ID   ACHA2_CHICK             Reviewed;         528 AA.
AC   P09480;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   02-SEP-2026, entry version 163.
DE   RecName: Full=Neuronal acetylcholine receptor subunit alpha-2;
DE   Flags: Precursor;
GN   Name=CHRNA2;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC   STRAIN=White leghorn; TISSUE=Brain;
RX   PubMed=3267226; DOI=10.1002/j.1460-2075.1988.tb02852.x;
RA   Nef P., Oneyser C., Alliod C., Couturier S., Ballivet M.;
RT   "Genes expressed in the brain define three distinct neuronal nicotinic
RT   acetylcholine receptors.";
RL   EMBO J. 7:595-601(1988).
CC   -!- FUNCTION: Component of neuronal acetylcholine receptors (nAChRs) that
CC       function as pentameric, ligand-gated cation channels with high calcium
CC       permeability among other activities. nAChRs are excitatory
CC       neurotrasnmitter receptors formed by a collection of nAChR subunits
CC       known to mediate synaptic transmission in the nervous system and the
CC       neuromuscular junction. Each nAchR subunit confers differential
CC       attributes to channel properties, including activation, deactivation
CC       and desensitization kinetics, pH sensitivity, cation permeability, and
CC       binding to allosteric modulators. CHRNA2 forms heteropentameric
CC       neuronal acetylcholine receptors with CHRNB2 and CHRNB4 and plays a
CC       role in nicotine dependence. {ECO:0000250|UniProtKB:Q15822}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Ca(2+)(in) = Ca(2+)(out); Xref=Rhea:RHEA:29671,
CC         ChEBI:CHEBI:29108; Evidence={ECO:0000250|UniProtKB:P43681};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=K(+)(in) = K(+)(out); Xref=Rhea:RHEA:29463, ChEBI:CHEBI:29103;
CC         Evidence={ECO:0000250|UniProtKB:P02709};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Na(+)(in) = Na(+)(out); Xref=Rhea:RHEA:34963,
CC         ChEBI:CHEBI:29101; Evidence={ECO:0000250|UniProtKB:P43681};
CC   -!- SUBUNIT: Neuronal AChR is composed of two different types of subunits:
CC       alpha and non-alpha (beta). CHRNA2/alpha-2 subunit can be combined to
CC       CHRNB2/beta-2 or CHRNB4/beta-4 to give rise to functional receptors.
CC       Both CHRNA2:CHRNB2 and CHRNA2:CHRNB4 nAChR complexes are
CC       heteropentamers with two subtypes: LS (low agonist sensitivity) with a
CC       (CHRNA2)3:(CHRNB2/4)2 and HS (high agonist sensitivity) with a
CC       (CHRNA2)2:(CHRNB2/4)3 stoichiometries; the subtypes differ in their
CC       subunit binding interfaces which are involved in ligand binding.
CC       {ECO:0000250|UniProtKB:Q15822}.
CC   -!- SUBCELLULAR LOCATION: Synaptic cell membrane
CC       {ECO:0000250|UniProtKB:Q15822}; Multi-pass membrane protein
CC       {ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:Q15822}; Multi-pass
CC       membrane protein {ECO:0000255}.
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; X07339; CAB59645.1; -; Genomic_DNA.
DR   EMBL; X07340; CAB59645.1; JOINED; Genomic_DNA.
DR   EMBL; X07341; CAB59645.1; JOINED; Genomic_DNA.
DR   EMBL; X07342; CAB59645.1; JOINED; Genomic_DNA.
DR   EMBL; X07343; CAB59645.1; JOINED; Genomic_DNA.
DR   EMBL; X07344; CAB59645.1; JOINED; Genomic_DNA.
DR   EMBL; AJ250360; CAB59625.1; -; mRNA.
DR   PIR; S00377; ACCH2N.
DR   RefSeq; NP_990146.1; NM_204815.2.
DR   AlphaFoldDB; P09480; -.
DR   SMR; P09480; -.
DR   ComplexPortal; CPX-179; Neuronal nicotinic acetylcholine receptor complex, alpha2-beta2.
DR   ComplexPortal; CPX-184; Neuronal nicotinic acetylcholine receptor complex, alpha2-beta4.
DR   FunCoup; P09480; 47.
DR   IntAct; P09480; 2.
DR   STRING; 9031.ENSGALP00000026687; -.
DR   GlyCosmos; P09480; 2 sites, No reported glycans.
DR   GlyGen; P09480; 2 sites.
DR   PaxDb; 9031-ENSGALP00000026687; -.
DR   GeneID; 395607; -.
DR   KEGG; gga:395607; -.
DR   CTD; 1135; -.
DR   VEuPathDB; HostDB:geneid_395607; -.
DR   eggNOG; KOG3645; Eukaryota.
DR   InParanoid; P09480; -.
DR   OMA; SSYHWLE; -.
DR   OrthoDB; 5975154at2759; -.
DR   PhylomeDB; P09480; -.
DR   PRO; PR:P09480; -.
DR   Proteomes; UP000000539; Unassembled WGS sequence.
DR   GO; GO:0005892; C:acetylcholine-gated channel complex; IBA:GO_Central.
DR   GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0045211; C:postsynaptic membrane; IEA:InterPro.
DR   GO; GO:0098793; C:presynapse; IEA:GOC.
DR   GO; GO:0045202; C:synapse; IBA:GO_Central.
DR   GO; GO:0097060; C:synaptic membrane; ISS:UniProtKB.
DR   GO; GO:0022848; F:acetylcholine-gated monoatomic cation-selective channel activity; IEA:InterPro.
DR   GO; GO:0030594; F:neurotransmitter receptor activity; IBA:GO_Central.
DR   GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
DR   GO; GO:0095500; P:acetylcholine receptor signaling pathway; IBA:GO_Central.
DR   GO; GO:0006816; P:calcium ion transport; IBA:GO_Central.
DR   GO; GO:0051899; P:membrane depolarization; IBA:GO_Central.
DR   GO; GO:0034220; P:monoatomic ion transmembrane transport; IBA:GO_Central.
DR   GO; GO:0007274; P:neuromuscular synaptic transmission; IBA:GO_Central.
DR   GO; GO:0099171; P:presynaptic modulation of chemical synaptic transmission; IBA:GO_Central.
DR   GO; GO:0035094; P:response to nicotine; IBA:GO_Central.
DR   GO; GO:0007271; P:synaptic transmission, cholinergic; IBA:GO_Central.
DR   CDD; cd19015; LGIC_ECD_nAChR_A2; 1.
DR   CDD; cd19064; LGIC_TM_nAChR; 1.
DR   FunFam; 1.20.58.390:FF:000014; Neuronal nicotinic acetylcholine receptor alpha4 subunit; 1.
DR   FunFam; 2.70.170.10:FF:000005; Neuronal nicotinic acetylcholine receptor alpha4 subunit; 1.
DR   FunFam; 1.20.58.390:FF:000001; Neuronal nicotinic acetylcholine receptor subunit 3; 1.
DR   Gene3D; 2.70.170.10; Neurotransmitter-gated ion-channel ligand-binding domain; 1.
DR   Gene3D; 1.20.58.390; Neurotransmitter-gated ion-channel transmembrane domain; 2.
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   NCBIfam; TIGR00860; LIC; 1.
DR   PANTHER; PTHR18945; NEUROTRANSMITTER GATED ION CHANNEL; 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; SSF90112; Neurotransmitter-gated ion-channel transmembrane pore; 1.
DR   SUPFAM; SSF63712; Nicotinic receptor ligand binding domain-like; 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; Receptor; Reference proteome; Signal;
KW   Synapse; Transmembrane; Transmembrane helix; Transport.
FT   SIGNAL          1..23
FT   CHAIN           24..528
FT                   /note="Neuronal acetylcholine receptor subunit alpha-2"
FT                   /id="PRO_0000000344"
FT   TOPO_DOM        24..239
FT                   /note="Extracellular"
FT   TRANSMEM        240..264
FT                   /note="Helical"
FT   TRANSMEM        272..290
FT                   /note="Helical"
FT   TRANSMEM        306..327
FT                   /note="Helical"
FT   TOPO_DOM        328..501
FT                   /note="Cytoplasmic"
FT   TRANSMEM        502..520
FT                   /note="Helical"
FT   REGION          390..427
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        390..410
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        54
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        104
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        158..172
FT                   /evidence="ECO:0000250|UniProtKB:Q15822"
FT   DISULFID        222..223
FT                   /note="Associated with receptor activation"
FT                   /evidence="ECO:0000250|UniProtKB:Q15822"
SQ   SEQUENCE   528 AA;  60675 MW;  E76C6360AF876364 CRC64;
     MGWPCRSIIP LLVWCFVTLQ AATREQKQPH GFAEDRLFKH LFTGYNRWSR PVPNTSDVVI
     VKFGLSIAQL IDVDEKNQMM TTNVWLKQEW SDYKLRWNPE DFDNVTSIRV PSEMIWIPDI
     VLYNNADGEF AVTHMTKAHL FSNGKVKWVP PAIYKSSCSI DVTYFPFDQQ NCKMKFGSWT
     YDKAKIDLEN MEHHVDLKDY WESGEWAIIN AIGRYNSKKY DCCTEIYPDI TFYFVIRRLP
     LFYTINLIIP CLLISCLTVL VFYLPSDCGE KITLCISVLL SLTVFLLLIT EIIPSTSLVI
     PLIGEYLLFT MIFVTLSIII TVFVLNVHHR SPSTHTMPHW VRSFFLGFIP RWLFMKRPPL
     LLPAEGTTGQ YDPPGTRLST SRCWLETDVD DKWEEEEEEE EEEEEEEEEE KAYPSRVPSG
     GSQGTQCHYS CERQAGKASG GPAPQVPLKG EEVGSDQGLT LSPSILRALE GVQYIADHLR
     AEDADFSVKE DWKYVAMVID RIFLWMFIIV CLLGTVGLFL PPYLAGMI
//