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Database: UniProt
Entry: A0A3Q7U8S9_VULVU
LinkDB: A0A3Q7U8S9_VULVU
Original site: A0A3Q7U8S9_VULVU 
ID   A0A3Q7U8S9_VULVU        Unreviewed;       922 AA.
AC   A0A3Q7U8S9;
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=GRIA2 {ECO:0000313|RefSeq:XP_025863845.1};
OS   Vulpes vulpes (Red fox).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Vulpes.
OX   NCBI_TaxID=9627 {ECO:0000313|Proteomes:UP000286640, ECO:0000313|RefSeq:XP_025863845.1};
RN   [1]
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (JAN-2019) to UniProtKB.
RN   [2] {ECO:0000313|RefSeq:XP_025863845.1}
RP   IDENTIFICATION.
RC   STRAIN=TameXAggressive cross {ECO:0000313|RefSeq:XP_025863845.1};
RC   TISSUE=Blood {ECO:0000313|RefSeq:XP_025863845.1};
RG   RefSeq;
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|RuleBase:RU367118}. Endoplasmic
CC       reticulum membrane {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane
CC       protein {ECO:0000256|ARBA:ARBA00004477}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}. Postsynaptic density membrane
CC       {ECO:0000256|ARBA:ARBA00037872}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00037872}.
CC   -!- SIMILARITY: Belongs to the glutamate-gated ion channel (TC 1.A.10.1)
CC       family. GRIA2 subfamily. {ECO:0000256|ARBA:ARBA00037989}.
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DR   RefSeq; XP_025863845.1; XM_026008060.1.
DR   AlphaFoldDB; A0A3Q7U8S9; -.
DR   OrthoDB; 511851at2759; -.
DR   Proteomes; UP000286640; Unplaced.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0098839; C:postsynaptic density membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0022824; F:transmitter-gated monoatomic ion channel activity; IEA:UniProt.
DR   GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:UniProt.
DR   CDD; cd06389; PBP1_iGluR_AMPA_GluR2; 1.
DR   CDD; cd13715; PBP2_iGluR_AMPA; 1.
DR   Gene3D; 1.10.287.70; -; 2.
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; IPR028082; Peripla_BP_I.
DR   InterPro; IPR001638; Solute-binding_3/MltF_N.
DR   PANTHER; PTHR18966:SF99; GLUTAMATE RECEPTOR 2; 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; 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.
DR   SUPFAM; SSF81324; Voltage-gated potassium channels; 1.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475,
KW   ECO:0000256|RuleBase:RU367118};
KW   Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
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   Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU367118};
KW   Palmitate {ECO:0000256|ARBA:ARBA00023139};
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:UP000286640};
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};
KW   Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|RuleBase:RU367118"
FT   CHAIN           25..922
FT                   /note="Glutamate receptor"
FT                   /evidence="ECO:0000256|RuleBase:RU367118"
FT                   /id="PRO_5027137827"
FT   TRANSMEM        542..564
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367118"
FT   TRANSMEM        625..647
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367118"
FT   TRANSMEM        854..876
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367118"
FT   DOMAIN          415..790
FT                   /note="Ionotropic glutamate receptor C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00079"
FT   DOMAIN          425..490
FT                   /note="Ionotropic glutamate receptor L-glutamate and
FT                   glycine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00918"
SQ   SEQUENCE   922 AA;  103079 MW;  5BEBBCD1491BFD4D CRC64;
     MQKIMHISVL LSPVLWGLIF GVSSNSIQIG GLFPRGADQE YSAFRVGMVQ FSTSEFRLTP
     HIDNLEVANS FAVTNAFCSQ FSRGVYAIFG FYDKKSVNTI TSFCGTLHVS FITPSFPTDG
     THPFVIQMRP DLKGALLSLI EYYQWDKFAY LYDSDRGLST LQAVLDSAAE KKWQVTAINV
     GNINNDKKDE TYRSLFQDLE LKKERRVILD CERDKVNDIV DQVITIGKHV KGYHYIIANL
     GFTDGDLLKI QFGGANVSGF QIVDYDDSLV SKFIERWSTL EEKEYPGAHT TTIKYTSALT
     YDAVQVMTEA FRNLRKQRIE ISRRGNAGDC LANPAVPWGQ GVEIERALKQ VQVEGLSGNI
     KFDQNGKRIN YTINIMELKT NGPRKIGYWS EVDKMVVTLT ELPSGNDTSG LENKTVVVTT
     ILESPYVMMK KNHEMLEGNE RYEGYCVDLA AEIAKHCGFK YKLTIVGDGK YGARDADTKI
     WNGMVGELVY GKADIAIAPL TITLVREEVI DFSKPFMSLG ISIMIKKPQK SKPGVFSFLD
     PLAYEIWMCI VFAYIGVSVV LFLVSRFSPY EWHTEEFEDG RETQSSESTN EFGIFNSLWF
     SLGAFMQQGC DISPRSLSGR IVGGVWWFFT LIIISSYTAN LAAFLTVERM VSPIESAEDL
     SKQTEIAYGT LDSGSTKEFF RRSKIAVFDK MWTYMRSAEP SVFVRTTAEG VARVRKSKGK
     YAYLLESTMN EYIEQRKPCD TMKVGGNLDS KGYGIATPKG SSLRNAVNLA VLKLNEQGLL
     DKLKNKWWYD KGECGSGGGD SKVSPINLAV LKLSEQGVLD KLKNKWWYDK GECGAKDSGS
     KEKTSALSLS NVAGVFYILV GGLGLAMLVA LIEFCYKSRA EAKRMKVAKN AQNINPSSSQ
     NSQNFATYKE GYNVYGIESV KI
//
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