GLR21_ARATH
ID GLR21_ARATH Reviewed; 901 AA.
AC O04660; Q0WSC5;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-JAN-2004, sequence version 2.
DT 25-MAY-2022, entry version 147.
DE RecName: Full=Glutamate receptor 2.1;
DE AltName: Full=Ligand-gated ion channel 2.1;
DE Short=AtGLR3;
DE Flags: Precursor;
GN Name=GLR2.1; Synonyms=GLR3; OrderedLocusNames=At5g27100;
GN ORFNames=A_TM021B04.3, T21B4.10;
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=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 [5]
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. First strongly
CC detected in all cell types of the root except at the apex. Later
CC expressed at the root-shoot junction. {ECO:0000269|PubMed:12082126}.
CC -!- SIMILARITY: Belongs to the glutamate-gated ion channel (TC 1.A.10.1)
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB61068.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF007271; AAB61068.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED93650.1; -; Genomic_DNA.
DR EMBL; AK228008; BAE99973.1; -; mRNA.
DR PIR; T01809; T01809.
DR RefSeq; NP_198062.2; NM_122592.4.
DR AlphaFoldDB; O04660; -.
DR SMR; O04660; -.
DR BioGRID; 18042; 8.
DR IntAct; O04660; 1.
DR STRING; 3702.AT5G27100.1; -.
DR iPTMnet; O04660; -.
DR PaxDb; O04660; -.
DR PRIDE; O04660; -.
DR ProteomicsDB; 230401; -.
DR EnsemblPlants; AT5G27100.1; AT5G27100.1; AT5G27100.
DR GeneID; 832768; -.
DR Gramene; AT5G27100.1; AT5G27100.1; AT5G27100.
DR KEGG; ath:AT5G27100; -.
DR Araport; AT5G27100; -.
DR TAIR; locus:2181196; AT5G27100.
DR eggNOG; KOG1052; Eukaryota.
DR HOGENOM; CLU_007358_0_2_1; -.
DR InParanoid; O04660; -.
DR OMA; AQFMIEM; -.
DR OrthoDB; 188544at2759; -.
DR PhylomeDB; O04660; -.
DR PRO; PR:O04660; -.
DR Proteomes; UP000006548; Chromosome 5.
DR Genevisible; O04660; 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..901
FT /note="Glutamate receptor 2.1"
FT /id="PRO_0000011596"
FT TOPO_DOM 26..574
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 575..595
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 596..604
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 605..625
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 626..629
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 630..650
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 651..823
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 824..844
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 845..901
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 46
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 53
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 204
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 267
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 331
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 461
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 536
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 901 AA; 100905 MW; 45E29E2CC5A26DE8 CRC64;
MKRENNLVLS LLFFVIVFLM QVGEAQNRIT NVNVGIVNDI GTAYSNMTLL CINMSLSDFY
SSHPETQTRL VTTVVDSKND VVTAAAAALD LITNKEVKAI LGPWTSMQAQ FMIEMGQKSQ
VPIVTYSATS PSLASIRSQY FFRATYDDSS QVHAIKEIIK LFGWREVAPV YVDDTFGEGI
MPRLTDVLQE INVRIPYRTV ISPNATDDEI SVELLRMMTL PTRVFVVHLV ELLASRFFAK
ATEIGLMKQG YVWILTNTIT DVLSIMNETE IETMQGVLGV KTYVPRSKEL ENFRSRWTKR
FPISDLNVYG LWAYDATTAL ALAIEEAGTS NLTFVKMDAK RNVSELQGLG VSQYGPKLLQ
TLSRVRFQGL AGDFQFINGE LQPSVFEIVN VNGQGGRTIG FWMKEYGLFK NVDQKPASKT
TFSSWQDRLR PIIWPGDTTS VPKGWEIPTN GKRLQIGVPV NNTFQQFVKA TRDPITNSTI
FSGFSIDYFE AVIQAIPYDI SYDFIPFQDG GYDALVYQVY LGKYDAVVAD TTISSNRSMY
VDFSLPYTPS GVGLVVPVKD SVRRSSTIFL MPLTLALWLI SLLSFFIIGL VVWVLEHRVN
PDFDGPGQYQ LSTIFWFSFS IMVFAPRERV LSFWARVVVI IWYFLVLVLT QSYTASLASL
LTTQHLHPTV TNINSLLAKG ESVGYQSSFI LGRLRDSGFS EASLVSYGSP EHCDALLSKG
QAEGGVSAVL MEVPYVRIFL GQYCNKYKMV QTPFKVDGLG FVFPIGSPLV ADISRAILKV
EESNKANQLE NAWFKPIDES CPDPLTNPDP NPSVSFRQLG FDSFWVLFLV AAIVCTMALL
KFVYQFLKEN PNQRNLRVLW EKFNEPDQKS YIKDVTKCQC SSGQGMPKNG QEGANAVNNG
N
