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Protein

Acetylcholine receptor subunit alpha

Gene

Chrna1

Organism
Mus musculus (Mouse)
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

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-MMU-629594. Highly calcium permeable postsynaptic nicotinic acetylcholine receptors.
R-MMU-629597. Highly calcium permeable nicotinic acetylcholine receptors.

Names & Taxonomyi

Protein namesi
Recommended name:
Acetylcholine receptor subunit alpha
Gene namesi
Name:Chrna1
Synonyms:Acra
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:87885. Chrna1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini21 – 230210ExtracellularAdd
BLAST
Transmembranei231 – 25525HelicalAdd
BLAST
Transmembranei263 – 28119HelicalAdd
BLAST
Transmembranei297 – 31620HelicalAdd
BLAST
Topological domaini317 – 428112CytoplasmicAdd
BLAST
Transmembranei429 – 44719HelicalAdd
BLAST

GO - Cellular componenti

  • acetylcholine-gated channel complex Source: MGI
  • cell junction Source: UniProtKB-KW
  • cell surface Source: MGI
  • membrane Source: MGI
  • neuromuscular junction Source: MGI
  • plasma membrane Source: MGI
  • postsynaptic membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

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

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL3137264.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020Add
BLAST
Chaini21 – 457437Acetylcholine receptor subunit alphaPRO_0000000306Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi148 ↔ 1621 Publication
Glycosylationi161 – 1611N-linked (GlcNAc...)1 Publication
Disulfide bondi212 ↔ 213Associated with receptor activation1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiP04756.
PRIDEiP04756.

PTM databases

iPTMnetiP04756.
PhosphoSiteiP04756.
SwissPalmiP04756.

Expressioni

Gene expression databases

BgeeiP04756.
ExpressionAtlasiP04756. baseline and differential.
GenevisibleiP04756. MM.

Interactioni

Subunit structurei

Pentamer of two alpha chains, and one each of the beta, delta, and gamma (in immature muscle) or epsilon (in mature muscle) chains.1 Publication

Protein-protein interaction databases

BioGridi197931. 4 interactions.
DIPiDIP-59594N.
IntActiP04756. 1 interaction.
MINTiMINT-8388618.
STRINGi10090.ENSMUSP00000028515.

Chemistry

BindingDBiP04756.

Structurei

Secondary structure

1
457
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi22 – 3211Combined sources
Beta strandi37 – 393Combined sources
Beta strandi49 – 6416Combined sources
Turni65 – 684Combined sources
Beta strandi69 – 8113Combined sources
Helixi89 – 924Combined sources
Beta strandi97 – 1004Combined sources
Helixi102 – 1043Combined sources
Beta strandi110 – 1123Combined sources
Turni116 – 1183Combined sources
Beta strandi128 – 1314Combined sources
Beta strandi135 – 1384Combined sources
Beta strandi141 – 15010Combined sources
Beta strandi153 – 1564Combined sources
Beta strandi159 – 17012Combined sources
Turni173 – 1753Combined sources
Beta strandi176 – 1816Combined sources
Beta strandi194 – 21017Combined sources
Beta strandi218 – 22912Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2QC1X-ray1.94B21-231[»]
ProteinModelPortaliP04756.
SMRiP04756. Positions 21-335, 423-457.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP04756.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3645. Eukaryota.
ENOG410XQGR. LUCA.
HOGENOMiHOG000006756.
HOVERGENiHBG003756.
InParanoidiP04756.
KOiK04803.
OMAiRANKHVS.
OrthoDBiEOG72JWGV.
PhylomeDBiP04756.
TreeFamiTF315605.

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.

P04756-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MELSTVLLLL GLCSAGLVLG SEHETRLVAK LFEDYSSVVR PVEDHREIVQ
60 70 80 90 100
VTVGLQLIQL INVDEVNQIV TTNVRLKQQW VDYNLKWNPD DYGGVKKIHI
110 120 130 140 150
PSEKIWRPDV VLYNNADGDF AIVKFTKVLL DYTGHITWTP PAIFKSYCEI
160 170 180 190 200
IVTHFPFDEQ NCSMKLGTWT YDGSVVAINP ESDQPDLSNF MESGEWVIKE
210 220 230 240 250
ARGWKHWVFY SCCPTTPYLD ITYHFVMQRL PLYFIVNVII PCLLFSFLTS
260 270 280 290 300
LVFYLPTDSG EKMTLSISVL LSLTVFLLVI VELIPSTSSA VPLIGKYMLF
310 320 330 340 350
TMVFVIASII ITVIVINTHH RSPSTHIMPE WVRKVFIDTI PNIMFFSTMK
360 370 380 390 400
RPSRDKQEKR IFTEDIDISD ISGKPGPPPM GFHSPLIKHP EVKSAIEGVK
410 420 430 440 450
YIAETMKSDQ ESNNAAEEWK YVAMVMDHIL LGVFMLVCLI GTLAVFAGRL

IELHQQG
Length:457
Mass (Da):51,939
Last modified:August 13, 1987 - v1
Checksum:i5CB606D144F29436
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti13 – 131C → S in AAB53942 (Ref. 2) Curated
Sequence conflicti13 – 131C → S no nucleotide entry (PubMed:2993547).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X03986 mRNA. Translation: CAA27624.1.
M17640 mRNA. Translation: AAB53942.1.
AK029177 mRNA. Translation: BAC26337.1.
CCDSiCCDS16132.1.
PIRiA24383.
I49458.
RefSeqiNP_031415.2. NM_007389.5.
UniGeneiMm.4583.

Genome annotation databases

EnsembliENSMUST00000028515; ENSMUSP00000028515; ENSMUSG00000027107.
GeneIDi11435.
KEGGimmu:11435.
UCSCiuc008kcy.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X03986 mRNA. Translation: CAA27624.1.
M17640 mRNA. Translation: AAB53942.1.
AK029177 mRNA. Translation: BAC26337.1.
CCDSiCCDS16132.1.
PIRiA24383.
I49458.
RefSeqiNP_031415.2. NM_007389.5.
UniGeneiMm.4583.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2QC1X-ray1.94B21-231[»]
ProteinModelPortaliP04756.
SMRiP04756. Positions 21-335, 423-457.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi197931. 4 interactions.
DIPiDIP-59594N.
IntActiP04756. 1 interaction.
MINTiMINT-8388618.
STRINGi10090.ENSMUSP00000028515.

Chemistry

BindingDBiP04756.
ChEMBLiCHEMBL3137264.

PTM databases

iPTMnetiP04756.
PhosphoSiteiP04756.
SwissPalmiP04756.

Proteomic databases

PaxDbiP04756.
PRIDEiP04756.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000028515; ENSMUSP00000028515; ENSMUSG00000027107.
GeneIDi11435.
KEGGimmu:11435.
UCSCiuc008kcy.2. mouse.

Organism-specific databases

CTDi1134.
MGIiMGI:87885. Chrna1.

Phylogenomic databases

eggNOGiKOG3645. Eukaryota.
ENOG410XQGR. LUCA.
HOGENOMiHOG000006756.
HOVERGENiHBG003756.
InParanoidiP04756.
KOiK04803.
OMAiRANKHVS.
OrthoDBiEOG72JWGV.
PhylomeDBiP04756.
TreeFamiTF315605.

Enzyme and pathway databases

ReactomeiR-MMU-629594. Highly calcium permeable postsynaptic nicotinic acetylcholine receptors.
R-MMU-629597. Highly calcium permeable nicotinic acetylcholine receptors.

Miscellaneous databases

EvolutionaryTraceiP04756.
PROiP04756.
SOURCEiSearch...

Gene expression databases

BgeeiP04756.
ExpressionAtlasiP04756. baseline and differential.
GenevisibleiP04756. MM.

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

« Hide 'large scale' publications
  1. "Nucleotide sequence of the mouse muscle nicotinic acetylcholine receptor alpha subunit."
    Isenberg K.E., Mudd J., Shah V., Merlie J.P.
    Nucleic Acids Res. 14:5111-5111(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. Boulter J.
    Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "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.
    , 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: Head.
  4. "Isolation of a clone coding for the alpha-subunit of a mouse acetylcholine receptor."
    Boulter J., Luyten W., Evans K., Mason P., Ballivet M., Goldman D.J., Stengelin S.F., Martin G., Heinemann S.F., Patrick J.
    J. Neurosci. 5:2545-2552(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 13-457.
  5. "Crystal structure of the extracellular domain of nAChR alpha1 bound to alpha-bungarotoxin at 1.94 A resolution."
    Dellisanti C.D., Yao Y., Stroud J.C., Wang Z.Z., Chen L.
    Nat. Neurosci. 10:953-962(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.94 ANGSTROMS) OF 21-231 IN COMPLEX WITH ALPHA-BUNGAROTOXIN, DISULFIDE BONDS, GLYCOSYLATION AT ASN-161.

Entry informationi

Entry nameiACHA_MOUSE
AccessioniPrimary (citable) accession number: P04756
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: August 13, 1987
Last modified: June 8, 2016
This is version 158 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, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.