Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 114 (02 Dec 2020)
Sequence version 2 (23 Jan 2007)
Previous versions | rss
Add a publicationFeedback
Protein

Acyl-CoA thioesterase 2

Gene

tesB

Organism
Escherichia coli (strain K12)
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

Thioesterase that has relatively broad substrate specificity, hydrolyzing primarily medium- and long-chain acyl-CoA substrates to free fatty acids and CoA (PubMed:1645722, PubMed:24271180, PubMed:20547355). Functions in the thioesterase-dependent pathway of beta-oxidation of oleate and conjugated linoleate ((9Z,11E)-octadecadienoate or CLA), which provides all energy and carbon precursors required for the growth of E.coli. Thus, supports growth on oleate or conjugated linoleate as the sole source of carbon by hydrolyzing 3,5-tetradecadienoyl-CoA, the terminal metabolite of oleate beta-oxidation via the alternative thioesterase-dependent pathway, and 3,5-dodecadienoyl-CoA, the end product of CLA beta-oxidation, respectively (PubMed:18702504, PubMed:14707139). Seems to be involved in 3-hydroxyalkanoate production in E.coli (PubMed:20547355).5 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

<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 iodoacetamide and diethylpyrocarbonate in vitro, but is insensitive to iodoacetate treatment.1 Publication

<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 83 sec(-1) with decanoyl-CoA as substrate.1 Publication
  1. KM=13 µM for decanoyl-CoA1 Publication
  2. KM=9 µM for dodecanoyl-CoA1 Publication
  3. KM=6 µM for 3,5-dodecadienoyl-CoA1 Publication
  4. KM=13 µM for tetradecanoyl-CoA1 Publication
  5. KM=7 µM for 3,5-tetradecadienoyl-CoA1 Publication
  6. KM=75 µM for butanoyl-CoA1 Publication
  7. KM=60 µM for (2E)-butenoyl-CoA1 Publication
  8. KM=81 µM for (RS)-3-hydroxybutanoyl-CoA1 Publication
  9. KM=46 µM for 3-oxobutanoyl-CoA1 Publication
  10. KM=23 µM for dodecanoyl-CoA1 Publication
  11. KM=12 µM for (2E)-dodecenoyl-CoA1 Publication
  12. KM=6.3 µM for 3-hydroxydodecanoyl-CoA1 Publication
  13. KM=3.2 µM for 3-oxododecanoyl-CoA1 Publication
  1. Vmax=58 µmol/min/mg enzyme with butanoyl-CoA as substrate1 Publication
  2. Vmax=1.9 µmol/min/mg enzyme with (2E)-butenoyl-CoA as substrate1 Publication
  3. Vmax=34 µmol/min/mg enzyme with (RS)-3-hydroxybutanoyl-CoA as substrate1 Publication
  4. Vmax=21 µmol/min/mg enzyme with 3-oxobutanoyl-CoA as substrate1 Publication
  5. Vmax=234 µmol/min/mg enzyme with dodecanoyl-CoA as substrate1 Publication
  6. Vmax=36 µmol/min/mg enzyme with (2E)-dodecenoyl-CoA as substrate1 Publication
  7. Vmax=29 µmol/min/mg enzyme with 3-hydroxydodecanoyl-CoA as substrate1 Publication
  8. Vmax=77 µmol/min/mg enzyme with 3-oxododecanoyl-CoA as substrate1 Publication

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 sitei204Charge relay system1 Publication1
Active sitei228Charge relay system1 Publication1
Active sitei278Charge 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

  • acyl-CoA metabolic process Source: GO_Central
  • fatty acid catabolic process Source: EcoCyc

<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
Biological processLipid metabolism

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
EcoCyc:THIOESTERII-MONOMER
MetaCyc:THIOESTERII-MONOMER

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
3.1.2.2, 2026
3.1.2.20, 2026

Chemistry databases

SwissLipids knowledge resource for lipid biology

More...
SwissLipidsi
SLP:000001819

<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:
Acyl-CoA thioesterase 2 (EC:3.1.2.206 Publications)
Alternative name(s):
Thioesterase II1 Publication
Short name:
TEII1 Publication
<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:tesB1 Publication
Ordered Locus Names:b0452, JW0442
<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>OrganismiEscherichia coli (strain K12)
<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 identifieri83333 [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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
<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
  • UP000000318 <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
  • UP000000625 Componenti: Chromosome

<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

GO - Cellular componenti

<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

Has been used in the engineered enzymatic high-level production of enantiomerically pure (R)- and (S)-3-hydroxybutanoate, used as a building block for the synthesis of optically active fine chemicals, such as vitamins, antibiotics, pheromones, and flavor compounds. Chemical synthesis of chiral 3-hydroxybutanoate (3HB) is not economically feasible.2 Publications

<p>This subsection of the 'Pathology and Biotech' section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Deletion of this gene decreases the growth rate of cells on conjugated linoleate but not on palmitate (PubMed:18702504). Deletion of this gene also decreases 3-hydroxybutanoate, 3-hydroxyhexanoate, 3-hydroxyoctanoate, and hexanoate in medium after cultivation with oleate as a sole carbon source (PubMed:20547355).2 Publications

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>Mutagenesisi107S → C: 2-fold reduction in catalytic activity. 1 Publication1
Mutagenesisi204D → N or A: 1000-fold reduction in catalytic activity. No significant change in substrate affinity. 1 Publication1
Mutagenesisi279E → Q: 4-fold reduction in catalytic activity. 1 Publication1

Chemistry databases

Drug and drug target database

More...
DrugBanki
DB04147, Dodecyldimethylamine N-oxide

<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 indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved1 Publication
<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_00002021442 – 286Acyl-CoA thioesterase 2Add BLAST285

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
P0AGG2

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

More...
PaxDbi
P0AGG2

PRoteomics IDEntifications database

More...
PRIDEi
P0AGG2

<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

Homotetramer.

1 Publication

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
4259857, 17 interactors

Database of interacting proteins

More...
DIPi
DIP-10980N

Protein interaction database and analysis system

More...
IntActi
P0AGG2, 5 interactors

STRING: functional protein association networks

More...
STRINGi
511145.b0452

<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

1286
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
P0AGG2

Database of comparative protein structure models

More...
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
P0AGG2

<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 C/M/P thioester hydrolase family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
COG1946, Bacteria

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_032690_0_0_6

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P0AGG2

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P0AGG2

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR003703, Acyl_CoA_thio
IPR029069, HotDog_dom_sf

The PANTHER Classification System

More...
PANTHERi
PTHR11066, PTHR11066, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF54637, SSF54637, 2 hits

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR00189, tesB, 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.

P0AGG2-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSQALKNLLT LLNLEKIEEG LFRGQSEDLG LRQVFGGQVV GQALYAAKET
60 70 80 90 100
VPEERLVHSF HSYFLRPGDS KKPIIYDVET LRDGNSFSAR RVAAIQNGKP
110 120 130 140 150
IFYMTASFQA PEAGFEHQKT MPSAPAPDGL PSETQIAQSL AHLLPPVLKD
160 170 180 190 200
KFICDRPLEV RPVEFHNPLK GHVAEPHRQV WIRANGSVPD DLRVHQYLLG
210 220 230 240 250
YASDLNFLPV ALQPHGIGFL EPGIQIATID HSMWFHRPFN LNEWLLYSVE
260 270 280
STSASSARGF VRGEFYTQDG VLVASTVQEG VMRNHN
Length:286
Mass (Da):31,966
Last modified:January 23, 2007 - 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:i8E7C4A4BCF73CA4B
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
M63308 Genomic DNA Translation: AAA24665.1
U82664 Genomic DNA Translation: AAB40208.1
U00096 Genomic DNA Translation: AAC73555.1
AP009048 Genomic DNA Translation: BAE76232.1

Protein sequence database of the Protein Information Resource

More...
PIRi
D64775

NCBI Reference Sequences

More...
RefSeqi
NP_414986.1, NC_000913.3
WP_000075876.1, NZ_STEB01000007.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAC73555; AAC73555; b0452
BAE76232; BAE76232; BAE76232

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
945074

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ecj:JW0442
eco:b0452

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|1411691.4.peg.1823

<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
M63308 Genomic DNA Translation: AAA24665.1
U82664 Genomic DNA Translation: AAB40208.1
U00096 Genomic DNA Translation: AAC73555.1
AP009048 Genomic DNA Translation: BAE76232.1
PIRiD64775
RefSeqiNP_414986.1, NC_000913.3
WP_000075876.1, NZ_STEB01000007.1

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
1C8UX-ray1.90A/B2-286[»]
SMRiP0AGG2
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi4259857, 17 interactors
DIPiDIP-10980N
IntActiP0AGG2, 5 interactors
STRINGi511145.b0452

Chemistry databases

DrugBankiDB04147, Dodecyldimethylamine N-oxide
SwissLipidsiSLP:000001819

Proteomic databases

jPOSTiP0AGG2
PaxDbiP0AGG2
PRIDEiP0AGG2

Genome annotation databases

EnsemblBacteriaiAAC73555; AAC73555; b0452
BAE76232; BAE76232; BAE76232
GeneIDi945074
KEGGiecj:JW0442
eco:b0452
PATRICifig|1411691.4.peg.1823

Organism-specific databases

EchoBASE - an integrated post-genomic database for E. coli

More...
EchoBASEi
EB0988

Phylogenomic databases

eggNOGiCOG1946, Bacteria
HOGENOMiCLU_032690_0_0_6
InParanoidiP0AGG2
PhylomeDBiP0AGG2

Enzyme and pathway databases

BioCyciEcoCyc:THIOESTERII-MONOMER
MetaCyc:THIOESTERII-MONOMER
BRENDAi3.1.2.2, 2026
3.1.2.20, 2026

Miscellaneous databases

EvolutionaryTraceiP0AGG2

Protein Ontology

More...
PROi
PR:P0AGG2

Family and domain databases

InterProiView protein in InterPro
IPR003703, Acyl_CoA_thio
IPR029069, HotDog_dom_sf
PANTHERiPTHR11066, PTHR11066, 1 hit
SUPFAMiSSF54637, SSF54637, 2 hits
TIGRFAMsiTIGR00189, tesB, 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 nameiTESB_ECOLI
<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: P0AGG2
Secondary accession number(s): P23911, Q2MBX4
<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: December 20, 2005
Last sequence update: January 23, 2007
Last modified: December 2, 2020
This is version 114 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 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, Direct protein sequencing, 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
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