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Protein

Neuronal acetylcholine receptor subunit beta-2

Gene

Chrnb2

Organism
Rattus norvegicus (Rat)
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 permeable to sodiun ions.

GO - Molecular functioni

  • acetylcholine-activated cation-selective channel activity Source: RGD
  • acetylcholine binding Source: RGD
  • acetylcholine receptor activity Source: Ensembl
  • drug binding Source: RGD
  • protein heterodimerization activity Source: RGD

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ion channel, Ligand-gated ion channel, Receptor

Keywords - Biological processi

Ion transport, Transport

Enzyme and pathway databases

ReactomeiR-RNO-629587. Highly sodium permeable acetylcholine nicotinic receptors.
R-RNO-629597. Highly calcium permeable nicotinic acetylcholine receptors.

Names & Taxonomyi

Protein namesi
Recommended name:
Neuronal acetylcholine receptor subunit beta-2
Alternative name(s):
Neuronal acetylcholine receptor non-alpha-1 chain
Short name:
N-alpha 1
Gene namesi
Name:Chrnb2
Synonyms:Acrb2
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 2

Organism-specific databases

RGDi2350. Chrnb2.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini25 – 237213ExtracellularSequence analysisAdd
BLAST
Transmembranei238 – 25821HelicalSequence analysisAdd
BLAST
Topological domaini259 – 2668CytoplasmicSequence analysis
Transmembranei267 – 28721HelicalSequence analysisAdd
BLAST
Topological domaini288 – 29912ExtracellularSequence analysisAdd
BLAST
Transmembranei300 – 32021HelicalSequence analysisAdd
BLAST
Topological domaini321 – 458138CytoplasmicSequence analysisAdd
BLAST
Transmembranei459 – 47921HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

  • acetylcholine-gated channel complex Source: RGD
  • cell junction Source: UniProtKB-KW
  • external side of plasma membrane Source: Ensembl
  • membrane Source: RGD
  • plasma membrane Source: RGD
  • postsynaptic membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

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

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL2094110.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2424Sequence analysisAdd
BLAST
Chaini25 – 500476Neuronal acetylcholine receptor subunit beta-2PRO_0000000381Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi50 – 501N-linked (GlcNAc...)Sequence analysis
Disulfide bondi154 ↔ 168By similarity
Glycosylationi167 – 1671N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiP12390.
PRIDEiP12390.

PTM databases

SwissPalmiP12390.

Expressioni

Tissue specificityi

Expressed in most regions of the CNS.

Gene expression databases

GenevisibleiP12390. RN.

Interactioni

Subunit structurei

Neuronal AChR is composed of two different types of subunits: alpha and beta. Beta-2 subunit can be combined to alpha-2, alpha-3 or alpha-4 to give rise to functional receptors, complexes with beta-2 may be heteropentamers. Interacts with RIC3; which is required for proper folding and assembly (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
Chrna4P094836EBI-9008812,EBI-7842410

GO - Molecular functioni

  • protein heterodimerization activity Source: RGD

Protein-protein interaction databases

IntActiP12390. 4 interactions.
STRINGi10116.ENSRNOP00000028200.

Chemistry

BindingDBiP12390.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1OLEmodel-B/D/E27-233[»]
1OLFmodel-B/D/E27-233[»]
ProteinModelPortaliP12390.
SMRiP12390. Positions 230-324.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3645. Eukaryota.
ENOG410XQGR. LUCA.
GeneTreeiENSGT00760000118930.
HOGENOMiHOG000006757.
HOVERGENiHBG003756.
InParanoidiP12390.
KOiK04813.
OMAiKEDSDPC.
OrthoDBiEOG72JWGV.
PhylomeDBiP12390.
TreeFamiTF315605.

Family and domain databases

Gene3Di1.20.120.370. 2 hits.
2.70.170.10. 1 hit.
InterProiIPR027361. Acetylcholine_rcpt_TM.
IPR032932. CHRNB2.
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. 2 hits.
PTHR18945:SF80. PTHR18945:SF80. 2 hits.
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.

P12390-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAGHSNSMAL FSFSLLWLCS GVLGTDTEER LVEHLLDPSR YNKLIRPATN
60 70 80 90 100
GSELVTVQLM VSLAQLISVH EREQIMTTNV WLTQEWEDYR LTWKPEDFDN
110 120 130 140 150
MKKVRLPSKH IWLPDVVLYN NADGMYEVSF YSNAVVSYDG SIFWLPPAIY
160 170 180 190 200
KSACKIEVKH FPFDQQNCTM KFRSWTYDRT EIDLVLKSDV ASLDDFTPSG
210 220 230 240 250
EWDIIALPGR RNENPDDSTY VDITYDFIIR RKPLFYTINL IIPCVLITSL
260 270 280 290 300
AILVFYLPSD CGEKMTLCIS VLLALTVFLL LISKIVPPTS LDVPLVGKYL
310 320 330 340 350
MFTMVLVTFS IVTSVCVLNV HHRSPTTHTM APWVKVVFLE KLPTLLFLQQ
360 370 380 390 400
PRHRCARQRL RLRRRQRERE GAGALFFREG PAADPCTCFV NPASVQGLAG
410 420 430 440 450
AFRAEPTAAG PGRSVGPCSC GLREAVDGVR FIADHMRSED DDQSVREDWK
460 470 480 490 500
YVAMVIDRLF LWIFVFVCVF GTVGMFLQPL FQNYTATTFL HPDHSAPSSK
Length:500
Mass (Da):56,909
Last modified:May 30, 2000 - v2
Checksum:i54C007A48225931C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L31622 mRNA. Translation: AAC78724.1.
AY574258 mRNA. Translation: AAS90354.1.
PIRiJH0174.
RefSeqiNP_062170.1. NM_019297.1.
UniGeneiRn.53978.

Genome annotation databases

EnsembliENSRNOT00000028200; ENSRNOP00000028200; ENSRNOG00000020778.
GeneIDi54239.
KEGGirno:54239.
UCSCiRGD:2350. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L31622 mRNA. Translation: AAC78724.1.
AY574258 mRNA. Translation: AAS90354.1.
PIRiJH0174.
RefSeqiNP_062170.1. NM_019297.1.
UniGeneiRn.53978.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1OLEmodel-B/D/E27-233[»]
1OLFmodel-B/D/E27-233[»]
ProteinModelPortaliP12390.
SMRiP12390. Positions 230-324.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP12390. 4 interactions.
STRINGi10116.ENSRNOP00000028200.

Chemistry

BindingDBiP12390.
ChEMBLiCHEMBL2094110.

PTM databases

SwissPalmiP12390.

Proteomic databases

PaxDbiP12390.
PRIDEiP12390.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000028200; ENSRNOP00000028200; ENSRNOG00000020778.
GeneIDi54239.
KEGGirno:54239.
UCSCiRGD:2350. rat.

Organism-specific databases

CTDi1141.
RGDi2350. Chrnb2.

Phylogenomic databases

eggNOGiKOG3645. Eukaryota.
ENOG410XQGR. LUCA.
GeneTreeiENSGT00760000118930.
HOGENOMiHOG000006757.
HOVERGENiHBG003756.
InParanoidiP12390.
KOiK04813.
OMAiKEDSDPC.
OrthoDBiEOG72JWGV.
PhylomeDBiP12390.
TreeFamiTF315605.

Enzyme and pathway databases

ReactomeiR-RNO-629587. Highly sodium permeable acetylcholine nicotinic receptors.
R-RNO-629597. Highly calcium permeable nicotinic acetylcholine receptors.

Miscellaneous databases

PROiP12390.

Gene expression databases

GenevisibleiP12390. RN.

Family and domain databases

Gene3Di1.20.120.370. 2 hits.
2.70.170.10. 1 hit.
InterProiIPR027361. Acetylcholine_rcpt_TM.
IPR032932. CHRNB2.
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. 2 hits.
PTHR18945:SF80. PTHR18945:SF80. 2 hits.
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 structure and expression of beta 2: a novel subunit of neuronal nicotinic acetylcholine receptors."
    Deneris E.S., Connolly J.G., Boulter J., Wada E., Wada K., Swanson L.W., Patrick J., Heinemann S.F.
    Neuron 1:45-54(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Functional expression of two neuronal nicotinic acetylcholine receptors from cDNA clones identifies a gene family."
    Boulter J., Connolly J.G., Deneris E.S., Goldman D.J., Heinemann S.F., Patrick J.
    Proc. Natl. Acad. Sci. U.S.A. 84:7763-7767(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. Hartley M.
    Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION.
  4. Groot-Kormelink P.J.
    Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Sprague-Dawley.
    Tissue: Brain.

Entry informationi

Entry nameiACHB2_RAT
AccessioniPrimary (citable) accession number: P12390
Secondary accession number(s): Q53YK1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: May 30, 2000
Last modified: July 6, 2016
This is version 143 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

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.