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Database: UniProt
Entry: M3ZVJ8_XIPMA
LinkDB: M3ZVJ8_XIPMA
Original site: M3ZVJ8_XIPMA 
ID   M3ZVJ8_XIPMA            Unreviewed;      1709 AA.
AC   M3ZVJ8;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 71.
DE   RecName: Full=Glutamate receptor {ECO:0000256|RuleBase:RU367118};
GN   Name=GRIN2B {ECO:0000313|Ensembl:ENSXMAP00000006242.1};
OS   Xiphophorus maculatus (Southern platyfish) (Platypoecilus maculatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC   Xiphophorus.
OX   NCBI_TaxID=8083 {ECO:0000313|Ensembl:ENSXMAP00000006242.1, ECO:0000313|Proteomes:UP000002852};
RN   [1] {ECO:0000313|Proteomes:UP000002852}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RA   Walter R., Schartl M., Warren W.;
RL   Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000002852}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RX   PubMed=23542700; DOI=10.1038/ng.2604;
RA   Schartl M., Walter R.B., Shen Y., Garcia T., Catchen J., Amores A.,
RA   Braasch I., Chalopin D., Volff J.N., Lesch K.P., Bisazza A., Minx P.,
RA   Hillier L., Wilson R.K., Fuerstenberg S., Boore J., Searle S.,
RA   Postlethwait J.H., Warren W.C.;
RT   "The genome of the platyfish, Xiphophorus maculatus, provides insights into
RT   evolutionary adaptation and several complex traits.";
RL   Nat. Genet. 45:567-572(2013).
RN   [3] {ECO:0000313|Ensembl:ENSXMAP00000006242.1}
RP   IDENTIFICATION.
RC   STRAIN=JP 163 A {ECO:0000313|Ensembl:ENSXMAP00000006242.1};
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   RefSeq; XP_005810957.1; XM_005810900.1.
DR   RefSeq; XP_005810958.1; XM_005810901.2.
DR   STRING; 8083.ENSXMAP00000006242; -.
DR   Ensembl; ENSXMAT00000006249.2; ENSXMAP00000006242.1; ENSXMAG00000006209.2.
DR   GeneID; 102219598; -.
DR   KEGG; xma:102219598; -.
DR   CTD; 110438919; -.
DR   eggNOG; KOG1053; Eukaryota.
DR   GeneTree; ENSGT00940000155964; -.
DR   HOGENOM; CLU_002598_0_0_1; -.
DR   InParanoid; M3ZVJ8; -.
DR   OMA; KNDRYSG; -.
DR   OrthoDB; 1034721at2759; -.
DR   Proteomes; UP000002852; Unassembled WGS sequence.
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: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:UP000002852};
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}.
FT   TRANSMEM        647..669
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367118"
FT   TRANSMEM        719..744
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367118"
FT   TRANSMEM        837..854
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367118"
FT   TRANSMEM        910..933
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367118"
FT   DOMAIN          520..888
FT                   /note="Ionotropic glutamate receptor C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00079"
FT   DOMAIN          531..592
FT                   /note="Ionotropic glutamate receptor L-glutamate and
FT                   glycine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00918"
FT   REGION          1075..1099
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1203..1230
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1248..1280
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1438..1461
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1526..1580
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1209..1230
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1526..1543
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1564..1579
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1709 AA;  187788 MW;  366135D143A1A7C3 CRC64;
     MRLWLAKHEV FLSHSYIMPL RGRCSSSLPH QHAGAHFSPR MVAQVQHGAR TLHPPPPPSV
     HRTTGTSLCL PLLFLLLCLL HLPPACHSRR EKGGGGGGGH YMPIPQPPPH HMALPNILRG
     LSIAVVLVGN SSEVALAGAR EKEDFLHIAP NVEVLTMNET DPKSIIKSIC DLMTEHWLQG
     VVFGDDTDQE AIAQILDFIS AQTHIPILGV RGGSSMIMAA KDDNSMFFQF GPSIEQQASV
     ILNIMEEYDW YIFSIVTTYY PGYQDFVTKI RNTIENSFVG WELEEVLLLD MSVDDGDSKI
     QNQLKKLQSP VILLYCTKEE ANTIFEVAHS VGITGYGYTW IVPSLVAGDT VVVPAEFPTG
     LLSVSYDEWD YGLEARVRDG VAIITMATST MMMDRGPHTL LKSECHGAPE KKTPISGNPN
     EVLRYLMNVT FEGRNLSFSE DGYQMHPKLV IILLNKERQW DRVGKWENGS LSMKYHVWPR
     YELYGGAATR EDDHLSIVTL EEAPFVIVED VDPLSGTCMR NTVPCRKQIK TLNQTKESGI
     YIKRCCKGFC IDILKKIAKS VKFTYDLYLV TNGKHGKKIN GTWNGMVGEV VLKNAHMAVG
     SLTINEERSE VIDFSVPFIE TGISVMVSRS NGTVSPSAFL EPFSADVWVM MFVMLLLVSA
     VAVFVFEYIS PVGYNRCLAD GREPHGPSFT IGKAIWLLWG LVFNNSVPVQ NPKGTTSKIM
     VSVWAFFAVI FLASYTANLA AFMIQEEYVD QVTGLSDKKF QSPNKFSPPF RFGTVPNGST
     ERNIRNNYPE MHTYMTAFHQ RNVNEALQSL KAGKLDAFIY DAAVLNYMAG RDEGCKLVTI
     GSGYIFATTG YGIAIQKESG WKRHVDLAIL QLFGDGEMEE LESLWLTGIC HHEKNEVMSS
     QLDVDNMAGV FYMLGAAMAL SLITFICEHW FYWQLRFCFM GVCSGQPGFV FSVSRGIYSC
     IHGVQIEEKS SSALNSPSAT MNNTHSNIMR LLRTAKNMAS LSGVNGSPHS ALDFIRRDSS
     VYDISEHRRS LAGHSDCKPP YMPEDNMFSD YISEVERTFG NLHLKDSNLY QDHYLHHHGS
     TPGLTGPPPN RPHSLGSASS LEGGMFDCDS LGGGVAPIFT TQPCSALTHR NMSKFDLLSG
     QTPPSGQSFK GGLPDVYGKF SFKGGASSST YIPGPSYCGG RGDDDGNIRS DVSDISTHTV
     TYGNLEGNAK KRKQYRDSLK KRPASAKSRR ELDEIELGYR RKPYHISHHH YHSQRSVSPP
     LLPSERKRGG GGGNNNGNSY LFREKESVRD FYLDQFRPKE GVPQWEHVDL TEGPGNRDGG
     VPTCTSLVPV EDFLKSKPKK SDSKGGPGSG LAGGEWECRN CRASGGKQIS IHGGGGGYSS
     GMGCGSSAGG SRPSSATCMR CEGCKKTGNL YDISEDNNHP LEQMGGGKGG GGVGCMAAGP
     QAQSQAQQRR KSGGFGKQLR RQHSYDTFVD LQKEESGGMG SLMGGLGGGM GGPGMGGMLP
     PPRSVSLKEK ERYMEENSPF AHIFERHGGS ERERERDRDP LFYGGESQKG SGSPFGLFRG
     GEGLHRRSIG ERDMRDRSLM EGGGGAAFSL SKSLYPDRVN QNPFIPTFGD DQCLMHGAKQ
     YYLTKQQQQQ QQVAQNSRGD FRSQLSATSY LPASATAGVM PNVPPRFPKE LSLGGMNHHG
     SMLAVGPPRP FNGSNGHVYE KLSSIESDV
//
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