ID   ACHA6_RAT               Reviewed;         493 AA.
AC   P43143;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 150.
DE   RecName: Full=Neuronal acetylcholine receptor subunit alpha-6;
DE   Flags: Precursor;
GN   Name=Chrna6; Synonyms=Acra6;
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 [MRNA].
RA   Boulter J.;
RT   "Nucleotide sequence of a cDNA clone encoding the rat neuronal nicotinic
RT   acetylcholine receptor subunit gene alpha6.";
RL   Submitted (DEC-1992) 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). Interacts with LYPD6.
CC       {ECO:0000250|UniProtKB:Q15825}.
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-6/CHRNA6 sub-
CC       subfamily. {ECO:0000305}.
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DR   EMBL; L08227; AAA41674.1; -; mRNA.
DR   RefSeq; NP_476532.1; NM_057184.1.
DR   AlphaFoldDB; P43143; -.
DR   SMR; P43143; -.
DR   ComplexPortal; CPX-203; Neuronal nicotinic acetylcholine receptor complex, alpha3-alpha6-beta2-beta3.
DR   ComplexPortal; CPX-211; Neuronal nicotinic acetylcholine receptor complex, alpha3-alpha6-beta4.
DR   IntAct; P43143; 2.
DR   STRING; 10116.ENSRNOP00000016452; -.
DR   BindingDB; P43143; -.
DR   ChEMBL; CHEMBL4747; -.
DR   DrugCentral; P43143; -.
DR   GlyGen; P43143; 2 sites.
DR   PaxDb; P43143; -.
DR   PRIDE; P43143; -.
DR   GeneID; 81721; -.
DR   KEGG; rno:81721; -.
DR   UCSC; RGD:69281; rat.
DR   CTD; 8973; -.
DR   RGD; 69281; Chrna6.
DR   eggNOG; KOG3645; Eukaryota.
DR   InParanoid; P43143; -.
DR   OrthoDB; 381858at2759; -.
DR   PhylomeDB; P43143; -.
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:P43143; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005892; C:acetylcholine-gated channel complex; ISO:RGD.
DR   GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR   GO; GO:0098691; C:dopaminergic synapse; ISO:RGD.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR   GO; GO:0099055; C:integral component of postsynaptic membrane; IDA:SynGO.
DR   GO; GO:0099056; C:integral component of presynaptic membrane; IDA:SynGO.
DR   GO; GO:0016020; C:membrane; IDA:RGD.
DR   GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR   GO; GO:0032991; C:protein-containing complex; IDA:RGD.
DR   GO; GO:0045202; C:synapse; IBA:GO_Central.
DR   GO; GO:0022848; F:acetylcholine-gated cation-selective channel activity; ISO: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:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
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:0014059; P:regulation of dopamine secretion; ISO:RGD.
DR   GO; GO:0042391; P:regulation of membrane potential; IBA:GO_Central.
DR   GO; GO:2000300; P:regulation of synaptic vesicle exocytosis; ISO:RGD.
DR   GO; GO:0007165; P:signal transduction; 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; Phosphoprotein;
KW   Postsynaptic cell membrane; Receptor; Reference proteome; Signal; Synapse;
KW   Transmembrane; Transmembrane helix; Transport.
FT   SIGNAL          1..30
FT                   /evidence="ECO:0000250"
FT   CHAIN           31..493
FT                   /note="Neuronal acetylcholine receptor subunit alpha-6"
FT                   /id="PRO_0000000363"
FT   TOPO_DOM        31..240
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        241..265
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        272..290
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        306..327
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        328..464
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        465..484
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         401
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P04757"
FT   CARBOHYD        54
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        171
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        158..172
FT                   /evidence="ECO:0000250"
FT   DISULFID        222..223
FT                   /note="Associated with receptor activation"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   493 AA;  56947 MW;  A829FAF8FFB060FE CRC64;
     MLNGWGRGDL RSGLCLWICG FLAFFKGSRG CVSEEQLFHT LFAHYNRFIR PVENVSDPVT
     VHFELAITQL ANVDEVNQIM ETNLWLRHVW KDYRLCWDPT EYDGIETLRV PADNIWKPDI
     VLYNNAVGDF QVEGKTKALL KYDGVITWTP PAIFKSSCPM DITFFPFDHQ NCSLKFGSWT
     YDKAEIDLLI IGSKVDMNDF WENSEWEIVD ASGYKHDIKY NCCEEIYTDI TYSFYIRRLP
     MFYTINLIIP CLFISFLTVL VFYLPSDCGE KVTLCISVLL SLTVFLLVIT ETIPSTSLVI
     PLVGEYLLFT MIFVTLSIVV TVFVLNIHYR TPATHTMPKW VKTMFLQVFP SILMMRRPLD
     KTKEMDGVKD PKTHTKRPAK VKFTHRKEPK LLKECRHCHK SSEIAPGKRL SQQPAQWVTE
     NSEHPPDVED VIDSVQFIAE NMKSHNETKE VEDDWKYMAM VVDRVFLWVF IIVCVFGTVG
     LFLQPLLGNT GAS