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O70174 (ACHA4_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 124. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Neuronal acetylcholine receptor subunit alpha-4
Gene names
Name:Chrna4
Synonyms:Acra4
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length629 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

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 permeable to sodium ions.

Subunit structure

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.

Subcellular location

Cell junctionsynapsepostsynaptic cell membrane; Multi-pass membrane protein. Cell membrane; Multi-pass membrane protein. Cell membrane; Lipid-anchor By similarity.

Sequence similarities

Belongs to the ligand-gated ion channel (TC 1.A.9) family. Acetylcholine receptor (TC 1.A.9.1) subfamily. Alpha-4/CHRNA4 sub-subfamily. [View classification]

Ontologies

Keywords
   Biological processIon transport
Transport
   Cellular componentCell junction
Cell membrane
Membrane
Postsynaptic cell membrane
Synapse
   Coding sequence diversityPolymorphism
   DomainSignal
Transmembrane
Transmembrane helix
   Molecular functionIon channel
Ligand-gated ion channel
Receptor
   PTMDisulfide bond
Glycoprotein
Lipoprotein
Palmitate
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processB cell activation

Inferred from mutant phenotype PubMed 15963492. Source: MGI

DNA repair

Inferred from electronic annotation. Source: Ensembl

action potential

Inferred from mutant phenotype PubMed 10235262. Source: MGI

behavioral response to nicotine

Inferred from mutant phenotype PubMed 15528443. Source: MGI

calcium ion transport

Inferred from genetic interaction PubMed 15569257. Source: MGI

cognition

Inferred from electronic annotation. Source: Ensembl

exploration behavior

Inferred from mutant phenotype PubMed 10964949. Source: MGI

ion transmembrane transport

Inferred from direct assay PubMed 11906696. Source: GOC

locomotory behavior

Inferred from mutant phenotype PubMed 11226318. Source: MGI

membrane depolarization

Inferred from mutant phenotype PubMed 11222635PubMed 11226318PubMed 12944511. Source: MGI

neurological system process

Inferred from mutant phenotype PubMed 17146052. Source: MGI

regulation of dopamine secretion

Inferred from mutant phenotype PubMed 12944511. Source: MGI

regulation of inhibitory postsynaptic membrane potential

Inferred from mutant phenotype PubMed 17146052. Source: MGI

regulation of membrane potential

Inferred from genetic interaction PubMed 15569257. Source: MGI

respiratory gaseous exchange

Inferred from mutant phenotype PubMed 21606356. Source: MGI

response to hypoxia

Inferred from electronic annotation. Source: Ensembl

response to nicotine

Inferred from mutant phenotype PubMed 10235262. Source: MGI

response to oxidative stress

Inferred from electronic annotation. Source: Ensembl

sensory perception of pain

Inferred from mutant phenotype PubMed 10235262. Source: MGI

synaptic transmission, cholinergic

Inferred from direct assay PubMed 11906696. Source: MGI

   Cellular_componentacetylcholine-gated channel complex

Inferred from direct assay PubMed 12944511. Source: MGI

cell junction

Inferred from electronic annotation. Source: UniProtKB-KW

external side of plasma membrane

Inferred from direct assay PubMed 15963492. Source: MGI

membrane

Inferred from direct assay PubMed 11906696. Source: MGI

plasma membrane

Inferred from direct assay PubMed 15741168. Source: MGI

postsynaptic membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionacetylcholine receptor activity

Inferred from electronic annotation. Source: Ensembl

acetylcholine-activated cation-selective channel activity

Inferred from mutant phenotype PubMed 11222635PubMed 12130686PubMed 15528443. Source: MGI

ion channel activity

Inferred from direct assay PubMed 11906696. Source: MGI

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3030 Potential
Chain31 – 629599Neuronal acetylcholine receptor subunit alpha-4
PRO_0000000352

Regions

Topological domain32 – 249218Extracellular Potential
Transmembrane250 – 27021Helical; Potential
Transmembrane279 – 29921Helical; Potential
Transmembrane312 – 33221Helical; Potential
Topological domain333 – 603271Cytoplasmic Potential
Transmembrane604 – 62421Helical; Potential

Amino acid modifications

Lipidation2731S-palmitoyl cysteine By similarity
Glycosylation591N-linked (GlcNAc...) Potential
Glycosylation1091N-linked (GlcNAc...) Potential
Glycosylation1761N-linked (GlcNAc...) Potential
Disulfide bond163 ↔ 177 By similarity
Disulfide bond227 ↔ 228Associated with receptor activation By similarity

Natural variations

Natural variant5291T → A. Ref.1

Experimental info

Sequence conflict161P → L in AAF34716. Ref.1
Sequence conflict241G → A in BAA25752. Ref.4
Sequence conflict1341D → N in AAF34716. Ref.1

Sequences

Sequence LengthMass (Da)Tools
O70174 [UniParc].

Last modified September 19, 2003. Version 2.
Checksum: 261455B6ED50B41C

FASTA62970,305
        10         20         30         40         50         60 
MEIGGSGAPP PLLLLPLLLL LGTGLLPASS HIETRAHAEE RLLKRLFSGY NKWSRPVANI 

        70         80         90        100        110        120 
SDVVLVRFGL SIAQLIDVDE KNQMMTTNVW VKQEWHDYKL RWDPGDYENV TSIRIPSELI 

       130        140        150        160        170        180 
WRPDIVLYNN ADGDFAVTHL TKAHLFYDGR VQWTPPAIYK SSCSIDVTFF PFDQQNCTMK 

       190        200        210        220        230        240 
FGSWTYDKAK IDLVSMHSRV DQLDFWESGE WVIVDAVGTY NTRKYECCAE IYPDITYAFI 

       250        260        270        280        290        300 
IRRLPLFYTI NLIIPCLLIS CLTVLVFYLP SECGEKVTLC ISVLLSLTVF LLLITEIIPS 

       310        320        330        340        350        360 
TSLVIPLIGE YLLFTMIFVT LSIVITVFVL NVHHRSPRTH TMPAWVRRVF LDIVPRLLFM 

       370        380        390        400        410        420 
KRPSVVKDNC RRLIESMHKM ANAPRFWPEP ESEPGILGDI CNQGLSPAPT FCNRMDTAVE 

       430        440        450        460        470        480 
TQPTCRSPSH KVPDLKTSEV EKASPCPSPG SCHPPNSSGA PVLIKARSLS VQHVPSSQEA 

       490        500        510        520        530        540 
AEGSIRCRSR SIQYCVSQDG AASLTESKPT GSPASLKTRP SQLPVSDQTS PCKCTCKEPS 

       550        560        570        580        590        600 
PVSPITVLKA GGTKAPPQHL PLSPALTRAV EGVQYIADHL KAEDTDFSVK EDWKYVAMVI 

       610        620 
DRIFLWMFII VCLLGTVGLF LPPWLAGMI 

« Hide

References

« Hide 'large scale' references
[1]"Long sleep and short sleep mice differ in nicotine-stimulated 86Rb+ efflux and alpha4 nicotinic receptor subunit cDNA sequence."
Stitzel J.A., Dobelis P., Jimenez M., Collins A.C.
Pharmacogenetics 11:331-339(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ALA-529.
Strain: Long sleep selected line.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Diencephalon and Hippocampus.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6.
Tissue: Brain.
[4]"Promoter analysis of the neuronal nicotinic acetylcholine receptor alpha4 gene: methylation and expression of the transgene."
Watanabe H., Zoli M., Changeux J.-P.
Eur. J. Neurosci. 10:2244-2253(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-27.
[5]"Expression of mouse nicotinic acetylcholine receptor genes in the developing thymus."
Kuo Y.-P., Lukas R.J.
Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 118-357.
Strain: C57BL/6.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF225912 mRNA. Translation: AAF34716.2.
AK034228 mRNA. Translation: BAC28638.1.
AK083157 mRNA. Translation: BAC38788.1.
BC053013 mRNA. Translation: AAH53013.1.
AB010002 Genomic DNA. Translation: BAA25752.1.
AF325347 mRNA. Translation: AAL37363.1.
RefSeqNP_056545.3. NM_015730.5.
UniGeneMm.252369.

3D structure databases

ProteinModelPortalO70174.
SMRO70174. Positions 39-341, 600-627.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid197932. 1 interaction.
DIPDIP-48731N.

Chemistry

BindingDBO70174.

PTM databases

PhosphoSiteO70174.

Proteomic databases

PaxDbO70174.
PRIDEO70174.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000067120; ENSMUSP00000066338; ENSMUSG00000027577.
GeneID11438.
KEGGmmu:11438.
UCSCuc008okq.1. mouse.

Organism-specific databases

CTD1137.
MGIMGI:87888. Chrna4.

Phylogenomic databases

eggNOGNOG290206.
HOGENOMHOG000006756.
HOVERGENHBG003756.
KOK04806.
PhylomeDBO70174.
TreeFamTF315605.

Gene expression databases

BgeeO70174.
GenevestigatorO70174.

Family and domain databases

Gene3D1.20.120.370. 2 hits.
2.70.170.10. 1 hit.
InterProIPR027361. 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]
PANTHERPTHR18945. PTHR18945. 1 hit.
PfamPF02931. Neur_chan_LBD. 1 hit.
PF02932. Neur_chan_memb. 1 hit.
[Graphical view]
PRINTSPR00254. NICOTINICR.
PR00252. NRIONCHANNEL.
SUPFAMSSF63712. SSF63712. 1 hit.
SSF90112. SSF90112. 2 hits.
TIGRFAMsTIGR00860. LIC. 1 hit.
PROSITEPS00236. NEUROTR_ION_CHANNEL. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCHRNA4. mouse.
NextBio278736.
PROO70174.
SOURCESearch...

Entry information

Entry nameACHA4_MOUSE
AccessionPrimary (citable) accession number: O70174
Secondary accession number(s): Q8BHE9, Q8VI10, Q9ET51
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: September 19, 2003
Last modified: April 16, 2014
This is version 124 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot