GRIA3_RAT
ID GRIA3_RAT Reviewed; 888 AA.
AC P19492;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 03-AUG-2022, entry version 196.
DE RecName: Full=Glutamate receptor 3;
DE Short=GluR-3;
DE AltName: Full=AMPA-selective glutamate receptor 3;
DE AltName: Full=GluR-C;
DE AltName: Full=GluR-K3;
DE AltName: Full=Glutamate receptor ionotropic, AMPA 3;
DE Short=GluA3;
DE Flags: Precursor;
GN Name=Gria3; Synonyms=Glur3;
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].
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].
RC STRAIN=Sprague-Dawley; TISSUE=Forebrain;
RX PubMed=2168579; DOI=10.1126/science.2168579;
RA Boulter J., Hollmann M., O'Shea-Greenfield A., Hartley M., Deneris E.S.,
RA Maron C., Heinemann S.F.;
RT "Molecular cloning and functional expression of glutamate receptor subunit
RT genes.";
RL Science 249:1033-1037(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (VARIANT FLIP).
RC TISSUE=Brain cortex, and Hippocampus;
RX PubMed=1699567; DOI=10.1016/0896-6273(90)90212-x;
RA Nakanishi N., Schneider N.A., Axel R.;
RT "A family of glutamate receptor genes: evidence for the formation of
RT heteromultimeric receptors with distinct channel properties.";
RL Neuron 5:569-581(1990).
RN [4]
RP ALTERNATIVE SPLICING (ISOFORMS FLIP AND FLOP).
RC TISSUE=Brain;
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 [5]
RP INTERACTION WITH PRKCABP.
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 [6]
RP INTERACTION WITH GRIP1.
RC TISSUE=Hippocampus;
RX PubMed=9069286; DOI=10.1038/386279a0;
RA Dong H., O'Brien R.J., Fung E.T., Lanahan A.A., Worley P.F., Huganir R.L.;
RT "GRIP: a synaptic PDZ domain-containing protein that interacts with AMPA
RT receptors.";
RL Nature 386:279-284(1997).
RN [7]
RP INTERACTION WITH GRIP2.
RX PubMed=10414981; DOI=10.1523/jneurosci.19-15-06528.1999;
RA Wyszynski M., Valtschanoff J.G., Naisbitt S., Dunah A.W., Kim E.,
RA Standaert D.G., Weinberg R., Sheng M.;
RT "Association of AMPA receptors with a subset of glutamate receptor-
RT interacting protein in vivo.";
RL J. Neurosci. 19:6528-6537(1999).
RN [8]
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 [9]
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 [10]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-260, 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 [11]
RP X-RAY CRYSTALLOGRAPHY (1.91 ANGSTROMS) OF 407-800 IN COMPLEX WITH
RP GLUTAMATE, AND DISULFIDE BOND.
RX PubMed=19003990; DOI=10.1002/prot.22274;
RA Ahmed A.H., Wang Q., Sondermann H., Oswald R.E.;
RT "Structure of the S1S2 glutamate binding domain of GLuR3.";
RL Proteins 75:628-637(2009).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (1.79 ANGSTROMS) OF 417-799 IN COMPLEX WITH
RP GLUTAMATE, AND DISULFIDE BOND.
RX PubMed=20199107; DOI=10.1021/bi1000678;
RA Ahmed A.H., Ptak C.P., Oswald R.E.;
RT "Molecular mechanism of flop selectivity and subsite recognition for an
RT AMPA receptor allosteric modulator: structures of GluA2 and GluA3 in
RT complexes with PEPA.";
RL Biochemistry 49:2843-2850(2010).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 23-403, SUBUNIT, DISULFIDE BOND,
RP AND GLYCOSYLATION AT ASN-260 AND ASN-374.
RX PubMed=21317871; DOI=10.1038/emboj.2011.17;
RA Sukumaran M., Rossmann M., Shrivastava I., Dutta A., Bahar I., Greger I.H.;
RT "Dynamics and allosteric potential of the AMPA receptor N-terminal
RT domain.";
RL EMBO J. 30:972-982(2011).
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 -!- SUBUNIT: Homotetramer or heterotetramer of pore-forming glutamate
CC receptor subunits. Tetramers may be formed by the dimerization of
CC dimers. Interacts with PRKCABP, GRIP1 and GRIP2. Found in a complex
CC with GRIA1, GRIA2, GRIA4, CNIH2, CNIH3, CACNG2, CACNG3, CACNG4, CACNG5,
CC CACNG7 and CACNG8. Interacts with CACNG5. {ECO:0000269|PubMed:10027300,
CC ECO:0000269|PubMed:10414981, ECO:0000269|PubMed:18817736,
CC ECO:0000269|PubMed:19003990, ECO:0000269|PubMed:19265014,
CC ECO:0000269|PubMed:20199107, ECO:0000269|PubMed:21317871,
CC ECO:0000269|PubMed:9069286}.
CC -!- INTERACTION:
CC P19492; P97879: Grip1; NbExp=3; IntAct=EBI-77764, EBI-936113;
CC P19492; Q9EP80: Pick1; NbExp=7; IntAct=EBI-77764, EBI-77728;
CC P19492-2; P19491-2: Gria2; NbExp=6; IntAct=EBI-16201849, EBI-15817825;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19265014};
CC Multi-pass membrane protein {ECO:0000269|PubMed:19265014}. Postsynaptic
CC cell membrane {ECO:0000269|PubMed:19265014}; Multi-pass membrane
CC protein {ECO:0000269|PubMed:19265014}. Note=Interaction with CNIH2 and
CC CNIH3 promotes cell surface expression.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Flop;
CC IsoId=P19492-1; Sequence=Displayed;
CC Name=Flip;
CC IsoId=P19492-2; Sequence=VSP_000119, VSP_000120, VSP_000121,
CC VSP_000122;
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-615
CC palmitoylation leads to Golgi retention and decreased cell surface
CC expression. In contrast, Cys-841 palmitoylation does not affect cell
CC surface expression but regulates stimulation-dependent endocytosis (By
CC similarity). {ECO:0000250}.
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. GRIA3 subfamily. {ECO:0000305}.
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DR EMBL; M36420; AAA41245.1; -; mRNA.
DR EMBL; X54656; CAA38466.1; -; mRNA.
DR EMBL; M38062; AAA63480.1; -; mRNA.
DR EMBL; M85036; AAA41241.2; -; mRNA.
DR PIR; C40170; C40170.
DR RefSeq; NP_001106213.1; NM_001112742.1.
DR RefSeq; NP_116785.2; NM_032990.2.
DR PDB; 3DLN; X-ray; 1.91 A; A=416-530, A=658-799.
DR PDB; 3DP4; X-ray; 2.11 A; A=416-530, A=658-799.
DR PDB; 3LSW; X-ray; 1.75 A; A=417-530.
DR PDB; 3LSX; X-ray; 2.01 A; A=417-530.
DR PDB; 3M3F; X-ray; 2.50 A; A=417-530, A=658-799.
DR PDB; 3M3K; X-ray; 1.79 A; A/C/E=417-530, A/C/E=658-799.
DR PDB; 3O21; X-ray; 2.20 A; A/B/C/D=23-403.
DR PDB; 3P3W; X-ray; 4.20 A; A/B/C/D=23-403.
DR PDB; 3RT6; X-ray; 2.84 A; B=417-530, B=658-799.
DR PDB; 3RT8; X-ray; 2.43 A; A=417-530, A=658-799.
DR PDB; 4F1Y; X-ray; 1.79 A; A/C=417-530, A/C=658-799.
DR PDB; 4F22; X-ray; 2.06 A; A=417-530, A=658-799.
DR PDB; 4F29; X-ray; 1.75 A; A=417-530, A=658-799.
DR PDB; 4F2O; X-ray; 1.91 A; A=417-530, A=658-799.
DR PDB; 4F2Q; X-ray; 2.20 A; A=417-530, A=658-799.
DR PDB; 4F31; X-ray; 2.29 A; B/D=417-530, B/D=658-799.
DR PDB; 4F39; X-ray; 1.83 A; A=417-530, A=658-799.
DR PDB; 4F3B; X-ray; 1.82 A; A=417-530, A=658-799.
DR PDB; 4F3G; X-ray; 2.06 A; A=417-530, A=658-799.
DR PDB; 5FWY; X-ray; 2.12 A; B/D=23-403.
DR PDB; 5IDE; EM; 8.25 A; B/D=24-888.
DR PDB; 5IDF; EM; 10.31 A; B/D=24-888.
DR PDB; 6FLR; X-ray; 2.51 A; A/B=23-403.
DR PDB; 6FPJ; X-ray; 1.96 A; A/B/C=23-403.
DR PDB; 6NJM; EM; 6.50 A; A/C=1-888.
DR PDB; 6NJN; EM; 6.50 A; C=1-888.
DR PDBsum; 3DLN; -.
DR PDBsum; 3DP4; -.
DR PDBsum; 3LSW; -.
DR PDBsum; 3LSX; -.
DR PDBsum; 3M3F; -.
DR PDBsum; 3M3K; -.
DR PDBsum; 3O21; -.
DR PDBsum; 3P3W; -.
DR PDBsum; 3RT6; -.
DR PDBsum; 3RT8; -.
DR PDBsum; 4F1Y; -.
DR PDBsum; 4F22; -.
DR PDBsum; 4F29; -.
DR PDBsum; 4F2O; -.
DR PDBsum; 4F2Q; -.
DR PDBsum; 4F31; -.
DR PDBsum; 4F39; -.
DR PDBsum; 4F3B; -.
DR PDBsum; 4F3G; -.
DR PDBsum; 5FWY; -.
DR PDBsum; 5IDE; -.
DR PDBsum; 5IDF; -.
DR PDBsum; 6FLR; -.
DR PDBsum; 6FPJ; -.
DR PDBsum; 6NJM; -.
DR PDBsum; 6NJN; -.
DR AlphaFoldDB; P19492; -.
DR SMR; P19492; -.
DR BioGRID; 248251; 2.
DR CORUM; P19492; -.
DR DIP; DIP-30954N; -.
DR IntAct; P19492; 10.
DR MINT; P19492; -.
DR STRING; 10116.ENSRNOP00000010367; -.
DR BindingDB; P19492; -.
DR ChEMBL; CHEMBL3504; -.
DR DrugCentral; P19492; -.
DR GlyGen; P19492; 5 sites, 5 N-linked glycans (1 site).
DR iPTMnet; P19492; -.
DR PhosphoSitePlus; P19492; -.
DR SwissPalm; P19492; -.
DR PaxDb; P19492; -.
DR PRIDE; P19492; -.
DR GeneID; 29628; -.
DR KEGG; rno:29628; -.
DR UCSC; RGD:70958; rat. [P19492-1]
DR CTD; 2892; -.
DR RGD; 70958; Gria3.
DR eggNOG; KOG1054; Eukaryota.
DR InParanoid; P19492; -.
DR PhylomeDB; P19492; -.
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; P19492; -.
DR PRO; PR:P19492; -.
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:0032279; C:asymmetric synapse; IDA:RGD.
DR GO; GO:0030425; C:dendrite; IDA:RGD.
DR GO; GO:0043198; C:dendritic shaft; IDA:RGD.
DR GO; GO:0043197; C:dendritic spine; IDA:UniProtKB.
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:0099055; C:integral component of postsynaptic membrane; IDA:SynGO.
DR GO; GO:0099056; C:integral component of presynaptic membrane; IDA:SynGO.
DR GO; GO:0008328; C:ionotropic glutamate receptor complex; TAS:UniProtKB.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0098688; C:parallel fiber to Purkinje cell synapse; ISO:RGD.
DR GO; GO:0043204; C:perikaryon; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0014069; C:postsynaptic density; IDA:UniProtKB.
DR GO; GO:0045211; C:postsynaptic membrane; ISO:RGD.
DR GO; GO:0032991; C:protein-containing complex; IPI:UniProtKB.
DR GO; GO:0043083; C:synaptic cleft; IDA:RGD.
DR GO; GO:0043195; C:terminal bouton; IDA:RGD.
DR GO; GO:0004971; F:AMPA glutamate receptor activity; IDA:RGD.
DR GO; GO:0001540; F:amyloid-beta binding; IPI:ARUK-UCL.
DR GO; GO:0004970; F:ionotropic glutamate receptor activity; IDA:RGD.
DR GO; GO:0015276; F:ligand-gated ion channel activity; IBA:GO_Central.
DR GO; GO:0030165; F:PDZ domain binding; IPI:UniProtKB.
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:0001919; P:regulation of receptor recycling; IMP:UniProtKB.
DR GO; GO:0060992; P:response to fungicide; IEP:RGD.
DR GO; GO:0010226; P:response to lithium ion; IEP:UniProtKB.
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; Disulfide bond;
KW Glycoprotein; Ion channel; Ion transport; Ligand-gated ion channel;
KW Lipoprotein; Membrane; Palmitate; Phosphoprotein;
KW Postsynaptic cell membrane; Receptor; Reference proteome; Signal; Synapse;
KW Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..888
FT /note="Glutamate receptor 3"
FT /id="PRO_0000011537"
FT TOPO_DOM 23..546
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 547..567
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 568..596
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT INTRAMEM 597..612
FT /note="Helical; Pore-forming"
FT /evidence="ECO:0000250"
FT INTRAMEM 613..615
FT /evidence="ECO:0000250"
FT TOPO_DOM 616..621
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 622..642
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 643..817
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 818..838
FT /note="Helical; Name=M4"
FT /evidence="ECO:0000250"
FT TOPO_DOM 839..888
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT BINDING 474
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000269|PubMed:19003990,
FT ECO:0000269|PubMed:20199107"
FT BINDING 502..504
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT BINDING 509
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000269|PubMed:19003990,
FT ECO:0000269|PubMed:20199107"
FT BINDING 680..681
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT BINDING 731
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000269|PubMed:19003990,
FT ECO:0000269|PubMed:20199107"
FT MOD_RES 871
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z2W9"
FT MOD_RES 881
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z2W9"
FT LIPID 615
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 841
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT CARBOHYD 57
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 260
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:21317871,
FT ECO:0007744|PubMed:24090084"
FT CARBOHYD 374
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:21317871"
FT CARBOHYD 409
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 416
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 85..334
FT DISULFID 744..799
FT VAR_SEQ 770..771
FT /note="NA -> TP (in isoform Flip)"
FT /evidence="ECO:0000305"
FT /id="VSP_000119"
FT VAR_SEQ 780
FT /note="N -> S (in isoform Flip)"
FT /evidence="ECO:0000305"
FT /id="VSP_000120"
FT VAR_SEQ 784
FT /note="L -> I (in isoform Flip)"
FT /evidence="ECO:0000305"
FT /id="VSP_000121"
FT VAR_SEQ 801..805
FT /note="SGGGD -> AKDSG (in isoform Flip)"
FT /evidence="ECO:0000305"
FT /id="VSP_000122"
FT CONFLICT 517..518
FT /note="KP -> NA (in Ref. 2)"
FT /evidence="ECO:0000305"
FT STRAND 26..35
FT /evidence="ECO:0007829|PDB:6FPJ"
FT HELIX 39..53
FT /evidence="ECO:0007829|PDB:6FPJ"
FT TURN 58..60
FT /evidence="ECO:0007829|PDB:6FPJ"
FT STRAND 62..73
FT /evidence="ECO:0007829|PDB:6FPJ"
FT HELIX 77..90
FT /evidence="ECO:0007829|PDB:6FPJ"
FT STRAND 95..97
FT /evidence="ECO:0007829|PDB:6FPJ"
FT TURN 101..103
FT /evidence="ECO:0007829|PDB:6FPJ"
FT HELIX 104..113
FT /evidence="ECO:0007829|PDB:6FPJ"
FT STRAND 118..120
FT /evidence="ECO:0007829|PDB:6FPJ"
FT STRAND 130..134
FT /evidence="ECO:0007829|PDB:6FPJ"
FT HELIX 140..149
FT /evidence="ECO:0007829|PDB:6FPJ"
FT STRAND 154..159
FT /evidence="ECO:0007829|PDB:6FPJ"
FT HELIX 166..178
FT /evidence="ECO:0007829|PDB:6FPJ"
FT STRAND 181..186
FT /evidence="ECO:0007829|PDB:6FPJ"
FT HELIX 193..205
FT /evidence="ECO:0007829|PDB:6FPJ"
FT STRAND 210..215
FT /evidence="ECO:0007829|PDB:6FPJ"
FT HELIX 217..230
FT /evidence="ECO:0007829|PDB:6FPJ"
FT STRAND 232..234
FT /evidence="ECO:0007829|PDB:6FPJ"
FT STRAND 238..241
FT /evidence="ECO:0007829|PDB:6FPJ"
FT HELIX 246..248
FT /evidence="ECO:0007829|PDB:6FPJ"
FT HELIX 252..256
FT /evidence="ECO:0007829|PDB:6FPJ"
FT STRAND 260..266
FT /evidence="ECO:0007829|PDB:6FPJ"
FT HELIX 272..281
FT /evidence="ECO:0007829|PDB:6FPJ"
FT TURN 286..288
FT /evidence="ECO:0007829|PDB:6FPJ"
FT STRAND 292..295
FT /evidence="ECO:0007829|PDB:6FPJ"
FT HELIX 299..320
FT /evidence="ECO:0007829|PDB:6FPJ"
FT STRAND 327..329
FT /evidence="ECO:0007829|PDB:5FWY"
FT STRAND 336..338
FT /evidence="ECO:0007829|PDB:3O21"
FT HELIX 345..353
FT /evidence="ECO:0007829|PDB:6FPJ"
FT STRAND 357..359
FT /evidence="ECO:0007829|PDB:6FPJ"
FT STRAND 362..366
FT /evidence="ECO:0007829|PDB:6FPJ"
FT STRAND 370..374
FT /evidence="ECO:0007829|PDB:6FPJ"
FT STRAND 377..383
FT /evidence="ECO:0007829|PDB:6FPJ"
FT STRAND 386..394
FT /evidence="ECO:0007829|PDB:6FPJ"
FT TURN 395..397
FT /evidence="ECO:0007829|PDB:6FPJ"
FT STRAND 398..401
FT /evidence="ECO:0007829|PDB:6FPJ"
FT STRAND 418..423
FT /evidence="ECO:0007829|PDB:4F29"
FT TURN 427..429
FT /evidence="ECO:0007829|PDB:4F29"
FT STRAND 430..432
FT /evidence="ECO:0007829|PDB:4F29"
FT HELIX 436..438
FT /evidence="ECO:0007829|PDB:4F29"
FT HELIX 441..444
FT /evidence="ECO:0007829|PDB:4F29"
FT STRAND 445..447
FT /evidence="ECO:0007829|PDB:4F29"
FT HELIX 448..460
FT /evidence="ECO:0007829|PDB:4F29"
FT STRAND 463..468
FT /evidence="ECO:0007829|PDB:4F29"
FT TURN 479..481
FT /evidence="ECO:0007829|PDB:4F29"
FT HELIX 486..492
FT /evidence="ECO:0007829|PDB:4F29"
FT STRAND 497..499
FT /evidence="ECO:0007829|PDB:4F29"
FT HELIX 507..510
FT /evidence="ECO:0007829|PDB:4F29"
FT STRAND 513..515
FT /evidence="ECO:0007829|PDB:4F29"
FT STRAND 519..522
FT /evidence="ECO:0007829|PDB:4F29"
FT STRAND 524..529
FT /evidence="ECO:0007829|PDB:4F29"
FT HELIX 662..666
FT /evidence="ECO:0007829|PDB:4F29"
FT STRAND 669..676
FT /evidence="ECO:0007829|PDB:4F29"
FT HELIX 680..687
FT /evidence="ECO:0007829|PDB:4F29"
FT HELIX 691..702
FT /evidence="ECO:0007829|PDB:4F29"
FT TURN 704..706
FT /evidence="ECO:0007829|PDB:4F31"
FT STRAND 708..711
FT /evidence="ECO:0007829|PDB:4F29"
FT HELIX 712..721
FT /evidence="ECO:0007829|PDB:4F29"
FT TURN 722..724
FT /evidence="ECO:0007829|PDB:4F29"
FT STRAND 725..731
FT /evidence="ECO:0007829|PDB:4F29"
FT HELIX 732..739
FT /evidence="ECO:0007829|PDB:4F29"
FT STRAND 746..750
FT /evidence="ECO:0007829|PDB:4F29"
FT STRAND 756..758
FT /evidence="ECO:0007829|PDB:4F29"
FT STRAND 761..763
FT /evidence="ECO:0007829|PDB:4F29"
FT HELIX 769..781
FT /evidence="ECO:0007829|PDB:4F29"
FT HELIX 784..793
FT /evidence="ECO:0007829|PDB:4F29"
FT TURN 794..796
FT /evidence="ECO:0007829|PDB:4F29"
SQ SEQUENCE 888 AA; 100373 MW; 2981616375661703 CRC64;
MGQSVLRAVF FLVLGLLGHS HGGFPNTISI GGLFMRNTVQ EHSAFRFAVQ LYNTNQNTTE
KPFHLNYHVD HLDSSNSFSV TNAFCSQFSR GVYAIFGFYD QMSMNTLTSF CGALHTSFVT
PSFPTDADVQ FVIQMRPALK GAILSLLSYY KWEKFVYLYD TERGFSVLQA IMEAAVQNNW
QVTARSVGNI KDVQEFRRII EEMDRRQEKR YLIDCEVERI NTILEQVVIL GKHSRGYHYM
LANLGFTDIL LERVMHGGAN ITGFQIVNNE NPMVQQFIQR WVRLDEREFP EAKNAPLKYT
SALTHDAILV IAEAFRYLRR QRVDVSRRGS AGDCLANPAV PWSQGIDIER ALKMVQVQGM
TGNIQFDTYG RRTNYTIDVY EMKVSGSRKA GYWNEYERFV PFSDQQISND SSSSENRTIV
VTTILESPYV MYKKNHEQLE GNERYEGYCV DLAYEIAKHV RIKYKLSIVG DGKYGARDPE
TKIWNGMVGE LVYGRADIAV APLTITLVRE EVIDFSKPFM SLGISIMIKK PQKSKPGVFS
FLDPLAYEIW MCIVFAYIGV SVVLFLVSRF SPYEWHLEDN NEEPRDPQSP PDPPNEFGIF
NSLWFSLGAF MQQGCDISPR SLSGRIVGGV WWFFTLIIIS SYTANLAAFL TVERMVSPIE
SAEDLAKQTE IAYGTLDSGS TKEFFRRSKI AVYEKMWSYM KSAEPSVFTK TTADGVARVR
KSKGKFAFLL ESTMNEYIEQ RKPCDTMKVG GNLDSKGYGV ATPKGSALGN AVNLAVLKLN
EQGLLDKLKN KWWYDKGECG SGGGDSKDKT SALSLSNVAG VFYILVGGLG LAMMVALIEF
CYKSRAESKR MKLTKNTQNF KPAPATNTQN YATYREGYNV YGTESVKI
