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Entry version 125 (17 Jun 2020)
Sequence version 1 (01 Jun 2001)
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Protein

Acetylcholine-binding protein

Gene
N/A
Organism
Lymnaea stagnalis (Great pond snail) (Helix stagnalis)
Status
Reviewed-Annotation score:

Annotation score:4 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

Binds to acetylcholine. Modulates neuronal synaptic transmission.

<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

<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 functionReceptor

Protein family/group databases

Transport Classification Database

More...
TCDBi
1.A.9.1.19 the neurotransmitter receptor, cys loop, ligand-gated ion channel (lic) family

<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:
Acetylcholine-binding protein
Short name:
ACh-binding protein
Short name:
AchBP
<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>OrganismiLymnaea stagnalis (Great pond snail) (Helix stagnalis)
<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 identifieri6523 [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 lineageiEukaryotaMetazoaSpiraliaLophotrochozoaMolluscaGastropodaHeterobranchiaEuthyneuraPanpulmonataHygrophilaLymnaeoideaLymnaeidaeLymnaea

<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, Secreted, 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

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL6084

DrugCentral

More...
DrugCentrali
P58154

<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 – 191 PublicationAdd BLAST19
<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_000000040620 – 229Acetylcholine-binding proteinAdd BLAST210

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi85N-linked (GlcNAc...) asparagineCurated1
<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 bondi142 ↔ 155
Disulfide bondi207Interchain

<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

N-glycosylated.

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
P58154

<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

Expressed by glial cells.

<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

Homopentamer.

Protein-protein interaction databases

ComplexPortal: manually curated resource of macromolecular complexes

More...
ComplexPortali
CPX-259 Acetylcholine binding protein complex

Database of interacting proteins

More...
DIPi
DIP-43985N

Protein interaction database and analysis system

More...
IntActi
P58154, 3 interactors

Molecular INTeraction database

More...
MINTi
P58154

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
P58154

<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

1229
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
P58154

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
P58154

<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>Domaini114 – 217Ig-likeAdd BLAST104

<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

To the extracellular portion of ligand-gated ionic channels family.Curated

Keywords - Domaini

Immunoglobulin domain, Signal

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
2.70.170.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR007110 Ig-like_dom
IPR006202 Neur_chan_lig-bd
IPR036734 Neur_chan_lig-bd_sf
IPR006201 Neur_channel

The PANTHER Classification System

More...
PANTHERi
PTHR18945 PTHR18945, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF02931 Neur_chan_LBD, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF63712 SSF63712, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50835 IG_LIKE, 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.

P58154-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MRRNIFCLAC LWIVQACLSL DRADILYNIR QTSRPDVIPT QRDRPVAVSV
60 70 80 90 100
SLKFINILEV NEITNEVDVV FWQQTTWSDR TLAWNSSHSP DQVSVPISSL
110 120 130 140 150
WVPDLAAYNA ISKPEVLTPQ LARVVSDGEV LYMPSIRQRF SCDVSGVDTE
160 170 180 190 200
SGATCRIKIG SWTHHSREIS VDPTTENSDD SEYFSQYSRF EILDVTQKKN
210 220
SVTYSCCPEA YEDVEVSLNF RKKGRSEIL
Length:229
Mass (Da):26,061
Last modified:June 1, 2001 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iB76A3A13E7EF8FCB
GO

<p>This subsection of the 'Sequence' section reports information derived from mass spectrometry experiments done on the entire protein or on biologically active derived peptide(s).<p><a href='/help/mass_spectrometry' target='_top'>More...</a></p>Mass spectrometryi

Molecular mass is 24720.4 Da. Determined by ESI. 1 Publication

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
AF364899 mRNA Translation: AAK64377.1

<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
AF364899 mRNA Translation: AAK64377.1

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
1I9BX-ray2.70A/B/C/D/E21-229[»]
1UV6X-ray2.50A/B/C/D/E/F/G/H/I/J20-229[»]
1UW6X-ray2.20A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T21-229[»]
1UX2X-ray2.20A/B/C/D/E/F/G/H/I/J21-229[»]
1YI5X-ray4.20A/B/C/D/E20-229[»]
2ZJUX-ray2.58A/B/C/D/E18-229[»]
2ZJVX-ray2.70A/B/C/D/E18-229[»]
3U8JX-ray2.35A/B/C/D/E/F/G/H/I/J20-229[»]
3U8KX-ray2.47A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T20-229[»]
3U8LX-ray2.32A/B/C/D/E/F/G/H/I/J20-229[»]
3U8MX-ray2.70A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T20-229[»]
3U8NX-ray2.35A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T20-229[»]
3WIPX-ray2.60A/B/C/D/E/F/G/H/I/J1-229[»]
3WTHX-ray2.54A/B/C/D/E21-229[»]
3WTIX-ray2.68A/B/C/D/E21-229[»]
3WTJX-ray2.24A/B/C/D/E21-229[»]
3WTKX-ray2.69A/B/C/D/E21-229[»]
3WTLX-ray2.30A/B/C/D/E21-229[»]
3WTMX-ray2.48A/B/C/D/E21-229[»]
3WTNX-ray2.09A/B/C/D/E/F/G/H/I/J21-229[»]
3WTOX-ray2.25A/B/C/D/E21-229[»]
3ZDGX-ray2.48A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T20-229[»]
3ZDHX-ray2.20A/B/C/D/E/F/G/H/I/J20-229[»]
4ALXX-ray2.30A/B/C/D/E/F/G/H/I/J1-229[»]
4HQPX-ray3.51A/B/C/D/E35-224[»]
4NZBX-ray2.68A/B/C/D/E/F/G/H/I/J/K/L/M/N/O20-229[»]
4QAAX-ray2.70A/B/C/D/E/F/G/H/I/J20-228[»]
4QABX-ray2.98A/B/C/D/E/F/G/H/I/J20-228[»]
4QACX-ray2.10A/B/C/D/E/F/G/H/I/J20-228[»]
4UM1X-ray2.83A/B/C/D/E1-229[»]
4UM3X-ray2.70A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X/Y/Z/a/b/c/d1-229[»]
4ZJTX-ray1.85A/B/C/D/E/F/G/H/I/J20-229[»]
4ZK1X-ray1.75A/B/C/D/E/F/G/H/I/J20-229[»]
4ZR6X-ray2.60A/B/C/D/E20-229[»]
4ZRUX-ray1.90A/B/C/D/E/F/G/H/I/J20-229[»]
5AFHX-ray2.40A/B/C/D/E35-224[»]
5AFJX-ray2.20A/B/C/D/E35-65[»]
A/B/C/D/E67-71[»]
A/B/C/D/E92-224[»]
5AFKX-ray2.38A/B/C/D/E35-224[»]
5AFLX-ray2.38A/B/C/D/E35-224[»]
5AFMX-ray2.85A/C/D/E35-226[»]
5AFNX-ray2.15A/B/C/D/E35-226[»]
5BP0X-ray2.40A/B/C/D/E/F/G/H/I/J20-229[»]
5J5FX-ray2.04A/B/C/D/E/F/G/H/I/J20-229[»]
5J5GX-ray2.04A/B/C/D/E/F/G/H/I/J20-229[»]
5J5HX-ray2.70A/B/C/D/E/F/G/H/I/J20-229[»]
5J5IX-ray2.33A/B/C/D/E/F/G/H/I/J20-229[»]
5T90X-ray2.80A/B/C/D/E20-229[»]
5Y2QX-ray2.36A/B/C/D/E21-229[»]
SMRiP58154
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

ComplexPortaliCPX-259 Acetylcholine binding protein complex
DIPiDIP-43985N
IntActiP58154, 3 interactors
MINTiP58154

Chemistry databases

BindingDBiP58154
ChEMBLiCHEMBL6084
DrugCentraliP58154

Protein family/group databases

TCDBi1.A.9.1.19 the neurotransmitter receptor, cys loop, ligand-gated ion channel (lic) family

Proteomic databases

PRIDEiP58154

Miscellaneous databases

EvolutionaryTraceiP58154

Family and domain databases

Gene3Di2.70.170.10, 1 hit
InterProiView protein in InterPro
IPR007110 Ig-like_dom
IPR006202 Neur_chan_lig-bd
IPR036734 Neur_chan_lig-bd_sf
IPR006201 Neur_channel
PANTHERiPTHR18945 PTHR18945, 1 hit
PfamiView protein in Pfam
PF02931 Neur_chan_LBD, 1 hit
SUPFAMiSSF63712 SSF63712, 1 hit
PROSITEiView protein in PROSITE
PS50835 IG_LIKE, 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 nameiACHP_LYMST
<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: P58154
<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: June 1, 2001
Last sequence update: June 1, 2001
Last modified: June 17, 2020
This is version 125 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, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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