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GLR2_CAEEL
ID   GLR2_CAEEL              Reviewed;         977 AA.
AC   Q10914; Q86GT2; Q9BK24;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   15-AUG-2003, sequence version 3.
DT   03-AUG-2022, entry version 162.
DE   RecName: Full=Glutamate receptor 2;
DE   Flags: Precursor;
GN   Name=glr-2; ORFNames=B0280.12/K04G7.2;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B), AND FUNCTION.
RX   PubMed=12467596; DOI=10.1016/s0896-6273(02)01088-7;
RA   Mellem J.E., Brockie P.J., Zheng Y., Madsen D.M., Maricq A.V.;
RT   "Decoding of polymodal sensory stimuli by postsynaptic glutamate receptors
RT   in C. elegans.";
RL   Neuron 36:933-944(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 491-920 (ISOFORMS A AND B), AND TISSUE
RP   SPECIFICITY.
RX   PubMed=11222641; DOI=10.1523/jneurosci.21-05-01510.2001;
RA   Brockie P.J., Madsen D.M., Zheng Y., Mellem J., Maricq A.V.;
RT   "Differential expression of glutamate receptor subunits in the nervous
RT   system of Caenorhabditis elegans and their regulation by the homeodomain
RT   protein UNC-42.";
RL   J. Neurosci. 21:1510-1522(2001).
RN   [4]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-566, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RC   STRAIN=Bristol N2;
RX   PubMed=17761667; DOI=10.1074/mcp.m600392-mcp200;
RA   Kaji H., Kamiie J., Kawakami H., Kido K., Yamauchi Y., Shinkawa T.,
RA   Taoka M., Takahashi N., Isobe T.;
RT   "Proteomics reveals N-linked glycoprotein diversity in Caenorhabditis
RT   elegans and suggests an atypical translocation mechanism for integral
RT   membrane proteins.";
RL   Mol. Cell. Proteomics 6:2100-2109(2007).
CC   -!- FUNCTION: L-glutamate acts as an excitatory neurotransmitter at many
CC       synapses in the central nervous system. The postsynaptic actions of
CC       glutamate are mediated by a variety of receptors that are named
CC       according to their selective agonists. Required for response to
CC       mechanical and osmotic stimuli. {ECO:0000269|PubMed:12467596}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}. Postsynaptic cell membrane {ECO:0000305}; Multi-
CC       pass membrane protein {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=b;
CC         IsoId=Q10914-1; Sequence=Displayed;
CC       Name=a;
CC         IsoId=Q10914-2; Sequence=VSP_008031;
CC   -!- TISSUE SPECIFICITY: Command interneurons of the locomotory control
CC       circuit (AIA, AIB, AVA, AVD, AVE, PVC, RIA, RIG and RIR) and motor
CC       neurons (AVG, M1, RMDD and RMDV). {ECO:0000269|PubMed:11222641}.
CC   -!- SIMILARITY: Belongs to the glutamate-gated ion channel (TC 1.A.10.1)
CC       family. {ECO:0000305}.
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DR   EMBL; AF318606; AAK01094.2; -; mRNA.
DR   EMBL; FO080148; CCD61608.1; -; Genomic_DNA.
DR   EMBL; FO080148; CCD61609.1; -; Genomic_DNA.
DR   PIR; T15306; T15306.
DR   RefSeq; NP_001021113.1; NM_001025942.1. [Q10914-2]
DR   RefSeq; NP_001021114.1; NM_001025943.1. [Q10914-1]
DR   AlphaFoldDB; Q10914; -.
DR   SMR; Q10914; -.
DR   BioGRID; 41211; 3.
DR   STRING; 6239.B0280.12b; -.
DR   iPTMnet; Q10914; -.
DR   PaxDb; Q10914; -.
DR   PRIDE; Q10914; -.
DR   EnsemblMetazoa; B0280.12a.1; B0280.12a.1; WBGene00001613. [Q10914-2]
DR   EnsemblMetazoa; B0280.12b.1; B0280.12b.1; WBGene00001613. [Q10914-1]
DR   GeneID; 175999; -.
DR   KEGG; cel:CELE_B0280.12; -.
DR   UCSC; B0280.12b; c. elegans. [Q10914-1]
DR   CTD; 175999; -.
DR   WormBase; B0280.12a; CE31400; WBGene00001613; glr-2.
DR   WormBase; B0280.12b; CE33547; WBGene00001613; glr-2.
DR   eggNOG; KOG1054; Eukaryota.
DR   InParanoid; Q10914; -.
DR   OMA; RIASSCW; -.
DR   OrthoDB; 188544at2759; -.
DR   PhylomeDB; Q10914; -.
DR   Reactome; R-CEL-204005; COPII-mediated vesicle transport.
DR   Reactome; R-CEL-399710; Activation of AMPA receptors.
DR   Reactome; R-CEL-438066; Unblocking of NMDA receptors, glutamate binding and activation.
DR   Reactome; R-CEL-451308; Activation of Ca-permeable Kainate Receptor.
DR   Reactome; R-CEL-5694530; Cargo concentration in the ER.
DR   PRO; PR:Q10914; -.
DR   Proteomes; UP000001940; Chromosome III.
DR   Bgee; WBGene00001613; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR   GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004970; F:ionotropic glutamate receptor activity; IEA:InterPro.
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   InterPro; IPR001828; ANF_lig-bd_rcpt.
DR   InterPro; IPR019594; Glu/Gly-bd.
DR   InterPro; IPR001508; Iono_rcpt_met.
DR   InterPro; IPR001320; Iontro_rcpt.
DR   InterPro; IPR028082; Peripla_BP_I.
DR   Pfam; PF01094; ANF_receptor; 1.
DR   Pfam; PF00060; Lig_chan; 1.
DR   Pfam; PF10613; Lig_chan-Glu_bd; 1.
DR   PRINTS; PR00177; NMDARECEPTOR.
DR   SMART; SM00918; Lig_chan-Glu_bd; 1.
DR   SMART; SM00079; PBPe; 1.
DR   SUPFAM; SSF53822; SSF53822; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell membrane; Glycoprotein; Ion channel;
KW   Ion transport; Ligand-gated ion channel; Membrane;
KW   Postsynaptic cell membrane; Receptor; Reference proteome; Signal; Synapse;
KW   Transmembrane; Transmembrane helix; Transport.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..977
FT                   /note="Glutamate receptor 2"
FT                   /id="PRO_0000011591"
FT   TOPO_DOM        20..621
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        622..642
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        643..695
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        696..716
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        717..898
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        899..919
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        920..977
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          954..977
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        36
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        227
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        291
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        427
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        532
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        566
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:17761667"
FT   CARBOHYD        783
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        895
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         238..306
FT                   /note="Missing (in isoform a)"
FT                   /evidence="ECO:0000303|PubMed:11222641"
FT                   /id="VSP_008031"
SQ   SEQUENCE   977 AA;  111789 MW;  8D7A373BC70A8A42 CRC64;
     MNKNLLVFGF LIFVKIGETS KKFPLRAFVA STDIDNDTAH AIIEMLRLAE MTFNALSDVD
     FDVLLGTRDL PPMEMATMMW NLNRIICDEM KLGYMLMLAG TNFKNYGIYE DIANHMKMPL
     IDWEPSKSEN IGKTTENNPM IFSVAPSAEQ LLIDYIQYKG WRDVVYIHDG KNADRTLRTM
     FSYLHEKSPK YQLFVDNYVA PSDEEMFKEF LNEFHRRIST QHTLKSNDSS EEIDEPIPVN
     VIVDLEGSYR TRAFLRALEE SVLVKKEYHY VFSNFDVDET DLSGFHFSLI NITIFRIFDK
     NNKKFLKTRA EFHDVYRGGF SNTDSIPTAA AFAHDAILVA GKALQIAMNE HGKGIFDKSF
     VRHQLFNRGR KGLYCRPHED QTESRQFETF EHGKKIAEAI KKVVLTDKDG TLTGRIQFDK
     VTGKRTNFSA EIVEIKPGVN SLNSIWERFQ WAEGEGFLLG GERYVQEKKK DSSQTRKGIL
     PSKPWQLRFN VVTVLVKPFV MLKRRNPGEP ELKGNDRFEG YCIDLLNLLA KNITGFEYDV
     FISDGNKYGS RQADGSWDGM IGYLLNETAD VAVAPLTITQ ERERAVDFSK PFMTTGISIM
     IKKPEKQEFN IFSFMEPLGM TIWIFTLSSY FGVSLTIFLV SWFSPYEKRI EFKRGEFTVT
     NEFTLYNSLW FTLAAFMQQG TDILPRAVSG RIASSCWWFF TLIIVSSYTA NLAAFLTLER
     MTPPIESVED LANQNKILYG VNEGGSTAAF FEDSIVPLYK KMWNFMVSTT QKQIELEKQS
     ITNSTSNRIF VSSYADGIEK VRTSKGKYAF LLEETTNNYE SGRRPCDTMK VGQNLNTLGY
     GIATKIGNPL RVSLNLAILY LSEKGELKKL ENKWWYDRGQ CDTGTSDGGT SSSLNLSKVA
     GIFYILLAGM VLSMCTALVE FLFRKNKENR EKERNRMRSS RPLKPGILAS CERAKQKQLQ
     NRRTKSEEVS TPRSTLF
 
 
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