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Database: UniProt
Entry: A0A0V1PNI0_9BILA
LinkDB: A0A0V1PNI0_9BILA
Original site: A0A0V1PNI0_9BILA 
ID   A0A0V1PNI0_9BILA        Unreviewed;       901 AA.
AC   A0A0V1PNI0;
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:KRZ97745.1};
GN   Name=glr-1 {ECO:0000313|EMBL:KRZ97745.1};
GN   ORFNames=T08_8631 {ECO:0000313|EMBL:KRZ97745.1};
OS   Trichinella sp. T8.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=92180 {ECO:0000313|EMBL:KRZ97745.1, ECO:0000313|Proteomes:UP000054924};
RN   [1] {ECO:0000313|EMBL:KRZ97745.1, ECO:0000313|Proteomes:UP000054924}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS272 {ECO:0000313|EMBL:KRZ97745.1};
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:KRZ97745.1}.
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DR   EMBL; JYDM01000002; KRZ97745.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0V1PNI0; -.
DR   STRING; 92180.A0A0V1PNI0; -.
DR   Proteomes; UP000054924; 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:KRZ97745.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054924};
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..901
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5006884390"
FT   TRANSMEM        578..597
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        653..675
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        841..865
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          447..818
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   901 AA;  103236 MW;  BC9D6D9C9E5A553C CRC64;
     MFHVKWILFL LFNHANGNLR VPVGALFRDE MEDGLISVMT YATMENNYQQ NPPPFRLETK
     KGIIRTDSVN NWALTRLGCE VIKDGAFVLM GTANYPSREA FVALSNLLHL PLINWSTAKR
     ESQNGQFEIN MAQNTAEAVG DFIRLKMWKN FTYMYDSIDG LYEYELLNNY LKKTGTEVRT
     QMLYLKNIEP DYFRFFLNFH SSRFASDSYV ILHISNRKKL KFILRDLLDA AMKTKNFHYL
     ISGQEVLDAE IEKFKIGLIN VSGFQYEGRD KSSFKDFLEK WSRLDSQLLH YHKASTITAE
     EALVYDAIQI VIEAFKSIAK VNASALKRYY KKDEFINEDY HGLLCYTFED KMNPDRPFLP
     LRHGEMMYDA LKKTRLDGIS GNVQFDDDGN RVNYTLKLTE VLQTGHNAGV VNVQKRLWRQ
     KAGFQNGEDH PQKGEKINKN IQPFNRTRII TTIINEPFVM FKKDADQFTG NDRFEGFCVD
     LMKLLSEKIE NFPYIIKPVK DNQYGAVDQN GRWNGMVGEL IRGEADLAIA SLTINTLRER
     VVDFSKPFLT TGISIMIKKP DKQEFSIFSF MQPLSTEVWI FIIIAYGGVS IVIFFIARFS
     PYEWNYNQSS TYGCTSLSDF TIDNCLWVTL AALMQQGTDI MPRSASCRIA SSIWWFFTMI
     IVSSYTANLA AFLTLEKMHA PIESVEDLAR QTKIKYGIQA SGSTAQFFKE SKVDVHRRMW
     QYMSTQVPSP LVSSYAEGIQ RVRESKGQYA FLLEATTNEY ASTRKPCDTI KVGANLNSIG
     YGVATPFGSD LSEKINLAIL ELQEIGELKR LEMKWWYEKG QCEQGMSDSQ SASLTLSKVA
     GIFYILTVGI IIAMLVSFVE IFYYLNAEKH SKIPSEPFCI QSAVENYGKA EMLTNSKEIT
     T
//
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