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Database: UniProt
Entry: A0A0V0WK14_9BILA
LinkDB: A0A0V0WK14_9BILA
Original site: A0A0V0WK14_9BILA 
ID   A0A0V0WK14_9BILA        Unreviewed;       904 AA.
AC   A0A0V0WK14;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=Glutamate receptor 1 {ECO:0000313|EMBL:KRX75960.1};
GN   Name=glr-1 {ECO:0000313|EMBL:KRX75960.1};
GN   ORFNames=T06_8229 {ECO:0000313|EMBL:KRX75960.1};
OS   Trichinella sp. T6.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=92179 {ECO:0000313|EMBL:KRX75960.1, ECO:0000313|Proteomes:UP000054673};
RN   [1] {ECO:0000313|EMBL:KRX75960.1, ECO:0000313|Proteomes:UP000054673}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS34 {ECO:0000313|EMBL:KRX75960.1};
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}.
CC   -!- SIMILARITY: Belongs to the glutamate-gated ion channel (TC 1.A.10.1)
CC       family. {ECO:0000256|ARBA:ARBA00008685}.
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:KRX75960.1}.
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DR   EMBL; JYDK01000111; KRX75960.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0V0WK14; -.
DR   STRING; 92179.A0A0V0WK14; -.
DR   Proteomes; UP000054673; Unassembled WGS sequence.
DR   GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-KW.
DR   GO; GO:0015276; F:ligand-gated monoatomic ion channel activity; IEA:InterPro.
DR   GO; GO:0038023; F:signaling receptor activity; IEA:InterPro.
DR   CDD; cd06380; PBP1_iGluR_AMPA; 1.
DR   Gene3D; 1.10.287.70; -; 1.
DR   Gene3D; 3.40.50.2300; -; 2.
DR   Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 2.
DR   InterPro; IPR001828; ANF_lig-bd_rcpt.
DR   InterPro; IPR019594; Glu/Gly-bd.
DR   InterPro; IPR001508; Iono_Glu_rcpt_met.
DR   InterPro; IPR015683; Ionotropic_Glu_rcpt.
DR   InterPro; IPR001320; Iontro_rcpt_C.
DR   InterPro; IPR028082; Peripla_BP_I.
DR   PANTHER; PTHR18966:SF544; GLUTAMATE RECEPTOR 1; 1.
DR   PANTHER; PTHR18966; IONOTROPIC GLUTAMATE RECEPTOR; 1.
DR   Pfam; PF01094; ANF_receptor; 1.
DR   Pfam; PF00060; Lig_chan; 1.
DR   Pfam; PF10613; Lig_chan-Glu_bd; 1.
DR   PRINTS; PR00177; NMDARECEPTOR.
DR   SMART; SM00918; Lig_chan-Glu_bd; 1.
DR   SMART; SM00079; PBPe; 1.
DR   SUPFAM; SSF53822; Periplasmic binding protein-like I; 1.
DR   SUPFAM; SSF53850; Periplasmic binding protein-like II; 1.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Ion channel {ECO:0000256|ARBA:ARBA00023303};
KW   Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW   Ligand-gated ion channel {ECO:0000256|ARBA:ARBA00023286};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Postsynaptic cell membrane {ECO:0000256|ARBA:ARBA00023257};
KW   Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000313|EMBL:KRX75960.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054673};
KW   Signal {ECO:0000256|SAM:SignalP}; Synapse {ECO:0000256|ARBA:ARBA00023018};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           18..904
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5006871726"
FT   TRANSMEM        578..597
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        656..678
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        844..868
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          447..821
FT                   /note="Ionotropic glutamate receptor C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00079"
FT   DOMAIN          457..522
FT                   /note="Ionotropic glutamate receptor L-glutamate and
FT                   glycine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00918"
SQ   SEQUENCE   904 AA;  103506 MW;  2FD91F0CBC6A6859 CRC64;
     MFHVKWILFL LFNHANGNLR VPVGALFRDE MEDGLISVMT YATMENNYQQ SPPPFRLETK
     KGIIRTDSVN NWALTRLGCE VIKDGAFVLM GTANYPSREA FVALSNLLHL PLINWSTAKR
     ESQNGQFEIS MAQNTAEAVG DFIRLKMWKN FTYMYDSIDG LYEYELLNNY LKKTGTEVRT
     QMLYLKNIEP DYFRFFLNFH SSRFASDSYV ILHISNRKKL KFILRDLLDA AMKTKNFHYL
     ISGQEVLDAE IENFKIGLIN VSGFQYEGRD KSSFKDFLEK WSRLDSQLLH YHKASTITAE
     EALVYDAIQI VIEAFKSIAK VNASALKRYY KKDEFINEDY HGLLCYTFED KLNPDRPFLP
     LRHGEMMYDA LKKTRLDGIS GNVQFDNDGN RVNYTLKLTE VLQTGHNAGV VNVQKRLWRQ
     KAGFQNGENH PQKGEKINKN IQPFNRTRII TTIINEPFVM FKKDADQFTG NDRFEGFCVD
     LMKLLSEKIE NFPYIIKPVK DNQYGAVDQN GRWNGMVGEL IRGEADLAIA SLTINTLRER
     VVDFSKPFLT TGISIMIKKP DKQEFSIFSF MQPLSTEVWI FIIIAYGGVS IVIFFIARFS
     PYEWNYNQSS TYGCTSLSDF TIDNCLWVTL AALMQQGTDI MPRLMISASC RIASSIWWFF
     TMIIVSSYTA NLAAFLTLEK MHAPIESVED LARQTKIKYG IQASGSTAQF FKESKVDVHR
     RMWQYMSTQV PSPLVSSYAE GIQRVRESKG QYAFLLEATT NEYASTRKPC DTIKVGANLN
     SIGYGVATPF GSDLSEKINL AILELQEIGE LKRLEMKWWY EKGQCEQGMS DSQSASLTLS
     KVAGIFYILT VGIIIAMLVS FVEIFYYLNA EKHSKIPSEP FCIQSAVENY GKAEMLTNSK
     EITT
//
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