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GLR14_ARATH
ID   GLR14_ARATH             Reviewed;         861 AA.
AC   Q8LGN1; Q8LGN2; Q9SRR4;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   16-JAN-2004, sequence version 2.
DT   03-AUG-2022, entry version 128.
DE   RecName: Full=Glutamate receptor 1.4;
DE   AltName: Full=Ligand-gated ion channel 1.4;
DE   Flags: Precursor;
GN   Name=GLR1.4; OrderedLocusNames=At3g07520; ORFNames=F21O3.23;
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], AND TISSUE SPECIFICITY.
RC   STRAIN=cv. Columbia;
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).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130713; DOI=10.1038/35048706;
RA   Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA   Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA   Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA   Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA   Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA   Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA   Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA   Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA   Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA   Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA   Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA   de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA   Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA   Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA   Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA   Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA   Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA   Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA   Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA   Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA   Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA   Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA   Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL   Nature 408:820-822(2000).
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   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   FUNCTION.
RX   PubMed=18625242; DOI=10.1016/j.jmb.2008.06.076;
RA   Tapken D., Hollmann M.;
RT   "Arabidopsis thaliana glutamate receptor ion channel function demonstrated
RT   by ion pore transplantation.";
RL   J. Mol. Biol. 383:36-48(2008).
CC   -!- FUNCTION: Glutamate-gated receptor that probably acts as non-selective
CC       cation channel. Can transport calcium ions. May be involved in light-
CC       signal transduction and calcium homeostasis via the regulation of
CC       calcium influx into cells. {ECO:0000269|PubMed:18625242}.
CC   -!- SUBUNIT: May form heteromers. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC   -!- TISSUE SPECIFICITY: Expressed predominantly in roots and siliques.
CC       {ECO:0000269|PubMed:12082126}.
CC   -!- SIMILARITY: Belongs to the glutamate-gated ion channel (TC 1.A.10.1)
CC       family. {ECO:0000305}.
CC   -!- CAUTION: AAL61996 is a fragment and was originally reported as a
CC       spliced variant of AAL61995. {ECO:0000305|PubMed:12082126}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF02156.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AY072066; AAL61995.1; -; mRNA.
DR   EMBL; AY072067; AAL61996.1; -; mRNA.
DR   EMBL; AC009853; AAF02156.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002686; AEE74553.1; -; Genomic_DNA.
DR   RefSeq; NP_187408.2; NM_111630.2.
DR   AlphaFoldDB; Q8LGN1; -.
DR   SMR; Q8LGN1; -.
DR   BioGRID; 5275; 11.
DR   STRING; 3702.AT3G07520.1; -.
DR   iPTMnet; Q8LGN1; -.
DR   PaxDb; Q8LGN1; -.
DR   PRIDE; Q8LGN1; -.
DR   EnsemblPlants; AT3G07520.1; AT3G07520.1; AT3G07520.
DR   GeneID; 819940; -.
DR   Gramene; AT3G07520.1; AT3G07520.1; AT3G07520.
DR   KEGG; ath:AT3G07520; -.
DR   Araport; AT3G07520; -.
DR   TAIR; locus:2079681; AT3G07520.
DR   eggNOG; KOG1052; Eukaryota.
DR   HOGENOM; CLU_007358_0_0_1; -.
DR   InParanoid; Q8LGN1; -.
DR   OMA; QQNAIHI; -.
DR   OrthoDB; 188544at2759; -.
DR   PhylomeDB; Q8LGN1; -.
DR   PRO; PR:Q8LGN1; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q8LGN1; baseline and differential.
DR   Genevisible; Q8LGN1; 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; IDA:UniProtKB.
DR   GO; GO:0005261; F:cation channel activity; IDA:TAIR.
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; IDA:UniProtKB.
DR   GO; GO:0019722; P:calcium-mediated signaling; ISS:UniProtKB.
DR   GO; GO:0030003; P:cellular cation homeostasis; IDA:TAIR.
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..29
FT                   /evidence="ECO:0000255"
FT   CHAIN           30..861
FT                   /note="Glutamate receptor 1.4"
FT                   /id="PRO_0000011595"
FT   TOPO_DOM        30..568
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        569..589
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        590..598
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        599..619
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        620..630
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        631..651
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        652..800
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        801..821
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        822..861
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        306
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        534
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        707
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   861 AA;  97760 MW;  0782EE543B78BA63 CRC64;
     MENCMIRNTG YFLTIFFLAF ISFAVTCSGT NQKDNVDRLP VVYEDVRIGL VVDMGSMEGK
     LVTTSISMAL SDFYHVNNGY RTRVSVLSRD SHGDPLQALA AAMDLLQTEQ VEALVGGQSL
     LEAKNLAELG EKTKVPVISS FQVPSSLSLA KYNYFIQATH DTSSEAKGIA ALFSNFDWRT
     AVLIYEDDDD WRESIQPLVG HFQQNAIHIE YKAEFSVSSN EECIMKQLRK FKASGIRIFV
     AHISERIANR LFPCARRLGM MEEGYAWILT ARSMNNFQDT NYLAKEEMEG VIGFKSYIPL
     TEELHNFTLR WKRSLRLEEV VTRMSVCSIW AHDIAWSLAR AAEVAKLPGL SVYDLLEAIP
     ESAKHKGLSG DIKFIDKKFI SDKFEIVNMI GRGERSVGLW NSGSFISNRR RRLSSTKALE
     TIIWPGGSTR IPKIRSLKEK RHGKKKKLRV LVPAGNITPQ ILEVKTDFKT GVTAATGYCI
     DVFETSILPF NYEVEYIPWP GAINYKNYND LVYTLYSQKD KYDAAVGDIT ITDNRSLYVD
     FTLPFTDMGL AVVTAKDKSM WIIFKPLTLS LWLTIASFFI LTGAIVWLIE RHDNADFQGS
     CFQQIGTLLC FGFSTLVFAH RERLQHNMSR FVVIVWIFAV LILTSNYTAT LTSVMTVQQI
     RGLKSNENIG FFSASIAANV VNDNPTFQGP RYKGLKTADD FTNALRNGTI SFIVDEVPYV
     KLFVAKHPSE FVIVETESVT NGFGFAFQKG SPLVQKVSRE IEKLRRTEKL KAIENWWFQR
     QTTSATSEDT FHPLTVYTFR GLFMITGVSF AFALIVYLIP WNREQRQVVL KHFHRYVSHR
     FAREIRPSPT TPNRQNENSV I
 
 
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