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Protein

Acetylcholine receptor subunit beta

Gene

CHRNB1

Organism
Tetronarce californica (Pacific electric ray) (Torpedo californica)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Ion channel, Ligand-gated ion channel, Receptor

Keywords - Biological processi

Ion transport, Transport

Names & Taxonomyi

Protein namesi
Recommended name:
Acetylcholine receptor subunit beta
Gene namesi
Name:CHRNB1
OrganismiTetronarce californica (Pacific electric ray) (Torpedo californica)
Taxonomic identifieri7787 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataChondrichthyesElasmobranchiiBatoideaTorpediniformesTorpedinidaeTetronarce

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini25 – 240216ExtracellularSequence analysisAdd
BLAST
Transmembranei241 – 26525HelicalSequence analysisAdd
BLAST
Transmembranei273 – 29119HelicalSequence analysisAdd
BLAST
Transmembranei307 – 32822HelicalSequence analysisAdd
BLAST
Topological domaini329 – 461133CytoplasmicSequence analysisAdd
BLAST
Transmembranei462 – 48019HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Membrane, Postsynaptic cell membrane, Synapse

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL2096975.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 24241 PublicationAdd
BLAST
Chaini25 – 493469Acetylcholine receptor subunit betaPRO_0000000319Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi152 ↔ 1661 Publication
Glycosylationi165 – 1651N-linked (GlcNAc...)1 Publication
Modified residuei379 – 3791Phosphotyrosine; by Tyr-kinases1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

PTM databases

iPTMnetiP02712.
SwissPalmiP02712.
UniCarbKBiP02712.

Interactioni

Subunit structurei

Pentamer of two alpha chains, and one each of the beta, delta, and gamma chains.

Protein-protein interaction databases

IntActiP02712. 2 interactions.

Chemistry

BindingDBiP02712.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1LK1model-G26-241[»]
1OEDelectron microscopy4.00B241-490[»]
1OLKmodel-E23-241[»]
ProteinModelPortaliP02712.
SMRiP02712. Positions 25-493.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP02712.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

HOVERGENiHBG003756.

Family and domain databases

Gene3Di1.20.120.370. 2 hits.
2.70.170.10. 1 hit.
InterProiIPR027361. Acetylcholine_rcpt_TM.
IPR006202. Neur_chan_lig-bd.
IPR006201. Neur_channel.
IPR006029. Neurotrans-gated_channel_TM.
IPR018000. Neurotransmitter_ion_chnl_CS.
IPR002394. Nicotinic_acetylcholine_rcpt.
[Graphical view]
PANTHERiPTHR18945. PTHR18945. 1 hit.
PfamiPF02931. Neur_chan_LBD. 1 hit.
PF02932. Neur_chan_memb. 1 hit.
[Graphical view]
PRINTSiPR00254. NICOTINICR.
PR00252. NRIONCHANNEL.
SUPFAMiSSF63712. SSF63712. 1 hit.
SSF90112. SSF90112. 1 hit.
TIGRFAMsiTIGR00860. LIC. 1 hit.
PROSITEiPS00236. NEUROTR_ION_CHANNEL. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P02712-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MENVRRMALG LVVMMALALS GVGASVMEDT LLSVLFETYN PKVRPAQTVG
60 70 80 90 100
DKVTVRVGLT LTNLLILNEK IEEMTTNVFL NLAWTDYRLQ WDPAAYEGIK
110 120 130 140 150
DLRIPSSDVW QPDIVLMNNN DGSFEITLHV NVLVQHTGAV SWQPSAIYRS
160 170 180 190 200
SCTIKVMYFP FDWQNCTMVF KSYTYDTSEV TLQHALDAKG EREVKEIVIN
210 220 230 240 250
KDAFTENGQW SIEHKPSRKN WRSDDPSYED VTFYLIIQRK PLFYIVYTII
260 270 280 290 300
PCILISILAI LVFYLPPDAG EKMSLSISAL LAVTVFLLLL ADKVPETSLS
310 320 330 340 350
VPIIIRYLMF IMILVAFSVI LSVVVLNLHH RSPNTHTMPN WIRQIFIETL
360 370 380 390 400
PPFLWIQRPV TTPSPDSKPT IISRANDEYF IRKPAGDFVC PVDNARVAVQ
410 420 430 440 450
PERLFSEMKW HLNGLTQPVT LPQDLKEAVE AIKYIAEQLE SASEFDDLKK
460 470 480 490
DWQYVAMVAD RLFLYVFFVI CSIGTFSIFL DASHNVPPDN PFA
Length:493
Mass (Da):56,156
Last modified:July 21, 1986 - v1
Checksum:i4E145192584D8F5F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti75 – 751T → R AA sequence (PubMed:7384786).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti3 – 31N → D in a second clone.
Natural varianti11 – 111L → V in a second clone.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J00964 mRNA. Translation: AAA49274.1.
PIRiA93294. ACRYB1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J00964 mRNA. Translation: AAA49274.1.
PIRiA93294. ACRYB1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1LK1model-G26-241[»]
1OEDelectron microscopy4.00B241-490[»]
1OLKmodel-E23-241[»]
ProteinModelPortaliP02712.
SMRiP02712. Positions 25-493.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP02712. 2 interactions.

Chemistry

BindingDBiP02712.
ChEMBLiCHEMBL2096975.

PTM databases

iPTMnetiP02712.
SwissPalmiP02712.
UniCarbKBiP02712.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG003756.

Miscellaneous databases

EvolutionaryTraceiP02712.

Family and domain databases

Gene3Di1.20.120.370. 2 hits.
2.70.170.10. 1 hit.
InterProiIPR027361. Acetylcholine_rcpt_TM.
IPR006202. Neur_chan_lig-bd.
IPR006201. Neur_channel.
IPR006029. Neurotrans-gated_channel_TM.
IPR018000. Neurotransmitter_ion_chnl_CS.
IPR002394. Nicotinic_acetylcholine_rcpt.
[Graphical view]
PANTHERiPTHR18945. PTHR18945. 1 hit.
PfamiPF02931. Neur_chan_LBD. 1 hit.
PF02932. Neur_chan_memb. 1 hit.
[Graphical view]
PRINTSiPR00254. NICOTINICR.
PR00252. NRIONCHANNEL.
SUPFAMiSSF63712. SSF63712. 1 hit.
SSF90112. SSF90112. 1 hit.
TIGRFAMsiTIGR00860. LIC. 1 hit.
PROSITEiPS00236. NEUROTR_ION_CHANNEL. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Primary structures of beta- and delta-subunit precursors of Torpedo californica acetylcholine receptor deduced from cDNA sequences."
    Noda M., Takahashi H., Tanabe T., Toyosato M., Kikyotani S., Hirose T., Asai M., Takashima H., Inayama S., Miyata T., Numa S.
    Nature 301:251-255(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Acetylcholine receptor: complex of homologous subunits."
    Raftery M.A., Hunkapiller M.W., Strader C.D., Hood L.E.
    Science 208:1454-1457(1980) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 25-78.
  3. "Assessment of the number of free cysteines and isolation and identification of cystine-containing peptides from acetylcholine receptor."
    Kellaris K.V., Ware D.K., Smith S., Kyte J.
    Biochemistry 28:3469-3482(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 126-147, GLYCOSYLATION AT ASN-165, DISULFIDE BOND.
  4. "Determination of the tyrosine phosphorylation sites of the nicotinic acetylcholine receptor."
    Wagner K., Edson K., Heginbotham L., Post M., Huganir R.L., Czernik A.J.
    J. Biol. Chem. 266:23784-23789(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT TYR-379.

Entry informationi

Entry nameiACHB_TETCF
AccessioniPrimary (citable) accession number: P02712
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: April 13, 2016
This is version 119 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

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.