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Protein

Neuronal acetylcholine receptor subunit alpha-4

Gene

Chrna4

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 sodium ions.

GO - Molecular functioni

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

GO - Biological processi

  • chemical synaptic transmission, postsynaptic Source: GOC
  • neuromuscular synaptic transmission Source: GO_Central
  • positive regulation of dopamine secretion Source: RGD
  • protein heterooligomerization Source: RGD
  • regulation of acetylcholine-gated cation channel activity Source: RGD
  • response to nicotine Source: GO_Central
  • synaptic transmission, cholinergic Source: RGD
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:
Neuronal acetylcholine receptor subunit alpha-4
Gene namesi
Name:Chrna4
Synonyms:Acra4
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi2346. Chrna4.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini32 – 249218ExtracellularSequence analysisAdd
BLAST
Transmembranei250 – 27021HelicalSequence analysisAdd
BLAST
Transmembranei279 – 29921HelicalSequence analysisAdd
BLAST
Transmembranei313 – 33321HelicalSequence analysisAdd
BLAST
Topological domaini334 – 604271CytoplasmicSequence analysisAdd
BLAST
Transmembranei605 – 62521HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

  • acetylcholine-gated channel complex Source: RGD
  • cell junction Source: UniProtKB-KW
  • dendrite Source: RGD
  • membrane Source: RGD
  • neuronal cell body 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.
GuidetoPHARMACOLOGYi465.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3030Sequence analysisAdd
BLAST
Chaini31 – 630600Neuronal acetylcholine receptor subunit alpha-4PRO_0000000354Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi59 – 591N-linked (GlcNAc...)Sequence analysis
Glycosylationi109 – 1091N-linked (GlcNAc...)Sequence analysis
Disulfide bondi163 ↔ 177By similarity
Glycosylationi176 – 1761N-linked (GlcNAc...)Sequence analysis
Disulfide bondi227 ↔ 228Associated with receptor activationBy similarity
Lipidationi273 – 2731S-palmitoyl cysteine1 Publication
Modified residuei428 – 4281PhosphoserineCombined sources
Modified residuei542 – 5421PhosphoserineBy similarity
Modified residuei545 – 5451PhosphoserineBy similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Lipoprotein, Palmitate, Phosphoprotein

Proteomic databases

PaxDbiP09483.
PRIDEiP09483.

PTM databases

iPTMnetiP09483.
PhosphoSiteiP09483.
SwissPalmiP09483.

Expressioni

Tissue specificityi

In various regions of the central nervous system.

Interactioni

Subunit structurei

Neuronal AChR is composed of two different types of subunits: alpha and beta. Alpha-4 subunit can be combined to beta-2 or beta-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
Chrna5P204206EBI-7842410,EBI-10828372
Chrnb2P123906EBI-7842410,EBI-9008812
Chrnb4P123924EBI-7842410,EBI-9008856

GO - Molecular functioni

  • protein heterodimerization activity Source: RGD

Protein-protein interaction databases

IntActiP09483. 4 interactions.
MINTiMINT-198047.
STRINGi10116.ENSRNOP00000009041.

Chemistry

BindingDBiP09483.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1OLEmodel-A/C38-245[»]
ProteinModelPortaliP09483.
SMRiP09483. Positions 245-337.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3645. Eukaryota.
ENOG410XQGR. LUCA.
HOGENOMiHOG000006756.
HOVERGENiHBG003756.
InParanoidiP09483.
KOiK04806.
PhylomeDBiP09483.

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. 4 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. 2 hits.
TIGRFAMsiTIGR00860. LIC. 1 hit.
PROSITEiPS00236. NEUROTR_ION_CHANNEL. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform Alpha-4-1 (identifier: P09483-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MANSGTGAPP PLLLLPLLLL LGTGLLPASS HIETRAHAEE RLLKRLFSGY
60 70 80 90 100
NKWSRPVANI SDVVLVRFGL SIAQLIDVDE KNQMMTTNVW VKQEWHDYKL
110 120 130 140 150
RWDPGDYENV TSIRIPSELI WRPDIVLYNN ADGDFAVTHL TKAHLFYDGR
160 170 180 190 200
VQWTPPAIYK SSCSIDVTFF PFDQQNCTMK FGSWTYDKAK IDLVSMHSRV
210 220 230 240 250
DQLDFWESGE WVIVDAVGTY NTRKYECCAE IYPDITYAFI IRRLPLFYTI
260 270 280 290 300
NLIIPCLLIS CLTVLVFYLP SECGEKVTLC ISVLLSLTVF LLLITEIIPS
310 320 330 340 350
PTSLVIPLIG EYLLFTMIFV TLSIVITVFV LNVHHRSPRT HTMPAWVRRV
360 370 380 390 400
FLDIVPRLLF MKRPSVVKDN CRRLIESMHK MANAPRFWPE PVGEPGILSD
410 420 430 440 450
ICNQGLSPAP TFCNPTDTAV ETQPTCRSPP LEVPDLKTSE VEKASPCPSP
460 470 480 490 500
GSCPPPKSSS GAPMLIKARS LSVQHVPSSQ EAAEDGIRCR SRSIQYCVSQ
510 520 530 540 550
DGAASLADSK PTSSPTSLKA RPSQLPVSDQ ASPCKCTCKE PSPVSPVTVL
560 570 580 590 600
KAGGTKAPPQ HLPLSPALTR AVEGVQYIAD HLKAEDTDFS VKEDWKYVAM
610 620 630
VIDRIFLWMF IIVCLLGTVG LFLPPWLAAC
Length:630
Mass (Da):70,193
Last modified:May 30, 2000 - v3
Checksum:i1DFFC9E1378E5417
GO
Isoform Alpha-4-2 (identifier: P09483-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     629-630: AC → GMI

Show »
Length:631
Mass (Da):70,320
Checksum:i7F35DA69E1378E54
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1 – 44MANS → MEIGGPGA in AAA41676 (PubMed:3829125).Curated
Sequence conflicti6 – 61T → P in AAB64439 (Ref. 3) Curated
Sequence conflicti58 – 581A → G in AAA41676 (PubMed:3829125).Curated
Sequence conflicti58 – 581A → G in AAB64439 (Ref. 3) Curated
Sequence conflicti196 – 1961M → I in AAA41676 (PubMed:3829125).Curated
Sequence conflicti196 – 1961M → I in AAB64439 (Ref. 3) Curated
Sequence conflicti301 – 3011Missing in AAA41676 (PubMed:3829125).Curated
Sequence conflicti301 – 3011Missing in AAC97071 (PubMed:3829125).Curated
Sequence conflicti301 – 3011Missing in AAB64439 (Ref. 3) Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei629 – 6302AC → GMI in isoform Alpha-4-2. 2 PublicationsVSP_000074

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M15682 mRNA. Translation: AAA41676.1.
L31620 mRNA. Translation: AAC97071.1.
AF007212 mRNA. Translation: AAB64439.1.
RefSeqiNP_077330.1. NM_024354.1.
UniGeneiRn.9697.

Genome annotation databases

GeneIDi25590.
KEGGirno:25590.
UCSCiRGD:2346. rat. [P09483-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M15682 mRNA. Translation: AAA41676.1.
L31620 mRNA. Translation: AAC97071.1.
AF007212 mRNA. Translation: AAB64439.1.
RefSeqiNP_077330.1. NM_024354.1.
UniGeneiRn.9697.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1OLEmodel-A/C38-245[»]
ProteinModelPortaliP09483.
SMRiP09483. Positions 245-337.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP09483. 4 interactions.
MINTiMINT-198047.
STRINGi10116.ENSRNOP00000009041.

Chemistry

BindingDBiP09483.
ChEMBLiCHEMBL2094110.
GuidetoPHARMACOLOGYi465.

PTM databases

iPTMnetiP09483.
PhosphoSiteiP09483.
SwissPalmiP09483.

Proteomic databases

PaxDbiP09483.
PRIDEiP09483.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi25590.
KEGGirno:25590.
UCSCiRGD:2346. rat. [P09483-1]

Organism-specific databases

CTDi1137.
RGDi2346. Chrna4.

Phylogenomic databases

eggNOGiKOG3645. Eukaryota.
ENOG410XQGR. LUCA.
HOGENOMiHOG000006756.
HOVERGENiHBG003756.
InParanoidiP09483.
KOiK04806.
PhylomeDBiP09483.

Miscellaneous databases

PROiP09483.

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. 4 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. 2 hits.
TIGRFAMsiTIGR00860. LIC. 1 hit.
PROSITEiPS00236. NEUROTR_ION_CHANNEL. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Members of a nicotinic acetylcholine receptor gene family are expressed in different regions of the mammalian central nervous system."
    Goldman D.J., Deneris E.S., Luyten W., Kochhar A., Patrick J., Heinemann S.F.
    Cell 48:965-973(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA-4-1), NUCLEOTIDE SEQUENCE [MRNA] OF 5-630 (ISOFORM ALPHA-4-2).
    Strain: Sprague-Dawley.
    Tissue: Hippocampus and Hypothalamus.
  2. Hartley M., Goldman D.J., Heinemann S.F.
    Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION.
  3. Boulter J., Deneris E.S., Evans K., Heinemann S.F.
    Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA-4-2).
  4. "Neuronal nicotinic acetylcholine receptor beta-subunit is coded for by the cDNA clone alpha 4."
    Whiting P., Esch F., Shimasaki S., Lindstrom J.
    FEBS Lett. 219:459-463(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 31-47.
  5. "A highly conserved cytoplasmic cysteine residue in the alpha4 nicotinic acetylcholine receptor is palmitoylated and regulates protein expression."
    Amici S.A., McKay S.B., Wells G.B., Robson J.I., Nasir M., Ponath G., Anand R.
    J. Biol. Chem. 287:23119-23127(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PALMITOYLATION AT CYS-273, SUBCELLULAR LOCATION.
  6. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-428, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiACHA4_RAT
AccessioniPrimary (citable) accession number: P09483
Secondary accession number(s): O35769
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: May 30, 2000
Last modified: July 6, 2016
This is version 152 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, 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.