ID M7ASV4_CHEMY Unreviewed; 922 AA.
AC M7ASV4;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=Neuronal acetylcholine receptor subunit alpha-3 {ECO:0000256|ARBA:ARBA00039990};
GN ORFNames=UY3_15141 {ECO:0000313|EMBL:EMP27749.1};
OS Chelonia mydas (Green sea-turtle) (Chelonia agassizi).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC Americhelydia; Chelonioidea; Cheloniidae; Chelonia.
OX NCBI_TaxID=8469 {ECO:0000313|EMBL:EMP27749.1, ECO:0000313|Proteomes:UP000031443};
RN [1] {ECO:0000313|Proteomes:UP000031443}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23624526; DOI=10.1038/ng.2615;
RA Wang Z., Pascual-Anaya J., Zadissa A., Li W., Niimura Y., Huang Z., Li C.,
RA White S., Xiong Z., Fang D., Wang B., Ming Y., Chen Y., Zheng Y.,
RA Kuraku S., Pignatelli M., Herrero J., Beal K., Nozawa M., Li Q., Wang J.,
RA Zhang H., Yu L., Shigenobu S., Wang J., Liu J., Flicek P., Searle S.,
RA Wang J., Kuratani S., Yin Y., Aken B., Zhang G., Irie N.;
RT "The draft genomes of soft-shell turtle and green sea turtle yield insights
RT into the development and evolution of the turtle-specific body plan.";
RL Nat. Genet. 45:701-706(2013).
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; KB567559; EMP27749.1; -; Genomic_DNA.
DR AlphaFoldDB; M7ASV4; -.
DR STRING; 8469.M7ASV4; -.
DR eggNOG; KOG3645; Eukaryota.
DR Proteomes; UP000031443; Unassembled WGS sequence.
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; 2.
DR Gene3D; 2.70.170.10; Neurotransmitter-gated ion-channel ligand-binding domain; 2.
DR Gene3D; 1.20.58.390; Neurotransmitter-gated ion-channel transmembrane domain; 3.
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; 2.
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; 2.
DR Pfam; PF02932; Neur_chan_memb; 2.
DR PRINTS; PR00254; NICOTINICR.
DR PRINTS; PR00252; NRIONCHANNEL.
DR SUPFAM; SSF90112; Neurotransmitter-gated ion-channel transmembrane pore; 2.
DR SUPFAM; SSF63712; Nicotinic receptor ligand binding domain-like; 2.
DR PROSITE; PS00236; NEUROTR_ION_CHANNEL; 2.
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, ECO:0000313|EMBL:EMP27749.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000031443};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
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 TRANSMEM 203..226
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU000687"
FT TRANSMEM 238..256
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU000687"
FT TRANSMEM 268..289
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU000687"
FT TRANSMEM 659..683
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU000687"
FT TRANSMEM 690..712
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU000687"
FT TRANSMEM 724..745
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU000687"
FT TRANSMEM 895..917
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU000687"
FT DOMAIN 2..202
FT /note="Neurotransmitter-gated ion-channel ligand-binding"
FT /evidence="ECO:0000259|Pfam:PF02931"
FT DOMAIN 209..414
FT /note="Neurotransmitter-gated ion-channel transmembrane"
FT /evidence="ECO:0000259|Pfam:PF02932"
FT DOMAIN 452..657
FT /note="Neurotransmitter-gated ion-channel ligand-binding"
FT /evidence="ECO:0000259|Pfam:PF02931"
FT DOMAIN 665..912
FT /note="Neurotransmitter-gated ion-channel transmembrane"
FT /evidence="ECO:0000259|Pfam:PF02932"
SQ SEQUENCE 922 AA; 106065 MW; F56825297B9AF3BE CRC64;
MNHLLSPARY NKLIRPAVNS SQLVSIELLV SLAQLISVNE REQIMTTNVW LNQEWTDYRL
AWQPSDYEGI NKLRIPSKQI WLPDIVLYNN ADGTYEVSVY TNVILKNNGS IFWLPPAIYK
SACRIEVKHF PFDQQNCTLK FRSWTYDHTE IDLVLKTSMA SMDDFRPSGE WDIVALPGRR
TVNPLDPKYV DVTYDFIIKR KPLFYTINLI IPCVLITSLA ILVFYLPSDC GEKMTLCISV
LLALTVFLLL ISKIVPPTSL DVPLIGKYLM FTMVLVTFSI VTSVCVLNVH HRSPSTHTMP
PWVKVVFLHK LPTFLFMKRP ENNSARQRLS KRRKNKSDNL CTDAANLYKN STYFVNTASA
KKYDLKVTEN PDNISGHQDF RLRSSMKFSP EVQEAIDGVS FIADHMKSED NDQSDYTVFF
GNSIWPQEAS WVVSKPEAKH NLFSGCSCSE AEHRLFAALF ANYSQFIRPV ENVSDPAIIQ
FEVSMSQLVK VDEVNQIMET KLWLKHIWND YKLKWNPEEY GGVEFIRVPA DRIWKPDIVL
YNNAVGDFQV DDKTKAFLKY TGEVTWIPPA IFKSSCKIDV TYFPFDYQNC TMKFGSWSYD
KVKIDLVLIG STMNLQDYWE SGEWVIIKAP GYKHDIKYNC CEEVYPDITY SLYIRRLPLF
YTINMIIPCL LISFLTVLVF YLPSDCGEKV TLCISVLLSL TVFLLVITET IPSTSLVIPL
IGEYLLFTMI FVTLSIVITV FVLNVHYRTP KTHTMPEWVK TIFLNLLPKI MFMTRPANDK
EKNQKPKPLY SAELSDLNCF SSSETKCCKD GFICQDITCS CCWCQRIKFS DFSGNLTRST
SYESVDAPLS FSVLSPEMRD AIESVKYIAE NMKMQNEAKE IQDDWKYVAM VIDRIFLWVF
ILVCILGTAG LFLQPLMAGD EM
//
