GLRK_LYMST
ID GLRK_LYMST Reviewed; 917 AA.
AC P26591;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Glutamate receptor;
DE Flags: Precursor;
OS Lymnaea stagnalis (Great pond snail) (Helix stagnalis).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Heterobranchia; Euthyneura; Panpulmonata; Hygrophila; Lymnaeoidea;
OC Lymnaeidae; Lymnaea.
OX NCBI_TaxID=6523;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1659993; DOI=10.1016/0014-5793(91)80846-u;
RA Hutton M.L., Harvey R.J., Barnard E.A., Darlison M.G.;
RT "Cloning of a cDNA that encodes an invertebrate glutamate receptor
RT subunit.";
RL FEBS Lett. 292:111-114(1991).
CC -!- FUNCTION: Receptor for glutamate. L-glutamate acts as an excitatory
CC neurotransmitter at many synapses in the central nervous system. The
CC postsynaptic actions of Glu are mediated by a variety of receptors.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC Postsynaptic cell membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the glutamate-gated ion channel (TC 1.A.10.1)
CC family. {ECO:0000305}.
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DR EMBL; X60086; CAA42683.1; -; mRNA.
DR PIR; S18443; ACGAE.
DR AlphaFoldDB; P26591; -.
DR SMR; P26591; -.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004970; F:ionotropic glutamate receptor activity; IEA:InterPro.
DR InterPro; IPR001828; ANF_lig-bd_rcpt.
DR InterPro; IPR019594; Glu/Gly-bd.
DR InterPro; IPR001508; Iono_rcpt_met.
DR InterPro; IPR001320; Iontro_rcpt.
DR InterPro; IPR028082; Peripla_BP_I.
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; SSF53822; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Glycoprotein; Ion channel; Ion transport;
KW Ligand-gated ion channel; Membrane; Postsynaptic cell membrane; Receptor;
KW Signal; Synapse; Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..917
FT /note="Glutamate receptor"
FT /id="PRO_0000011560"
FT TOPO_DOM 20..556
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 557..577
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 578..631
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 632..652
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 653..818
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 819..839
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 840..917
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 871..896
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 62
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 95
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 121
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 125
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 229
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 251
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 261
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 272
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 418
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 419
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 424
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 491
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 775
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 917 AA; 103139 MW; 4928113CE2CA0527 CRC64;
MDTCVFPLVV LWISMRITST LDEVPIGGIF DSRSVQALTA FRHEIHMFNR AYSHVYRYKL
KNDTTILDVT DSFAVSNALC HHLSRGDLAI FGVSNASSLA TIQSYTDTFN VPFVTISMAQ
NNSHNGSYQI YMRPMYINAL VDVIVHYRWE KVAFYYDSDE GLVRLQQLFQ ATNKYDKMII
SIDTKRITSV ENGYHMLKEL HLMDPEMEHR VLLDVRTDKA EQIILKVMND SKINNAKFHF
LLGDLGMLEI NTTHFKIGGV NITGFQLVDP FNSTSELFIS TWSSLDPVYW PGAGTNHVNY
EAALAADSVR LFKSAFGSIL QKDPNFLRRS RSGTAGKSMK CTDDSEIKTG HGQMILEEMK
KVKFEGVTGH VAFNEQGHRK DFTLGVYNVA MTRGTAKIGY WNEREGKLHA HNPRLFQNNS
SDMNRTRIVT TIIKEPYVMV NNVIRDGKPL VGNEPVEGFC IDLTKAVAEK VGFDFVIQFV
KDGSYGSVLS NGTWDGIVGE LIRHEADMAI APFTITADRS RVIDFTKPFM SLGISIMIKR
PQPAGKHFFS FMEPLSSEIW MCIVFAYIGV SVVLFLVSRF SPNEWHLSEA HHSYIANDFS
ISNSLWFSLG AFMQQGCDIS PRSMSGRIVG SVWWFFTLII ISSYTANLAA FLTVERMLTP
IDSAEDLARQ TEIQYGTIMS GSTKAFFKNS QFQTYQRMWA YMTSAQPSVF VKTHEEGIQR
VRQSNGKYAY LTESSTIDYV SNRKPCDTLK VGSNLNSDGF GIGTPVGSDL RDKLNFSVLE
LRENGDLAKW EKIWFDRGEC PQHSSNKEGA QSALTLANVA GIFYILIGGL VVAVLSAAFE
FLYKSRMDSR KSRMSFGSAL RTKARLSFKG HIDSEQKTTG NGTRRRSHNS VTYTYTGPTN
VMGGSHAFED SNTHTEV