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Database: UniProt
Entry: M4VNF2_APLCA
LinkDB: M4VNF2_APLCA
Original site: M4VNF2_APLCA 
ID   M4VNF2_APLCA            Unreviewed;       515 AA.
AC   M4VNF2;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 49.
DE   SubName: Full=Nicotinic acetylcholine receptor subunit type D {ECO:0000313|EMBL:AGI03860.1};
OS   Aplysia californica (California sea hare).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Heterobranchia; Euthyneura; Tectipleura; Aplysiida; Aplysioidea;
OC   Aplysiidae; Aplysia.
OX   NCBI_TaxID=6500 {ECO:0000313|EMBL:AGI03860.1};
RN   [1] {ECO:0000313|EMBL:AGI03860.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=24740855; DOI=10.1152/jn.00796.2013;
RA   White S.H., Carter C.J., Magoski N.S.;
RT   "A potentially novel nicotinic receptor in Aplysia neuroendocrine cells.";
RL   J. Neurophysiol. 112:446-462(2014).
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   EMBL; KC411668; AGI03860.1; -; mRNA.
DR   RefSeq; NP_001267772.1; NM_001280843.1.
DR   AlphaFoldDB; M4VNF2; -.
DR   EnsemblMetazoa; NM_001280843.1; NP_001267772.1; LOC101851082.
DR   GeneID; 101851082; -.
DR   OrthoDB; 2938410at2759; -.
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; cd18997; LGIC_ECD_nAChR; 1.
DR   CDD; cd19051; LGIC_TM_cation; 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; NEUROTRANSMITTER GATED ION CHANNEL; 1.
DR   PANTHER; PTHR18945:SF895; NICOTINIC ACETYLCHOLINE RECEPTOR ALPHA3, ISOFORM B; 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   2: Evidence at transcript level;
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, ECO:0000313|EMBL:AGI03860.1};
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..22
FT                   /evidence="ECO:0000256|RuleBase:RU000687"
FT   CHAIN           23..515
FT                   /evidence="ECO:0000256|RuleBase:RU000687"
FT                   /id="PRO_5022260976"
FT   TRANSMEM        248..271
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU000687"
FT   TRANSMEM        278..296
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU000687"
FT   TRANSMEM        308..334
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU000687"
FT   TRANSMEM        483..505
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU000687"
FT   DOMAIN          40..246
FT                   /note="Neurotransmitter-gated ion-channel ligand-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02931"
FT   DOMAIN          253..499
FT                   /note="Neurotransmitter-gated ion-channel transmembrane"
FT                   /evidence="ECO:0000259|Pfam:PF02932"
SQ   SEQUENCE   515 AA;  59189 MW;  F3645D6F99E909DA CRC64;
     MNILLRVFQF LISLSLQVPL RAQSGNYFDD MDYTRNLTDE QRLFRKLLLG YDKNTRPVFN
     ASDPVTIFLG ITLTQIFDLD EKNQVLTTNV WLDQEWHDQK LIWKPEDFNG LNKIRIPCRH
     IWKPDIVLYN SVEDYTDGYM QSLAMVSHDG TVFWPPIVKF QSTCQIDITY FPFDDQICNM
     KLGSWAYDGF QVDVNNRSVP VDLSNYVSNG EWHLVSVTAK RNVVYYPCCP EPFPDVIFTI
     HLQRRTLYYT YNVIIPCVML SSLTLLVFWM SPDSGEKVTL GLTVLLAFSV FMLLIAENMP
     ATSNFVPLIG MYLTSVMGIT SMSVMLAVLV SNISYKGQHQ IPLPRLMRYF IVGLARIMCT
     KLYYISPPNK TGGRVLSPAR NRRNFYRVGN GTHVSNDSGC ALVEYELGDT LGVNLENLRL
     PSSVRHQQAP ASVRSRSGER IKEDDIDLIL SLLKKLLVRE SEREEEDDLN KQWEEAARVI
     DRFLFYIFFL LTILATIVTL VIMPLTKPEK PTVLT
//
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