Neuronal acetylcholine receptor subunit alpha-2 precursor

Contribute

Send feedback

Read comments (?) or add your own

P12389 (ACHA2_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 112. History...

Clusters with 100%, 90%, 50% identity |

Documents (1) |

Third-party data

text xml rdf/xml gff fasta

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Neuronal acetylcholine receptor subunit alpha-2

Gene names

Name:	Chrna2
Synonyms:	Acra2

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	511 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.
Subunit structure	Neuronal AChR seems to be composed of two different types of subunits: alpha and non-alpha (beta). Alpha-2 subunit can be combined to beta-2 or beta-4 to give rise to functional receptors.
Subcellular location	Cell junction › synapse › postsynaptic cell membrane; Multi-pass membrane protein. Cell membrane; Multi-pass membrane protein.
Sequence similarities	Belongs to the ligand-gated ion channel (TC 1.A.9) family. Acetylcholine receptor (TC 1.A.9.1) subfamily. Alpha-2/CHRNA2 sub-subfamily. [View classification]

Ontologies

Keywords
Biological process	Ion transport Transport
Cellular component	Cell junction Cell membrane Membrane Postsynaptic cell membrane Synapse
Domain	Signal Transmembrane Transmembrane helix
Molecular function	Ion channel Ligand-gated ion channel Receptor
PTM	Disulfide bond Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	protein heterooligomerization Inferred from direct assay PubMed 16129735. Source: RGD
Cellular_component	acetylcholine-gated channel complex Inferred from direct assay PubMed 16129735. Source: RGD cell junction Inferred from electronic annotation. Source: UniProtKB-KW postsynaptic membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	acetylcholine binding Inferred from direct assay PubMed 15016836. Source: RGD acetylcholine receptor activity Inferred from electronic annotation. Source: Compara acetylcholine-activated cation-selective channel activity Inferred from direct assay Ref.1. Source: RGD drug binding Inferred from direct assay PubMed 15016836 PubMed 16129735. Source: RGD
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 27

Potential

Chain

28 – 511

484

Neuronal acetylcholine receptor subunit alpha-2

PRO_0000000343

Regions

Topological domain

28 – 241

214

Extracellular Potential

Transmembrane

242 – 266

Helical; Potential

Transmembrane

274 – 292

Helical; Potential

Transmembrane

308 – 329

Helical; Potential

Topological domain

330 – 484

155

Cytoplasmic Potential

Transmembrane

485 – 503

Helical; Potential

Compositional bias

391 – 402

Poly-Glu

Amino acid modifications

Glycosylation

N-linked (GlcNAc...) Potential

Glycosylation

106

N-linked (GlcNAc...) Potential

Glycosylation

212

N-linked (GlcNAc...) Potential

Disulfide bond

160 ↔ 174

By similarity

Disulfide bond

224 ↔ 225

Associated with receptor activation By similarity

Experimental info

Sequence conflict

494

C → S in AAA40664. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

P12389 [UniParc].

Last modified July 15, 1998. Version 2.
Checksum: 3824E83BB01D613B
Show »

FASTA

511

58,611

        10         20         30         40         50         60 
MTLSHSALQF WTHLYLWCLL LVPAVLTQQG SHTHAEDRLF KHLFGGYNRW ARPVPNTSDV 

        70         80         90        100        110        120 
VIVRFGLSIA QLIDVDEKNQ MMTTNVWLKQ EWNDYKLRWD PAEFGNVTSL RVPSEMIWIP 

       130        140        150        160        170        180 
DIVLYNNADG EFAVTHMTKA HLFFTGTVHW VPPAIYKSSC SIDVTFFPFD QQNCKMKFGS 

       190        200        210        220        230        240 
WTYDKAKIDL EQMERTVDLK DYWESGEWAI INATGTYNSK KYDCCAEIYP DVTYYFVIRR 

       250        260        270        280        290        300 
LPLFYTINLI IPCLLISCLT VLVFYLPSEC GEKITLCISV LLSLTVFLLL ITEIIPSTSL 

       310        320        330        340        350        360 
VIPLIGEYLL FTMIFVTLSI VITVFVLNVH HRSPSTHNMP NWVRVALLGR VPRWLMMNRP 

       370        380        390        400        410        420 
LPPMELHGSP DLKLSPSYHW LETNMDAGER EETEEEEEEE DENICVCAGL PDSSMGVLYG 

       430        440        450        460        470        480 
HGGLHLRAME PETKTPSQAS EILLSPQIQK ALEGVHYIAD RLRSEDADSS VKEDWKYVAM 

       490        500        510 
VVDRIFLWLF IIVCFLGTIG LFLPPFLAGM I

« Hide

References

[1]	"Functional expression of a new pharmacological subtype of brain nicotinic acetylcholine receptor." Wada K., Ballivet M., Boulter J., Connolly J.G., Wada E., Deneris E.S., Swanson L.W., Heinemann S.F., Patrick J. Science 240:330-334(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. Strain: Sprague-Dawley. Tissue: Brain.
[2]	Boulter J. Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION.
[3]	Groot-Kormelink P.J. Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: Sprague-Dawley. Tissue: Brain.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L10077 mRNA. Translation: AAB60900.1. M20297 , M20292, M20293, M20294, M20295, M20296 Genomic DNA. Translation: AAA40664.1. AY574253 mRNA. Translation: AAS90349.1.
IPI	IPI00196723.
PIR	A40110.
RefSeq	NP_596911.1. NM_133420.1.
UniGene	Rn.9713.
3D structure databases
ProteinModelPortal	P12389.
SMR	P12389. Positions 242-333.
ModBase	Search...
Protein-protein interaction databases
STRING	10116.ENSRNOP00000023475.
PTM databases
PhosphoSite	P12389.
Proteomic databases
PaxDb	P12389.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSRNOT00000023475; ENSRNOP00000023475; ENSRNOG00000017424.
GeneID	170945.
KEGG	rno:170945.
UCSC	RGD:621533. rat.
Organism-specific databases
CTD	1135.
RGD	621533. Chrna2.
Phylogenomic databases
eggNOG	NOG290206.
GeneTree	ENSGT00620000087732.
HOGENOM	HOG000006756.
HOVERGEN	HBG003756.
InParanoid	P12389.
KO	K04804.
OMA	ACAGHVA.
OrthoDB	EOG480HWN.
Gene expression databases
Genevestigator	P12389.
GermOnline	ENSRNOG00000017424. Rattus norvegicus.
Family and domain databases
Gene3D	2.70.170.10. 1 hit.
InterPro	IPR006202. Neur_chan_lig-bd. IPR006201. Neur_channel. IPR006029. Neurotrans-gated_channel_TM. IPR018000. Neurotransmitter_ion_chnl_CS. IPR002394. Nicotinic_acetylcholine_rcpt. [Graphical view]
PANTHER	PTHR18945. PTHR18945. 1 hit.
Pfam	PF02931. Neur_chan_LBD. 1 hit. PF02932. Neur_chan_memb. 1 hit. [Graphical view]
PRINTS	PR00254. NICOTINICR. PR00252. NRIONCHANNEL.
SUPFAM	SSF90112. Neu_channel_TM. 1 hit. SSF63712. Neur_chan_LBD. 1 hit.
TIGRFAMs	TIGR00860. LIC. 1 hit.
PROSITE	PS00236. NEUROTR_ION_CHANNEL. 1 hit. [Graphical view]
ProtoNet	Search...
Other
BindingDB	P12389.
ChEMBL	CHEMBL2584.
NextBio	621469.

Entry information

Entry name

ACHA2_RAT

Accession

Primary (citable) accession number: P12389
Secondary accession number(s): O08952, Q53YK3

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1989
Last sequence update:	July 15, 1998
Last modified:	April 3, 2013
This is version 112 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents