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Database: UniProt
Entry: A0A0M3JQW2_ANISI
LinkDB: A0A0M3JQW2_ANISI
Original site: A0A0M3JQW2_ANISI 
ID   A0A0M3JQW2_ANISI        Unreviewed;       743 AA.
AC   A0A0M3JQW2;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   SubName: Full=Glutamate receptor {ECO:0000313|WBParaSite:ASIM_0001007901-mRNA-1};
GN   ORFNames=ASIM_LOCUS9810 {ECO:0000313|EMBL:VDK41779.1};
OS   Anisakis simplex (Herring worm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Ascaridomorpha; Ascaridoidea; Anisakidae; Anisakis;
OC   Anisakis simplex complex.
OX   NCBI_TaxID=6269 {ECO:0000313|Proteomes:UP000036680, ECO:0000313|WBParaSite:ASIM_0001007901-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:ASIM_0001007901-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (FEB-2017) to UniProtKB.
RN   [2] {ECO:0000313|EMBL:VDK41779.1, ECO:0000313|Proteomes:UP000267096}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   Pathogen Informatics;
RL   Submitted (NOV-2018) 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}.
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DR   EMBL; UYRR01030972; VDK41779.1; -; Genomic_DNA.
DR   WBParaSite; ASIM_0001007901-mRNA-1; ASIM_0001007901-mRNA-1; ASIM_0001007901.
DR   Proteomes; UP000036680; Unplaced.
DR   Proteomes; UP000267096; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004970; F:ionotropic glutamate receptor activity; IEA:InterPro.
DR   Gene3D; 1.10.287.70; -; 1.
DR   Gene3D; 3.40.50.2300; -; 1.
DR   Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 2.
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:SF575; EYE-ENRICHED KAINATE RECEPTOR, ISOFORM B-RELATED; 1.
DR   PANTHER; PTHR18966; IONOTROPIC GLUTAMATE 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:ARBA00023286};
KW   Ion transport {ECO:0000256|ARBA:ARBA00023286};
KW   Ligand-gated ion channel {ECO:0000256|ARBA:ARBA00023286};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Receptor {ECO:0000256|ARBA:ARBA00023170};
KW   Reference proteome {ECO:0000313|Proteomes:UP000267096};
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   TRANSMEM        442..463
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        525..549
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          312..694
FT                   /note="Ionotropic glutamate receptor C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00079"
FT   DOMAIN          320..386
FT                   /note="Ionotropic glutamate receptor L-glutamate and
FT                   glycine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00918"
SQ   SEQUENCE   743 AA;  84151 MW;  A2BE756D85DD19DF CRC64;
     MFDHFELTID LTNRICEQLT ERCVAIFGPK HYPANVIASS YTNHLSVPHF HIGPRSAIRI
     PSSDIDRFLF EIRIQCEIKN QNVAHYAHSK SLENIINFCR SVDLFPPPRT ISDVLLGVVH
     YYKWTSMVLL YGHPSGIFDT MTLDLSEERI AECNITAFSF VHPSTATEAL RNALIEHHFP
     VPASSVHMKL AVWSDSLLLL AESIKSTNEL ILNKDVFSCD KSWQYGAQLT ERIINSYSKG
     ITGSIALDRS GKRANSSIIV MKRSKSGFEE LGQWQSANAE FVLAVASQNE TKKKESLENK
     TLKITVYLVY ILFDVFVEEP FVMLKKLEKG EQLNGNDQYE GYCIDLLQKI AEIRKFKYIL
     HEVKDKSYGS KEANGKWNGM VGELQRGDAD LAVASLTISY SRSEVIDFTV PYMHLGISIL
     FKKPETTDPS FFAFMSPLSV DVWVSMLAAY VVTSLAIWLL AAISPYERLD SNRDRSLVIL
     PKQFTFLNSF WFTVSSLMQQ SRITVNSHLS LQGSDLSPRA ASTRIAAVIW WFFTLIIISS
     YTANLAAFLT AQRMVSPIES ADDLAKQTKI KYGTLGRGST MIFFSVLFTE SKIDTYERMW
     KLMSSQPNLL VNSSKEGIWR VKTSDYAYLM ESSMLEYAVE RDCDLVQIGG LIDQKGYGIG
     LPKGSPYREL ISTTILQLQE KTVLTEMKDR WWKRKRGGGY CDASTTIGTD LGTVSLYGIF
     IILVRYTHFF HLEKLIGQVH VPE
//
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