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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: 5 out of 5-Experimental evidence at protein leveli

Functioni

Binds to acetylcholine. Modulates neuronal synaptic transmission.

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Receptor

Names & Taxonomyi

Protein namesi
Recommended name:
Acetylcholine-binding protein
Short name:
ACh-binding protein
Short name:
AchBP
OrganismiLymnaea stagnalis (Great pond snail) (Helix stagnalis)
Taxonomic identifieri6523 [NCBI]
Taxonomic lineageiEukaryotaMetazoaLophotrochozoaMolluscaGastropodaHeterobranchiaEuthyneuraPanpulmonataHygrophilaLymnaeoideaLymnaeidaeLymnaea

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Secreted, Synapse

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL6084.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 19191 PublicationAdd
BLAST
Chaini20 – 229210Acetylcholine-binding proteinPRO_0000000406Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi85 – 851N-linked (GlcNAc...)Curated
Disulfide bondi142 ↔ 155
Disulfide bondi207 – 207Interchain

Post-translational modificationi

N-glycosylated.

Keywords - PTMi

Disulfide bond, Glycoprotein

Expressioni

Tissue specificityi

Expressed by glial cells.

Interactioni

Subunit structurei

Homopentamer.

Protein-protein interaction databases

DIPiDIP-43985N.
IntActiP58154. 2 interactions.
MINTiMINT-5223682.

Chemistry

BindingDBiP58154.

Structurei

Secondary structure

1
229
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi20 – 3213Combined sources
Beta strandi46 – 6116Combined sources
Turni62 – 654Combined sources
Beta strandi66 – 7813Combined sources
Helixi80 – 823Combined sources
Turni86 – 883Combined sources
Beta strandi91 – 966Combined sources
Helixi97 – 993Combined sources
Beta strandi105 – 1073Combined sources
Beta strandi110 – 1123Combined sources
Beta strandi121 – 1255Combined sources
Beta strandi128 – 1325Combined sources
Beta strandi135 – 1417Combined sources
Turni145 – 1484Combined sources
Beta strandi149 – 1513Combined sources
Beta strandi153 – 16311Combined sources
Turni166 – 1683Combined sources
Beta strandi169 – 1724Combined sources
Beta strandi176 – 1783Combined sources
Turni181 – 1833Combined sources
Beta strandi188 – 20316Combined sources
Beta strandi205 – 2095Combined sources
Beta strandi210 – 22213Combined sources
Turni225 – 2273Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP58154.
SMRiP58154. Positions 20-224.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP58154.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini114 – 217104Ig-likeAdd
BLAST

Sequence similaritiesi

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

Keywords - Domaini

Immunoglobulin domain, Signal

Family and domain databases

Gene3Di2.70.170.10. 1 hit.
InterProiIPR007110. Ig-like_dom.
IPR006202. Neur_chan_lig-bd.
IPR006201. Neur_channel.
[Graphical view]
PANTHERiPTHR18945. PTHR18945. 1 hit.
PfamiPF02931. Neur_chan_LBD. 1 hit.
[Graphical view]
SUPFAMiSSF63712. SSF63712. 1 hit.
PROSITEiPS50835. IG_LIKE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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
Checksum:iB76A3A13E7EF8FCB
GO

Mass spectrometryi

Molecular mass is 24720.4 Da from positions 20 - 229. Determined by ESI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF364899 mRNA. Translation: AAK64377.1.

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:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP58154.
SMRiP58154. Positions 20-224.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-43985N.
IntActiP58154. 2 interactions.
MINTiMINT-5223682.

Chemistry

BindingDBiP58154.
ChEMBLiCHEMBL6084.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP58154.

Family and domain databases

Gene3Di2.70.170.10. 1 hit.
InterProiIPR007110. Ig-like_dom.
IPR006202. Neur_chan_lig-bd.
IPR006201. Neur_channel.
[Graphical view]
PANTHERiPTHR18945. PTHR18945. 1 hit.
PfamiPF02931. Neur_chan_LBD. 1 hit.
[Graphical view]
SUPFAMiSSF63712. SSF63712. 1 hit.
PROSITEiPS50835. IG_LIKE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiACHP_LYMST
AccessioniPrimary (citable) accession number: P58154
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 2001
Last sequence update: June 1, 2001
Last modified: July 6, 2016
This is version 103 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.