ACHP_LYMST
ID ACHP_LYMST Reviewed; 229 AA.
AC P58154;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Acetylcholine-binding protein;
DE Short=ACh-binding protein;
DE Short=AchBP;
DE Flags: Precursor;
OS Lymnaea stagnalis (Great pond snail) (Helix stagnalis).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Heterobranchia; Euthyneura; Panpulmonata; Hygrophila; Lymnaeoidea;
OC Lymnaeidae; Lymnaea.
OX NCBI_TaxID=6523;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 20-30, MASS SPECTROMETRY,
RP AND SUBCELLULAR LOCATION.
RC TISSUE=CNS;
RX PubMed=11357121; DOI=10.1038/35077000;
RA Smit A.B., Syed N.I., Schaap D., van Minnen J., Klumperman J., Kits K.S.,
RA Lodder H., van Der Schors R.C., van Elk R., Sorgedrager B., Brejc K.,
RA Sixma T.K., Geraerts W.P.M.;
RT "A glia-derived acetylcholine-binding protein that modulates synaptic
RT transmission.";
RL Nature 411:261-268(2001).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 20-229.
RX PubMed=11357122; DOI=10.1038/35077011;
RA Brejc K., van Dijk W.J., Klaassen R.V., Schuurmans M., van Der Oost J.,
RA Smit A.B., Sixma T.K.;
RT "Crystal structure of an ACh-binding protein reveals the ligand-binding
RT domain of nicotinic receptors.";
RL Nature 411:269-276(2001).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.46 ANGSTROMS) IN COMPLEX WITH ALPHA-CONOTOXIN
RP AUSIA.
RX PubMed=34753970; DOI=10.1038/s41598-021-01277-4;
RA Ho T.N.T., Abraham N., Lewis R.J.;
RT "Rigidity of loop 1 contributes to equipotency of globular and ribbon
RT isomers of alpha-conotoxin AusIA.";
RL Sci. Rep. 11:21928-21928(2021).
CC -!- FUNCTION: Binds to acetylcholine. Modulates neuronal synaptic
CC transmission.
CC -!- SUBUNIT: Homopentamer.
CC -!- SUBCELLULAR LOCATION: Synaptic cleft {ECO:0000269|PubMed:11357121}.
CC Note=Released in an acetylcholine-dependent manner in the synaptic
CC cleft. {ECO:0000269|PubMed:11357121}.
CC -!- TISSUE SPECIFICITY: Expressed by glial cells.
CC -!- PTM: N-glycosylated.
CC -!- MASS SPECTROMETRY: Mass=24720.4; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:11357121};
CC -!- SIMILARITY: To the extracellular portion of ligand-gated ionic channels
CC family. {ECO:0000305}.
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DR EMBL; AF364899; AAK64377.1; -; mRNA.
DR PDB; 1I9B; X-ray; 2.70 A; A/B/C/D/E=21-229.
DR PDB; 1UV6; X-ray; 2.50 A; A/B/C/D/E/F/G/H/I/J=20-229.
DR PDB; 1UW6; X-ray; 2.20 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T=21-229.
DR PDB; 1UX2; X-ray; 2.20 A; A/B/C/D/E/F/G/H/I/J=21-229.
DR PDB; 1YI5; X-ray; 4.20 A; A/B/C/D/E=20-229.
DR PDB; 2ZJU; X-ray; 2.58 A; A/B/C/D/E=18-229.
DR PDB; 2ZJV; X-ray; 2.70 A; A/B/C/D/E=18-229.
DR PDB; 3U8J; X-ray; 2.35 A; A/B/C/D/E/F/G/H/I/J=20-229.
DR PDB; 3U8K; X-ray; 2.47 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T=20-229.
DR PDB; 3U8L; X-ray; 2.32 A; A/B/C/D/E/F/G/H/I/J=20-229.
DR PDB; 3U8M; X-ray; 2.70 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T=20-229.
DR PDB; 3U8N; X-ray; 2.35 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T=20-229.
DR PDB; 3WIP; X-ray; 2.60 A; A/B/C/D/E/F/G/H/I/J=1-229.
DR PDB; 3WTH; X-ray; 2.54 A; A/B/C/D/E=21-229.
DR PDB; 3WTI; X-ray; 2.68 A; A/B/C/D/E=21-229.
DR PDB; 3WTJ; X-ray; 2.24 A; A/B/C/D/E=21-229.
DR PDB; 3WTK; X-ray; 2.69 A; A/B/C/D/E=21-229.
DR PDB; 3WTL; X-ray; 2.30 A; A/B/C/D/E=21-229.
DR PDB; 3WTM; X-ray; 2.48 A; A/B/C/D/E=21-229.
DR PDB; 3WTN; X-ray; 2.09 A; A/B/C/D/E/F/G/H/I/J=21-229.
DR PDB; 3WTO; X-ray; 2.25 A; A/B/C/D/E=21-229.
DR PDB; 3ZDG; X-ray; 2.48 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T=20-229.
DR PDB; 3ZDH; X-ray; 2.20 A; A/B/C/D/E/F/G/H/I/J=20-229.
DR PDB; 4ALX; X-ray; 2.30 A; A/B/C/D/E/F/G/H/I/J=1-229.
DR PDB; 4HQP; X-ray; 3.51 A; A/B/C/D/E=35-224.
DR PDB; 4NZB; X-ray; 2.68 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O=20-229.
DR PDB; 4QAA; X-ray; 2.70 A; A/B/C/D/E/F/G/H/I/J=20-228.
DR PDB; 4QAB; X-ray; 2.98 A; A/B/C/D/E/F/G/H/I/J=20-228.
DR PDB; 4QAC; X-ray; 2.10 A; A/B/C/D/E/F/G/H/I/J=20-228.
DR PDB; 4UM1; X-ray; 2.83 A; A/B/C/D/E=1-229.
DR PDB; 4UM3; X-ray; 2.70 A; A/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/d=1-229.
DR PDB; 4ZJT; X-ray; 1.85 A; A/B/C/D/E/F/G/H/I/J=20-229.
DR PDB; 4ZK1; X-ray; 1.75 A; A/B/C/D/E/F/G/H/I/J=20-229.
DR PDB; 4ZR6; X-ray; 2.60 A; A/B/C/D/E=20-229.
DR PDB; 4ZRU; X-ray; 1.90 A; A/B/C/D/E/F/G/H/I/J=20-229.
DR PDB; 5AFH; X-ray; 2.40 A; A/B/C/D/E=35-224.
DR PDB; 5AFJ; X-ray; 2.20 A; A/B/C/D/E=35-65, A/B/C/D/E=67-71, A/B/C/D/E=92-224.
DR PDB; 5AFK; X-ray; 2.38 A; A/B/C/D/E=35-224.
DR PDB; 5AFL; X-ray; 2.38 A; A/B/C/D/E=35-224.
DR PDB; 5AFM; X-ray; 2.85 A; A/C/D/E=35-226.
DR PDB; 5AFN; X-ray; 2.15 A; A/B/C/D/E=35-226.
DR PDB; 5BP0; X-ray; 2.40 A; A/B/C/D/E/F/G/H/I/J=20-229.
DR PDB; 5J5F; X-ray; 2.04 A; A/B/C/D/E/F/G/H/I/J=20-229.
DR PDB; 5J5G; X-ray; 2.04 A; A/B/C/D/E/F/G/H/I/J=20-229.
DR PDB; 5J5H; X-ray; 2.70 A; A/B/C/D/E/F/G/H/I/J=20-229.
DR PDB; 5J5I; X-ray; 2.33 A; A/B/C/D/E/F/G/H/I/J=20-229.
DR PDB; 5T90; X-ray; 2.80 A; A/B/C/D/E=20-229.
DR PDB; 5Y2Q; X-ray; 2.36 A; A/B/C/D/E=21-229.
DR PDB; 7DJI; X-ray; 2.20 A; A/B/C/D/E=21-229.
DR PDB; 7N0W; X-ray; 2.46 A; A/B/C/D/E=20-224.
DR PDB; 7N0Y; X-ray; 2.58 A; A/B/C/D/E=20-224.
DR PDB; 7N43; X-ray; 2.47 A; A/B/C/D/E=20-229.
DR PDB; 7NDP; X-ray; 2.00 A; A/B/C/D/E/F/G/H/I/J=1-229.
DR PDB; 7NDV; X-ray; 1.70 A; A/B/C/D/E/F/G/H/I/J=1-229.
DR PDB; 7PD6; X-ray; 2.00 A; AaA/BaB/CaC/DaD/EaE/FaF/GaG/HaH/IaI/JJJ=21-229.
DR PDB; 7PDB; X-ray; 2.33 A; AaA/BaB/CaC/DaD/EaE=21-229.
DR PDB; 7PDR; X-ray; 2.33 A; AaA/BaB/CaC/DaD/EaE=21-229.
DR PDB; 7PE5; X-ray; 2.10 A; AaA/BaB/CaC/DaD/EaE=21-229.
DR PDB; 7PE6; X-ray; 2.01 A; AaA/BaB/CaC/DaD/EaE=21-229.
DR PDBsum; 1I9B; -.
DR PDBsum; 1UV6; -.
DR PDBsum; 1UW6; -.
DR PDBsum; 1UX2; -.
DR PDBsum; 1YI5; -.
DR PDBsum; 2ZJU; -.
DR PDBsum; 2ZJV; -.
DR PDBsum; 3U8J; -.
DR PDBsum; 3U8K; -.
DR PDBsum; 3U8L; -.
DR PDBsum; 3U8M; -.
DR PDBsum; 3U8N; -.
DR PDBsum; 3WIP; -.
DR PDBsum; 3WTH; -.
DR PDBsum; 3WTI; -.
DR PDBsum; 3WTJ; -.
DR PDBsum; 3WTK; -.
DR PDBsum; 3WTL; -.
DR PDBsum; 3WTM; -.
DR PDBsum; 3WTN; -.
DR PDBsum; 3WTO; -.
DR PDBsum; 3ZDG; -.
DR PDBsum; 3ZDH; -.
DR PDBsum; 4ALX; -.
DR PDBsum; 4HQP; -.
DR PDBsum; 4NZB; -.
DR PDBsum; 4QAA; -.
DR PDBsum; 4QAB; -.
DR PDBsum; 4QAC; -.
DR PDBsum; 4UM1; -.
DR PDBsum; 4UM3; -.
DR PDBsum; 4ZJT; -.
DR PDBsum; 4ZK1; -.
DR PDBsum; 4ZR6; -.
DR PDBsum; 4ZRU; -.
DR PDBsum; 5AFH; -.
DR PDBsum; 5AFJ; -.
DR PDBsum; 5AFK; -.
DR PDBsum; 5AFL; -.
DR PDBsum; 5AFM; -.
DR PDBsum; 5AFN; -.
DR PDBsum; 5BP0; -.
DR PDBsum; 5J5F; -.
DR PDBsum; 5J5G; -.
DR PDBsum; 5J5H; -.
DR PDBsum; 5J5I; -.
DR PDBsum; 5T90; -.
DR PDBsum; 5Y2Q; -.
DR PDBsum; 7DJI; -.
DR PDBsum; 7N0W; -.
DR PDBsum; 7N0Y; -.
DR PDBsum; 7N43; -.
DR PDBsum; 7NDP; -.
DR PDBsum; 7NDV; -.
DR PDBsum; 7PD6; -.
DR PDBsum; 7PDB; -.
DR PDBsum; 7PDR; -.
DR PDBsum; 7PE5; -.
DR PDBsum; 7PE6; -.
DR AlphaFoldDB; P58154; -.
DR SMR; P58154; -.
DR ComplexPortal; CPX-259; Acetylcholine binding protein complex.
DR DIP; DIP-43985N; -.
DR IntAct; P58154; 3.
DR MINT; P58154; -.
DR BindingDB; P58154; -.
DR ChEMBL; CHEMBL6084; -.
DR DrugCentral; P58154; -.
DR TCDB; 1.A.9.1.19; the neurotransmitter receptor, cys loop, ligand-gated ion channel (lic) family.
DR PRIDE; P58154; -.
DR EvolutionaryTrace; P58154; -.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0016021; C:integral component of membrane; IEA:InterPro.
DR GO; GO:0032991; C:protein-containing complex; IPI:ComplexPortal.
DR GO; GO:0045202; C:synapse; IEA:UniProtKB-KW.
DR GO; GO:0043083; C:synaptic cleft; IDA:ComplexPortal.
DR GO; GO:0005230; F:extracellular ligand-gated ion channel activity; IEA:InterPro.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
DR GO; GO:0032223; P:negative regulation of synaptic transmission, cholinergic; IDA:ComplexPortal.
DR Gene3D; 2.70.170.10; -; 1.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR006202; Neur_chan_lig-bd.
DR InterPro; IPR036734; Neur_chan_lig-bd_sf.
DR InterPro; IPR006201; Neur_channel.
DR PANTHER; PTHR18945; PTHR18945; 1.
DR Pfam; PF02931; Neur_chan_LBD; 1.
DR SUPFAM; SSF63712; SSF63712; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Immunoglobulin domain; Receptor; Secreted; Signal; Synapse.
FT SIGNAL 1..19
FT /evidence="ECO:0000269|PubMed:11357121"
FT CHAIN 20..229
FT /note="Acetylcholine-binding protein"
FT /id="PRO_0000000406"
FT DOMAIN 114..217
FT /note="Ig-like"
FT CARBOHYD 85
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT DISULFID 142..155
FT /evidence="ECO:0000269|PubMed:34753970,
FT ECO:0007744|PDB:7N0W, ECO:0007744|PDB:7N0Y"
FT DISULFID 207
FT /note="Interchain"
FT HELIX 22..32
FT /evidence="ECO:0007829|PDB:7NDV"
FT STRAND 46..61
FT /evidence="ECO:0007829|PDB:7NDV"
FT TURN 62..65
FT /evidence="ECO:0007829|PDB:7NDV"
FT STRAND 66..78
FT /evidence="ECO:0007829|PDB:7NDV"
FT HELIX 80..82
FT /evidence="ECO:0007829|PDB:7NDV"
FT STRAND 87..89
FT /evidence="ECO:0007829|PDB:3WTH"
FT STRAND 91..96
FT /evidence="ECO:0007829|PDB:7NDV"
FT HELIX 97..99
FT /evidence="ECO:0007829|PDB:7NDV"
FT STRAND 105..107
FT /evidence="ECO:0007829|PDB:7NDV"
FT STRAND 110..112
FT /evidence="ECO:0007829|PDB:7NDV"
FT STRAND 121..125
FT /evidence="ECO:0007829|PDB:7NDV"
FT STRAND 128..132
FT /evidence="ECO:0007829|PDB:7NDV"
FT STRAND 135..141
FT /evidence="ECO:0007829|PDB:7NDV"
FT TURN 145..148
FT /evidence="ECO:0007829|PDB:7NDV"
FT STRAND 149..151
FT /evidence="ECO:0007829|PDB:7NDV"
FT STRAND 153..163
FT /evidence="ECO:0007829|PDB:7NDV"
FT TURN 166..168
FT /evidence="ECO:0007829|PDB:7NDV"
FT STRAND 169..172
FT /evidence="ECO:0007829|PDB:7NDV"
FT STRAND 176..178
FT /evidence="ECO:0007829|PDB:5J5G"
FT TURN 180..183
FT /evidence="ECO:0007829|PDB:7NDV"
FT STRAND 188..203
FT /evidence="ECO:0007829|PDB:7NDV"
FT STRAND 205..209
FT /evidence="ECO:0007829|PDB:3WTM"
FT STRAND 210..222
FT /evidence="ECO:0007829|PDB:7NDV"
FT TURN 225..227
FT /evidence="ECO:0007829|PDB:3U8K"
SQ SEQUENCE 229 AA; 26061 MW; B76A3A13E7EF8FCB CRC64;
MRRNIFCLAC LWIVQACLSL DRADILYNIR QTSRPDVIPT QRDRPVAVSV SLKFINILEV
NEITNEVDVV FWQQTTWSDR TLAWNSSHSP DQVSVPISSL WVPDLAAYNA ISKPEVLTPQ
LARVVSDGEV LYMPSIRQRF SCDVSGVDTE SGATCRIKIG SWTHHSREIS VDPTTENSDD
SEYFSQYSRF EILDVTQKKN SVTYSCCPEA YEDVEVSLNF RKKGRSEIL
