ID   ACHA2_RAT               Reviewed;         511 AA.
AC   P12389; O08952; Q53YK3;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1998, sequence version 2.
DT   03-AUG-2022, entry version 170.
DE   RecName: Full=Neuronal acetylcholine receptor subunit alpha-2;
DE   Flags: Precursor;
GN   Name=Chrna2; Synonyms=Acra2;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC   STRAIN=Sprague-Dawley; TISSUE=Brain;
RX   PubMed=2832952; DOI=10.1126/science.2832952;
RA   Wada K., Ballivet M., Boulter J., Connolly J.G., Wada E., Deneris E.S.,
RA   Swanson L.W., Heinemann S.F., Patrick J.;
RT   "Functional expression of a new pharmacological subtype of brain nicotinic
RT   acetylcholine receptor.";
RL   Science 240:330-334(1988).
RN   [2]
RP   SEQUENCE REVISION.
RA   Boulter J.;
RL   Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Sprague-Dawley; TISSUE=Brain;
RA   Groot-Kormelink P.J.;
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: After binding acetylcholine, the AChR responds by an
CC       extensive change in conformation that affects all subunits and leads to
CC       opening of an ion-conducting channel across the plasma membrane.
CC   -!- SUBUNIT: Neuronal AChR seems to be composed of two different types of
CC       subunits: alpha and non-alpha (beta). Alpha-2 subunit can be combined
CC       to beta-2 or beta-4 to give rise to functional receptors. The alpha-
CC       2:beta-2 nAChR complex is proposed to be a heteropentamer with two
CC       subtypes: LS (low agonist sensitivity) with a (alpha-2)3:(beta-2)2 and
CC       HS (high agonist sensitivity) with a (alpha-2)2:(beta-2)3
CC       stoichiometry; the subtypes differ in their subunit binding interfaces
CC       which are involved in ligand binding. {ECO:0000250|UniProtKB:Q15822}.
CC   -!- SUBCELLULAR LOCATION: Postsynaptic cell membrane; Multi-pass membrane
CC       protein. Cell membrane; Multi-pass membrane protein.
CC   -!- SIMILARITY: Belongs to the ligand-gated ion channel (TC 1.A.9) family.
CC       Acetylcholine receptor (TC 1.A.9.1) subfamily. Alpha-2/CHRNA2 sub-
CC       subfamily. {ECO:0000305}.
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DR   EMBL; L10077; AAB60900.1; -; mRNA.
DR   EMBL; M20297; AAA40664.1; -; Genomic_DNA.
DR   EMBL; M20292; AAA40664.1; JOINED; Genomic_DNA.
DR   EMBL; M20293; AAA40664.1; JOINED; Genomic_DNA.
DR   EMBL; M20294; AAA40664.1; JOINED; Genomic_DNA.
DR   EMBL; M20295; AAA40664.1; JOINED; Genomic_DNA.
DR   EMBL; M20296; AAA40664.1; JOINED; Genomic_DNA.
DR   EMBL; AY574253; AAS90349.1; -; mRNA.
DR   PIR; A40110; A40110.
DR   RefSeq; NP_596911.1; NM_133420.1.
DR   AlphaFoldDB; P12389; -.
DR   SMR; P12389; -.
DR   ComplexPortal; CPX-178; Neuronal nicotinic acetylcholine receptor complex, alpha2-beta2.
DR   ComplexPortal; CPX-183; Neuronal nicotinic acetylcholine receptor complex, alpha2-beta4.
DR   STRING; 10116.ENSRNOP00000023475; -.
DR   BindingDB; P12389; -.
DR   ChEMBL; CHEMBL2584; -.
DR   DrugCentral; P12389; -.
DR   GuidetoPHARMACOLOGY; 463; -.
DR   GlyGen; P12389; 3 sites.
DR   PhosphoSitePlus; P12389; -.
DR   PaxDb; P12389; -.
DR   Ensembl; ENSRNOT00000023475; ENSRNOP00000023475; ENSRNOG00000017424.
DR   GeneID; 170945; -.
DR   KEGG; rno:170945; -.
DR   UCSC; RGD:621533; rat.
DR   CTD; 1135; -.
DR   RGD; 621533; Chrna2.
DR   eggNOG; KOG3645; Eukaryota.
DR   GeneTree; ENSGT00940000158299; -.
DR   HOGENOM; CLU_018074_1_0_1; -.
DR   InParanoid; P12389; -.
DR   OMA; QHAKNKD; -.
DR   OrthoDB; 381858at2759; -.
DR   PhylomeDB; P12389; -.
DR   TreeFam; TF315605; -.
DR   Reactome; R-RNO-629594; Highly calcium permeable postsynaptic nicotinic acetylcholine receptors.
DR   Reactome; R-RNO-629597; Highly calcium permeable nicotinic acetylcholine receptors.
DR   PRO; PR:P12389; -.
DR   Proteomes; UP000002494; Chromosome 15.
DR   Bgee; ENSRNOG00000017424; Expressed in adult mammalian kidney and 11 other tissues.
DR   Genevisible; P12389; RN.
DR   GO; GO:0005892; C:acetylcholine-gated channel complex; ISO:RGD.
DR   GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR   GO; GO:0071944; C:cell periphery; ISO:RGD.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR   GO; GO:0045171; C:intercellular bridge; IEA:Ensembl.
DR   GO; GO:0016020; C:membrane; IDA:RGD.
DR   GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0032991; C:protein-containing complex; IDA:RGD.
DR   GO; GO:0045202; C:synapse; IBA:GO_Central.
DR   GO; GO:0015464; F:acetylcholine receptor activity; ISO:RGD.
DR   GO; GO:0022848; F:acetylcholine-gated cation-selective channel activity; IDA:RGD.
DR   GO; GO:0005231; F:excitatory extracellular ligand-gated ion channel activity; IBA:GO_Central.
DR   GO; GO:0030594; F:neurotransmitter receptor activity; IBA:GO_Central.
DR   GO; GO:0050997; F:quaternary ammonium group binding; IDA:RGD.
DR   GO; GO:1904315; F:transmitter-gated ion channel activity involved in regulation of postsynaptic membrane potential; IBA:GO_Central.
DR   GO; GO:0007268; P:chemical synaptic transmission; IBA:GO_Central.
DR   GO; GO:0034220; P:ion transmembrane transport; IBA:GO_Central.
DR   GO; GO:0051899; P:membrane depolarization; ISO:RGD.
DR   GO; GO:0050877; P:nervous system process; IBA:GO_Central.
DR   GO; GO:0042391; P:regulation of membrane potential; IBA:GO_Central.
DR   GO; GO:1905144; P:response to acetylcholine; IDA:RGD.
DR   GO; GO:0035094; P:response to nicotine; IBA:GO_Central.
DR   GO; GO:0007165; P:signal transduction; ISO:RGD.
DR   GO; GO:0007271; P:synaptic transmission, cholinergic; IBA:GO_Central.
DR   Gene3D; 1.20.58.390; -; 2.
DR   Gene3D; 2.70.170.10; -; 1.
DR   InterPro; IPR006202; Neur_chan_lig-bd.
DR   InterPro; IPR036734; Neur_chan_lig-bd_sf.
DR   InterPro; IPR006201; Neur_channel.
DR   InterPro; IPR036719; Neuro-gated_channel_TM_sf.
DR   InterPro; IPR038050; Neuro_actylchol_rec.
DR   InterPro; IPR006029; Neurotrans-gated_channel_TM.
DR   InterPro; IPR018000; Neurotransmitter_ion_chnl_CS.
DR   InterPro; IPR002394; Nicotinic_acetylcholine_rcpt.
DR   PANTHER; PTHR18945; PTHR18945; 1.
DR   Pfam; PF02931; Neur_chan_LBD; 1.
DR   Pfam; PF02932; Neur_chan_memb; 1.
DR   PRINTS; PR00254; NICOTINICR.
DR   PRINTS; PR00252; NRIONCHANNEL.
DR   SUPFAM; SSF63712; SSF63712; 1.
DR   SUPFAM; SSF90112; SSF90112; 1.
DR   TIGRFAMs; TIGR00860; LIC; 1.
DR   PROSITE; PS00236; NEUROTR_ION_CHANNEL; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Disulfide bond; Glycoprotein; Ion channel; Ion transport;
KW   Ligand-gated ion channel; Membrane; Postsynaptic cell membrane; Receptor;
KW   Reference proteome; Signal; Synapse; Transmembrane; Transmembrane helix;
KW   Transport.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000255"
FT   CHAIN           28..511
FT                   /note="Neuronal acetylcholine receptor subunit alpha-2"
FT                   /id="PRO_0000000343"
FT   TOPO_DOM        28..241
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        242..266
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        274..292
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        308..329
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        330..484
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        485..503
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        56
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        106
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        212
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        160..174
FT                   /evidence="ECO:0000250"
FT   DISULFID        224..225
FT                   /note="Associated with receptor activation"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        494
FT                   /note="C -> S (in Ref. 1; AAA40664)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   511 AA;  58611 MW;  3824E83BB01D613B CRC64;
     MTLSHSALQF WTHLYLWCLL LVPAVLTQQG SHTHAEDRLF KHLFGGYNRW ARPVPNTSDV
     VIVRFGLSIA QLIDVDEKNQ MMTTNVWLKQ EWNDYKLRWD PAEFGNVTSL RVPSEMIWIP
     DIVLYNNADG EFAVTHMTKA HLFFTGTVHW VPPAIYKSSC SIDVTFFPFD QQNCKMKFGS
     WTYDKAKIDL EQMERTVDLK DYWESGEWAI INATGTYNSK KYDCCAEIYP DVTYYFVIRR
     LPLFYTINLI IPCLLISCLT VLVFYLPSEC GEKITLCISV LLSLTVFLLL ITEIIPSTSL
     VIPLIGEYLL FTMIFVTLSI VITVFVLNVH HRSPSTHNMP NWVRVALLGR VPRWLMMNRP
     LPPMELHGSP DLKLSPSYHW LETNMDAGER EETEEEEEEE DENICVCAGL PDSSMGVLYG
     HGGLHLRAME PETKTPSQAS EILLSPQIQK ALEGVHYIAD RLRSEDADSS VKEDWKYVAM
     VVDRIFLWLF IIVCFLGTIG LFLPPFLAGM I