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Database: UniProt
Entry: F1MQ06_BOVIN
LinkDB: F1MQ06_BOVIN
Original site: F1MQ06_BOVIN 
ID   F1MQ06_BOVIN            Unreviewed;       494 AA.
AC   F1MQ06;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 2.
DT   27-MAR-2024, entry version 87.
DE   SubName: Full=Cholinergic receptor nicotinic alpha 6 subunit {ECO:0000313|Ensembl:ENSBTAP00000018679.4};
GN   Name=CHRNA6 {ECO:0000313|Ensembl:ENSBTAP00000018679.4,
GN   ECO:0000313|VGNC:VGNC:27328};
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913 {ECO:0000313|Ensembl:ENSBTAP00000018679.4, ECO:0000313|Proteomes:UP000009136};
RN   [1] {ECO:0000313|Ensembl:ENSBTAP00000018679.4, ECO:0000313|Proteomes:UP000009136}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000018679.4,
RC   ECO:0000313|Proteomes:UP000009136};
RA   Rosen B.D., Bickhart D.M., Koren S., Schnabel R.D., Hall R., Zimin A.,
RA   Dreischer C., Schultheiss S., Schroeder S.G., Elsik C.G., Couldrey C.,
RA   Liu G.E., Van Tassell C.P., Phillippy A.M., Smith T.P.L., Medrano J.F.;
RT   "ARS-UCD1.2.";
RL   Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSBTAP00000018679.4}
RP   IDENTIFICATION.
RC   STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000018679.4};
RG   Ensembl;
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       {ECO:0000256|RuleBase:RU000687}.
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DR   RefSeq; XP_002698774.2; XM_002698728.3.
DR   RefSeq; XP_584902.4; XM_584902.5.
DR   AlphaFoldDB; F1MQ06; -.
DR   STRING; 9913.ENSBTAP00000018679; -.
DR   PaxDb; 9913-ENSBTAP00000018679; -.
DR   Ensembl; ENSBTAT00000018679.5; ENSBTAP00000018679.4; ENSBTAG00000014056.5.
DR   GeneID; 539113; -.
DR   KEGG; bta:539113; -.
DR   CTD; 8973; -.
DR   VEuPathDB; HostDB:ENSBTAG00000014056; -.
DR   VGNC; VGNC:27328; CHRNA6.
DR   eggNOG; KOG3645; Eukaryota.
DR   GeneTree; ENSGT00940000158062; -.
DR   HOGENOM; CLU_018074_1_0_1; -.
DR   InParanoid; F1MQ06; -.
DR   OMA; HKDTKLH; -.
DR   OrthoDB; 5489962at2759; -.
DR   TreeFam; TF315605; -.
DR   Reactome; R-BTA-629594; Highly calcium permeable postsynaptic nicotinic acetylcholine receptors.
DR   Reactome; R-BTA-629597; Highly calcium permeable nicotinic acetylcholine receptors.
DR   Proteomes; UP000009136; Chromosome 27.
DR   Bgee; ENSBTAG00000014056; Expressed in retina and 27 other cell types or tissues.
DR   GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR   GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0045202; C:synapse; IBA:GO_Central.
DR   GO; GO:0022848; F:acetylcholine-gated monoatomic cation-selective channel activity; IBA:GO_Central.
DR   GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
DR   GO; GO:0035094; P:response to nicotine; IBA:GO_Central.
DR   GO; GO:0007271; P:synaptic transmission, cholinergic; IBA:GO_Central.
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:SF82; NEURONAL ACETYLCHOLINE RECEPTOR SUBUNIT ALPHA-6; 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:UP000009136};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, 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..30
FT                   /evidence="ECO:0000256|RuleBase:RU000687"
FT   CHAIN           31..494
FT                   /evidence="ECO:0000256|RuleBase:RU000687"
FT                   /id="PRO_5022272833"
FT   TRANSMEM        241..265
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU000687"
FT   TRANSMEM        272..294
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU000687"
FT   TRANSMEM        306..327
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU000687"
FT   TRANSMEM        466..488
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU000687"
FT   DOMAIN          34..239
FT                   /note="Neurotransmitter-gated ion-channel ligand-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02931"
FT   DOMAIN          247..483
FT                   /note="Neurotransmitter-gated ion-channel transmembrane"
FT                   /evidence="ECO:0000259|Pfam:PF02932"
SQ   SEQUENCE   494 AA;  57077 MW;  51AC7DF024DDBD45 CRC64;
     MLPRGGQGAL RFALCVWWCV FALCFKGCAG CASEERLFHK LFAHYNQFIR PVENVSDPIT
     VYFEVAITQL ADVDEVNQIM ETNLWLRHIW NDYKLRWDPT EYDGIETLRV PAEMIWKPDI
     VLYNNAVGDF QVKGKTKALL KYDGMITWTP PAIFKSSCPM DITFFPFDHQ NCSLKFGSWT
     YDKAEIDLLI IGSKVDMNEF WENSEWEIVD ASGYKHDIKY NCCEEIYTDI TYSFYIRRLP
     MFYTINLIIP CLFISFLTVL VFYLPSDCGE KVTLCISVLL SLTVFLLVIT ETIPSTSLVI
     PLVGEYLLFT MIFVTLSIVV TVFVLNIHYR TPTTHSMPTW VKAVFLRLLP QMLMMKRPLD
     KMKETGAHRN PKGVSSRPAK VKFEHHKEPR LLKECCHCHR SGEPATSKRR LSHQPLQWMA
     ENSELSPEVE DVIDSVHFIA ENMKTQNETK EVEDDWKYVA MVVDRVFLWV FIIVCVFGTA
     GLFLQPLLGN TGHS
//
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