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Database: UniProt
Entry: G1RBG3_NOMLE
LinkDB: G1RBG3_NOMLE
Original site: G1RBG3_NOMLE 
ID   G1RBG3_NOMLE            Unreviewed;       487 AA.
AC   G1RBG3;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 72.
DE   RecName: Full=Neuronal acetylcholine receptor subunit alpha-3 {ECO:0000256|ARBA:ARBA00039990};
GN   Name=CHRNA3 {ECO:0000313|Ensembl:ENSNLEP00000010560.1};
OS   Nomascus leucogenys (Northern white-cheeked gibbon) (Hylobates leucogenys).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hylobatidae;
OC   Nomascus.
OX   NCBI_TaxID=61853 {ECO:0000313|Ensembl:ENSNLEP00000010560.1, ECO:0000313|Proteomes:UP000001073};
RN   [1] {ECO:0000313|Ensembl:ENSNLEP00000010560.1, ECO:0000313|Proteomes:UP000001073}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   Gibbon Genome Sequencing Consortium;
RL   Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSNLEP00000010560.1}
RP   IDENTIFICATION.
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}. Golgi
CC       apparatus {ECO:0000256|ARBA:ARBA00004555}. 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-3/CHRNA3 sub-
CC       subfamily. {ECO:0000256|ARBA:ARBA00038373}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|RuleBase:RU000687}.
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DR   EMBL; ADFV01087516; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ADFV01087517; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ADFV01087518; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ADFV01087519; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ADFV01087520; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; G1RBG3; -.
DR   Ensembl; ENSNLET00000011076.2; ENSNLEP00000010560.1; ENSNLEG00000008651.2.
DR   eggNOG; KOG3645; Eukaryota.
DR   GeneTree; ENSGT00940000158487; -.
DR   TreeFam; TF315605; -.
DR   Proteomes; UP000001073; Chromosome 6.
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; cd19016; LGIC_ECD_nAChR_A3; 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; 1.
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:SF831; NEURONAL ACETYLCHOLINE RECEPTOR SUBUNIT ALPHA-3; 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   Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
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:UP000001073};
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..29
FT                   /evidence="ECO:0000256|RuleBase:RU000687"
FT   CHAIN           30..487
FT                   /note="Neuronal acetylcholine receptor subunit alpha-3"
FT                   /evidence="ECO:0000256|RuleBase:RU000687"
FT                   /id="PRO_5022273076"
FT   TRANSMEM        240..264
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU000687"
FT   TRANSMEM        271..293
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU000687"
FT   TRANSMEM        305..326
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU000687"
FT   DOMAIN          33..238
FT                   /note="Neurotransmitter-gated ion-channel ligand-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02931"
FT   DOMAIN          246..465
FT                   /note="Neurotransmitter-gated ion-channel transmembrane"
FT                   /evidence="ECO:0000259|Pfam:PF02932"
FT   REGION          455..487
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        455..481
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   487 AA;  55396 MW;  07B655229A233D55 CRC64;
     MGSGPLSLLL ALSPPRLLLL LSLLPVARAS EAEHRLFERL FEDYNEIIRP VANVSDPVII
     HFEVSMSQLV KVDEVNQIME TNLWLKQIWN DYKLKWNPSD YGGAEFMRVP AQKIWKPDIV
     LYNNAVGDFQ VDDKTKALLK YTGEVTWIPP AIFKSSCKID VTYFPFDYQN CTMKFGSWSY
     DKAKIDLVLI GSSMNLKDYW ESGEWAIIKA PGYKHDIKYN CCEEIYPDIT YSLYIRRLPL
     FYTINLIIPC LLISFLTVLV FYLPSDCGEK VTLCISVLLS LTVFLLVITE TIPSTSLVIP
     LIGEYLLFTM IFVTLSIVIT VFVLNVHYRT PTTHTMPSWV KTVFLNLLPR VMFMTRPTGN
     EGNAQKPRPL YGAELSNLNC FSRAESKGCK EGYPCQDGMC GYCHHRRIKI SNFSANLTRS
     SSSESVDAVL SLSALSPEIK EAIQSVKYIA ENMKAQNEAK EEQKAQEIQQ LKRKEKSTET
     SDQEPGL
//
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