GLR37_ARATH
ID GLR37_ARATH Reviewed; 921 AA.
AC Q9SDQ4; Q9ZV68;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-JAN-2004, sequence version 2.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Glutamate receptor 3.7;
DE AltName: Full=Ionotropic glutamate receptor GLR5;
DE AltName: Full=Ligand-gated ion channel 3.7;
DE Flags: Precursor;
GN Name=GLR3.7; Synonyms=GLR5; OrderedLocusNames=At2g32400; ORFNames=T32F6.8;
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], GENE FAMILY, AND NOMENCLATURE.
RC STRAIN=cv. Columbia; TISSUE=Seedling;
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 [2]
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 [3]
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 [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 leaves and siliques.
CC Also detected in roots. {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; AF210701; AAF21042.1; -; mRNA.
DR EMBL; AC005700; AAC69938.2; -; Genomic_DNA.
DR EMBL; CP002685; AEC08679.1; -; Genomic_DNA.
DR PIR; F84732; F84732.
DR PIR; T51136; T51136.
DR RefSeq; NP_565744.1; NM_128799.4.
DR AlphaFoldDB; Q9SDQ4; -.
DR SMR; Q9SDQ4; -.
DR BioGRID; 3148; 2.
DR IntAct; Q9SDQ4; 1.
DR STRING; 3702.AT2G32400.1; -.
DR PaxDb; Q9SDQ4; -.
DR PRIDE; Q9SDQ4; -.
DR ProteomicsDB; 230404; -.
DR EnsemblPlants; AT2G32400.1; AT2G32400.1; AT2G32400.
DR GeneID; 817801; -.
DR Gramene; AT2G32400.1; AT2G32400.1; AT2G32400.
DR KEGG; ath:AT2G32400; -.
DR Araport; AT2G32400; -.
DR TAIR; locus:2062586; AT2G32400.
DR eggNOG; KOG1052; Eukaryota.
DR HOGENOM; CLU_007358_0_1_1; -.
DR InParanoid; Q9SDQ4; -.
DR OMA; VFAFDSV; -.
DR OrthoDB; 188544at2759; -.
DR PhylomeDB; Q9SDQ4; -.
DR PRO; PR:Q9SDQ4; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9SDQ4; baseline and differential.
DR Genevisible; Q9SDQ4; 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:0009506; C:plasmodesma; HDA:TAIR.
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..921
FT /note="Glutamate receptor 3.7"
FT /id="PRO_0000011611"
FT TOPO_DOM 26..580
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 581..601
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 602..608
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 609..629
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 630..640
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 641..661
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 662..822
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 823..843
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 844..921
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 896..921
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 214
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 300
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 369
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 396
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 478
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 568
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 385
FT /note="V -> I (in Ref. 1; AAF21042)"
FT /evidence="ECO:0000305"
FT CONFLICT 694
FT /note="F -> V (in Ref. 1; AAF21042)"
FT /evidence="ECO:0000305"
FT CONFLICT 858
FT /note="T -> I (in Ref. 1; AAF21042)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 921 AA; 103514 MW; 80600BFE9C778EA1 CRC64;
MGLGIDPSVA ITALIVVILV VPMDCQRPQL VNIGAVFAFD SVIGRAAKVA LEAAVSDVNN
DKSFLKETEL RLLMEDSACN VFRGSFGAFE LLEKEVVAMI GPISSSVAHT ISDIAKGLHF
PLVSFAATDP TLSALQFPFF LRTTPNDAHQ MSALVDLINF YGWKEVISVY SDDELGRNGV
SALDDELYKK RSRISYKVPL SVHSDEKFLT NALNKSKSIG PRVYILHFGP DPLLRIFDIA
QKLQMMTHEY VWLATDWLSV TLDSLSDKGT LKRLEGVVGL RQHIPESVKM EHFTHKLQSN
RSMNAYALHA YDTVWMIAHG IEELLNEGIN ITFSYSEKLL HARGTKLHLE KIKFFNSGEL
LLEKLLKVNF TGIAGQVQFG SGRNVIGCDY EIINVNKTDV HTVGFWSKNG GFSVVAPKTR
HSQKKTSFVS DEKLGDITWP GGGREKPRGW VIADSADPLK IVVPRRVSFV EFVTEEKNSS
HRIQGFCIDV FIEALKFVPY SVPYIFEPFG NGHSSPNYNH LIQMVTDGVY DAAVGDIAIV
PSRSKLVDFS QPYASTGLVV VIPANDDNAT WIFLRPFTSR LWCVVLVSFL VIAVVIWILE
HRINEDFRGP PRRQLSTMLL FSFSTLFKRN QEDTISNLAR LVMIVWLFLL MVLTASYTAN
LTSILTVQQL PSAITGIDSL RASEVPIGYQ AGTFTLEYLT YSLGMARSRL VPLDSTEEYE
KALKLGPTNW GGVAAIVDEL PYIELFLAER TGFKIVGEPF MHRGWGFAFK RDSPLAIDMS
TAILKLSETR KLQEIRKKWL CKTNCAGKSN WNPEPNQLHL KSFKGLYLVC IAITVSAFLV
FVLRMIRQFV RYRRMERTSS MPRASWSASP TLRLRELVFD FVEFVDEKEE AIKRMFRRSD
DSNNNPSHVG EVQADTEVPR N
