ID A0A3Q3A4D7_KRYMA Unreviewed; 1547 AA.
AC A0A3Q3A4D7;
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};
GN Name=GRIN2A {ECO:0000313|Ensembl:ENSKMAP00000010700.1};
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:ENSKMAP00000010700.1, ECO:0000313|Proteomes:UP000264800};
RN [1] {ECO:0000313|Ensembl:ENSKMAP00000010700.1}
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. {ECO:0000256|RuleBase:RU367118}.
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DR RefSeq; XP_017283640.1; XM_017428151.1.
DR STRING; 37003.ENSKMAP00000010700; -.
DR Ensembl; ENSKMAT00000010863.1; ENSKMAP00000010700.1; ENSKMAG00000008004.1.
DR GeneID; 108242983; -.
DR KEGG; kmr:108242983; -.
DR CTD; 563297; -.
DR GeneTree; ENSGT00940000156222; -.
DR OrthoDB; 1034721at2759; -.
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; 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; IPR018884; NMDAR2_C.
DR InterPro; IPR028082; Peripla_BP_I.
DR InterPro; IPR001638; Solute-binding_3/MltF_N.
DR PANTHER; PTHR18966:SF407; GLUTAMATE RECEPTOR IONOTROPIC, NMDA 2A; 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 Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475,
KW ECO:0000256|RuleBase:RU367118};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
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}; Magnesium {ECO:0000256|ARBA:ARBA00022842};
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};
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};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT TRANSMEM 585..607
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367118"
FT TRANSMEM 657..679
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367118"
FT TRANSMEM 848..871
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367118"
FT DOMAIN 459..826
FT /note="Ionotropic glutamate receptor C-terminal"
FT /evidence="ECO:0000259|SMART:SM00079"
FT DOMAIN 467..530
FT /note="Ionotropic glutamate receptor L-glutamate and
FT glycine-binding"
FT /evidence="ECO:0000259|SMART:SM00918"
FT REGION 1026..1061
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1079..1118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1096..1118
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1547 AA; 172660 MW; 7A596688069BF34A CRC64;
MKWISTMSLS SKRSKRRIRR RSICSSGGDG VLLSLVLLAA VTMMASPAAT QKQRTGSGSE
KVPVLNIAVI LGRTRYISER DIRALWSKED PIDINVVTLL VNETDPKSII THMCNLMSGT
KIHGVVFGDG TDQEAIAQIL DFISSQTLIP ILGIHGGSSM IMADKDVKST FFQFGASIQQ
EALLMLNIME EYDWHVFSIV TSKFPGYQEF INILKTTVDN SFVGWDLQNI ITLDAVEEDS
RSQIMLKKVQ SPVVLLYCSK DEAVYVLEEA RSLGLTGFGY IWIVPSLTTG NTEITPEAFP
SGMISVSYDD WDYPLEARVR DGLGIITSAA AAMLDEYGDI PEAKTSCYGQ MEKTTKLPPS
ALHKYMMNVT WDGRDLSFTE DGYQENPKLV VIVLNKEREW EKMGKLDNGS LTVKYPVWPR
FNSFGDAELD DNHLSIVTLE EKPFVIVEDV ERLTGTCMRN SVPCRKHIKD NTTEAGGTYI
KKCCKGFCID ILKKIAKYVK FTYDLYLVTN GKHGKKINNV WNGMVGEVVY KKAVMAVGSL
TINEERSEVI DFSVPFVETG ISVMVSRSNG TVSPSAFLEP FSASVWVMMF VMLLLVTAMA
VFMFEYISPL GFNRNLAQGK DPHGPSFTMG KAVWLLWGLV FNNSVPVQNP KGTTSKFIVS
VWAFFAVIFL ASYTANLAAF MIQEEFVDQV TGLSDNKFQN PYAYSPPFRF GTVPNGSTER
NIKKNYPAMH QYMVKYHQTG VVDALVSLKS GKLDAFIYDA AVLNYMAGRD EGCKLVTIGS
GYIFATTGYG IALQKGSYWK RQVDLAILAI IGDGEMEELE AQWLTGICHN EKNEVMSSQL
DVDNMAGVFY MLATAMGLSL ITFVSEHLFY WRLRYCFTGV CSGRPGLLFS ISRGIWSCIH
GVHIDMKKKT DLDFSPQDKM LKLIKSAKQM TNMSNLGGSH MNSPKREFMH SAGPMIMDMM
AEKGNFIYTD NRSYAPKDMI YGDTGDLQSY LANRHKDHLN NYIFQGGQHP LTLNDANPNT
VEVSVSPDTV QTNAKPPRTL WKKSGDTLRS VPPGPAPMPD MLMPDPRISM KTQRYLPEDT
AHSDISDCSS RAASYKDPEN NKHLKPKDNL KKRSVTSKYP RDCSEVELSY LKTKQVSSGT
NQSGRGGGVG EKIYTIDSDR ELSLHSDPIH FRESHGLATD DVDYPEIYSD HSDNYRKCEQ
PIIHLNSSPL HHPDSDLLSD SAYSKHYNLK EKNLSLSPHE TIDRYKQTHC RSCLSKVTAS
YPPAGPYGSA GSASASGTRS PYNRCEACLH TANLYDISED QLLADPLVSP TMHHQEQQPD
EMFGLYWPQT DGPHVQKRNR LRLSRQHSFD NIMLEKPKDL DLGRPARSVS LKEKDRFLDS
ASDSHYANLF GMRPYSGKLF GTGSKSMLFN HNLEESKRSK SLYPAHGSEN PFLSHSLRDD
TSSRLVHGRS SSDIYKQLAV GSPAVALGAA PIKTRNDANN LRSSVKSTSS YCSRDGRIAN
DMYNKEHVMP YSANKTSAYP ASRGVLNSAQ FSNRRVYKKI PSLESDV
//
