GLR23_ARATH
ID GLR23_ARATH Reviewed; 895 AA.
AC Q9SHV2;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Glutamate receptor 2.3;
DE AltName: Full=Ligand-gated ion channel 2.3;
DE Flags: Precursor;
GN Name=GLR2.3; OrderedLocusNames=At2g24710; ORFNames=F27A10.2;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=11379626; DOI=10.1126/science.292.5521.1486b;
RA Lacombe B., Becker D., Hedrich R., DeSalle R., Hollmann M., Kwak J.M.,
RA Schroeder J.I., Le Novere N., Nam H.G., Spalding E.P., Tester M.,
RA Turano F.J., Chiu J., Coruzzi G.;
RT "The identity of plant glutamate receptors.";
RL Science 292:1486-1487(2001).
RN [4]
RP TISSUE SPECIFICITY.
RX PubMed=12082126; DOI=10.1093/oxfordjournals.molbev.a004165;
RA Chiu J.C., Brenner E.D., DeSalle R., Nitabach M.N., Holmes T.C.,
RA Coruzzi G.M.;
RT "Phylogenetic and expression analysis of the glutamate-receptor-like gene
RT family in Arabidopsis thaliana.";
RL Mol. Biol. Evol. 19:1066-1082(2002).
CC -!- FUNCTION: Glutamate-gated receptor that probably acts as non-selective
CC cation channel. May be involved in light-signal transduction and
CC calcium homeostasis via the regulation of calcium influx into cells.
CC -!- SUBUNIT: May form heteromers. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Expressed predominantly in roots.
CC {ECO:0000269|PubMed:12082126}.
CC -!- SIMILARITY: Belongs to the glutamate-gated ion channel (TC 1.A.10.1)
CC family. {ECO:0000305}.
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DR EMBL; AC007266; AAD26894.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC07621.1; -; Genomic_DNA.
DR PIR; A84640; A84640.
DR RefSeq; NP_180047.1; NM_128032.1.
DR AlphaFoldDB; Q9SHV2; -.
DR SMR; Q9SHV2; -.
DR STRING; 3702.AT2G24710.1; -.
DR PaxDb; Q9SHV2; -.
DR PRIDE; Q9SHV2; -.
DR ProteomicsDB; 247400; -.
DR EnsemblPlants; AT2G24710.1; AT2G24710.1; AT2G24710.
DR GeneID; 817007; -.
DR Gramene; AT2G24710.1; AT2G24710.1; AT2G24710.
DR KEGG; ath:AT2G24710; -.
DR Araport; AT2G24710; -.
DR TAIR; locus:2047251; AT2G24710.
DR eggNOG; KOG1052; Eukaryota.
DR HOGENOM; CLU_007358_0_2_1; -.
DR InParanoid; Q9SHV2; -.
DR PhylomeDB; Q9SHV2; -.
DR PRO; PR:Q9SHV2; -.
DR Proteomes; UP000006548; Chromosome 2.
DR Genevisible; Q9SHV2; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0005262; F:calcium channel activity; ISS:UniProtKB.
DR GO; GO:0008066; F:glutamate receptor activity; ISS:UniProtKB.
DR GO; GO:0015276; F:ligand-gated ion channel activity; IBA:GO_Central.
DR GO; GO:0038023; F:signaling receptor activity; IBA:GO_Central.
DR GO; GO:0006816; P:calcium ion transport; ISS:UniProtKB.
DR GO; GO:0019722; P:calcium-mediated signaling; ISS:UniProtKB.
DR GO; GO:0071230; P:cellular response to amino acid stimulus; ISS:UniProtKB.
DR CDD; cd19990; PBP1_GABAb_receptor_plant; 1.
DR InterPro; IPR001828; ANF_lig-bd_rcpt.
DR InterPro; IPR044440; GABAb_receptor_plant_PBP1.
DR InterPro; IPR001320; Iontro_rcpt.
DR InterPro; IPR017103; Iontropic_Glu_rcpt_pln.
DR InterPro; IPR028082; Peripla_BP_I.
DR InterPro; IPR001638; Solute-binding_3/MltF_N.
DR Pfam; PF01094; ANF_receptor; 1.
DR Pfam; PF00060; Lig_chan; 1.
DR Pfam; PF00497; SBP_bac_3; 1.
DR PIRSF; PIRSF037090; Iontro_Glu-like_rcpt_pln; 1.
DR SMART; SM00079; PBPe; 1.
DR SUPFAM; SSF53822; SSF53822; 1.
PE 2: Evidence at transcript level;
KW Glycoprotein; Ion channel; Ion transport; Ligand-gated ion channel;
KW Membrane; Receptor; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix; Transport.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..895
FT /note="Glutamate receptor 2.3"
FT /id="PRO_0000011598"
FT TOPO_DOM 24..582
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 583..603
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 604..610
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 611..631
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 632..635
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 636..656
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 657..830
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 831..851
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 852..895
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 873..895
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 52
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 203
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 266
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 330
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 342
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 477
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 542
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 895 AA; 100809 MW; E86D1BADCD73AB94 CRC64;
MRTEKLFFCI LLVFFFCLEF NRGQNNGKTL VDVGVVTDVD TSHSKVVMLC INMSISDFYS
SNPQFETRLV VNVGDSKSDV VGAAIAALDL IKNKQVKAIL GPWTSMQAHF LIEIGQKSRV
PIVSYSATSP ILTSLRSPYF LRATYEDSFQ VQPIKAIIKL FGWREVVPVY IDNTFGEGIM
PRLTDALQDI NVRIPYRSVI AINATDHEIS VELLKMMNMP TRVFLVHMYY DLASRFFIKA
KELGLMEPGY VWILTNGVID DLSLINETAV EAMEGVLGIK TYIPKSPDLE KFRSRWRSLF
PRVELSVYGL WAYDATTALA VAIEEAGTNN MTFSKVVDTG RNVSELEALG LSQFGPKLLQ
TLLTVQFRGL AGEFRFFRGQ LQPSVFEIVN IINTGEKSIG FWKEGNGLVK KLDQQASSIS
ALSTWKDHLK HIVWPGEADS VPKGWQIPTK GKKLRIGVPK RTGYTDLVKV TRDPITNSTV
VTGFCIDFFE AVIRELPYDV SYEFIPFEKP DGKTAGNYND LVYQVYLGRY DAVVGDTTIL
VNRSSYVDFT FPFIKSGVGL IVEMTDPVKR DYILFMKPLS WKLWLTSFIS FFLVGCTVWV
LEYKRNPDFS GPPRFQASTI CWFAFSTMVF APRERVFSFW ARALVIAWYF LVLVLTQSYT
ASLASLLTSQ KLNPTITSMS SLLEKGETVG YQRTSFILGK LKERGFPQSS LVPFDTAEEC
DELLSKGPKK GGVSGAFLEI PYLRLFLGQF CNTYKMVEEP FNVDGFGFVF PIGSPLVADV
SRAILKVAES PKAMELERAW FKKKEQSCPD PITNPDPNPS FTSRQLDIDS FLFLFVGVLL
VCVMALGNFT YCFLAKDQVS YLDKVEMSPC SSSQQMPVKR KTQLNMSQVH DQDSL
