GRIA4_RAT
ID GRIA4_RAT Reviewed; 902 AA.
AC P19493; Q64241;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 03-AUG-2022, entry version 193.
DE RecName: Full=Glutamate receptor 4;
DE Short=GluR-4;
DE Short=GluR4;
DE AltName: Full=AMPA-selective glutamate receptor 4;
DE AltName: Full=GluR-D;
DE AltName: Full=Glutamate receptor ionotropic, AMPA 4;
DE Short=GluA4;
DE Flags: Precursor;
GN Name=Gria4; Synonyms=Glur4;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=2166337; DOI=10.1126/science.2166337;
RA Keinaenen K., Wisden W., Sommer B., Werner P., Herb A., Verdoorn T.A.,
RA Sakmann B., Seeburg P.H.;
RT "A family of AMPA-selective glutamate receptors.";
RL Science 249:556-560(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RX PubMed=1977421; DOI=10.1016/0896-6273(90)90213-y;
RA Bettler B., Boulter J., Hermans-Borgmeyer I., O'Shea-Greenfield A.,
RA Deneris E.S., Moll C., Borgmeyer U., Hollmann M., Heinemann S.F.;
RT "Cloning of a novel glutamate receptor subunit, GluR5: expression in the
RT nervous system during development.";
RL Neuron 5:583-595(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RX PubMed=1699275; DOI=10.1126/science.1699275;
RA Sommer B., Keinaenen K., Verdoorn T.A., Wisden W., Burnashev N., Herb A.,
RA Koehler M., Takagi T., Sakmann B., Seeburg P.H.;
RT "Flip and flop: a cell-specific functional switch in glutamate-operated
RT channels of the CNS.";
RL Science 249:1580-1585(1990).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RX PubMed=1372042; DOI=10.1523/jneurosci.12-03-01010.1992;
RA Gallo V., Upson L.M., Hayes W.P., Vyklicky L. Jr., Winters C.A.,
RA Buonanno A.;
RT "Molecular cloning and development analysis of a new glutamate receptor
RT subunit isoform in cerebellum.";
RL J. Neurosci. 12:1010-1023(1992).
RN [5]
RP PARTIAL PROTEIN SEQUENCE, GLYCOSYLATION AT ASN-407 AND ASN-414, SUBCELLULAR
RP LOCATION, FUNCTION, AND MUTAGENESIS OF ASN-407 AND ASN-414.
RX PubMed=12603841; DOI=10.1046/j.1471-4159.2003.01611.x;
RA Pasternack A., Coleman S.K., Fethiere J., Madden D.R., LeCaer J.P.,
RA Rossier J., Pasternack M., Keinaenen K.;
RT "Characterization of the functional role of the N-glycans in the AMPA
RT receptor ligand-binding domain.";
RL J. Neurochem. 84:1184-1192(2003).
RN [6]
RP INTERACTION WITH PRKCABP (ISOFORM 3).
RX PubMed=10027300; DOI=10.1016/s0896-6273(00)80689-3;
RA Xia J., Zhang X., Staudinger J., Huganir R.L.;
RT "Clustering of AMPA receptors by the synaptic PDZ domain-containing protein
RT PICK1.";
RL Neuron 22:179-187(1999).
RN [7]
RP PHOSPHORYLATION AT SER-862, INTERACTION WITH PRKCG, AND SUBCELLULAR
RP LOCATION.
RX PubMed=12471040; DOI=10.1074/jbc.m205587200;
RA Correia S.S., Duarte C.B., Faro C.J., Pires E.V., Carvalho A.L.;
RT "Protein kinase C gamma associates directly with the GluR4 alpha-amino-3-
RT hydroxy-5-methyl-4-isoxazole propionate receptor subunit. Effect on
RT receptor phosphorylation.";
RL J. Biol. Chem. 278:6307-6313(2003).
RN [8]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH EPB41L1.
RX PubMed=12574408; DOI=10.1523/jneurosci.23-03-00798.2003;
RA Coleman S.K., Cai C., Mottershead D.G., Haapalahti J.-P., Keinaenen K.;
RT "Surface expression of GluR-D AMPA receptor is dependent on an interaction
RT between its C-terminal domain and a 4.1 protein.";
RL J. Neurosci. 23:798-806(2003).
RN [9]
RP INTERACTION WITH CACNG5.
RX PubMed=18817736; DOI=10.1016/j.neuron.2008.07.034;
RA Kato A.S., Siuda E.R., Nisenbaum E.S., Bredt D.S.;
RT "AMPA receptor subunit-specific regulation by a distinct family of type II
RT TARPs.";
RL Neuron 59:986-996(2008).
RN [10]
RP INTERACTION WITH CACNG5.
RX PubMed=19234459; DOI=10.1038/nn.2266;
RA Soto D., Coombs I.D., Renzi M., Zonouzi M., Farrant M., Cull-Candy S.G.;
RT "Selective regulation of long-form calcium-permeable AMPA receptors by an
RT atypical TARP, gamma-5.";
RL Nat. Neurosci. 12:277-285(2009).
RN [11]
RP ERRATUM OF PUBMED:19234459.
RX DOI=10.1038/nn0609-808c;
RA Soto D., Coombs I.D., Renzi M., Zonouzi M., Farrant M., Cull-Candy S.G.;
RL Nat. Neurosci. 12:808-808(2009).
RN [12]
RP SUBUNIT, SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=19265014; DOI=10.1126/science.1167852;
RA Schwenk J., Harmel N., Zolles G., Bildl W., Kulik A., Heimrich B.,
RA Chisaka O., Jonas P., Schulte U., Fakler B., Kloecker N.;
RT "Functional proteomics identify cornichon proteins as auxiliary subunits of
RT AMPA receptors.";
RL Science 323:1313-1319(2009).
RN [13]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-258, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=24090084; DOI=10.1021/pr400783j;
RA Parker B.L., Thaysen-Andersen M., Solis N., Scott N.E., Larsen M.R.,
RA Graham M.E., Packer N.H., Cordwell S.J.;
RT "Site-specific glycan-peptide analysis for determination of N-glycoproteome
RT heterogeneity.";
RL J. Proteome Res. 12:5791-5800(2013).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 416-795 IN COMPLEX WITH GLUTAMATE
RP AND DIHYDROKAINIC ACID, FUNCTION, AND SUBUNIT.
RX PubMed=19102704; DOI=10.1021/bi8013196;
RA Gill A., Birdsey-Benson A., Jones B.L., Henderson L.P., Madden D.R.;
RT "Correlating AMPA receptor activation and cleft closure across subunits:
RT crystal structures of the GluR4 ligand-binding domain in complex with full
RT and partial agonists.";
RL Biochemistry 47:13831-13841(2008).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) OF 415-796 IN COMPLEX WITH
RP GLUTAMATE, AMPA BINDING, AND DISULFIDE BOND.
RX PubMed=19022251; DOI=10.1016/j.febslet.2008.11.005;
RA Kasper C., Frydenvang K., Naur P., Gajhede M., Pickering D.S.,
RA Kastrup J.S.;
RT "Molecular mechanism of agonist recognition by the ligand-binding core of
RT the ionotropic glutamate receptor 4.";
RL FEBS Lett. 582:4089-4094(2008).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 416-795 IN COMPLEX WITH GLUTAMATE
RP AND DIHYDROKAINIC ACID, AND FUNCTION.
RX PubMed=20107073; DOI=10.1523/jneurosci.4558-09.2010;
RA Birdsey-Benson A., Gill A., Henderson L.P., Madden D.R.;
RT "Enhanced efficacy without further cleft closure: reevaluating twist as a
RT source of agonist efficacy in AMPA receptors.";
RL J. Neurosci. 30:1463-1470(2010).
CC -!- FUNCTION: Receptor for glutamate that functions as ligand-gated ion
CC channel in the central nervous system and plays an important role in
CC excitatory synaptic transmission. L-glutamate acts as an excitatory
CC neurotransmitter at many synapses in the central nervous system.
CC Binding of the excitatory neurotransmitter L-glutamate induces a
CC conformation change, leading to the opening of the cation channel, and
CC thereby converts the chemical signal to an electrical impulse. The
CC receptor then desensitizes rapidly and enters a transient inactive
CC state, characterized by the presence of bound agonist. In the presence
CC of CACNG4 or CACNG7 or CACNG8, shows resensitization which is
CC characterized by a delayed accumulation of current flux upon continued
CC application of glutamate (By similarity). {ECO:0000250,
CC ECO:0000269|PubMed:12603841, ECO:0000269|PubMed:19102704,
CC ECO:0000269|PubMed:20107073}.
CC -!- SUBUNIT: Homotetramer or heterotetramer of pore-forming glutamate
CC receptor subunits. Tetramers may be formed by the dimerization of
CC dimers. Interacts with EPB41L1 via its C-terminus. Isoform 3 interacts
CC with PRKCABP. Found in a complex with GRIA1, GRIA2, GRIA3, CNIH2,
CC CNIH3, CACNG2, CACNG3, CACNG4, CACNG5, CACNG7 and CACNG8. Interacts
CC with CACNG5 and PRKCG. {ECO:0000269|PubMed:12471040,
CC ECO:0000269|PubMed:12574408, ECO:0000269|PubMed:18817736,
CC ECO:0000269|PubMed:19022251, ECO:0000269|PubMed:19102704,
CC ECO:0000269|PubMed:19234459, ECO:0000269|PubMed:19265014,
CC ECO:0000269|PubMed:20107073}.
CC -!- INTERACTION:
CC P19493; P19493: Gria4; NbExp=2; IntAct=EBI-7761834, EBI-7761834;
CC P19493; P97879: Grip1; NbExp=3; IntAct=EBI-7761834, EBI-936113;
CC P19493; P49185: Mapk8; NbExp=2; IntAct=EBI-7761834, EBI-7456505;
CC P19493-2; P19491-2: Gria2; NbExp=2; IntAct=EBI-15852899, EBI-15817825;
CC P19493-2; P19493-2: Gria4; NbExp=4; IntAct=EBI-15852899, EBI-15852899;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC Postsynaptic cell membrane; Multi-pass membrane protein. Cell
CC projection, dendrite. Note=Interaction with CNIH2, CNIH3 and PRKCG
CC promotes cell surface expression.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=Flop;
CC IsoId=P19493-1; Sequence=Displayed;
CC Name=2; Synonyms=Flip;
CC IsoId=P19493-2; Sequence=VSP_000123, VSP_000124, VSP_000125;
CC Name=3; Synonyms=4C flop;
CC IsoId=P19493-3; Sequence=VSP_000126;
CC -!- TISSUE SPECIFICITY: Detected in cerebellum (at protein level).
CC -!- DOMAIN: The M4 transmembrane segment mediates tetramerization and is
CC required for cell surface expression. {ECO:0000250}.
CC -!- PTM: Palmitoylated. Depalmitoylated upon glutamate stimulation. Cys-611
CC palmitoylation leads to Golgi retention and decreased cell surface
CC expression. In contrast, Cys-837 palmitoylation does not affect cell
CC surface expression but regulates stimulation-dependent endocytosis (By
CC similarity). {ECO:0000250}.
CC -!- PTM: Phosphorylated at Ser-862 by PRKCG; phosphorylation increases
CC plasma membrane-associated GRI4 expression.
CC {ECO:0000269|PubMed:12471040}.
CC -!- MISCELLANEOUS: The postsynaptic actions of Glu are mediated by a
CC variety of receptors that are named according to their selective
CC agonists. This receptor binds AMPA (quisqualate) > glutamate > kainate.
CC -!- SIMILARITY: Belongs to the glutamate-gated ion channel (TC 1.A.10.1)
CC family. GRIA4 subfamily. {ECO:0000305}.
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DR EMBL; M36421; AAA41246.1; -; mRNA.
DR EMBL; M85037; AAA41242.1; -; mRNA.
DR EMBL; M38063; AAA63481.1; -; mRNA.
DR EMBL; S94371; AAB21763.1; -; mRNA.
DR PIR; A44839; A44839.
DR PIR; D40170; D40170.
DR RefSeq; NP_001106655.1; NM_001113184.1.
DR RefSeq; NP_058959.2; NM_017263.2.
DR PDB; 3EN3; X-ray; 2.43 A; A=416-528, A=654-795.
DR PDB; 3EPE; X-ray; 1.85 A; A/B=416-528, A/B=654-795.
DR PDB; 3FAS; X-ray; 1.40 A; A/B=415-528, A/B=654-796.
DR PDB; 3FAT; X-ray; 1.90 A; A/B/C=415-528, A/B/C=654-796.
DR PDB; 3KEI; X-ray; 1.90 A; A/B=416-528, A/B=654-795.
DR PDB; 3KFM; X-ray; 2.20 A; A=416-528, A=654-795.
DR PDB; 4GPA; X-ray; 2.25 A; A=22-401.
DR PDB; 5FWX; X-ray; 2.50 A; B/D=22-401.
DR PDBsum; 3EN3; -.
DR PDBsum; 3EPE; -.
DR PDBsum; 3FAS; -.
DR PDBsum; 3FAT; -.
DR PDBsum; 3KEI; -.
DR PDBsum; 3KFM; -.
DR PDBsum; 4GPA; -.
DR PDBsum; 5FWX; -.
DR AlphaFoldDB; P19493; -.
DR SMR; P19493; -.
DR BioGRID; 248252; 34.
DR CORUM; P19493; -.
DR DIP; DIP-41142N; -.
DR IntAct; P19493; 5.
DR MINT; P19493; -.
DR STRING; 10116.ENSRNOP00000009542; -.
DR BindingDB; P19493; -.
DR ChEMBL; CHEMBL3505; -.
DR DrugCentral; P19493; -.
DR TCDB; 1.A.10.1.2; the glutamate-gated ion channel (gic) family of neurotransmitter receptors.
DR GlyGen; P19493; 6 sites, 9 N-linked glycans (1 site).
DR iPTMnet; P19493; -.
DR PhosphoSitePlus; P19493; -.
DR SwissPalm; P19493; -.
DR PaxDb; P19493; -.
DR PRIDE; P19493; -.
DR GeneID; 29629; -.
DR KEGG; rno:29629; -.
DR UCSC; RGD:61863; rat. [P19493-1]
DR CTD; 2893; -.
DR RGD; 61863; Gria4.
DR eggNOG; KOG1054; Eukaryota.
DR InParanoid; P19493; -.
DR OrthoDB; 188544at2759; -.
DR PhylomeDB; P19493; -.
DR Reactome; R-RNO-399710; Activation of AMPA receptors.
DR Reactome; R-RNO-416993; Trafficking of GluR2-containing AMPA receptors.
DR Reactome; R-RNO-438066; Unblocking of NMDA receptors, glutamate binding and activation.
DR Reactome; R-RNO-8849932; Synaptic adhesion-like molecules.
DR EvolutionaryTrace; P19493; -.
DR PRO; PR:P19493; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0032281; C:AMPA glutamate receptor complex; IDA:UniProtKB.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030425; C:dendrite; IDA:RGD.
DR GO; GO:0043197; C:dendritic spine; IDA:ARUK-UCL.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0099061; C:integral component of postsynaptic density membrane; IDA:SynGO.
DR GO; GO:0008328; C:ionotropic glutamate receptor complex; TAS:UniProtKB.
DR GO; GO:0032983; C:kainate selective glutamate receptor complex; IDA:UniProtKB.
DR GO; GO:0043025; C:neuronal cell body; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0014069; C:postsynaptic density; IDA:UniProtKB.
DR GO; GO:0045202; C:synapse; IMP:UniProtKB.
DR GO; GO:0043195; C:terminal bouton; IDA:RGD.
DR GO; GO:0004971; F:AMPA glutamate receptor activity; IMP:RGD.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0004970; F:ionotropic glutamate receptor activity; IDA: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:1904315; F:transmitter-gated ion channel activity involved in regulation of postsynaptic membrane potential; ISO:RGD.
DR GO; GO:0007268; P:chemical synaptic transmission; IMP:RGD.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; IMP:UniProtKB.
DR GO; GO:0034392; P:negative regulation of smooth muscle cell apoptotic process; ISO:RGD.
DR GO; GO:0051968; P:positive regulation of synaptic transmission, glutamatergic; IMP:UniProtKB.
DR GO; GO:0050803; P:regulation of synapse structure or activity; TAS:UniProtKB.
DR GO; GO:0060992; P:response to fungicide; IEP:RGD.
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 3D-structure; Alternative splicing; Cell membrane; Cell projection;
KW Direct protein sequencing; Disulfide bond; Glycoprotein; Ion channel;
KW Ion transport; Ligand-gated ion channel; Lipoprotein; Membrane; Palmitate;
KW Phosphoprotein; Postsynaptic cell membrane; Receptor; Reference proteome;
KW Signal; Synapse; Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..902
FT /note="Glutamate receptor 4"
FT /id="PRO_0000011540"
FT TOPO_DOM 22..544
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 545..565
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 566..592
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT INTRAMEM 593..608
FT /note="Helical; Pore-forming"
FT /evidence="ECO:0000250"
FT INTRAMEM 609..611
FT /evidence="ECO:0000250"
FT TOPO_DOM 612..617
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 618..638
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 639..813
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 814..834
FT /note="Helical; Name=M4"
FT /evidence="ECO:0000250"
FT TOPO_DOM 835..902
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT BINDING 472
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000269|PubMed:19022251,
FT ECO:0000269|PubMed:19102704, ECO:0000269|PubMed:20107073"
FT BINDING 500..502
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT BINDING 507
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000269|PubMed:19022251,
FT ECO:0000269|PubMed:19102704, ECO:0000269|PubMed:20107073"
FT BINDING 676..677
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT BINDING 727
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT MOD_RES 862
FT /note="Phosphoserine; by PKC/PRKCG"
FT /evidence="ECO:0000269|PubMed:12471040"
FT LIPID 611
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 837
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT CARBOHYD 52
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 56
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 258
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0007744|PubMed:24090084"
FT CARBOHYD 371
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 407
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12603841"
FT CARBOHYD 414
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12603841"
FT DISULFID 84..331
FT /evidence="ECO:0000250"
FT DISULFID 740..795
FT /evidence="ECO:0000269|PubMed:19022251"
FT VAR_SEQ 765..767
FT /note="GNA -> RTP (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:1699275,
FT ECO:0000303|PubMed:1977421"
FT /id="VSP_000123"
FT VAR_SEQ 776..780
FT /note="NEQGL -> SEAGV (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:1699275,
FT ECO:0000303|PubMed:1977421"
FT /id="VSP_000124"
FT VAR_SEQ 797..801
FT /note="SGGGD -> PKDSG (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:1699275,
FT ECO:0000303|PubMed:1977421"
FT /id="VSP_000125"
FT VAR_SEQ 849..902
FT /note="LTFSEATRNKARLSITGSVGENGRVLTPDCPKAVHTGTAIRQSSGLAVIASD
FT LP -> VAKSAQTFNPTSSQNTHNLATYREGYNVYGTESIKI (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:1372042"
FT /id="VSP_000126"
FT MUTAGEN 407
FT /note="N->Q: No effect on surface expression and channel
FT activity; when associated with Q-414."
FT /evidence="ECO:0000269|PubMed:12603841"
FT MUTAGEN 414
FT /note="N->Q: No effect on surface expression and channel
FT activity; when associated with Q-407."
FT /evidence="ECO:0000269|PubMed:12603841"
FT CONFLICT 111..112
FT /note="SA -> RR (in Ref. 2; AAA41242)"
FT /evidence="ECO:0000305"
FT CONFLICT 454
FT /note="I -> S (in Ref. 2; AAA41242)"
FT /evidence="ECO:0000305"
FT CONFLICT 734
FT /note="T -> I (in Ref. 2; AAA41242)"
FT /evidence="ECO:0000305"
FT CONFLICT 855
FT /note="T -> I (in Ref. 2; AAA41242)"
FT /evidence="ECO:0000305"
FT STRAND 25..33
FT /evidence="ECO:0007829|PDB:4GPA"
FT HELIX 38..52
FT /evidence="ECO:0007829|PDB:4GPA"
FT TURN 57..59
FT /evidence="ECO:0007829|PDB:4GPA"
FT STRAND 61..70
FT /evidence="ECO:0007829|PDB:4GPA"
FT HELIX 76..88
FT /evidence="ECO:0007829|PDB:4GPA"
FT STRAND 92..96
FT /evidence="ECO:0007829|PDB:4GPA"
FT TURN 100..102
FT /evidence="ECO:0007829|PDB:4GPA"
FT HELIX 103..112
FT /evidence="ECO:0007829|PDB:4GPA"
FT STRAND 116..119
FT /evidence="ECO:0007829|PDB:4GPA"
FT STRAND 129..133
FT /evidence="ECO:0007829|PDB:4GPA"
FT HELIX 139..148
FT /evidence="ECO:0007829|PDB:4GPA"
FT STRAND 153..158
FT /evidence="ECO:0007829|PDB:4GPA"
FT HELIX 165..175
FT /evidence="ECO:0007829|PDB:4GPA"
FT TURN 176..178
FT /evidence="ECO:0007829|PDB:4GPA"
FT STRAND 180..185
FT /evidence="ECO:0007829|PDB:4GPA"
FT HELIX 191..204
FT /evidence="ECO:0007829|PDB:4GPA"
FT STRAND 208..212
FT /evidence="ECO:0007829|PDB:4GPA"
FT HELIX 215..228
FT /evidence="ECO:0007829|PDB:4GPA"
FT STRAND 236..239
FT /evidence="ECO:0007829|PDB:4GPA"
FT STRAND 241..243
FT /evidence="ECO:0007829|PDB:4GPA"
FT HELIX 244..246
FT /evidence="ECO:0007829|PDB:4GPA"
FT HELIX 250..255
FT /evidence="ECO:0007829|PDB:4GPA"
FT STRAND 258..263
FT /evidence="ECO:0007829|PDB:4GPA"
FT HELIX 270..279
FT /evidence="ECO:0007829|PDB:4GPA"
FT TURN 284..286
FT /evidence="ECO:0007829|PDB:4GPA"
FT TURN 288..291
FT /evidence="ECO:0007829|PDB:4GPA"
FT HELIX 296..317
FT /evidence="ECO:0007829|PDB:4GPA"
FT HELIX 342..350
FT /evidence="ECO:0007829|PDB:4GPA"
FT STRAND 353..356
FT /evidence="ECO:0007829|PDB:4GPA"
FT STRAND 359..363
FT /evidence="ECO:0007829|PDB:4GPA"
FT STRAND 367..369
FT /evidence="ECO:0007829|PDB:5FWX"
FT STRAND 373..380
FT /evidence="ECO:0007829|PDB:4GPA"
FT STRAND 383..391
FT /evidence="ECO:0007829|PDB:4GPA"
FT TURN 392..394
FT /evidence="ECO:0007829|PDB:4GPA"
FT STRAND 395..398
FT /evidence="ECO:0007829|PDB:4GPA"
FT STRAND 416..421
FT /evidence="ECO:0007829|PDB:3FAS"
FT TURN 425..427
FT /evidence="ECO:0007829|PDB:3FAS"
FT STRAND 428..430
FT /evidence="ECO:0007829|PDB:3FAS"
FT HELIX 434..436
FT /evidence="ECO:0007829|PDB:3FAS"
FT HELIX 439..442
FT /evidence="ECO:0007829|PDB:3FAS"
FT STRAND 443..445
FT /evidence="ECO:0007829|PDB:3FAS"
FT HELIX 446..458
FT /evidence="ECO:0007829|PDB:3FAS"
FT STRAND 461..466
FT /evidence="ECO:0007829|PDB:3FAS"
FT TURN 477..479
FT /evidence="ECO:0007829|PDB:3FAS"
FT HELIX 484..490
FT /evidence="ECO:0007829|PDB:3FAS"
FT STRAND 495..497
FT /evidence="ECO:0007829|PDB:3FAS"
FT HELIX 505..508
FT /evidence="ECO:0007829|PDB:3FAS"
FT STRAND 511..513
FT /evidence="ECO:0007829|PDB:3FAS"
FT STRAND 517..520
FT /evidence="ECO:0007829|PDB:3FAS"
FT STRAND 522..527
FT /evidence="ECO:0007829|PDB:3FAS"
FT HELIX 658..662
FT /evidence="ECO:0007829|PDB:3FAS"
FT STRAND 665..670
FT /evidence="ECO:0007829|PDB:3FAS"
FT STRAND 672..675
FT /evidence="ECO:0007829|PDB:3KEI"
FT HELIX 676..683
FT /evidence="ECO:0007829|PDB:3FAS"
FT HELIX 687..698
FT /evidence="ECO:0007829|PDB:3FAS"
FT STRAND 705..707
FT /evidence="ECO:0007829|PDB:3FAS"
FT HELIX 708..717
FT /evidence="ECO:0007829|PDB:3FAS"
FT TURN 718..720
FT /evidence="ECO:0007829|PDB:3FAS"
FT STRAND 721..727
FT /evidence="ECO:0007829|PDB:3FAS"
FT HELIX 728..735
FT /evidence="ECO:0007829|PDB:3FAS"
FT STRAND 742..746
FT /evidence="ECO:0007829|PDB:3FAS"
FT STRAND 752..754
FT /evidence="ECO:0007829|PDB:3FAS"
FT STRAND 757..759
FT /evidence="ECO:0007829|PDB:3FAS"
FT HELIX 765..777
FT /evidence="ECO:0007829|PDB:3FAS"
FT HELIX 780..789
FT /evidence="ECO:0007829|PDB:3FAS"
FT TURN 790..792
FT /evidence="ECO:0007829|PDB:3FAS"
SQ SEQUENCE 902 AA; 100758 MW; 873D1B4C710C4459 CRC64;
MRIICRQIVL LFSGFWGLAM GAFPSSVQIG GLFIRNTDQE YTAFRLAIFL HNTSPNASEA
PFNLVPHVDN IETANSFAVT NAFCSQYSRG VFAIFGLYDK RSVHTLTSFC SALHISLITP
SFPTEGESQF VLQLRPSLRG ALLSLLDHYE WNCFVFLYDT DRGYSILQAI MEKAGQNGWH
VSAICVENFN DVSYRQLLEE LDRRQEKKFV IDCEIERLQN ILEQIVSVGK HVKGYHYIIA
NLGFKDISLE RFIHGGANVT GFQLVDFNTP MVTKLMDRWK KLDQREYPGS ETPPKYTSAL
TYDGVLVMAE TFRSLRRQKI DISRRGNAGD CLANPAAPWG QGIDMERTLK QVRIQGLTGN
VQFDHYGRRV NYTMDVFELK STGPRKVGYW NDMDKLVLIQ DMPTLGNDTA AIENRTVVVT
TIMESPYVMY KKNHEMFEGN DKYEGYCVDL ASEIAKHIGI KYKIAIVPDG KYGARDADTK
IWNGMVGELV YGKAEIAIAP LTITLVREEV IDFSKPFMSL GISIMIKKPQ KSKPGVFSFL
DPLAYEIWMC IVFAYIGVSV VLFLVSRFSP YEWHTEEPED GKEGPSDQPP NEFGIFNSLW
FSLGAFMQQG CDISPRSLSG RIVGGVWWFF TLIIISSYTA NLAAFLTVER MVSPIESAED
LAKQTEIAYG TLDSGSTKEF FRRSKIAVYE KMWTYMRSAE PSVFTRTTAE GVARVRKSKG
KFAFLLESTM NEYTEQRKPC DTMKVGGNLD SKGYGVATPK GSSLGNAVNL AVLKLNEQGL
LDKLKNKWWY DKGECGSGGG DSKDKTSALS LSNVAGVFYI LVGGLGLAML VALIEFCYKS
RAEAKRMKLT FSEATRNKAR LSITGSVGEN GRVLTPDCPK AVHTGTAIRQ SSGLAVIASD
LP
