ID A0A1S3RTE3_SALSA Unreviewed; 451 AA.
AC A0A1S3RTE3;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Neuronal acetylcholine receptor subunit alpha-2 {ECO:0000256|ARBA:ARBA00039992};
GN Name=LOC106604907 {ECO:0000313|RefSeq:XP_014055543.1};
OS Salmo salar (Atlantic salmon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8030 {ECO:0000313|Proteomes:UP000087266, ECO:0000313|RefSeq:XP_014055543.1};
RN [1] {ECO:0000313|RefSeq:XP_014055543.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_014055543.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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 {ECO:0000256|ARBA:ARBA00003328}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}. Postsynaptic cell membrane
CC {ECO:0000256|ARBA:ARBA00034104}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00034104}. Synaptic cell membrane
CC {ECO:0000256|ARBA:ARBA00034099}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00034099}.
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:0000256|ARBA:ARBA00038428}.
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DR RefSeq; XP_014055543.1; XM_014200068.1.
DR AlphaFoldDB; A0A1S3RTE3; -.
DR STRING; 8030.ENSSSAP00000028536; -.
DR KEGG; sasa:106604907; -.
DR OrthoDB; 5489962at2759; -.
DR Proteomes; UP000087266; Chromosome ssa01.
DR GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0022848; F:acetylcholine-gated monoatomic cation-selective channel activity; IEA:InterPro.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
DR CDD; cd19064; LGIC_TM_nAChR; 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:SF757; NEURONAL ACETYLCHOLINE RECEPTOR SUBUNIT ALPHA-2; 1.
DR PANTHER; PTHR18945; NEUROTRANSMITTER GATED ION CHANNEL; 1.
DR Pfam; PF02931; Neur_chan_LBD; 1.
DR Pfam; PF02932; Neur_chan_memb; 2.
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 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Ion channel {ECO:0000256|ARBA:ARBA00023303, ECO:0000256|RuleBase:RU000687};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065,
KW ECO:0000256|RuleBase:RU000687};
KW Ligand-gated ion channel {ECO:0000256|ARBA:ARBA00023286};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU000687};
KW Postsynaptic cell membrane {ECO:0000256|ARBA:ARBA00023257};
KW Receptor {ECO:0000256|ARBA:ARBA00023170,
KW ECO:0000313|RefSeq:XP_014055543.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000087266};
KW Synapse {ECO:0000256|ARBA:ARBA00023018};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU000687};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU000687};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU000687}.
FT TRANSMEM 231..255
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU000687"
FT TRANSMEM 261..284
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU000687"
FT TRANSMEM 296..315
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU000687"
FT TRANSMEM 425..447
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU000687"
FT DOMAIN 24..229
FT /note="Neurotransmitter-gated ion-channel ligand-binding"
FT /evidence="ECO:0000259|Pfam:PF02931"
FT DOMAIN 237..353
FT /note="Neurotransmitter-gated ion-channel transmembrane"
FT /evidence="ECO:0000259|Pfam:PF02932"
FT DOMAIN 376..442
FT /note="Neurotransmitter-gated ion-channel transmembrane"
FT /evidence="ECO:0000259|Pfam:PF02932"
SQ SEQUENCE 451 AA; 51765 MW; 0D5AF1C98A7B1A81 CRC64;
MCVCGWGGGS FSGLSDDWTH AHAEDKLFNR LFIGYNKWSR PVRNISDVVI VKFGLSIAQL
IDVDEKNQMM TTNVWLKQEW SDYKLRWRPS DYDNVTSIRV PSELIWVPDI VLYNNADGEF
SVTHMTKAHL FHSGHVRWVP PAIYKSSCSI DVTFFPFDQQ NCKMKFGSWT YDRAKIDLEP
IGDTVDLKDY WESGEWAIVT AVGTYNTKKY DCCHEIYPDI TYYFRIRRLP LFYTVNLIIP
CLLISCLTVL VFYLPSDCGE KITLCISVLL SLTVFLLLIT EIIPSTSLVI PLIGEYLLFT
MIFVTLSIVI TVFVLNVHHR SSATHTMPRW VRTLFLSAIP RWLCMKRPPL DLRRRGLVGK
LHPFGTFGTA GPSRYSSHST AHTLSPAVLR ALEGVTYIAE HLRAEDQDFS VKEDWKYVAM
VIDRIFLWMF IIVCLLGTIG LFLPPWLAGM I
//
