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Database: UniProt
Entry: L8HNU3_9CETA
LinkDB: L8HNU3_9CETA
Original site: L8HNU3_9CETA 
ID   L8HNU3_9CETA            Unreviewed;       516 AA.
AC   L8HNU3;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   24-JAN-2024, entry version 56.
DE   RecName: Full=Acetylcholine receptor subunit delta {ECO:0000256|ARBA:ARBA00039504};
GN   ORFNames=M91_21242 {ECO:0000313|EMBL:ELR44959.1};
OS   Bos mutus (wild yak).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=72004 {ECO:0000313|EMBL:ELR44959.1, ECO:0000313|Proteomes:UP000011080};
RN   [1] {ECO:0000313|EMBL:ELR44959.1, ECO:0000313|Proteomes:UP000011080}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=yakQH1 {ECO:0000313|Proteomes:UP000011080};
RX   PubMed=22751099; DOI=10.1038/ng.2343;
RA   Qiu Q., Zhang G., Ma T., Qian W., Wang J., Ye Z., Cao C., Hu Q., Kim J.,
RA   Larkin D.M., Auvil L., Capitanu B., Ma J., Lewin H.A., Qian X., Lang Y.,
RA   Zhou R., Wang L., Wang K., Xia J., Liao S., Pan S., Lu X., Hou H., Wang Y.,
RA   Zang X., Yin Y., Ma H., Zhang J., Wang Z., Zhang Y., Zhang D., Yonezawa T.,
RA   Hasegawa M., Zhong Y., Liu W., Zhang Y., Huang Z., Zhang S., Long R.,
RA   Yang H., Wang J., Lenstra J.A., Cooper D.N., Wu Y., Wang J., Shi P.,
RA   Wang J., Liu J.;
RT   "The yak genome and adaptation to life at high altitude.";
RL   Nat. Genet. 44:946-949(2012).
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}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|RuleBase:RU000687}.
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DR   EMBL; JH884893; ELR44959.1; -; Genomic_DNA.
DR   RefSeq; XP_005911143.1; XM_005911081.1.
DR   AlphaFoldDB; L8HNU3; -.
DR   SMR; L8HNU3; -.
DR   STRING; 72004.ENSBMUP00000007481; -.
DR   Ensembl; ENSBMUT00000008748; ENSBMUP00000007481; ENSBMUG00000005876.
DR   GeneID; 102267007; -.
DR   KEGG; bom:102267007; -.
DR   CTD; 1144; -.
DR   OrthoDB; 5489962at2759; -.
DR   Proteomes; UP000011080; Unassembled WGS sequence.
DR   GO; GO:0005892; C:acetylcholine-gated channel complex; 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:0022848; F:acetylcholine-gated monoatomic cation-selective channel activity; IEA:Ensembl.
DR   GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
DR   GO; GO:0050881; P:musculoskeletal movement; IEA:Ensembl.
DR   GO; GO:0048630; P:skeletal muscle tissue growth; IEA:Ensembl.
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:SF61; ACETYLCHOLINE RECEPTOR SUBUNIT DELTA; 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   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Postsynaptic cell membrane {ECO:0000256|ARBA:ARBA00023257};
KW   Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000313|EMBL:ELR44959.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011080};
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..21
FT                   /evidence="ECO:0000256|RuleBase:RU000687"
FT   CHAIN           22..516
FT                   /note="Acetylcholine receptor subunit delta"
FT                   /evidence="ECO:0000256|RuleBase:RU000687"
FT                   /id="PRO_5022254533"
FT   TRANSMEM        246..267
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU000687"
FT   TRANSMEM        307..330
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU000687"
FT   TRANSMEM        471..489
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU000687"
FT   DOMAIN          25..245
FT                   /note="Neurotransmitter-gated ion-channel ligand-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02931"
FT   DOMAIN          252..488
FT                   /note="Neurotransmitter-gated ion-channel transmembrane"
FT                   /evidence="ECO:0000259|Pfam:PF02932"
SQ   SEQUENCE   516 AA;  58588 MW;  6EBFA6AC00AB93A0 CRC64;
     MEGSVLTLVL LAALVVCGSW GLNEEERLIR HLFEEKAYNK ELRPAAHKES VEISLALTLS
     NLISLKEVEE TLTTNVWIEQ GWTDSRLQWD AEDFGNISVL RLPADMVWLP EIVLENNNDG
     SFQISYSCNV LIYPSGSVYW LPPAIFRSSC PISVTYFPFD WQNCSLKFSS LKYTTKEITL
     SLKQAEEDGR SYPVEWIIID PEGFTENGEW EIVHRPARVN VDPSVPLDSP NRQDVTFYLI
     IRRKPLFYVI NILVPCVLIS FMINLVFYLP ADCGEKTSMA ISVLLAQSVF LLLISKRLPA
     TSMAIPLIGK FLLFGMVLVT MVVVICVIVL NIHFRTPSTH VLSEPVKKLF LETLPEILHM
     SRPAEDGPSP GTLIRRSSSL GYISKAEEYF SLKSRSDLMF EKQSERHGLA RRLTTARRPP
     AGSEQAQQEL FSELKPAVDG ANFIVNHMKD QNNYNEEKDC WNRVARTVDR LCLFVVTPIM
     VVGTAWIFLQ GAYNQPPPQP FPGDPFSYLE KDKRFI
//
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