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Protein

Acetylcholine-binding protein

Gene
N/A
Organism
Lymnaea stagnalis (Great pond snail) (Helix stagnalis)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Binds to acetylcholine. Modulates neuronal synaptic transmission.

GO - Molecular functioni

Keywordsi

Molecular functionReceptor

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

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

Keywords - Cellular componenti

Cell junction, Secreted, Synapse

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL6084

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 191 PublicationAdd BLAST19
ChainiPRO_000000040620 – 229Acetylcholine-binding proteinAdd BLAST210

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi85N-linked (GlcNAc...) asparagineCurated1
Disulfide bondi142 ↔ 155
Disulfide bondi207Interchain

Post-translational modificationi

N-glycosylated.

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PRIDEiP58154

Expressioni

Tissue specificityi

Expressed by glial cells.

Interactioni

Subunit structurei

Homopentamer.

Protein-protein interaction databases

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

Chemistry databases

BindingDBiP58154

Structurei

Secondary structure

1229
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliP58154
SMRiP58154
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP58154

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini114 – 217Ig-likeAdd BLAST104

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
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

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
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[»]
ProteinModelPortaliP58154
SMRiP58154
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

Chemistry databases

BindingDBiP58154
ChEMBLiCHEMBL6084

Proteomic databases

PRIDEiP58154

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

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
ProtoNetiSearch...

Entry informationi

Entry nameiACHP_LYMST
AccessioniPrimary (citable) accession number: P58154
Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 1, 2001
Last sequence update: June 1, 2001
Last modified: October 10, 2018
This is version 117 of the entry and version 1 of the sequence. See 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
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