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Database: UniProt
Entry: G3T6T5_LOXAF
LinkDB: G3T6T5_LOXAF
Original site: G3T6T5_LOXAF 
ID   G3T6T5_LOXAF            Unreviewed;       457 AA.
AC   G3T6T5;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 74.
DE   RecName: Full=Acetylcholine receptor subunit alpha {ECO:0000256|ARBA:ARBA00041177};
GN   Name=CHRNA1 {ECO:0000313|Ensembl:ENSLAFP00000009262.2};
OS   Loxodonta africana (African elephant).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Afrotheria; Proboscidea; Elephantidae; Loxodonta.
OX   NCBI_TaxID=9785 {ECO:0000313|Ensembl:ENSLAFP00000009262.2, ECO:0000313|Proteomes:UP000007646};
RN   [1] {ECO:0000313|Ensembl:ENSLAFP00000009262.2, ECO:0000313|Proteomes:UP000007646}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000009262.2,
RC   ECO:0000313|Proteomes:UP000007646};
RA   Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., Lindblad-Toh K.;
RT   "The Genome Sequence of Loxodonta africana (African elephant).";
RL   Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSLAFP00000009262.2}
RP   IDENTIFICATION.
RC   STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000009262.2};
RG   Ensembl;
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   -!- 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_003406261.1; XM_003406213.2.
DR   AlphaFoldDB; G3T6T5; -.
DR   STRING; 9785.ENSLAFP00000009262; -.
DR   Ensembl; ENSLAFT00000011068.2; ENSLAFP00000009262.2; ENSLAFG00000011067.2.
DR   eggNOG; KOG3645; Eukaryota.
DR   GeneTree; ENSGT00940000156851; -.
DR   HOGENOM; CLU_018074_1_0_1; -.
DR   InParanoid; G3T6T5; -.
DR   TreeFam; TF315605; -.
DR   Proteomes; UP000007646; Unassembled WGS sequence.
DR   GO; GO:0005892; C:acetylcholine-gated channel complex; IEA:Ensembl.
DR   GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR   GO; GO:0031594; C:neuromuscular junction; IEA:Ensembl.
DR   GO; GO:0099634; C:postsynaptic specialization membrane; IEA:Ensembl.
DR   GO; GO:0042166; F:acetylcholine binding; IEA:Ensembl.
DR   GO; GO:0015464; F:acetylcholine receptor activity; IEA:Ensembl.
DR   GO; GO:0022848; F:acetylcholine-gated monoatomic cation-selective channel activity; IEA:Ensembl.
DR   GO; GO:0046716; P:muscle cell cellular homeostasis; IEA:Ensembl.
DR   GO; GO:0007528; P:neuromuscular junction development; IEA:Ensembl.
DR   GO; GO:0007274; P:neuromuscular synaptic transmission; IEA:Ensembl.
DR   GO; GO:0070050; P:neuron cellular homeostasis; IEA:Ensembl.
DR   GO; GO:0019228; P:neuronal action potential; IEA:Ensembl.
DR   GO; GO:0003009; P:skeletal muscle contraction; IEA:Ensembl.
DR   GO; GO:0048630; P:skeletal muscle tissue growth; IEA:Ensembl.
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   Reference proteome {ECO:0000313|Proteomes:UP000007646};
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_5022270809"
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;  51953 MW;  0CA9731CE41BA381 CRC64;
     MEHQPLLLLL GLCSAGLVLG SEHETRLVAK LFENYNSVVR PVEDHRQAVE VTVGLQLIQL
     INVDEVNQIV TTNVRLKQQW VDYNLKWNPE DYGGVKKIHV PSEKIWRPDF VLYNNADGDF
     AIVKFTKVLL DYTGHITWTP PAIFKSYCEI IVTHFPFDEQ NCSMKLGTWT HDGSVVVINA
     ESDQPDLSNF MESGEWVIKE SRGWKHWVFY ACCPATPYLD ITYHFVMQRL PLYFIINVII
     PCLLFSFLTG LVFYLPTDSG EKMTLSISVL LSLTVFLLVI VELIPSTSSA VPLIGKYMLF
     TMVFVITSII ITVIVINTHH RSPSTHVMPE WVRKVFIDTI PNIMFFSTMK RPSREKRDKK
     IFTEDIDISD ISGKPGPPPM GFHSPLIKHP EVKSAIEGVK YIAETMKADQ ESNNAAEEWK
     YVAMVMDHLL LGVFMLVCII GTLAVFAGRL IELNQQG
//
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