P30926 · ACHB4_HUMAN
- ProteinNeuronal acetylcholine receptor subunit beta-4
- GeneCHRNB4
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids498 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane.
Features
Showing features for site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 82 | Key residue that facilitates effective access of the conotoxin BuIA to the channel binding site | ||||
Sequence: K | ||||||
Site | 134 | Key residue for a low dissociation (K(off)) from the conotoxin BuIA | ||||
Sequence: I |
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameNeuronal acetylcholine receptor subunit beta-4
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionP30926
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Postsynaptic cell membrane ; Multi-pass membrane protein
Cell membrane ; Multi-pass membrane protein
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 22-236 | Extracellular | ||||
Sequence: RVANAEEKLMDDLLNKTRYNNLIRPATSSSQLISIKLQLSLAQLISVNEREQIMTTNVWLKQEWTDYRLTWNSSRYEGVNILRIPAKRIWLPDIVLYNNADGTYEVSVYTNLIVRSNGSVLWLPPAIYKSACKIEVKYFPFDQQNCTLKFRSWTYDHTEIDMVLMTPTASMDDFTPSGEWDIVALPGRRTVNPQDPSYVDVTYDFIIKRKPLFYT | ||||||
Transmembrane | 237-257 | Helical | ||||
Sequence: INLIIPCVLTTLLAILVFYLP | ||||||
Topological domain | 258-265 | Cytoplasmic | ||||
Sequence: SDCGEKMT | ||||||
Transmembrane | 266-286 | Helical | ||||
Sequence: LCISVLLALTFFLLLISKIVP | ||||||
Topological domain | 287-298 | Extracellular | ||||
Sequence: PTSLDVPLIGKY | ||||||
Transmembrane | 299-319 | Helical | ||||
Sequence: LMFTMVLVTFSIVTSVCVLNV | ||||||
Topological domain | 320-460 | Cytoplasmic | ||||
Sequence: HHRSPSTHTMAPWVKRCFLHKLPTFLFMKRPGPDSSPARAFPPSKSCVTKPEATATSTSPSNFYGNSMYFVNPASAASKSPAGSTPVAIPRDFWLRSSGRFRQDVQEALEGVSFIAQHMKNDDEDQSVVEDWKYVAMVVDR | ||||||
Transmembrane | 461-481 | Helical | ||||
Sequence: LFLWVFMFVCVLGTVGLFLPP | ||||||
Topological domain | 482-498 | Extracellular | ||||
Sequence: LFQTHAASEGPYAAQRD |
Keywords
- Cellular component
Disease & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_048174 | 91 | in dbSNP:rs12914008 | |||
Sequence: T → I | ||||||
Natural variant | VAR_013241 | 136 | in dbSNP:rs141876090 | |||
Sequence: R → W | ||||||
Natural variant | VAR_013242 | 140 | in dbSNP:rs56218866 | |||
Sequence: S → G | ||||||
Natural variant | VAR_013243 | 467 | in dbSNP:rs61737502 | |||
Sequence: M → V |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 556 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for signal, chain, glycosylation, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-21 | |||||
Sequence: MRRAPSLVLFFLVALCGRGNC | ||||||
Chain | PRO_0000000389 | 22-498 | Neuronal acetylcholine receptor subunit beta-4 | |||
Sequence: RVANAEEKLMDDLLNKTRYNNLIRPATSSSQLISIKLQLSLAQLISVNEREQIMTTNVWLKQEWTDYRLTWNSSRYEGVNILRIPAKRIWLPDIVLYNNADGTYEVSVYTNLIVRSNGSVLWLPPAIYKSACKIEVKYFPFDQQNCTLKFRSWTYDHTEIDMVLMTPTASMDDFTPSGEWDIVALPGRRTVNPQDPSYVDVTYDFIIKRKPLFYTINLIIPCVLTTLLAILVFYLPSDCGEKMTLCISVLLALTFFLLLISKIVPPTSLDVPLIGKYLMFTMVLVTFSIVTSVCVLNVHHRSPSTHTMAPWVKRCFLHKLPTFLFMKRPGPDSSPARAFPPSKSCVTKPEATATSTSPSNFYGNSMYFVNPASAASKSPAGSTPVAIPRDFWLRSSGRFRQDVQEALEGVSFIAQHMKNDDEDQSVVEDWKYVAMVVDRLFLWVFMFVCVLGTVGLFLPPLFQTHAASEGPYAAQRD | ||||||
Glycosylation | 36 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 93 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 138 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 153↔167 | |||||
Sequence: CKIEVKYFPFDQQNC | ||||||
Glycosylation | 166 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Subunit
Neuronal AChR is composed of two different types of subunits: alpha and beta. Beta-4 subunit can be combined to alpha-2, alpha-3 or alpha-4 to give rise to functional receptors. Interacts with RIC3; which is required for proper folding and assembly (PubMed:16120769).
Interacts with LYPD6 (PubMed:27344019).
The pentamer alpha3-beta-4 interacts with the conotoxin BuIA (By similarity).
The heteropentamer composed of alpha-3 and beta-4 subunits interacts with the alpha-conotoxin ImI (PubMed:15609996).
Interacts with LYPD6 (PubMed:27344019).
The pentamer alpha3-beta-4 interacts with the conotoxin BuIA (By similarity).
The heteropentamer composed of alpha-3 and beta-4 subunits interacts with the alpha-conotoxin ImI (PubMed:15609996).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P30926 | MEOX2 Q6FHY5 | 3 | EBI-9009018, EBI-16439278 |
Protein-protein interaction databases
Chemistry
Miscellaneous
Structure
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 357-377 | Disordered | ||||
Sequence: ARAFPPSKSCVTKPEATATST |
Sequence similarities
Belongs to the ligand-gated ion channel (TC 1.A.9) family. Acetylcholine receptor (TC 1.A.9.1) subfamily. Beta-4/CHRNB4 sub-subfamily.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
This entry describes 2 isoforms produced by Alternative splicing.
P30926-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- Length498
- Mass (Da)56,380
- Last updated1997-11-01 v2
- Checksum0D48AB203F3FD03E
P30926-2
- Name2
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
H3BU02 | H3BU02_HUMAN | CHRNB4 | 66 |
Features
Showing features for sequence conflict, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 72-73 | in Ref. 9; CAA48336 | ||||
Sequence: EQ → DE | ||||||
Alternative sequence | VSP_046674 | 120-217 | in isoform 2 | |||
Sequence: NADGTYEVSVYTNLIVRSNGSVLWLPPAIYKSACKIEVKYFPFDQQNCTLKFRSWTYDHTEIDMVLMTPTASMDDFTPSGEWDIVALPGRRTVNPQDP → KSLRTGSTWLWWWTGCSCGCSCLCASWALWGSSYRPSSRPMQLLRGPTLPSVTEGPLGCGVRGCEWPGGHFAASFWVVADEALSKYVSIGHQPHQTSHSRGTGKDGGLGCPL | ||||||
Sequence conflict | 121 | in Ref. 4; CAC34819 | ||||
Sequence: Missing | ||||||
Alternative sequence | VSP_046675 | 218-498 | in isoform 2 | |||
Sequence: Missing |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U62439 EMBL· GenBank· DDBJ | AAB40117.1 EMBL· GenBank· DDBJ | mRNA | ||
U48861 EMBL· GenBank· DDBJ | AAA92123.1 EMBL· GenBank· DDBJ | mRNA | ||
Y08416 EMBL· GenBank· DDBJ | CAA69693.1 EMBL· GenBank· DDBJ | mRNA | ||
AJ306454 EMBL· GenBank· DDBJ | CAC34819.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AJ306455 EMBL· GenBank· DDBJ | CAC34819.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AJ306456 EMBL· GenBank· DDBJ | CAC34819.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AJ306457 EMBL· GenBank· DDBJ | CAC34819.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AJ306458 EMBL· GenBank· DDBJ | CAC34819.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AJ306459 EMBL· GenBank· DDBJ | CAC34819.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF306329 EMBL· GenBank· DDBJ | AAL02062.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF306325 EMBL· GenBank· DDBJ | AAL02062.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF306326 EMBL· GenBank· DDBJ | AAL02062.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF306327 EMBL· GenBank· DDBJ | AAL02062.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF306328 EMBL· GenBank· DDBJ | AAL02062.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AC022748 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC067863 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC096080 EMBL· GenBank· DDBJ | AAH96080.1 EMBL· GenBank· DDBJ | mRNA | ||
BC096081 EMBL· GenBank· DDBJ | AAH96081.1 EMBL· GenBank· DDBJ | mRNA | ||
BC096083 EMBL· GenBank· DDBJ | AAH96083.1 EMBL· GenBank· DDBJ | mRNA | ||
BC096082 EMBL· GenBank· DDBJ | AAH96082.1 EMBL· GenBank· DDBJ | mRNA | ||
AF453877 EMBL· GenBank· DDBJ | AAL57840.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X68275 EMBL· GenBank· DDBJ | CAA48336.1 EMBL· GenBank· DDBJ | mRNA |