ID A0A0V1CW34_TRIBR Unreviewed; 1037 AA.
AC A0A0V1CW34;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE SubName: Full=Acetylcholine receptor subunit beta-type unc-29 {ECO:0000313|EMBL:KRY53525.1};
GN Name=unc-29 {ECO:0000313|EMBL:KRY53525.1};
GN ORFNames=T03_17620 {ECO:0000313|EMBL:KRY53525.1};
OS Trichinella britovi (Parasitic roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=45882 {ECO:0000313|EMBL:KRY53525.1, ECO:0000313|Proteomes:UP000054653};
RN [1] {ECO:0000313|EMBL:KRY53525.1, ECO:0000313|Proteomes:UP000054653}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS120 {ECO:0000313|EMBL:KRY53525.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) 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}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {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:KRY53525.1}.
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DR EMBL; JYDI01000084; KRY53525.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1CW34; -.
DR Proteomes; UP000054653; 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; cd19032; LGIC_ECD_nAChR_proto_beta-like; 1.
DR CDD; cd19064; LGIC_TM_nAChR; 1.
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; 4.
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 PANTHER; PTHR18945:SF471; ACETYLCHOLINE RECEPTOR SUBUNIT BETA-TYPE UNC-29; 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 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:KRY53525.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000054653};
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..21
FT /evidence="ECO:0000256|RuleBase:RU000687"
FT CHAIN 22..1037
FT /evidence="ECO:0000256|RuleBase:RU000687"
FT /id="PRO_5022270774"
FT TRANSMEM 251..274
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU000687"
FT TRANSMEM 286..304
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU000687"
FT TRANSMEM 316..339
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU000687"
FT TRANSMEM 491..509
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU000687"
FT TRANSMEM 768..791
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU000687"
FT TRANSMEM 803..821
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU000687"
FT TRANSMEM 833..856
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU000687"
FT TRANSMEM 993..1013
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU000687"
FT DOMAIN 51..249
FT /note="Neurotransmitter-gated ion-channel ligand-binding"
FT /evidence="ECO:0000259|Pfam:PF02931"
FT DOMAIN 259..508
FT /note="Neurotransmitter-gated ion-channel transmembrane"
FT /evidence="ECO:0000259|Pfam:PF02932"
FT DOMAIN 566..766
FT /note="Neurotransmitter-gated ion-channel ligand-binding"
FT /evidence="ECO:0000259|Pfam:PF02931"
FT DOMAIN 774..1009
FT /note="Neurotransmitter-gated ion-channel transmembrane"
FT /evidence="ECO:0000259|Pfam:PF02932"
SQ SEQUENCE 1037 AA; 120196 MW; 51F2E583D1068866 CRC64;
MPSAYYLQCL LLLWLFLKHL SRFIVHFCFT SVYNNNNNNF SKDLCAYDED LIYSDIFHGY
NPLVLPIASE NESRVVIEFG MSMILLVNVD EKNQILQTNV WLTMSWKDPY LRWNPADYNM
IKDIRVPVKH IWVPDVVLFN NADGHYEVSF FSNVMVESDG TILWVPPAIY KSSCTIDVEN
FPFDEQTCLL VFGSWTYTHQ EVHLTFYRNK KFIELQDYSY SGVWDIIDVP GIVHDSGSKL
TFCIKIKRKP LFYTVLFGIP TMMMAYLSVF VFYLPAGASE KITLSINLLL ALVVFMLLIS
KILPSNSNTL PLIAKYLLLT FILDIMAIIM TVIILNIYFR RPGCSRLPHW ARSLFLVYLP
RVLLMKRPST QRNSVVEYVG KKCDNQICLI NELSKRVSPK EALPNESNQS VNDDLKQMFN
NTADVEITLP ELLDQPGNLQ DSIFNLNTVN FQMLNQVLIS TDQIFDHFRR VRSTEAVREE
WRFVSLVLDR LLLYVFFGIT LGGTAHIFFQ IPNLFLRVDQ REIIERIYAQ YATQEDFADD
QFFLEKLILL LATNIPLYLA LCSEDEDRLM IDLFRGYNSL VQPIANANST PLLLRFGLQL
ILLINLDEKN QIMHTNVWLT LKWYDFQMRW NPVNYGEIRQ IRVATDKVWL PDIVLFNNAD
GNYEVSYHSN VVIDHDGKML WVPPAIYKSS CIIDVEYFPF DEQVCTLLFG SWTYNEREII
LSFNDGVEGV DLQDYSFSSI WDIIEAPAVL TRQKSRIEFR IRVRRKSLFY TVVLIIPTVL
MAFLSMMVFY LPACAGEKIT LTINVLLSLV VFLLLVSKIL PPTSSTIPLM AKYLLLTFLL
NIITILVTVI IINVFFRGPT THRMPQWVRH TFLDFLPKML MMKRPKRVSK QPYYGCVDTF
RRNNASRLNV PQPQPSYLDA NESIQAVPQY SVPDHQSSES FAYCQLAGQY PLTREACKAI
EAIEYISEHL RTDEEYQSVR EDWKYVAMVI DRLLLYIFFG VTLGGTVGVL LSAPNVFEFV
DQAQIVSRLS LLYRGET
//
