GLR31_ARATH
ID GLR31_ARATH Reviewed; 925 AA.
AC Q7XJL2; F4IMH4; O49119; Q6RKN5; Q9ZT36;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 31-JAN-2018, sequence version 3.
DT 25-MAY-2022, entry version 135.
DE RecName: Full=Glutamate receptor 3.1;
DE Short=AtGLR2;
DE AltName: Full=Ligand-gated ion channel 3.1;
DE Flags: Precursor;
GN Name=GLR3.1; Synonyms=ACL1, GLR2; OrderedLocusNames=At2g17260;
GN ORFNames=F5J6.2;
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 [MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=9823891; DOI=10.1038/24066;
RA Lam H.-M., Chiu J.C., Hsieh M.-H., Meisel L., Oliveira I.C., Shin M.,
RA Coruzzi G.M.;
RT "Glutamate-receptor genes in plants.";
RL Nature 396:125-126(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=19143998; DOI=10.1111/j.1365-313x.2009.03789.x;
RA Cho D., Kim S.A., Murata Y., Lee S., Jae S.-K., Nam H.G., Kwak J.M.;
RT "De-regulated expression of the plant glutamate receptor homolog AtGLR3.1
RT impairs long-term Ca2+-programmed stomatal closure.";
RL Plant J. 58:437-449(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Liu L.-H., Tester M.;
RT "A full length cDNA of AtGLR3.1 identified and sequenced from an EST.";
RL Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 [5]
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 [6]
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 [7]
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 Required for the long-term calcium oscillation-regulated stomatal
CC movements. {ECO:0000269|PubMed:19143998}.
CC -!- SUBUNIT: May form heteromers. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Expressed predominantly in roots. Firt detected in
CC the vascular tissues of the cotyledons, and later in the vasculature of
CC all organs. In leaves, preferentially expressed in guard cells.
CC {ECO:0000269|PubMed:12082126, ECO:0000269|PubMed:19143998}.
CC -!- SIMILARITY: Belongs to the glutamate-gated ion channel (TC 1.A.10.1)
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB92421.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAD09174.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF079999; AAD09174.1; ALT_INIT; mRNA.
DR EMBL; AF038557; AAB92421.1; ALT_INIT; mRNA.
DR EMBL; AY495448; AAR88099.1; -; mRNA.
DR EMBL; CP002685; AEC06604.2; -; Genomic_DNA.
DR PIR; T51132; T51132.
DR PIR; T51133; T51133.
DR RefSeq; NP_001318239.1; NM_001335544.1.
DR AlphaFoldDB; Q7XJL2; -.
DR SMR; Q7XJL2; -.
DR BioGRID; 1588; 2.
DR STRING; 3702.AT2G17260.1; -.
DR PaxDb; Q7XJL2; -.
DR PRIDE; Q7XJL2; -.
DR EnsemblPlants; AT2G17260.1; AT2G17260.1; AT2G17260.
DR GeneID; 816231; -.
DR Gramene; AT2G17260.1; AT2G17260.1; AT2G17260.
DR KEGG; ath:AT2G17260; -.
DR Araport; AT2G17260; -.
DR eggNOG; KOG1052; Eukaryota.
DR HOGENOM; CLU_007358_0_1_1; -.
DR InParanoid; Q7XJL2; -.
DR OMA; NFFMTSA; -.
DR OrthoDB; 188544at2759; -.
DR PhylomeDB; Q7XJL2; -.
DR PRO; PR:Q7XJL2; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q7XJL2; baseline and differential.
DR Genevisible; Q7XJL2; 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..25
FT /evidence="ECO:0000255"
FT CHAIN 26..925
FT /note="Glutamate receptor 3.1"
FT /id="PRO_0000011605"
FT TOPO_DOM 26..591
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 592..612
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 613..621
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 622..642
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 643..653
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 654..674
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 675..831
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 832..852
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 853..925
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 897..925
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 909..925
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 309
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 341
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 359
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 419
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 437
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 488
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 738
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 812
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 5
FT /note="M -> V (in Ref. 2; AAB92421)"
FT /evidence="ECO:0000305"
FT CONFLICT 13
FT /note="I -> M (in Ref. 2; AAB92421)"
FT /evidence="ECO:0000305"
FT CONFLICT 830..831
FT /note="HS -> RT (in Ref. 2; AAB92421)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 925 AA; 103031 MW; 043B1AA1931EC682 CRC64;
MLSSMNWVLL SFIIVLGGGL LLSEGASSSR PPVIKVGAIF GLNTMYGETA NIAFKAAEED
VNSDPSFLGG SKLRILMNDA KRSGFLSIMG ALQFMETDVV AIIGPQTSIM AHVLSHLANE
LTVPMLSFTA LDPTLSPLQF PFFVQTAPSD LFLMRAIAEM ITYYGWSDVV ALYNDDDNSR
NGVTALGDEL EERRCKISYK AVLPLDVVIT SPVEIIEELI KIRGMESRVI VVNTFPNTGK
MIFKEAERLG MMEKGYVWIA TTWLSSVLDS NLPLDTKLVN GVLTLRLHTP DSRKKRDFAA
RWKNKLSNNK TIGLNVYGLY AYDTVWIIAR AVKTLLEAGG NLSFSNDAKL GSLKGEALNL
SALSRFDQGS QLLDYIVHTK MSGLTGPVQF HPDRSMLQPS YDIINLVDDR VHQIGYWSNY
SGLSIVPPES FYSKPPNRSS SNQHLNSVTW PGGTSVTPRG WIFRNNGRRL RIGVPDRASF
KDFVSRVNGS SNKVQGYCID VFEAAVKLLS YPVPHEFIFF GDGLTNPNYN ELVNKVTTGV
DFDAVVGDIA IVTKRTRIVD FTQPYIESGL VVVAPVTRLN ENPWAFLRPF TLPMWAVTAS
FFVIVGAAIW ILEHRINDEF RGPPRRQIIT ILWFTFSTMF FSHRETTVST LGRMVLLIWL
FVVLIITSSY TASLTSILTV QQLNSPIKGV DTLISSTGRI GFQVGSFAEN YMTDELNIAS
SRLVPLASPE EYANALQNGT VAAIVDERPY IDLFLSDYCK FAIRGQEFTR CGWGFAFPRD
SPLAVDMSTA ILGLSETGEL QKIHDRWLSK SNCSSPHGSQ SGDSEQLNVH SFWGMFLVVG
IACLVALFIH FFKIIRDFCK DTPEVVVEEA IPSPKSSRLT KLQTFLAFVD EKEEETKRRL
KRKRNNDHSM NANSIISRTA SRRPI
