ID E3LRP0_CAERE Unreviewed; 486 AA.
AC E3LRP0;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 24-JAN-2024, entry version 67.
DE SubName: Full=CRE-EAT-2 protein {ECO:0000313|EMBL:EFP07617.1};
GN Name=Cre-eat-2 {ECO:0000313|EMBL:EFP07617.1};
GN ORFNames=CRE_26372 {ECO:0000313|EMBL:EFP07617.1};
OS Caenorhabditis remanei (Caenorhabditis vulgaris).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=31234 {ECO:0000313|Proteomes:UP000008281};
RN [1] {ECO:0000313|Proteomes:UP000008281}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PB4641 {ECO:0000313|Proteomes:UP000008281};
RG Caenorhabditis remanei Sequencing Consortium;
RA Wilson R.K.;
RT "PCAP assembly of the Caenorhabditis remanei genome.";
RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
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; DS268413; EFP07617.1; -; Genomic_DNA.
DR RefSeq; XP_003113705.1; XM_003113657.1.
DR AlphaFoldDB; E3LRP0; -.
DR STRING; 31234.E3LRP0; -.
DR EnsemblMetazoa; CRE26372.1; CRE26372.1; WBGene00054416.
DR GeneID; 9815775; -.
DR KEGG; crq:GCK72_006580; -.
DR CTD; 9815775; -.
DR eggNOG; KOG3646; Eukaryota.
DR HOGENOM; CLU_018074_1_0_1; -.
DR InParanoid; E3LRP0; -.
DR OMA; FNSANEH; -.
DR OrthoDB; 2878913at2759; -.
DR Proteomes; UP000008281; 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; 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:SF829; NEURONAL ACETYLCHOLINE RECEPTOR SUBUNIT EAT-2; 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 Postsynaptic cell membrane {ECO:0000256|ARBA:ARBA00023257};
KW Receptor {ECO:0000256|ARBA:ARBA00023170};
KW Reference proteome {ECO:0000313|Proteomes:UP000008281};
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..25
FT /evidence="ECO:0000256|RuleBase:RU000687"
FT CHAIN 26..486
FT /evidence="ECO:0000256|RuleBase:RU000687"
FT /id="PRO_5022263729"
FT TRANSMEM 239..258
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU000687"
FT TRANSMEM 270..288
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU000687"
FT TRANSMEM 300..327
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU000687"
FT TRANSMEM 450..469
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU000687"
FT DOMAIN 29..238
FT /note="Neurotransmitter-gated ion-channel ligand-binding"
FT /evidence="ECO:0000259|Pfam:PF02931"
FT DOMAIN 246..467
FT /note="Neurotransmitter-gated ion-channel transmembrane"
FT /evidence="ECO:0000259|Pfam:PF02932"
SQ SEQUENCE 486 AA; 56669 MW; 6F646BE1A3CD182B CRC64;
MNFYFFLFLK LFTIYLCFLT KSVDSSDDEY RLLKDLREGY DPMERPVSDH MKPVNVKLRL
ILQQLVDVDE KNQVITLVVW TQYTWSDYKM KWSPDEYGNI TTLQIPYGTL WKPDILLFNS
ANEHFDSSFP VNMVVSSDGS VLFAPPGIMQ FSCSLSMTWF PYDEQVCYLK FGSWTYGKKL
DLQIDDADLP DGHKMDLQYY VPNGEFDLIS TPAFRKSTTF LDETYVELYF HMHLKRRTMY
YGLNWIIPSI LISLSNILGF TMPVECGEKV TLQITNFLSI MVFLAMVSEV APPTSESIPI
IAAFFSFAIV ILGVSICVSL ITVNIFYRHP KMHRMGDWTR YIFLEWLPWI LLMSRPDHVF
RKPKREKKKE EDEESNTGKV EIMELLSEQQ NQNPRPRLLV NSQIVMDSTI PFLEEVIGYL
KVFKAKLDDD EEEEEEILNW RFMAMVIDRF SLFLFTGLIF GTTFVIFAAC PNLLSADQII
ETAHVP
//
