ID H6S0J1_PLEBA Unreviewed; 861 AA.
AC H6S0J1;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE SubName: Full=Glutamate receptor kainate-like protein {ECO:0000313|EMBL:ADV31314.1};
OS Pleurobrachia bachei (Sea gooseberry).
OC Eukaryota; Metazoa; Ctenophora; Tentaculata; Cydippida; Pleurobrachiidae;
OC Pleurobrachia.
OX NCBI_TaxID=34499 {ECO:0000313|EMBL:ADV31314.1};
RN [1] {ECO:0000313|EMBL:ADV31314.1}
RP NUCLEOTIDE SEQUENCE.
RA Kohn A.B., Moroz L.;
RT "Cloning and characterization of glutamate receptors from the ctenophore,
RT Pleurobrachia bachei.";
RL Submitted (JAN-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0007829|PDB:4ZDM}
RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 347-743, AND DISULFIDE BONDS.
RX PubMed=26460032; DOI=10.1073/pnas.1513771112;
RA Alberstein R., Grey R., Zimmet A., Simmons D.K., Mayer M.L.;
RT "Glycine activated ion channel subunits encoded by ctenophore glutamate
RT receptor genes.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:E6048-E6057(2015).
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}.
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DR EMBL; GU395550; ADV31314.1; -; mRNA.
DR PDB; 4ZDM; X-ray; 1.50 A; A=346-743.
DR PDBsum; 4ZDM; -.
DR AlphaFoldDB; H6S0J1; -.
DR SMR; H6S0J1; -.
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 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; IONOTROPIC GLUTAMATE RECEPTOR; 1.
DR PANTHER; PTHR18966:SF422; KAINATE-TYPE IONOTROPIC GLUTAMATE RECEPTOR SUBUNIT 1D; 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 1: Evidence at protein level;
KW 3D-structure {ECO:0007829|PDB:4ZDM};
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:ADV31314.1};
KW 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 TRANSMEM 483..502
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 581..606
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 758..779
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 353..735
FT /note="Ionotropic glutamate receptor C-terminal"
FT /evidence="ECO:0000259|SMART:SM00079"
FT DOMAIN 363..429
FT /note="Ionotropic glutamate receptor L-glutamate and
FT glycine-binding"
FT /evidence="ECO:0000259|SMART:SM00918"
FT REGION 822..848
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 372..380
FT /evidence="ECO:0007829|PDB:4ZDM"
SQ SEQUENCE 861 AA; 95439 MW; 2CC3727FC76BC066 CRC64;
MLNYVTSSNT ACSMLESGIS VVLQRGPSDD SIMYSGYFGV FNIPVMTVSA SSSQLRRKTS
SVVTMVPSDK YQAAAIIDLL RYYKWSEVSI LSSNDDYGIN AIVDLQTRFL ADGNFEVKNI
LIFDTYNDTP DVGDQLDTLW NSLDRVIIYF GSSKYISSIL KQAKSVGLLE QEFVWVVSDS
VAANVGTLAF NGSYMGYYEG LIGIRPQISR STMYDDFKEE YVKSVPHSED HLTDYNLLTY
DGLMFIDKAL SGLTLADQEL VCDAHKSQWG SGDDVLNALT STEYDGITGS IGFTGEGEVE
DVSYDIVNFV GGTFVPVGSW HLKTGLEMTS SVQFLGNKTT QPEGIANELN GMHLRLGIIP
EMPFISEPSL GCTDIKDPSC YTGVNVEIVS MMSQDLNFTY NFITPDDMKF GGKNTTTGEW
NGLIRDLLDN RTDMIVVALS NNAVRKADID FSLSMMDGGL GALVKSDSEG RDMFFFLRPF
HSTVWIAVIL GCALVTFMTY ILSKLSPYGV NGALLYAQNT CKCEECCQGG KESDCRIERL
EDKNNGLDIR ESLWLISAGL VGQTGETLPK SPAGRIMIST WWFFILLIIT MYTANMTAFL
TLSYSISDLN HPLELLNQDK YQWGVVDSRN PELLLASNQN ADYNRIADEA VKVGSYGEGL
ERMRAGGFVF IDEIPGINYA TKGECDIVQI GETFQPFELA FGLRKNSPFK NLVDTFMLGI
REQGVISELY EKYENQKASK TCNAGNSLTM YFSSLAGVFW IIPMGMAAAL ICLFAEYVFV
AIKDARTNKV GLDVALGERL TKHCRNSRGL TRQKRVTFVE NHITKDITPS PDQTSSSESQ
DDKDSNLRLS IRESLASFKE E
//
