
Length:347
Mass (Da):37,779
Last modified:May 10, 2005 - 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:i00523E8CCF7B214A
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
CP000069 Genomic DNA Translation: AAZ11657.1
AC073906 Genomic DNA Translation: AAX80349.1

NCBI Reference Sequences

More...RefSeqi		XP_845216.1, XM_840123.1

Genome annotation databases

GeneDB pathogen genome database from Sanger Institute

More...GeneDBi		Tb927.6.940:pep

Database of genes from NCBI RefSeq genomes

More...GeneIDi		3657732

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		tbr:Tb927.6.940

<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
CP000069 Genomic DNA Translation: AAZ11657.1
AC073906 Genomic DNA Translation: AAX80349.1
RefSeqiXP_845216.1, XM_840123.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4AF8X-ray1.40A1-347[»]
4AFPX-ray2.10A1-347[»]
4AFRX-ray1.60A1-347[»]
4AFVX-ray1.50A1-347[»]
SMRiQ585F3
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

STRINGi5691.AAZ11657

Protein family/group databases

MEROPSiC14.044

Genome annotation databases

GeneDBiTb927.6.940:pep
GeneIDi3657732
KEGGitbr:Tb927.6.940

Organism-specific databases

VEuPathDBiTriTrypDB:Tb927.6.940

Phylogenomic databases

eggNOGiKOG1546, Eukaryota
OMAiWAFISAI

Family and domain databases

InterProiView protein in InterPro
IPR029030, Caspase-like_dom_sf
SUPFAMiSSF52129, SSF52129, 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 nameiMCA2_TRYB2
<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: Q585F3
Secondary accession number(s): D6XHH8
<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: October 7, 2020
Last sequence update: May 10, 2005
Last modified: April 7, 2021
This is version 94 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)

<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, Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again