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Entry version 104 (07 Apr 2021)
Sequence version 1 (01 Jun 2002)
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Protein

L-asparaginase

Gene

PF2047

Organism
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
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

Catalyzes the hydrolysis of L-asparagine into L-aspartate and ammonia. Displays no glutaminase activity, a highly desirable therapeutic property.2 Publications

Miscellaneous

Microbial L-asparaginase is considered as an important biopharmaceutical drug enzyme in the treatment of childhood acute lymphoblastic leukemia (ALL). It functions by reducing the availability of circulatory L-asparagine to tumor cells. The principle behind the cytotoxic effect of L-asparaginase stems from the fact that the leukemic lymphoblastic tumor cells and other blood tumor cells are auxotrophs towards the L-asparagine and exhibit low L-asparagine synthetase (ASNS) activity for de novo synthesis of L-asparagine. Therefore, these tumor cells are required for exogenous supply of L-asparagine for proliferation and survival. L-Asparaginase has also been used for making a diagnostic biosensor as the amount of ammonia produced by the action of the enzyme directly correlates to the level of L-asparagine in a patient's blood (Probable). P.furiosus L-asparaginase and its mutants show significant killing of cultured human leukemic cell lines HL60, MCF7, and K562 (PubMed:22166247).Curated1 Publication

<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

<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>Kineticsi

kcat is 870 sec(-1) (at pH 9.0 and 80 degrees Celsius) (PubMed:20370616). kcat is 888.6 sec(-1) (at pH 8.2 and 80 degrees Celsius) (PubMed:22166247). kcat is 17.98 sec(-1) (at pH 7.4 and 37 degrees Celsius) (PubMed:22166247).2 Publications
  1. KM=12 mM for L-asparagine (at pH 9.0 and 80 degrees Celsius)1 Publication
  2. KM=12.1 mM for L-asparagine (at pH 8.2 and 80 degrees Celsius)1 Publication
  3. KM=8.12 mM for L-asparagine (at pH 7.4 and 37 degrees Celsius)1 Publication

    pH dependencei

    Optimum pH is 9.0.1 Publication

    Temperature dependencei

    Optimum temperature is around 90 degrees Celsius (PubMed:20370616). Thermostable (PubMed:20370616, PubMed:25862541). The extreme thermal stability of this enzyme is due to the presence of high intersubunit associative forces supported by extensive H-bonding and ionic interactions network (PubMed:25862541).2 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 sitei11Nucleophile; O-isoaspartyl threonine intermediate1 Publication1
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei11L-aspartateCombined sources1 Publication1
    Active sitei83Charge relay system1 Publication1
    Active sitei84Charge relay system1 Publication1
    Binding sitei109L-aspartate; via carbonyl oxygenCombined sources1
    Active sitei154Charge relay system1 Publication1
    Active sitei273Charge relay system1 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

    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

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    PFUR186497:G1FZR-2113-MONOMER

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    3.5.1.1, 5243

    <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:
    L-asparaginase1 Publication (EC:3.5.1.12 Publications)
    <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
    Ordered Locus Names:PF2047Imported
    <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>OrganismiPyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
    <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 identifieri186497 [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 lineageiArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaePyrococcus
    <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
    • UP000001013 <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

    <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

    <p>This subsection of the 'Pathology and Biotech' section describes the use of a specific protein in the biotechnological industry.<p><a href='/help/biotechnological_use' target='_top'>More...</a></p>Biotechnological usei

    Absence of glutaminase activity, higher stability, and mesoactivity makes P.furiosus L-asparaginase and its mutants promising candidates for clinical as well as industrial usage.1 Publication

    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>Mutagenesisi53T → Q: Shows improved enzymatic properties at physiological conditions (pH 7.4 and 37 degrees Celsius) as compared to the wild type with a 2-fold increase in catalytic efficiency. Shows higher and significant killing of human leukemic and breast carcinoma cell lines as compared to the E.coli L-asparaginase. 1 Publication1
    Mutagenesisi273Y → A: 95% reduction in activity compared to wild type. 1 Publication1
    Mutagenesisi274K → E: Shows improved enzymatic properties at physiological conditions (pH 7.4 and 37 degrees Celsius) as compared to the wild type with a 2.6-fold increase in catalytic efficiency. Shows higher and significant killing of human leukemic and breast carcinoma cell lines as compared to the E.coli L-asparaginase. 1 Publication1

    <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 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_00004517481 – 326L-asparaginaseAdd BLAST326

    <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

    Homodimer.

    2 Publications

    Protein-protein interaction databases

    STRING: functional protein association networks

    More...
    STRINGi
    186497.PF2047

    <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
    Q8TZE8

    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

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini1 – 319Asparaginase/glutaminasePROSITE-ProRule annotationAdd BLAST319

    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>Regioni51 – 52L-aspartate bindingCombined sources1 Publication2
    Regioni83 – 84L-aspartate bindingCombined sources1 Publication2

    <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

    Consists of distinct N- and C-terminal domains (NPfA and CPfA, respectively), connected by a linker. NPfA acts as specific internal chaperone by mediating folding of its own C-domain (CPfA), but also functions as a non-specific molecular chaperone by preventing aggregation of unrelated proteins (PubMed:23551356, PubMed:25862541). The linker is dispensable since domains of this enzyme can assemble without the linker into a conjoined tetrameric form that exhibits higher activity than the parent enzyme, while each domain is inactive independently. The structural integrity of the conjoined enzyme is maintained through domain-domain interactions rather than the covalent linker (PubMed:25478837).3 Publications

    <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 asparaginase 1 family.Curated

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    arCOG01924, Archaea

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    CLU_019134_2_3_2

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    YFEYKLY

    Database of Orthologous Groups

    More...
    OrthoDBi
    69694at2157

    Family and domain databases

    Conserved Domains Database

    More...
    CDDi
    cd08963, L-asparaginase_I, 1 hit

    Gene3D Structural and Functional Annotation of Protein Families

    More...
    Gene3Di
    3.40.50.1170, 1 hit
    3.40.50.40, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR006033, AsnA_fam
    IPR036152, Asp/glu_Ase-like_sf
    IPR006034, Asparaginase/glutaminase-like
    IPR027475, Asparaginase/glutaminase_AS2
    IPR040919, Asparaginase_C
    IPR027473, L-asparaginase_C
    IPR041725, L-asparaginase_I
    IPR027474, L-asparaginase_N
    IPR037152, L-asparaginase_N_sf

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF00710, Asparaginase, 1 hit
    PF17763, Asparaginase_C, 1 hit

    PIRSF; a whole-protein classification database

    More...
    PIRSFi
    PIRSF001220, L-ASNase_gatD, 1 hit

    Protein Motif fingerprint database; a protein domain database

    More...
    PRINTSi
    PR00139, ASNGLNASE

    Simple Modular Architecture Research Tool; a protein domain database

    More...
    SMARTi
    View protein in SMART
    SM00870, Asparaginase, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF53774, SSF53774, 1 hit

    TIGRFAMs; a protein family database

    More...
    TIGRFAMsi
    TIGR00519, asnASE_I, 1 hit

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS00917, ASN_GLN_ASE_2, 1 hit
    PS51732, ASN_GLN_ASE_3, 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.

    Q8TZE8-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MKILLIGMGG TIASVKGENG YEASLSVKEV LDIAGIKDCE DCDFLDLKNV
    60 70 80 90 100
    DSTLIQPEDW VDLAETLYKN VKKYDGIIVT HGTDTLAYTS SMISFMLRNP
    110 120 130 140 150
    PIPIVFTGSM IPATEENSDA PLNLQTAIKF ATSGIRGVYV AFNGKVMLGV
    160 170 180 190 200
    RTSKVRTMSR DAFESINYPI IAELRGEDLV VNFIPKFNNG EVTLDLRHDP
    210 220 230 240 250
    KVLVIKLIPG LSGDIFRAAV ELGYRGIVIE GYGAGGIPYR GSDLLQTIEE
    260 270 280 290 300
    LSKEIPIVMT TQAMYDGVDL TRYKVGRLAL RAGVIPAGDM TKEATVTKLM
    310 320
    WILGHTNNVE EIKVLMRKNL VGELRD
    Length:326
    Mass (Da):35,765
    Last modified:June 1, 2002 - 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:i8A9DB1F01F52CA0C
    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
    AE009950 Genomic DNA Translation: AAL82171.1

    NCBI Reference Sequences

    More...
    RefSeqi
    WP_011013191.1, NZ_CP023154.1

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...
    EnsemblBacteriai
    AAL82171; AAL82171; PF2047

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    41713869

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    pfu:PF2047

    Pathosystems Resource Integration Center (PATRIC)

    More...
    PATRICi
    fig|186497.12.peg.2124

    <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
    AE009950 Genomic DNA Translation: AAL82171.1
    RefSeqiWP_011013191.1, NZ_CP023154.1

    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
    4NJEX-ray2.50A1-182[»]
    B202-326[»]
    4Q0MX-ray2.23A1-326[»]
    4RA6X-ray2.50A/P1-182[»]
    B/Q202-326[»]
    4RA9X-ray2.05A1-182[»]
    B202-326[»]
    5B5UX-ray2.61A1-178[»]
    B202-326[»]
    5B74X-ray2.04A1-182[»]
    B202-326[»]
    5CBPX-ray2.36A1-182[»]
    B202-326[»]
    SMRiQ8TZE8
    ModBaseiSearch...
    PDBe-KBiSearch...

    Protein-protein interaction databases

    STRINGi186497.PF2047

    Genome annotation databases

    EnsemblBacteriaiAAL82171; AAL82171; PF2047
    GeneIDi41713869
    KEGGipfu:PF2047
    PATRICifig|186497.12.peg.2124

    Phylogenomic databases

    eggNOGiarCOG01924, Archaea
    HOGENOMiCLU_019134_2_3_2
    OMAiYFEYKLY
    OrthoDBi69694at2157

    Enzyme and pathway databases

    BioCyciPFUR186497:G1FZR-2113-MONOMER
    BRENDAi3.5.1.1, 5243

    Family and domain databases

    CDDicd08963, L-asparaginase_I, 1 hit
    Gene3Di3.40.50.1170, 1 hit
    3.40.50.40, 1 hit
    InterProiView protein in InterPro
    IPR006033, AsnA_fam
    IPR036152, Asp/glu_Ase-like_sf
    IPR006034, Asparaginase/glutaminase-like
    IPR027475, Asparaginase/glutaminase_AS2
    IPR040919, Asparaginase_C
    IPR027473, L-asparaginase_C
    IPR041725, L-asparaginase_I
    IPR027474, L-asparaginase_N
    IPR037152, L-asparaginase_N_sf
    PfamiView protein in Pfam
    PF00710, Asparaginase, 1 hit
    PF17763, Asparaginase_C, 1 hit
    PIRSFiPIRSF001220, L-ASNase_gatD, 1 hit
    PRINTSiPR00139, ASNGLNASE
    SMARTiView protein in SMART
    SM00870, Asparaginase, 1 hit
    SUPFAMiSSF53774, SSF53774, 1 hit
    TIGRFAMsiTIGR00519, asnASE_I, 1 hit
    PROSITEiView protein in PROSITE
    PS00917, ASN_GLN_ASE_2, 1 hit
    PS51732, ASN_GLN_ASE_3, 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 nameiASPG_PYRFU
    <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: Q8TZE8
    <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: February 10, 2021
    Last sequence update: June 1, 2002
    Last modified: April 7, 2021
    This is version 104 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 programProkaryotic 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

    3D-structure, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families
    UniProt is an ELIXIR core data resource
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