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Database: UniProt
Entry: U3JEX6_FICAL
LinkDB: U3JEX6_FICAL
Original site: U3JEX6_FICAL 
ID   U3JEX6_FICAL            Unreviewed;      1333 AA.
AC   U3JEX6;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   29-SEP-2021, sequence version 2.
DT   24-JAN-2024, entry version 63.
DE   RecName: Full=Glutamate receptor {ECO:0000256|RuleBase:RU367118};
GN   Name=GRIN2C {ECO:0000313|Ensembl:ENSFALP00000001330.2};
OS   Ficedula albicollis (Collared flycatcher) (Muscicapa albicollis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Passeriformes; Muscicapidae; Ficedula.
OX   NCBI_TaxID=59894 {ECO:0000313|Ensembl:ENSFALP00000001330.2, ECO:0000313|Proteomes:UP000016665};
RN   [1] {ECO:0000313|Ensembl:ENSFALP00000001330.2, ECO:0000313|Proteomes:UP000016665}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23103876; DOI=10.1038/nature11584;
RA   Ellegren H., Smeds L., Burri R., Olason P.I., Backstrom N., Kawakami T.,
RA   Kunstner A., Makinen H., Nadachowska-Brzyska K., Qvarnstrom A., Uebbing S.,
RA   Wolf J.B.;
RT   "The genomic landscape of species divergence in Ficedula flycatchers.";
RL   Nature 491:756-760(2012).
RN   [2] {ECO:0000313|Ensembl:ENSFALP00000001330.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-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   STRING; 59894.ENSFALP00000001330; -.
DR   Ensembl; ENSFALT00000001337.2; ENSFALP00000001330.2; ENSFALG00000001279.2.
DR   eggNOG; KOG1053; Eukaryota.
DR   GeneTree; ENSGT00940000156964; -.
DR   HOGENOM; CLU_002039_3_1_1; -.
DR   Proteomes; UP000016665; Chromosome 18.
DR   GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR   GO; GO:0017146; C:NMDA selective glutamate receptor complex; IEA:Ensembl.
DR   GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0022849; F:glutamate-gated calcium ion channel activity; IEA:Ensembl.
DR   GO; GO:0004972; F:NMDA glutamate receptor activity; IEA:Ensembl.
DR   GO; GO:1904315; F:transmitter-gated monoatomic ion channel activity involved in regulation of postsynaptic membrane potential; IEA:Ensembl.
DR   GO; GO:0097553; P:calcium ion transmembrane import into cytosol; IEA:Ensembl.
DR   GO; GO:0033058; P:directional locomotion; IEA:Ensembl.
DR   GO; GO:0060079; P:excitatory postsynaptic potential; IEA:Ensembl.
DR   GO; GO:0042177; P:negative regulation of protein catabolic process; IEA:Ensembl.
DR   GO; GO:0050885; P:neuromuscular process controlling balance; IEA:Ensembl.
DR   GO; GO:1903539; P:protein localization to postsynaptic membrane; IEA:Ensembl.
DR   GO; GO:0009611; P:response to wounding; IEA:Ensembl.
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:SF361; GLUTAMATE RECEPTOR IONOTROPIC, NMDA 2C; 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.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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   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:UP000016665};
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..34
FT                   /evidence="ECO:0000256|RuleBase:RU367118"
FT   CHAIN           35..1333
FT                   /note="Glutamate receptor"
FT                   /evidence="ECO:0000256|RuleBase:RU367118"
FT                   /id="PRO_5033109545"
FT   TRANSMEM        572..595
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367118"
FT   TRANSMEM        616..633
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367118"
FT   TRANSMEM        645..670
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367118"
FT   TRANSMEM        836..859
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367118"
FT   DOMAIN          456..814
FT                   /note="Ionotropic glutamate receptor C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00079"
FT   DOMAIN          466..518
FT                   /note="Ionotropic glutamate receptor L-glutamate and
FT                   glycine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00918"
FT   REGION          1084..1114
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1148..1217
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1262..1333
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1148..1185
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1267..1306
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1333 AA;  146075 MW;  60BD9259A89AC40E CRC64;
     MRGAVCCAGR DTLVDMGRAP AHTLLLWMVL GCSAAFTDIL LPGPEEPVVN VAVVFGGTSY
     PLHIRSRLSP QSFLDMPLEI HPITVVVNNT NPSTLLTQIC DILASHKIHG IVFEDNVGTE
     AVAQILDFIS SQTQVPIISI SGGSAVVLTP KEPGSAFLQL GVSIEQQIQV IFKVLEEYDW
     GSFAVITSLY PGYNIFLDVI RSFTDASYFG WELQEVLTFE MSQEQGSSRT QRLLRQIDAQ
     VLIVYCSREE AEYLFSMAEQ AGLVGPGYIW IVPSMTVGNM EVPPSSFPVG LISVVTESWK
     LSLRQKVRDG VAIIAMGAAS FFRAHGYLPE VGRDCWAPAR ATTTNTSFYR HLLNVTWEHK
     DFSFNEGGYL IRPTMVVITL NQHRLWEMVG KWEKGIIHMK YPVWPRYGAF MQPVVDNRHL
     TVATLEERPF VIVENTDPST GVCVRNTVPC RKQTNSSHSG DGLVDPYTKL CCKGFCIDIL
     KKLAKTVKFS YDLYLVTNGK HGKIVRGVWN GMIGEVYYKR ADMAIGSLTI NEERSEIVDF
     SVPFVETGIS VMVARSNGTV SPSAFLEPYS PAVWVMMFVM CLTVVAITVF VFEYFSPVGY
     NQNLTSGKRP GGPSFTIGKS IWLLWALVFN NSVPIENPKG TTSKIMVLIW AFFAVIFLAS
     YTANLAAFMI QEQYIDTVSG LSDRKFQRPQ EQYPPFRFGT VPNGSTERNI RSNYPDMHTH
     MVKYNQRTVE DALTSLKMGK LDAFIYDAAV LNYMAGKDEG CKLVTIGSGK VFATTGYGIA
     LQKDSRWKRA IDLALLQFLG DGDTQKLETV WLSGICQNEK NEVMSSKLDI DNMAGVFYML
     LVAMGLSLLV FAWEHLIYWK LRHSVRKSHK LDFLLAISRG IYSCFNGVQT LSSPGRAPRP
     DVTASSAQAN VLKMLQAAKE MVQTASVGGS LEQATRTIED WSNHSERLQT TFSLRTPQLV
     VQNSTGAHRG PPSSPHPAER LGRAYAAKGA PLGLPLPQPI PVDPRLHGEE NWRGENEYPR
     LIHPLKFRGG CVGDEALTNF PHLLVKTSPG GDYGEQMLVG NHIGAPLPPP TSPRDLPPPD
     IYREHKRPSG RGERLQNTPL LQRDGTHGGS GTLPRLLSAA EKKRELGSAF LPPSCSRGAF
     PRVTRTCRAR AEPARPEAAA MEREKLSRWA SSARLPGERG DKRRAAGLGG GGGGGGGGGG
     GGGGGGGAGR LPPHSPVIRL PSYREACRQN PRATATVPAC APRACMNSYA NLPLYARPLW
     RGSPPPRERP GPHRCERGSG RWDSACRDCG RRGEPAVLRA DRRDPPLARG GGGGGGGGAG
     GSWRRVSSLE SEV
//
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