ID W8BRS1_CERCA Unreviewed; 476 AA.
AC W8BRS1;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 24-JAN-2024, entry version 41.
DE SubName: Full=(Mediterranean fruit fly) hypothetical protein {ECO:0000313|EMBL:CAD6992012.1};
DE SubName: Full=Glycine receptor subunit alpha-3 {ECO:0000313|EMBL:JAB99583.1};
GN Name=GLRA3 {ECO:0000313|EMBL:JAB99583.1};
GN ORFNames=CCAP1982_LOCUS898 {ECO:0000313|EMBL:CAD6992012.1};
OS Ceratitis capitata (Mediterranean fruit fly) (Tephritis capitata).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Tephritoidea;
OC Tephritidae; Ceratitis; Ceratitis.
OX NCBI_TaxID=7213 {ECO:0000313|EMBL:JAB99583.1};
RN [1] {ECO:0000313|EMBL:JAB99583.1}
RP NUCLEOTIDE SEQUENCE.
RA Geib S.;
RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:JAB99583.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=24495485; DOI=10.1186/1471-2164-15-98;
RA Calla B., Hall B., Hou S., Geib S.M.;
RT "A genomic perspective to assessing quality of mass-reared SIT flies used
RT in Mediterranean fruit fly (Ceratitis capitata) eradication in
RT California.";
RL BMC Genomics 15:98-98(2014).
RN [3] {ECO:0000313|EMBL:CAD6992012.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=EGII {ECO:0000313|EMBL:CAD6992012.1};
RA Whitehead M.;
RL Submitted (NOV-2020) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CAJHJT010000001; CAD6992012.1; -; Genomic_DNA.
DR EMBL; GAMC01006972; JAB99583.1; -; mRNA.
DR AlphaFoldDB; W8BRS1; -.
DR Proteomes; UP000606786; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0005254; F:chloride channel activity; IEA:UniProt.
DR GO; GO:0005230; F:extracellular ligand-gated monoatomic ion channel activity; IEA:InterPro.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
DR CDD; cd18992; LGIC_ECD_HisCl; 1.
DR CDD; cd19049; LGIC_TM_anion; 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; IPR006028; GABAA/Glycine_rcpt.
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 NCBIfam; TIGR00860; LIC; 1.
DR PANTHER; PTHR18945:SF598; HISTAMINE-GATED CHLORIDE CHANNEL ALPHA1 SUBUNIT; 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; PR00253; GABAARECEPTR.
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 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 Receptor {ECO:0000313|EMBL:JAB99583.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000606786};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU000687};
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..476
FT /evidence="ECO:0000256|RuleBase:RU000687"
FT /id="PRO_5036511862"
FT TRANSMEM 236..260
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU000687"
FT TRANSMEM 301..324
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU000687"
FT TRANSMEM 455..473
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU000687"
FT DOMAIN 37..235
FT /note="Neurotransmitter-gated ion-channel ligand-binding"
FT /evidence="ECO:0000259|Pfam:PF02931"
FT DOMAIN 243..328
FT /note="Neurotransmitter-gated ion-channel transmembrane"
FT /evidence="ECO:0000259|Pfam:PF02932"
FT REGION 340..363
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 415..440
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 416..434
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 476 AA; 54973 MW; 1C3050B9BCAB0044 CRC64;
MEYQIFLLVI FSICLEKFTT GEYQQSLAIT DILPEDIKRY DKMRPPKKDG QPTIVYFHVT
VMGLDSIDEN SMTYVADVFF AQTWKDHRLR LPENMTQEYR LLEVDWLKNM WRPDSFFKNA
KSVTFQTMTI PNHYMWLYKD KTILYMVKLT LKLSCIMNFA IYPHDTQECK LQMESLSHTT
DDMIFQWDPT TPLVVDENIE LPQVALIRNE TADCTQVYST GNFTCLEVVF TLKRRLVYYV
FNTYIPTCMI VIMSWVSFWI KPEAAPARVT LGVTSLLTLS TQHAKSQSSL PPVSYLKAVD
AFMSVCTVFV FMALMEYCLI NIVLSDTPIP KPIAYPPKPV PEGAKKEPEK PPAPTPAPAV
TPAKVVPDEK IEKIEKIFDE MTKNRRVVHS RRVVRPPLDA DGPWIPRQES RIILTPTIAP
PPPPPPPEPE PPKPKLTPQQ ERLKRAIYID RTSRVLFPAL FASLNGIYWV IFYEYL
//
