Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

Autoinhibited structure

Activated structure

1 structures for Q8BMN3

Entry ID Method Resolution Chain Position Source
AF-Q8BMN3-F1 Predicted AlphaFoldDB

27 variants for Q8BMN3

Variant ID(s) Position Change Description Diseaes Association Provenance
rs1133022154 13 A>T No EVA
rs3388971737 46 Y>* No EVA
rs3388965011 70 Q>R No EVA
rs3388970943 119 P>L No EVA
rs3388949476 120 D>H No EVA
rs3388977048 124 F>I No EVA
rs3388974715 144 S>R No EVA
rs45803685 170 K>R No EVA
rs3388960512 213 K>E No EVA
rs3388979837 228 F>Y No EVA
rs3388982944 270 K>E No EVA
rs3388955010 283 V>M No EVA
rs36532908 304 E>K No EVA
rs36532908 304 E>Q No EVA
rs3388979586 307 L>F No EVA
rs3388979640 313 V>I No EVA
rs3388979661 330 S>F No EVA
rs36244171 348 K>R No EVA
rs3388974733 361 R>C No EVA
rs259877074 368 T>K No EVA
rs259877074 368 T>M No EVA
rs245908373 378 F>V No EVA
rs212466953 396 A>T No EVA
rs3388949489 409 S>* No EVA
rs3388970961 451 I>F No EVA
rs3388964995 458 M>I No EVA
rs1131884955 462 R>H No EVA

No associated diseases with Q8BMN3

3 regional properties for Q8BMN3

Type Name Position InterPro Accession
domain Neurotransmitter-gated ion-channel transmembrane domain 246 - 452 IPR006029
domain Neurotransmitter-gated ion-channel ligand-binding domain 36 - 238 IPR006202
conserved_site Neurotransmitter-gated ion-channel, conserved site 159 - 173 IPR018000

Functions

Description
EC Number
Subcellular Localization
  • Postsynaptic cell membrane; Multi-pass membrane protein
  • Cell membrane; Multi-pass membrane protein
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

9 GO annotations of cellular component

Name Definition
acetylcholine-gated channel complex A homo- or hetero-pentameric protein complex that forms a transmembrane channel through which ions may pass in response to acetylcholine binding.
anchoring junction A cell junction that mechanically attaches a cell (and its cytoskeleton) to neighboring cells or to the extracellular matrix.
dopaminergic synapse A synapse that uses dopamine as a neurotransmitter.
integral component of plasma membrane The component of the plasma membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane.
membrane A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it.
neuron projection A prolongation or process extending from a nerve cell, e.g. an axon or dendrite.
postsynaptic membrane A specialized area of membrane facing the presynaptic membrane on the tip of the nerve ending and separated from it by a minute cleft (the synaptic cleft). Neurotransmitters cross the synaptic cleft and transmit the signal to the postsynaptic membrane.
protein-containing complex A stable assembly of two or more macromolecules, i.e. proteins, nucleic acids, carbohydrates or lipids, in which at least one component is a protein and the constituent parts function together.
synapse The junction between an axon of one neuron and a dendrite of another neuron, a muscle fiber or a glial cell. As the axon approaches the synapse it enlarges into a specialized structure, the presynaptic terminal bouton, which contains mitochondria and synaptic vesicles. At the tip of the terminal bouton is the presynaptic membrane; facing it, and separated from it by a minute cleft (the synaptic cleft) is a specialized area of membrane on the receiving cell, known as the postsynaptic membrane. In response to the arrival of nerve impulses, the presynaptic terminal bouton secretes molecules of neurotransmitters into the synaptic cleft. These diffuse across the cleft and transmit the signal to the postsynaptic membrane.

7 GO annotations of molecular function

Name Definition
acetylcholine binding Binding to acetylcholine, an acetic acid ester of the organic base choline that functions as a neurotransmitter, released at the synapses of parasympathetic nerves and at neuromuscular junctions.
acetylcholine-gated cation-selective channel activity Selectively enables the transmembrane transfer of a cation by a channel that opens upon binding acetylcholine.
excitatory extracellular ligand-gated ion channel activity Enables the transmembrane transfer of an ion by a channel that opens when a specific extracellular ligand has been bound by the channel complex or one of its constituent parts, where channel opening contributes to an increase in membrane potential.
heterocyclic compound binding Binding to heterocyclic compound.
neurotransmitter receptor activity Combining with a neurotransmitter and transmitting the signal to initiate a change in cell activity.
transmembrane signaling receptor activity Combining with an extracellular or intracellular signal and transmitting the signal from one side of the membrane to the other to initiate a change in cell activity or state as part of signal transduction.
transmitter-gated ion channel activity involved in regulation of postsynaptic membrane potential Any transmitter-gated ion channel activity that is involved in regulation of postsynaptic membrane potential.

9 GO annotations of biological process

Name Definition
chemical synaptic transmission The vesicular release of classical neurotransmitter molecules from a presynapse, across a chemical synapse, the subsequent activation of neurotransmitter receptors at the postsynapse of a target cell (neuron, muscle, or secretory cell) and the effects of this activation on the postsynaptic membrane potential and ionic composition of the postsynaptic cytosol. This process encompasses both spontaneous and evoked release of neurotransmitter and all parts of synaptic vesicle exocytosis. Evoked transmission starts with the arrival of an action potential at the presynapse.
ion transmembrane transport A process in which an ion is transported across a membrane.
membrane depolarization The process in which membrane potential decreases with respect to its steady-state potential, usually from negative potential to a more positive potential. For example, the initial depolarization during the rising phase of an action potential is in the direction from the negative steady-state resting potential towards the positive membrane potential that will be the peak of the action potential.
nervous system process A organ system process carried out by any of the organs or tissues of neurological system.
regulation of membrane potential Any process that modulates the establishment or extent of a membrane potential, the electric potential existing across any membrane arising from charges in the membrane itself and from the charges present in the media on either side of the membrane.
regulation of synaptic vesicle exocytosis Any process that modulates the frequency, rate or extent of synaptic vesicle exocytosis.
response to nicotine Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a nicotine stimulus.
signal transduction The cellular process in which a signal is conveyed to trigger a change in the activity or state of a cell. Signal transduction begins with reception of a signal (e.g. a ligand binding to a receptor or receptor activation by a stimulus such as light), or for signal transduction in the absence of ligand, signal-withdrawal or the activity of a constitutively active receptor. Signal transduction ends with regulation of a downstream cellular process, e.g. regulation of transcription or regulation of a metabolic process. Signal transduction covers signaling from receptors located on the surface of the cell and signaling via molecules located within the cell. For signaling between cells, signal transduction is restricted to events at and within the receiving cell.
synaptic transmission, cholinergic The vesicular release of acetylcholine from a presynapse, across a chemical synapse, the subsequent activation of dopamine receptors at the postsynapse of a target cell (neuron, muscle, or secretory cell) and the effects of this activation on the postsynaptic membrane potential and ionic composition of the postsynaptic cytosol. This process encompasses both spontaneous and evoked release of neurotransmitter and all parts of synaptic vesicle exocytosis. Evoked transmission starts with the arrival of an action potential at the presynapse.

37 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q07263 CHRNA3 Neuronal acetylcholine receptor subunit alpha-3 Bos taurus (Bovine) PR
P04758 CHRNB1 Acetylcholine receptor subunit beta Bos taurus (Bovine) PR
Q8SPU7 CHRNA5 Neuronal acetylcholine receptor subunit alpha-5 Bos taurus (Bovine) PR
P09481 CHRNA3 Neuronal acetylcholine receptor subunit alpha-3 Gallus gallus (Chicken) PR
P26152 CHRNA5 Neuronal acetylcholine receptor subunit alpha-5 Gallus gallus (Chicken) PR
Q9I8C7 CHRNA10 Neuronal acetylcholine receptor subunit alpha-10 Gallus gallus (Chicken) PR
P43679 CHRNB3 Neuronal acetylcholine receptor subunit beta-3 Gallus gallus (Chicken) PR
Q5IS76 CHRNA6 Neuronal acetylcholine receptor subunit alpha-6 Pan troglodytes (Chimpanzee) PR
Q5IS75 CHRNB3 Neuronal acetylcholine receptor subunit beta-3 Pan troglodytes (Chimpanzee) PR
P25162 nAChRbeta2 Acetylcholine receptor subunit beta-like 2 Drosophila melanogaster (Fruit fly) PR
Q15825 CHRNA6 Neuronal acetylcholine receptor subunit alpha-6 Homo sapiens (Human) PR
P30532 CHRNA5 Neuronal acetylcholine receptor subunit alpha-5 Homo sapiens (Human) PR
P11230 CHRNB1 Acetylcholine receptor subunit beta Homo sapiens (Human) PR
P32297 CHRNA3 Neuronal acetylcholine receptor subunit alpha-3 Homo sapiens (Human) PR
Q05901 CHRNB3 Neuronal acetylcholine receptor subunit beta-3 Homo sapiens (Human) PR
P22723 Gabrg2 Gamma-aminobutyric acid receptor subunit gamma-2 Mus musculus (Mouse) PR
P62812 Gabra1 Gamma-aminobutyric acid receptor subunit alpha-1 Mus musculus (Mouse) PR
P22933 Gabrd Gamma-aminobutyric acid receptor subunit delta Mus musculus (Mouse) PR
P23979 Htr3a 5-hydroxytryptamine receptor 3A Mus musculus (Mouse) PR
P09690 Chrnb1 Acetylcholine receptor subunit beta Mus musculus (Mouse) PR
Q9R0W9 Chrna6 Neuronal acetylcholine receptor subunit alpha-6 Mus musculus (Mouse) PR
Q2MKA5 Chrna5 Neuronal acetylcholine receptor subunit alpha-5 Mus musculus (Mouse) PR
P04756 Chrna1 Acetylcholine receptor subunit alpha Mus musculus (Mouse) PR
P48168 Glrb Glycine receptor subunit beta Mus musculus (Mouse) PR
Q64018 Glra1 Glycine receptor subunit alpha-1 Mus musculus (Mouse) PR
Q91XP5 Glra3 Glycine receptor subunit alpha-3 Mus musculus (Mouse) PR
P43144 Chrna9 Neuronal acetylcholine receptor subunit alpha-9 Rattus norvegicus (Rat) PR
P35563 Htr3a 5-hydroxytryptamine receptor 3A Rattus norvegicus (Rat) PR
P43143 Chrna6 Neuronal acetylcholine receptor subunit alpha-6 Rattus norvegicus (Rat) PR
P04757 Chrna3 Neuronal acetylcholine receptor subunit alpha-3 Rattus norvegicus (Rat) PR
P25109 Chrnb1 Acetylcholine receptor subunit beta Rattus norvegicus (Rat) PR
P25108 Chrna1 Acetylcholine receptor subunit alpha Rattus norvegicus (Rat) PR
P20420 Chrna5 Neuronal acetylcholine receptor subunit alpha-5 Rattus norvegicus (Rat) PR
P12391 Chrnb3 Neuronal acetylcholine receptor subunit beta-3 Rattus norvegicus (Rat) PR
P54244 deg-3 Acetylcholine receptor subunit alpha-type deg-3 Caenorhabditis elegans PR
P54246 acr-5 Acetylcholine receptor subunit alpha-type acr-5 Caenorhabditis elegans PR
Q93149 acr-3 Acetylcholine receptor subunit beta-type acr-3 Caenorhabditis elegans PR
10 20 30 40 50 60
MTGFLRVFLA LSATLSGSWV TLTATAGLSS VAEHEDALLR HLFQGYQKCV RPVLNSSDII
70 80 90 100 110 120
KVYFGLKISQ LVDVDEKNQL MTTNVWLKQE WTDQKLRWNP EDYGGINSIK VPSESLWLPD
130 140 150 160 170 180
IVLFENADGR FEGSLMTKAI VKSSGTVSWT PPASYKSSCT MDVTFFPFDK QNCSMKFGSW
190 200 210 220 230 240
TYDGTMVDLI LINENVDRKD FFDNGEWEIL NAKGMKGNRR EGFYSYPFVT YSFVLRRLPL
250 260 270 280 290 300
FYTLFLIIPC LGLSFLTVLV FYLPSDEGEK LSLSTSVLVS LTVFLLVIEE IIPSSSKVIP
310 320 330 340 350 360
LIGEYLLFIM IFVTLSIIVT VFVINVHHRS SSTYHPMAPW VKRLFLEKLP RWLCMKDPRD
370 380 390 400 410 420
RFSFPDGTES KGTVRGKFPG KKKQTPTSDG ERVLVAFLEK ASESIRYISR HVKKEHFISQ
430 440 450 460
VVQDWKFVAQ VLDRIFLWLF LTASVLGSVL IFIPALKMWI HRFH