ID A0A3L8Q8J4_CHLGU Unreviewed; 950 AA.
AC A0A3L8Q8J4;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=Neuronal acetylcholine receptor subunit alpha-2 {ECO:0008006|Google:ProtNLM};
GN ORFNames=DV515_00018083 {ECO:0000313|EMBL:RLV63626.1};
OS Chloebia gouldiae (Gouldian finch) (Erythrura gouldiae).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Passeridae;
OC Chloebia.
OX NCBI_TaxID=44316 {ECO:0000313|EMBL:RLV63626.1, ECO:0000313|Proteomes:UP000276834};
RN [1] {ECO:0000313|EMBL:RLV63626.1, ECO:0000313|Proteomes:UP000276834}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Red01 {ECO:0000313|EMBL:RLV63626.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:RLV63626.1};
RX PubMed=30282656;
RA Toomey M.B., Marques C.I., Andrade P., Araujo P.M., Sabatino S.,
RA Gazda M.A., Afonso S., Lopes R.J., Corbo J.C., Carneiro M.;
RT "A non-coding region near Follistatin controls head colour polymorphism in
RT the Gouldian finch.";
RL Proc. R. Soc. B 285:0-0(2018).
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: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the ligand-gated ion channel (TC 1.A.9) family.
CC {ECO:0000256|RuleBase:RU000687}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RLV63626.1}.
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DR EMBL; QUSF01002298; RLV63626.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3L8Q8J4; -.
DR STRING; 44316.ENSEGOP00005022267; -.
DR Proteomes; UP000276834; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005230; F:extracellular ligand-gated monoatomic ion 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 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; PR00252; NRIONCHANNEL.
DR SUPFAM; SSF90112; Neurotransmitter-gated ion-channel transmembrane pore; 2.
DR SUPFAM; SSF63712; Nicotinic receptor ligand binding domain-like; 1.
DR PROSITE; PS00236; NEUROTR_ION_CHANNEL; 1.
PE 3: Inferred from homology;
KW Ion channel {ECO:0000256|RuleBase:RU000687};
KW Ion transport {ECO:0000256|RuleBase:RU000687};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU000687};
KW Reference proteome {ECO:0000313|Proteomes:UP000276834};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU000687};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU000687}; Transport {ECO:0000256|RuleBase:RU000687}.
FT TRANSMEM 107..131
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU000687"
FT TRANSMEM 138..160
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU000687"
FT TRANSMEM 172..193
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU000687"
FT TRANSMEM 924..946
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU000687"
FT DOMAIN 2..105
FT /note="Neurotransmitter-gated ion-channel ligand-binding"
FT /evidence="ECO:0000259|Pfam:PF02931"
FT DOMAIN 113..345
FT /note="Neurotransmitter-gated ion-channel transmembrane"
FT /evidence="ECO:0000259|Pfam:PF02932"
FT DOMAIN 907..941
FT /note="Neurotransmitter-gated ion-channel transmembrane"
FT /evidence="ECO:0000259|Pfam:PF02932"
FT REGION 262..315
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 950 AA; 106295 MW; 6A0D60E9610491B0 CRC64;
MTKAHLSWDG TVKWSPPAIY KSSCSIDVTF FPFDQQSCKM KFGSWTYDKA KIDLENMDHQ
VDLKNYWESG EWAIIDAVAT YNSKKYDCCT EIYPDITFYF VIRRLPLFYT INLIIPCLLI
SCLTVLVFYL PSDCGEKITL CISVLLSLTV FLLLITEIIP STSLVIPLIG EYLLFTMIFV
TLSIVITVFV LNVHHRSPGT HAMPTWVRRF FLGLLPRWLA MKRPPPSSSS SSPVVVALDE
GTGGQHERLS ASRCWLETDV DDKWDEEEEE EEEEKTFPGR PAEFRRGQGG KAPGGTSEKI
QEEEEEEEEG SGRGLALSPG VLKALQGLQD IAEHLRAEDA DSAVSAGRHR GGRRAQSWEG
KFWDLWMGLE IPKLGSSGIY RWGWRSQKLG SSGIPFLFLT AKIGKGSSGI CGWGWRSQKL
GRAGLGSMGG AGDPKIGKGS SGIYKWGRRA QKLEVLGSTN GAGDPKIGNG SSGIYKWVWR
SPNLGMEVLG FVDGPGDPNI WKGSSGIYKW GRRSQHWEGP GICKWGWRSP NLGMEVLGFL
GSSGIHRWGW RSQNWEWKFW DPWMGLEIPK IGNGSSGIHG WGWRSQNWEG KFWDLQMGLE
IPKLGNGSSG ICGWAWRSQH MEGKFWDLQM GQEIPTLGRS WDLQMGLEIP KLGMEVLGSM
GGAGDLKNRE WKFWDLWMGL EIPKLEGPGS HGWGWRSQTW KWKFWDSGLV PEIPKLGREV
LSQNREVLGS TDGAGDPKTG NWEWKFLDLW VGLEIPNLGS SGIPFLFLRA KIGNGSSGIH
KWGWRSQHWE VLGSTNGAGD PKNWEGPFRH PWLVPKAPQT REKLHDPSPS SMDLHGLQDQ
PRVPPAPVGC GNAAFPLFPK RIWKTPGGTS SSLEISTSIR IPRKNSEFSE EALGGLLIPG
DSRGIFHRQV KEDWKYVAMV IDRIFLWIFI IVCLLGTAGL FLPPYLAGMI
//
