ID A0A2Y9IPE2_ENHLU Unreviewed; 457 AA.
AC A0A2Y9IPE2;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Acetylcholine receptor subunit alpha {ECO:0000256|ARBA:ARBA00041177};
GN Name=LOC111141829 {ECO:0000313|RefSeq:XP_022350373.1};
OS Enhydra lutris kenyoni (northern sea otter).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Lutrinae; Enhydra.
OX NCBI_TaxID=391180 {ECO:0000313|Proteomes:UP000248482, ECO:0000313|RefSeq:XP_022350373.1};
RN [1] {ECO:0000313|RefSeq:XP_022350373.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_022350373.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Upon acetylcholine binding, the AChR responds by an extensive
CC change in conformation that affects all subunits and leads to opening
CC of an ion-conducting channel across the plasma membrane.
CC {ECO:0000256|ARBA:ARBA00037634}.
CC -!- SUBUNIT: One of the alpha chains that assemble within the acetylcholine
CC receptor, a pentamer of two alpha chains, a beta, a delta, and a gamma
CC (in immature muscle) or epsilon (in mature muscle) chains. The muscle
CC heteropentamer composed of alpha-1, beta-1, delta, epsilon subunits
CC interacts with the alpha-conotoxin ImII.
CC {ECO:0000256|ARBA:ARBA00038643}.
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-1/CHRNA1 sub-
CC subfamily. {ECO:0000256|ARBA:ARBA00038312}.
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DR RefSeq; XP_022350373.1; XM_022494665.1.
DR AlphaFoldDB; A0A2Y9IPE2; -.
DR STRING; 391180.A0A2Y9IPE2; -.
DR KEGG; elk:111141829; -.
DR OrthoDB; 5489962at2759; -.
DR Proteomes; UP000248482; Unplaced.
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; cd19014; LGIC_ECD_nAChR_A1; 1.
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:SF74; ACETYLCHOLINE RECEPTOR SUBUNIT ALPHA; 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 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_022350373.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000248482};
KW Signal {ECO:0000256|RuleBase:RU000687};
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 SIGNAL 1..20
FT /evidence="ECO:0000256|RuleBase:RU000687"
FT CHAIN 21..457
FT /note="Acetylcholine receptor subunit alpha"
FT /evidence="ECO:0000256|RuleBase:RU000687"
FT /id="PRO_5022259719"
FT TRANSMEM 232..255
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU000687"
FT TRANSMEM 267..285
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU000687"
FT TRANSMEM 297..316
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU000687"
FT TRANSMEM 429..451
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU000687"
FT DOMAIN 24..230
FT /note="Neurotransmitter-gated ion-channel ligand-binding"
FT /evidence="ECO:0000259|Pfam:PF02931"
FT DOMAIN 238..446
FT /note="Neurotransmitter-gated ion-channel transmembrane"
FT /evidence="ECO:0000259|Pfam:PF02932"
SQ SEQUENCE 457 AA; 51844 MW; CF2B3785FD0DEE52 CRC64;
MEPRPLLLLL GLCSAGLVLG SEHETRLVAK LFEDYNSVVR PVEDHRQAVE VTVGLQLIQL
INVDEVNQIV TTNVRLKQQW VDYNLKWNPD DYGGVKKIHI PSEKIWHPDL VLYNNADGDF
AIVKFTKVLL DYTGHITWTP PAIFKSYCEI IVTHFPFDEQ NCSMKLGTWT YDGSVVAINP
ESDQPDLSNF MESGEWVIKE SRGWKHWVFY ACCPSTPYLD ITYHFVMQRL PLYFIVNVII
PCLLFSFLTG LVFYLPTDSG EKMTLSISVL LSLTVFLLVI VELIPSTSSA VPLIGKYMLF
TMVFVIASIV ITVIVINTHH RSPSTHVMPD WVRKVFIDTI PNIMFFSTMK RPSREKQDKK
IFTEDIDISD ISGKPGPPPM GFHSPLIKHP EVKSAIEGVK YIAETMKSDQ ESNNAAEEWK
YVAMVMDHIL LGVFMLVCII GTLAVFAGRL IELNQQG
//
