ID A0A3Q3BJ19_KRYMA Unreviewed; 1564 AA.
AC A0A3Q3BJ19;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Glutamate receptor {ECO:0000256|RuleBase:RU367118};
OS Kryptolebias marmoratus (Mangrove killifish) (Rivulus marmoratus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Rivulidae; Kryptolebias.
OX NCBI_TaxID=37003 {ECO:0000313|Ensembl:ENSKMAP00000029431.1, ECO:0000313|Proteomes:UP000264800};
RN [1] {ECO:0000313|Ensembl:ENSKMAP00000029431.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Receptor for glutamate that functions as a ligand-gated ion
CC channel in the central nervous system and plays an important role in
CC excitatory synaptic transmission. L-glutamate acts as an excitatory
CC neurotransmitter at many synapses in the central nervous system.
CC {ECO:0000256|RuleBase:RU367118}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|RuleBase:RU367118};
CC Multi-pass membrane protein {ECO:0000256|RuleBase:RU367118}.
CC Postsynaptic cell membrane {ECO:0000256|ARBA:ARBA00034104,
CC ECO:0000256|RuleBase:RU367118}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00034104}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}. Synaptic cell membrane
CC {ECO:0000256|ARBA:ARBA00034099}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00034099}.
CC -!- SIMILARITY: Belongs to the glutamate-gated ion channel (TC 1.A.10.1)
CC family. NR2B/GRIN2B subfamily. {ECO:0000256|ARBA:ARBA00038189}.
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DR Ensembl; ENSKMAT00000029797.1; ENSKMAP00000029431.1; ENSKMAG00000021761.1.
DR GeneTree; ENSGT00940000155964; -.
DR Proteomes; UP000264800; Unplaced.
DR GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004970; F:glutamate-gated receptor activity; IEA:UniProt.
DR GO; GO:0022890; F:inorganic cation transmembrane transporter activity; IEA:UniProt.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd06378; PBP1_iGluR_NMDA_NR2; 1.
DR CDD; cd13718; PBP2_iGluR_NMDA_Nr2; 1.
DR Gene3D; 3.40.50.2300; -; 2.
DR Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 3.
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; IPR018884; NMDAR2_C.
DR InterPro; IPR028082; Peripla_BP_I.
DR InterPro; IPR001638; Solute-binding_3/MltF_N.
DR PANTHER; PTHR18966:SF382; GLUTAMATE RECEPTOR IONOTROPIC, NMDA 2B; 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 Pfam; PF10565; NMDAR2_C; 1.
DR Pfam; PF00497; SBP_bac_3; 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 ECO:0000256|RuleBase:RU367118};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Ion channel {ECO:0000256|ARBA:ARBA00023303, ECO:0000256|RuleBase:RU367118};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065,
KW ECO:0000256|RuleBase:RU367118};
KW Ligand-gated ion channel {ECO:0000256|ARBA:ARBA00023286,
KW ECO:0000256|RuleBase:RU367118};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU367118};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Postsynaptic cell membrane {ECO:0000256|ARBA:ARBA00023257,
KW ECO:0000256|RuleBase:RU367118};
KW Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|RuleBase:RU367118};
KW Reference proteome {ECO:0000313|Proteomes:UP000264800};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU367118};
KW Synapse {ECO:0000256|ARBA:ARBA00023018, ECO:0000256|RuleBase:RU367118};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU367118};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU367118};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU367118}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|RuleBase:RU367118"
FT CHAIN 26..1564
FT /note="Glutamate receptor"
FT /evidence="ECO:0000256|RuleBase:RU367118"
FT /id="PRO_5027148827"
FT TRANSMEM 523..545
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367118"
FT TRANSMEM 565..583
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367118"
FT TRANSMEM 595..620
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367118"
FT TRANSMEM 786..808
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367118"
FT DOMAIN 396..764
FT /note="Ionotropic glutamate receptor C-terminal"
FT /evidence="ECO:0000259|SMART:SM00079"
FT DOMAIN 414..468
FT /note="Ionotropic glutamate receptor L-glutamate and
FT glycine-binding"
FT /evidence="ECO:0000259|SMART:SM00918"
FT REGION 962..989
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1091..1119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1132..1170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1371..1390
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1523..1551
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1097..1119
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1564 AA; 171229 MW; 4D8BF364D5AA6A31 CRC64;
LFCGCHYLFF PLPALLFSPL PSSHSLPPSS IFFSVFLGFA VLAENPARLQ LALEVVTMNE
TDPRSIINQI CGQMMRNSLQ GVVFGDDTDQ EAIAQILDFI SAQTHIPILG IRGGSSMVMA
AKDDHSMFFQ FGPSIEQQAS VMLNIMEEYD WYIFSIVTSY YPGHEDFIRS TIENSFVGWE
LEEVLLLDMS MDDHNHGDSK IQNQMKKLQS PVILLYCTKE EATTIFEVAH SVGLTGYGYT
WIVPSLVAGD ADHPPTVFPI GLISVSYDEW DYNIEARVRD AVAVIATATS TMMLDRGPHT
LYVMNVTFEG RNLSFSEKGH QMFPKLVIIL LDKDRQWDRV GKWERGSLTM RYHVWPRFEL
YSDVEERDDH LSIVTLEEAP FVIVEDVDPL SGTCMRNTVP CRKQLKLSNH TGDSGIYIKR
CCKGFCIDIL KKIAKTVKFT YDLYLVTNGK HGKKVNGTWN GMVGEVVFKN AHMAVGSLTI
NEERSEVIDF SVPFIETGIS VMVSRSNGTV SPSAFLEPFS ADVWVMMFVM LLIVSAVAVF
VFEYFSPVGY NRCLADGREP GGPSFTIGKA IWLLWGLVFN NSVPVQNPKG TTSKIMVSVW
AFFAVIFLAS YTANLAAFMI QEEYVDQVSG LSDKKFQKPN EFSPPFRFGT VPNGSTERNI
RNNYRDMHAY MTSFHQKNVD EALYSLKTGK LDAFIYDAAV LNYMAGRDEG CKLVTIGSGK
VFASTGYGIA IQKDSGWKRA VDLAILMLFG DGEMEELEAL WLTGICHNEK NEVMSSQLDV
DNMAGVFYML GAAMVLSLIT FICEHLFYWQ LRFCFMGMCS GKPGVTFSIS RGIYSCIHGI
QIEENKSTAD SPSSTIKKNM NNTHSNILRL LRTAKDMTAV PGINGSPHPA LEYSHSGRES
GIYDIQEHRR SLVGHPVDCT PAPPYMAEDN MFSDYISEVE RTFGNLPLKD SNLYQDHYRH
HHPASALGMS GPPPNRPRSL GSASSLEGGM FDGDSLGGGV APIFTTQPRP SMTHRNTSKF
DLIAGHTPAD SSQGGFKGSN VYGRFSFKGG ASSTGLIGGH DRYCGGGGSG GDDGNIRSDV
SDISTHTVTY GNLEGNTKRR KQYRDSLKKR PASAKCRREQ DEIELNAFRK RPHHHTVHHH
FPHGPLAHRP VSPPLERKRG GGAGNSSPYL FRKDRDSLRD FYADQFRSME GKAKWEQEGG
SGGSGVGSGS GGGICKSLVP VEDFLKGKGK KQECKGGLGA ISAGQQAHTC WEKGGSGLGG
GGIAGGDWEC RNCHSVCHHS GSVGGGSACQ ASGVGGNSSR PSSATCKRCD SCKIQPSNLY
NISEDNNMMF SGSKSSIGPS QTQTQRRKLG PGGKVLRRQH SYDTFVDLQR EGAGRMGGPR
SVSLKDKDRY MEGPSPYAHM FERTMMGGGG CGGGGSRGAG TYSLSKSLYP DKVNQNPFIP
TFGDDQCLLH GAKPYYIKKP QTQQQQQQQL LNNSRGGGDF RGSMGATSYL PASATAGVMS
NVGTRYPKEL CLGGVGGPMG NHHGANKLLQ GGRDTLGLGQ GQRPFNGASN GHVYEKLSSI
ESDV
//
