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Entry version 168 (31 Jul 2019)
Sequence version 2 (01 Jun 1994)
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Protein

Acetylcholinesterase

Gene

ache

Organism
Tetronarce californica (Pacific electric ray) (Torpedo californica)
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

Terminates signal transduction at the neuromuscular junction by rapid hydrolysis of the acetylcholine released into the synaptic cleft. May be involved in cell-cell interactions.

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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_section">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 substrate concentrations above 0.5 mM.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 sitei221Acyl-ester intermediate1
Active sitei348Charge relay system1
Active sitei461Charge relay system1

<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, Serine esterase
Biological processNeurotransmitter degradation

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
MetaCyc:MONOMER-16823

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
3.1.1.7 6395

Protein family/group databases

ESTHER database of the Alpha/Beta-hydrolase fold superfamily of proteins

More...
ESTHERi
torca-ACHE AChE

MEROPS protease database

More...
MEROPSi
S09.980

<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_and_taxonomy_section">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:
Acetylcholinesterase (EC:3.1.1.7)
Short name:
AChE
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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:ache
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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>OrganismiTetronarce californica (Pacific electric ray) (Torpedo californica)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 identifieri7787 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 lineageiEukaryotaMetazoaChordataCraniataVertebrataChondrichthyesElasmobranchiiBatoideaTorpediniformesTorpedinidaeTetronarce

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell junction, Cell membrane, Membrane, Synapse

<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_and_biotech_section">'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>Mutagenesisi220E → H: Loss of activity. 1 Publication1
Mutagenesisi220E → Q or D: Decrease in activity. 1 Publication1
Mutagenesisi221S → C: Loss of activity. 1 Publication1
Mutagenesisi221S → V: Loss of activity. 1 Publication1
Mutagenesisi446H → Q: Almost no loss of activity. 1 Publication1
Mutagenesisi461H → Q: Loss of activity. 1 Publication1

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL4780

<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 – 211 PublicationAdd BLAST21
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000000859522 – 564AcetylcholinesteraseAdd BLAST543
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">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_0000008596565 – 586Removed in mature formAdd BLAST22

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">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>Glycosylationi80N-linked (GlcNAc...) asparagine2 Publications1
<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 bondi88 ↔ 115
Disulfide bondi275 ↔ 286
Disulfide bondi423 ↔ 542
Glycosylationi437N-linked (GlcNAc...) asparagine3 Publications1
Glycosylationi478N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi554N-linked (GlcNAc...) asparagine1 Publication1
Disulfide bondi558Interchain
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position(s) and the type of covalently attached lipid group(s).<p><a href='/help/lipid' target='_top'>More...</a></p>Lipidationi564GPI-anchor amidated serine1 Publication1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">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

An interchain disulfide bond is present in what becomes position 593 of the T isoform.

Keywords - PTMi

Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P04058

<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

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Found in the synapses and to a lower extent in extrajunctional areas of muscle and nerve, and on erythrocyte membranes.

<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_section">'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_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Isoform H form is a homodimer; the asymmetric form is a disulfide-bonded oligomer composed of a collagenic subunit (Q) and a variable number of T catalytic subunits.

11 Publications

Protein-protein interaction databases

Molecular INTeraction database

More...
MINTi
P04058

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
P04058

<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

1586
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
P04058

Database of comparative protein structure models

More...
ModBasei
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P04058

<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

Keywords - Domaini

Signal

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.40.50.1820, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR029058 AB_hydrolase
IPR000908 Acylcholinesterase_fish/snake
IPR002018 CarbesteraseB
IPR019826 Carboxylesterase_B_AS
IPR019819 Carboxylesterase_B_CS
IPR000997 Cholinesterase

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00135 COesterase, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00879 ACHEFISH
PR00878 CHOLNESTRASE

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF53474 SSF53474, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00122 CARBOXYLESTERASE_B_1, 1 hit
PS00941 CARBOXYLESTERASE_B_2, 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_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2)i

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

This entry describes 2 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket
Note: Additional isoforms seem to exist.
Isoform H (identifier: P04058-1) [UniParc]FASTAAdd to basket
Also known as: Globular

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

« Hide
        10         20         30         40         50
MNLLVTSSLG VLLHLVVLCQ ADDHSELLVN TKSGKVMGTR VPVLSSHISA
60 70 80 90 100
FLGIPFAEPP VGNMRFRRPE PKKPWSGVWN ASTYPNNCQQ YVDEQFPGFS
110 120 130 140 150
GSEMWNPNRE MSEDCLYLNI WVPSPRPKST TVMVWIYGGG FYSGSSTLDV
160 170 180 190 200
YNGKYLAYTE EVVLVSLSYR VGAFGFLALH GSQEAPGNVG LLDQRMALQW
210 220 230 240 250
VHDNIQFFGG DPKTVTIFGE SAGGASVGMH ILSPGSRDLF RRAILQSGSP
260 270 280 290 300
NCPWASVSVA EGRRRAVELG RNLNCNLNSD EELIHCLREK KPQELIDVEW
310 320 330 340 350
NVLPFDSIFR FSFVPVIDGE FFPTSLESML NSGNFKKTQI LLGVNKDEGS
360 370 380 390 400
FFLLYGAPGF SKDSESKISR EDFMSGVKLS VPHANDLGLD AVTLQYTDWM
410 420 430 440 450
DDNNGIKNRD GLDDIVGDHN VICPLMHFVN KYTKFGNGTY LYFFNHRASN
460 470 480 490 500
LVWPEWMGVI HGYEIEFVFG LPLVKELNYT AEEEALSRRI MHYWATFAKT
510 520 530 540 550
GNPNEPHSQE SKWPLFTTKE QKFIDLNTEP MKVHQRLRVQ MCVFWNQFLP
560 570 580
KLLNATACDG ELSSSGTSSS KGIIFYVLFS ILYLIF
Note: GPI-anchored form.
Length:586
Mass (Da):65,906
Last modified:June 1, 1994 - 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:i731D5F0F3ABA62A8
GO
Isoform T (identifier: P04058-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     557-586: ACDGELSSSGTSSSKGIIFYVLFSILYLIF → ETIDEAERQWKTEFHRWSSYMMHWKNQFDHYSRHESCAEL

Show »
Length:596
Mass (Da):67,818
Checksum:i36D5E9A30F9E6065
GO

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_001460557 – 586ACDGE…LYLIF → ETIDEAERQWKTEFHRWSSY MMHWKNQFDHYSRHESCAEL in isoform T. CuratedAdd BLAST30

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
X03439 mRNA Translation: CAA27169.1
X56516 Genomic DNA No translation available.
X56517 Genomic DNA No translation available.

Protein sequence database of the Protein Information Resource

More...
PIRi
A00773 ACRYE

Keywords - Coding sequence diversityi

Alternative splicing

<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
X03439 mRNA Translation: CAA27169.1
X56516 Genomic DNA No translation available.
X56517 Genomic DNA No translation available.
PIRiA00773 ACRYE

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
1ACJX-ray2.80A22-556[»]
1ACLX-ray2.80A22-556[»]
1AMNX-ray2.80A22-558[»]
1AX9X-ray2.80A22-558[»]
1CFJX-ray2.60A22-558[»]
1DX6X-ray2.30A22-564[»]
1E3QX-ray2.85A22-564[»]
1E66X-ray2.10A22-564[»]
1EA5X-ray1.80A22-558[»]
1EEAX-ray4.50A22-555[»]
1EVEX-ray2.50A22-564[»]
1FSSX-ray3.00A22-558[»]
1GPKX-ray2.10A22-558[»]
1GPNX-ray2.35A22-558[»]
1GQRX-ray2.20A25-556[»]
1GQSX-ray3.00A25-556[»]
1H22X-ray2.15A22-564[»]
1H23X-ray2.15A22-564[»]
1HBJX-ray2.50A22-564[»]
1JGAmodel-A1-586[»]
1JGBmodel-A1-586[»]
1JJBX-ray2.30A25-556[»]
1OCEX-ray2.70A22-558[»]
1ODCX-ray2.20A22-564[»]
1QIDX-ray2.05A22-558[»]
1QIEX-ray2.10A22-558[»]
1QIFX-ray2.10A22-558[»]
1QIGX-ray2.30A22-558[»]
1QIHX-ray2.50A22-558[»]
1QIIX-ray2.65A22-558[»]
1QIJX-ray2.80A22-558[»]
1QIKX-ray2.90A22-558[»]
1QIMX-ray3.00A22-558[»]
1QTIX-ray2.50A22-558[»]
1SOMX-ray2.20A22-564[»]
1U65X-ray2.61A22-564[»]
1UT6X-ray2.40A22-556[»]
1VOTX-ray2.50A22-558[»]
1VXOX-ray2.40A22-558[»]
1VXRX-ray2.20A22-558[»]
1W4LX-ray2.16A22-564[»]
1W6RX-ray2.05A22-564[»]
1W75X-ray2.40A/B22-564[»]
1W76X-ray2.30A/B22-564[»]
1ZGBX-ray2.30A22-564[»]
1ZGCX-ray2.10A/B22-564[»]
2ACEX-ray2.50A22-558[»]
2ACKX-ray2.40A22-558[»]
2BAGX-ray2.40A22-564[»]
2C4HX-ray2.15A22-558[»]
2C58X-ray2.30A22-558[»]
2C5FX-ray2.60A22-558[»]
2C5GX-ray1.95A22-558[»]
2CEKX-ray2.20A22-556[»]
2CKMX-ray2.15A22-564[»]
2CMFX-ray2.50A22-564[»]
2DFPX-ray2.30A23-556[»]
2J3DX-ray2.60A22-564[»]
2J3QX-ray2.80A22-564[»]
2J4FX-ray2.80A22-564[»]
2V96X-ray2.40A/B22-558[»]
2V97X-ray2.40A/B22-558[»]
2V98X-ray3.00A/B22-558[»]
2VA9X-ray2.40A/B22-558[»]
2VJAX-ray2.30A/B22-558[»]
2VJBX-ray2.39A/B22-558[»]
2VJCX-ray2.20A/B22-558[»]
2VJDX-ray2.30A/B22-558[»]
2VQ6X-ray2.71A22-564[»]
2VT6X-ray2.40A/B22-558[»]
2VT7X-ray2.20A/B22-558[»]
2W6CX-ray2.69X1-586[»]
2WFZX-ray1.95A22-558[»]
2WG0X-ray2.20A22-558[»]
2WG1X-ray2.20A22-558[»]
2WG2X-ray1.95A22-558[»]
2XI4X-ray2.30A/B22-558[»]
3ACEmodel-A22-558[»]
3GELX-ray2.39A25-556[»]
3I6MX-ray2.26A23-556[»]
3I6ZX-ray2.19A23-556[»]
3M3DX-ray2.34A22-564[»]
3ZV7X-ray2.26A22-564[»]
4ACEmodel-A22-558[»]
4TVKX-ray2.30A23-556[»]
4W63X-ray2.80A23-556[»]
4X3CX-ray2.60A23-556[»]
5BWBX-ray2.57A22-558[»]
5BWCX-ray2.45A22-558[»]
5DLPX-ray2.70A22-564[»]
5E2IX-ray2.65A25-556[»]
5E4JX-ray2.54A25-556[»]
5E4TX-ray2.43A22-564[»]
5EHXX-ray2.10A25-556[»]
5EI5X-ray2.10A23-556[»]
5IH7X-ray2.40A23-556[»]
5NAPX-ray2.17A22-564[»]
5NAUX-ray2.25A22-564[»]
5NUUX-ray2.50A22-564[»]
6EUCX-ray2.22A25-556[»]
6EUEX-ray2.00A24-556[»]
6EWKX-ray2.22A25-556[»]
6EZGX-ray2.20A/B22-558[»]
6EZHX-ray2.60A/B22-558[»]
6FLDX-ray2.40A25-556[»]
6FQNX-ray2.30A25-556[»]
6G17X-ray2.20A22-558[»]
6G1UX-ray1.79A/B1-586[»]
6G1VX-ray1.82A/B1-586[»]
6G1WX-ray1.90A/B1-586[»]
6G4MX-ray2.63A/B21-558[»]
6G4NX-ray2.90A/B21-558[»]
6G4OX-ray2.78A/B21-558[»]
6G4PX-ray2.83A/B21-558[»]
6H12X-ray2.20A/B22-586[»]
6H13X-ray2.80A/B22-586[»]
6H14X-ray1.86A/B22-586[»]
SMRiP04058
ModBaseiSearch...

Protein-protein interaction databases

MINTiP04058

Chemistry databases

BindingDBiP04058
ChEMBLiCHEMBL4780

Protein family/group databases

ESTHERitorca-ACHE AChE
MEROPSiS09.980

PTM databases

iPTMnetiP04058

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-16823
BRENDAi3.1.1.7 6395

Miscellaneous databases

EvolutionaryTraceiP04058

Family and domain databases

Gene3Di3.40.50.1820, 1 hit
InterProiView protein in InterPro
IPR029058 AB_hydrolase
IPR000908 Acylcholinesterase_fish/snake
IPR002018 CarbesteraseB
IPR019826 Carboxylesterase_B_AS
IPR019819 Carboxylesterase_B_CS
IPR000997 Cholinesterase
PfamiView protein in Pfam
PF00135 COesterase, 1 hit
PRINTSiPR00879 ACHEFISH
PR00878 CHOLNESTRASE
SUPFAMiSSF53474 SSF53474, 1 hit
PROSITEiView protein in PROSITE
PS00122 CARBOXYLESTERASE_B_1, 1 hit
PS00941 CARBOXYLESTERASE_B_2, 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 nameiACES_TETCF
<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: P04058
<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_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1986
Last sequence update: June 1, 1994
Last modified: July 31, 2019
This is version 168 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<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

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
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