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Glutamate receptor ionotropic, kainate 2 (GluK2) (Glutamate receptor 6) (GluR-6) (GluR6)

 GRIK2_RAT               Reviewed;         908 AA.
P42260;
01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
15-JUL-1998, sequence version 2.
31-JAN-2018, entry version 164.
RecName: Full=Glutamate receptor ionotropic, kainate 2;
Short=GluK2;
AltName: Full=Glutamate receptor 6;
Short=GluR-6;
Short=GluR6;
Flags: Precursor;
Name=Grik2; Synonyms=Glur6;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Sprague-Dawley; TISSUE=Brain;
PubMed=1648177; DOI=10.1038/351745a0;
Egebjerg J., Bettler B., Hermans-Borgmeyer I., Heinemann S.F.;
"Cloning of a cDNA for a glutamate receptor subunit activated by
kainate but not AMPA.";
Nature 351:745-748(1991).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Brain;
PubMed=1322826; DOI=10.1016/0014-5793(92)80753-4;
Lomeli H., Wisden W., Koehler M., Keinaenen K., Sommer B.,
Seeburg P.H.;
"High-affinity kainate and domoate receptors in rat brain.";
FEBS Lett. 307:139-143(1992).
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 560-585, AND RNA EDITING.
TISSUE=Brain;
PubMed=7681676; DOI=10.1016/0896-6273(93)90336-P;
Koehler M., Burnashev N., Sakmann B., Seeburg P.H.;
"Determinants of Ca2+ permeability in both TM1 and TM2 of high
affinity kainate receptor channels: diversity by RNA editing.";
Neuron 10:491-500(1993).
[4]
INTERACTION WITH DLG4.
PubMed=11744724; DOI=10.1074/jbc.M109453200;
Piserchio A., Pellegrini M., Mehta S., Blackman S.M., Garcia E.P.,
Marshall J., Mierke D.F.;
"The PDZ1 domain of SAP90. Characterization of structure and
binding.";
J. Biol. Chem. 277:6967-6973(2002).
[5]
INTERACTION WITH KLHL17, UBIQUITINATION, AND MUTAGENESIS OF VAL-883
AND ILE-884.
PubMed=17062563; DOI=10.1074/jbc.M608194200;
Salinas G.D., Blair L.A., Needleman L.A., Gonzales J.D., Chen Y.,
Li M., Singer J.D., Marshall J.;
"Actinfilin is a Cul3 substrate adaptor, linking GluR6 kainate
receptor subunits to the ubiquitin-proteasome pathway.";
J. Biol. Chem. 281:40164-40173(2006).
[6]
SUMOYLATION AT LYS-886, FUNCTION, SUBCELLULAR LOCATION, AND
MUTAGENESIS OF LYS-886.
PubMed=17486098; DOI=10.1038/nature05736;
Martin S., Nishimune A., Mellor J.R., Henley J.M.;
"SUMOylation regulates kainate-receptor-mediated synaptic
transmission.";
Nature 447:321-325(2007).
[7]
INTERACTION WITH NETO2.
PubMed=19217376; DOI=10.1016/j.neuron.2008.12.014;
Zhang W., St-Gelais F., Grabner C.P., Trinidad J.C., Sumioka A.,
Morimoto-Tomita M., Kim K.S., Straub C., Burlingame A.L., Howe J.R.,
Tomita S.;
"A transmembrane accessory subunit that modulates kainate-type
glutamate receptors.";
Neuron 61:385-396(2009).
[8]
X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 429-806 IN COMPLEXES WITH
GLUTAMATE; KAINATE; METHYLGLUTAMATE AND QUISQUALATE.
PubMed=15721240; DOI=10.1016/j.neuron.2005.01.031;
Mayer M.L.;
"Crystal structures of the GluR5 and GluR6 ligand binding cores:
molecular mechanisms underlying kainate receptor selectivity.";
Neuron 45:539-552(2005).
[9]
X-RAY CRYSTALLOGRAPHY (3.11 ANGSTROMS) OF 419-819 IN COMPLEX WITH
DOMOATE, SUBUNIT, AND GLYCOSYLATION AT ASN-423 AND ASN-751.
PubMed=15677325; DOI=10.1073/pnas.0409573102;
Nanao M.H., Green T., Stern-Bach Y., Heinemann S.F., Choe S.;
"Structure of the kainate receptor subunit GluR6 agonist-binding
domain complexed with domoic acid.";
Proc. Natl. Acad. Sci. U.S.A. 102:1708-1713(2005).
[10]
X-RAY CRYSTALLOGRAPHY (1.96 ANGSTROMS) OF 663-806, FUNCTION, AND
SUBUNIT.
PubMed=17115050; DOI=10.1038/nsmb1178;
Weston M.C., Schuck P., Ghosal A., Rosenmund C., Mayer M.L.;
"Conformational restriction blocks glutamate receptor
desensitization.";
Nat. Struct. Mol. Biol. 13:1120-1127(2006).
[11]
X-RAY CRYSTALLOGRAPHY (2.91 ANGSTROMS) OF 32-420 IN COMPLEX WITH
GRIK5, DISULFIDE BONDS, GLYCOSYLATION AT ASN-67; ASN-378 AND ASN-412,
AND SUBUNIT.
PubMed=21791290; DOI=10.1016/j.neuron.2011.05.038;
Kumar J., Schuck P., Mayer M.L.;
"Structure and assembly mechanism for heteromeric kainate receptors.";
Neuron 71:319-331(2011).
-!- FUNCTION: Ionotropic glutamate receptor. L-glutamate acts as an
excitatory neurotransmitter at many synapses in the central
nervous system. Binding of the excitatory neurotransmitter L-
glutamate induces a conformation change, leading to the opening of
the cation channel, and thereby converts the chemical signal to an
electrical impulse. The receptor then desensitizes rapidly and
enters a transient inactive state, characterized by the presence
of bound agonist (PubMed:17115050, PubMed:17486098). May be
involved in the transmission of light information from the retina
to the hypothalamus. Modulates cell surface expression of NETO2
(By similarity). {ECO:0000250|UniProtKB:P39087,
ECO:0000269|PubMed:17115050, ECO:0000269|PubMed:17486098}.
-!- SUBUNIT: Homotetramer or heterotetramer of pore-forming glutamate
receptor subunits. Tetramers may be formed by the dimerization of
dimers. Assembles into a kainate-gated homomeric channel that does
not bind AMPA (By similarity). GRIK2 associated to GRIK5 forms
functional channels that can be gated by AMPA. Interacts with
DLG4. Interacts with NETO2. Interacts (via C-terminus) with KLHL17
(via kelch repeats); the interaction targets GRIK2 for degradation
via ubiquitin-proteasome pathway. {ECO:0000250,
ECO:0000269|PubMed:11744724, ECO:0000269|PubMed:15677325,
ECO:0000269|PubMed:17062563, ECO:0000269|PubMed:17115050,
ECO:0000269|PubMed:19217376, ECO:0000269|PubMed:21791290}.
-!- INTERACTION:
Self; NbExp=10; IntAct=EBI-7809795, EBI-7809795;
Q66HA1:Map3k11; NbExp=2; IntAct=EBI-7809795, EBI-4279420;
O70260:Pias3; NbExp=3; IntAct=EBI-7809795, EBI-7974636;
Q5I0H3:Sumo1; NbExp=4; IntAct=EBI-7809795, EBI-7253100;
P63281:Ube2i; NbExp=3; IntAct=EBI-7809795, EBI-7974723;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17486098};
Multi-pass membrane protein {ECO:0000269|PubMed:17486098}. Cell
junction, synapse, postsynaptic cell membrane
{ECO:0000269|PubMed:17486098}; Multi-pass membrane protein
{ECO:0000269|PubMed:17486098}.
-!- TISSUE SPECIFICITY: Highest expression is found in the olfactory
lobe, piriform cortex, dentate gyrus, hippocampus, granular cell
layer of the cerebellum, and in caudate-putamen.
-!- PTM: Sumoylation mediates kainate receptor-mediated endocytosis
and regulates synaptic transmission. Sumoylation is enhanced by
PIAS3 and desumoylated by SENP1. {ECO:0000269|PubMed:17486098}.
-!- PTM: Ubiquitinated. Ubiquitination regulates the GRIK2 levels at
the synapse by leading kainate receptor degradation through
proteasome. {ECO:0000269|PubMed:17062563}.
-!- PTM: Phosphorylated by PKC at Ser-868 upon agonist activation,
this directly enhance sumoylation. {ECO:0000250}.
-!- RNA EDITING: Modified_positions=567 {ECO:0000269|PubMed:7681676},
571 {ECO:0000269|PubMed:7681676}, 621
{ECO:0000269|PubMed:7681676}; Note=Partially edited. The presence
of Gln at position 621 (non-edited) determines channels with low
calcium permeability, whereas an arginine residue (edited)
determines a higher calcium permeability especially if the
preceding sites are fully edited. This receptor is nearly
completely edited in all gray matter structures (90% of the
receptors).;
-!- MISCELLANEOUS: The postsynaptic actions of Glu are mediated by a
variety of receptors that are named according to their selective
agonists. This receptor binds domoate > kainate > quisqualate >
glutamate. It does not bind AMPA without coexpression with GRIK5.
-!- SIMILARITY: Belongs to the glutamate-gated ion channel (TC
1.A.10.1) family. GRIK2 subfamily. {ECO:0000305}.
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EMBL; Z11548; CAA77647.1; -; mRNA.
EMBL; Z11715; CAA77778.1; -; mRNA.
PIR; S19098; S19098.
RefSeq; NP_062182.1; NM_019309.2.
UniGene; Rn.87696; -.
PDB; 1S50; X-ray; 1.65 A; A=428-806.
PDB; 1S7Y; X-ray; 1.75 A; A/B=429-544, A/B=667-806.
PDB; 1S9T; X-ray; 1.80 A; A/B=429-544, A/B=667-806.
PDB; 1SD3; X-ray; 1.80 A; A/B=429-544, A/B=667-806.
PDB; 1TT1; X-ray; 1.93 A; A/B=429-806.
PDB; 1YAE; X-ray; 3.11 A; A/B/C/D/E/F=419-557, A/B/C/D/E/F=662-819.
PDB; 2I0B; X-ray; 1.96 A; A/B/C=429-544, A/B/C=667-806.
PDB; 2I0C; X-ray; 2.25 A; A/B=429-544, A/B=667-806.
PDB; 2XXR; X-ray; 1.60 A; A/B=429-544, A/B=667-806.
PDB; 2XXT; X-ray; 1.90 A; A/B=667-806.
PDB; 2XXU; X-ray; 1.50 A; A/B=667-806.
PDB; 2XXV; X-ray; 1.70 A; A/B=667-806.
PDB; 2XXW; X-ray; 2.30 A; A/B=667-806.
PDB; 2XXX; X-ray; 2.10 A; A/B/C/D=667-806.
PDB; 2XXY; X-ray; 3.00 A; A/B/C/D=667-806.
PDB; 3G3F; X-ray; 1.38 A; A/B=429-544, A/B=667-806.
PDB; 3G3G; X-ray; 1.30 A; A/B=429-544, A/B=667-806.
PDB; 3G3H; X-ray; 1.50 A; A/B=429-544, A/B=667-806.
PDB; 3G3I; X-ray; 1.37 A; A/B=429-544, A/B=667-806.
PDB; 3G3J; X-ray; 1.32 A; A/B=429-544, A/B=667-806.
PDB; 3G3K; X-ray; 1.24 A; A/B=429-544, A/B=667-806.
PDB; 3H6G; X-ray; 2.70 A; A/B=32-420.
PDB; 3H6H; X-ray; 2.90 A; A/B=32-420.
PDB; 3QLT; X-ray; 2.99 A; A/B=32-420.
PDB; 3QLU; X-ray; 2.91 A; C/D=32-420.
PDB; 3QLV; X-ray; 3.94 A; C/D/F/H/J=32-420.
PDB; 4BDL; X-ray; 1.75 A; A/B=429-544, A/B=667-806.
PDB; 4BDM; X-ray; 3.40 A; A/B/C/D=429-544, A/B/C/D=667-806.
PDB; 4BDN; X-ray; 2.50 A; A/B/C/D=429-544, A/B/C/D=667-806.
PDB; 4BDO; X-ray; 2.55 A; A/B/C/D=429-544, A/B/C/D=667-806.
PDB; 4BDQ; X-ray; 1.90 A; A/B=429-544, A/B=667-806.
PDB; 4BDR; X-ray; 1.65 A; A/B=429-544, A/B=667-806.
PDB; 4H8I; X-ray; 2.00 A; A/B=429-544, A/B=667-806.
PDB; 4UQQ; EM; 7.60 A; A/B/C/D=32-908.
PDB; 5CMK; X-ray; 1.80 A; A/B=429-544, A/B=667-806.
PDB; 5CMM; X-ray; 1.27 A; A=429-544.
PDB; 5KUF; EM; 3.80 A; A/B/C/D=32-908.
PDB; 5KUH; EM; 11.60 A; A/B/C/D=32-544, A/B/C/D=667-908.
PDBsum; 1S50; -.
PDBsum; 1S7Y; -.
PDBsum; 1S9T; -.
PDBsum; 1SD3; -.
PDBsum; 1TT1; -.
PDBsum; 1YAE; -.
PDBsum; 2I0B; -.
PDBsum; 2I0C; -.
PDBsum; 2XXR; -.
PDBsum; 2XXT; -.
PDBsum; 2XXU; -.
PDBsum; 2XXV; -.
PDBsum; 2XXW; -.
PDBsum; 2XXX; -.
PDBsum; 2XXY; -.
PDBsum; 3G3F; -.
PDBsum; 3G3G; -.
PDBsum; 3G3H; -.
PDBsum; 3G3I; -.
PDBsum; 3G3J; -.
PDBsum; 3G3K; -.
PDBsum; 3H6G; -.
PDBsum; 3H6H; -.
PDBsum; 3QLT; -.
PDBsum; 3QLU; -.
PDBsum; 3QLV; -.
PDBsum; 4BDL; -.
PDBsum; 4BDM; -.
PDBsum; 4BDN; -.
PDBsum; 4BDO; -.
PDBsum; 4BDQ; -.
PDBsum; 4BDR; -.
PDBsum; 4H8I; -.
PDBsum; 4UQQ; -.
PDBsum; 5CMK; -.
PDBsum; 5CMM; -.
PDBsum; 5KUF; -.
PDBsum; 5KUH; -.
ProteinModelPortal; P42260; -.
SMR; P42260; -.
BioGrid; 248480; 6.
DIP; DIP-29256N; -.
ELM; P42260; -.
IntAct; P42260; 5.
MINT; MINT-8359884; -.
STRING; 10116.ENSRNOP00000033070; -.
BindingDB; P42260; -.
ChEMBL; CHEMBL3607; -.
GuidetoPHARMACOLOGY; 451; -.
TCDB; 1.A.10.1.11; the glutamate-gated ion channel (gic) family of neurotransmitter receptors.
iPTMnet; P42260; -.
PhosphoSitePlus; P42260; -.
PaxDb; P42260; -.
PRIDE; P42260; -.
Ensembl; ENSRNOT00000076234; ENSRNOP00000068172; ENSRNOG00000000368.
GeneID; 54257; -.
KEGG; rno:54257; -.
UCSC; RGD:2733; rat.
CTD; 2898; -.
RGD; 2733; Grik2.
eggNOG; KOG1054; Eukaryota.
eggNOG; ENOG410XPSH; LUCA.
GeneTree; ENSGT00760000118920; -.
HOGENOM; HOG000234371; -.
HOVERGEN; HBG051839; -.
InParanoid; P42260; -.
KO; K05202; -.
OMA; DSDIQHS; -.
OrthoDB; EOG091G02LN; -.
PhylomeDB; P42260; -.
Reactome; R-RNO-451307; Activation of Na-permeable kainate receptors.
Reactome; R-RNO-451308; Activation of Ca-permeable Kainate Receptor.
EvolutionaryTrace; P42260; -.
PRO; PR:P42260; -.
Proteomes; UP000002494; Chromosome 20.
Bgee; ENSRNOG00000000368; -.
ExpressionAtlas; P42260; baseline and differential.
Genevisible; P42260; RN.
GO; GO:0030424; C:axon; IDA:RGD.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0030425; C:dendrite; IDA:UniProtKB.
GO; GO:0032839; C:dendrite cytoplasm; IDA:RGD.
GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
GO; GO:0008328; C:ionotropic glutamate receptor complex; IDA:UniProtKB.
GO; GO:0032983; C:kainate selective glutamate receptor complex; ISO:RGD.
GO; GO:0016020; C:membrane; ISO:RGD.
GO; GO:0043025; C:neuronal cell body; ISO:RGD.
GO; GO:0043204; C:perikaryon; IDA:RGD.
GO; GO:0014069; C:postsynaptic density; ISO:RGD.
GO; GO:0045211; C:postsynaptic membrane; ISO:RGD.
GO; GO:0042734; C:presynaptic membrane; ISO:RGD.
GO; GO:0045202; C:synapse; IDA:RGD.
GO; GO:0043195; C:terminal bouton; IDA:RGD.
GO; GO:0005234; F:extracellularly glutamate-gated ion channel activity; ISS:UniProtKB.
GO; GO:0008066; F:glutamate receptor activity; IDA:UniProtKB.
GO; GO:0042802; F:identical protein binding; IDA:RGD.
GO; GO:0004970; F:ionotropic glutamate receptor activity; ISO:RGD.
GO; GO:0015277; F:kainate selective glutamate receptor activity; IDA:RGD.
GO; GO:0030165; F:PDZ domain binding; IPI:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IDA:RGD.
GO; GO:0031624; F:ubiquitin conjugating enzyme binding; IPI:RGD.
GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:RGD.
GO; GO:0001662; P:behavioral fear response; ISO:RGD.
GO; GO:0006874; P:cellular calcium ion homeostasis; ISO:RGD.
GO; GO:0007268; P:chemical synaptic transmission; IMP:RGD.
GO; GO:0060079; P:excitatory postsynaptic potential; ISO:RGD.
GO; GO:0060080; P:inhibitory postsynaptic potential; ISO:RGD.
GO; GO:0006886; P:intracellular protein transport; ISO:RGD.
GO; GO:0050804; P:modulation of chemical synaptic transmission; ISO:RGD.
GO; GO:0043524; P:negative regulation of neuron apoptotic process; ISO:RGD.
GO; GO:0051967; P:negative regulation of synaptic transmission, glutamatergic; IDA:UniProtKB.
GO; GO:0051402; P:neuron apoptotic process; IMP:UniProtKB.
GO; GO:0019228; P:neuronal action potential; ISO:RGD.
GO; GO:0043525; P:positive regulation of neuron apoptotic process; IMP:RGD.
GO; GO:0050806; P:positive regulation of synaptic transmission; ISO:RGD.
GO; GO:0043113; P:receptor clustering; IDA:UniProtKB.
GO; GO:0046328; P:regulation of JNK cascade; IMP:UniProtKB.
GO; GO:0048169; P:regulation of long-term neuronal synaptic plasticity; ISO:RGD.
GO; GO:0042391; P:regulation of membrane potential; ISO:RGD.
GO; GO:0048172; P:regulation of short-term neuronal synaptic plasticity; ISO:RGD.
GO; GO:0035249; P:synaptic transmission, glutamatergic; ISO:RGD.
InterPro; IPR001828; ANF_lig-bd_rcpt.
InterPro; IPR019594; Glu/Gly-bd.
InterPro; IPR001508; Iono_rcpt_met.
InterPro; IPR001320; Iontro_rcpt.
InterPro; IPR028082; Peripla_BP_I.
Pfam; PF01094; ANF_receptor; 1.
Pfam; PF00060; Lig_chan; 1.
Pfam; PF10613; Lig_chan-Glu_bd; 1.
PRINTS; PR00177; NMDARECEPTOR.
SMART; SM00918; Lig_chan-Glu_bd; 1.
SMART; SM00079; PBPe; 1.
SUPFAM; SSF53822; SSF53822; 1.
1: Evidence at protein level;
3D-structure; Cell junction; Cell membrane; Complete proteome;
Disulfide bond; Glycoprotein; Ion channel; Ion transport;
Isopeptide bond; Ligand-gated ion channel; Membrane; Phosphoprotein;
Postsynaptic cell membrane; Receptor; Reference proteome; RNA editing;
Signal; Synapse; Transmembrane; Transmembrane helix; Transport;
Ubl conjugation.
SIGNAL 1 31 {ECO:0000255}.
CHAIN 32 908 Glutamate receptor ionotropic, kainate 2.
/FTId=PRO_0000011546.
TOPO_DOM 32 561 Extracellular. {ECO:0000255}.
TRANSMEM 562 582 Helical. {ECO:0000255}.
TOPO_DOM 583 638 Cytoplasmic. {ECO:0000255}.
TRANSMEM 639 659 Helical. {ECO:0000255}.
TOPO_DOM 660 819 Extracellular. {ECO:0000255}.
TRANSMEM 820 840 Helical. {ECO:0000255}.
TOPO_DOM 841 908 Cytoplasmic. {ECO:0000255}.
REGION 516 518 Glutamate binding.
REGION 689 690 Glutamate binding.
BINDING 523 523 Glutamate.
BINDING 738 738 Glutamate.
MOD_RES 846 846 Phosphoserine; by PKC.
{ECO:0000250|UniProtKB:Q13002}.
MOD_RES 868 868 Phosphoserine; by PKC.
{ECO:0000250|UniProtKB:Q13002}.
CARBOHYD 67 67 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:21791290}.
CARBOHYD 73 73 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 275 275 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 378 378 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:21791290}.
CARBOHYD 412 412 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:21791290}.
CARBOHYD 423 423 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:15677325}.
CARBOHYD 430 430 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 546 546 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 751 751 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:15677325}.
DISULFID 96 347 {ECO:0000269|PubMed:21791290}.
CROSSLNK 886 886 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1).
{ECO:0000269|PubMed:17486098}.
VARIANT 567 567 I -> C (in RNA edited version).
VARIANT 571 571 Y -> C (in RNA edited version).
VARIANT 621 621 Q -> R (in RNA edited version).
MUTAGEN 883 883 V->A: Abolishes interaction with KLHL17.
Abolishes actinfilin-mediated
degradation.
{ECO:0000269|PubMed:17062563}.
MUTAGEN 884 884 I->A: Abolishes interaction with KLHL17.
Abolishes actinfilin-mediated
degradation.
{ECO:0000269|PubMed:17062563}.
MUTAGEN 886 886 K->R: Abolishes sumoylation. Loss of
kainate-mediated endocytosis.
{ECO:0000269|PubMed:17486098}.
STRAND 34 47 {ECO:0000244|PDB:3H6G}.
HELIX 52 66 {ECO:0000244|PDB:3H6G}.
STRAND 68 84 {ECO:0000244|PDB:3H6G}.
HELIX 88 101 {ECO:0000244|PDB:3H6G}.
HELIX 112 124 {ECO:0000244|PDB:3H6G}.
STRAND 129 131 {ECO:0000244|PDB:3H6G}.
STRAND 145 151 {ECO:0000244|PDB:3H6G}.
HELIX 153 166 {ECO:0000244|PDB:3H6G}.
STRAND 170 178 {ECO:0000244|PDB:3H6G}.
HELIX 180 184 {ECO:0000244|PDB:3H6G}.
HELIX 186 189 {ECO:0000244|PDB:3H6G}.
HELIX 191 193 {ECO:0000244|PDB:3H6G}.
STRAND 198 203 {ECO:0000244|PDB:3H6G}.
HELIX 208 211 {ECO:0000244|PDB:3H6G}.
HELIX 212 220 {ECO:0000244|PDB:3H6G}.
STRAND 225 230 {ECO:0000244|PDB:3H6G}.
HELIX 232 244 {ECO:0000244|PDB:3H6G}.
STRAND 249 251 {ECO:0000244|PDB:3QLT}.
STRAND 253 256 {ECO:0000244|PDB:3H6G}.
HELIX 261 263 {ECO:0000244|PDB:3H6G}.
TURN 267 271 {ECO:0000244|PDB:3H6G}.
STRAND 275 280 {ECO:0000244|PDB:3H6G}.
HELIX 287 298 {ECO:0000244|PDB:3H6G}.
STRAND 309 311 {ECO:0000244|PDB:3QLT}.
HELIX 318 335 {ECO:0000244|PDB:3H6G}.
STRAND 347 349 {ECO:0000244|PDB:3H6H}.
HELIX 351 357 {ECO:0000244|PDB:2XXU}.
HELIX 359 362 {ECO:0000244|PDB:2XXU}.
STRAND 364 366 {ECO:0000244|PDB:2XXU}.
HELIX 367 372 {ECO:0000244|PDB:2XXU}.
HELIX 374 377 {ECO:0000244|PDB:2XXU}.
STRAND 378 385 {ECO:0000244|PDB:2XXU}.
HELIX 386 393 {ECO:0000244|PDB:2XXU}.
STRAND 399 404 {ECO:0000244|PDB:2XXU}.
STRAND 409 411 {ECO:0000244|PDB:2XXU}.
HELIX 424 429 {ECO:0000244|PDB:2XXU}.
STRAND 433 437 {ECO:0000244|PDB:3G3K}.
TURN 441 443 {ECO:0000244|PDB:3G3K}.
STRAND 444 446 {ECO:0000244|PDB:3G3K}.
HELIX 448 451 {ECO:0000244|PDB:2XXU}.
HELIX 455 458 {ECO:0000244|PDB:3G3K}.
STRAND 459 461 {ECO:0000244|PDB:3G3K}.
HELIX 462 474 {ECO:0000244|PDB:3G3K}.
STRAND 478 482 {ECO:0000244|PDB:3G3K}.
TURN 493 495 {ECO:0000244|PDB:3G3K}.
HELIX 500 506 {ECO:0000244|PDB:3G3K}.
STRAND 511 513 {ECO:0000244|PDB:3G3K}.
HELIX 521 524 {ECO:0000244|PDB:3G3K}.
STRAND 527 529 {ECO:0000244|PDB:3G3K}.
STRAND 533 536 {ECO:0000244|PDB:3G3K}.
STRAND 538 544 {ECO:0000244|PDB:3G3K}.
HELIX 671 675 {ECO:0000244|PDB:3G3K}.
STRAND 678 685 {ECO:0000244|PDB:3G3K}.
HELIX 689 696 {ECO:0000244|PDB:3G3K}.
HELIX 700 711 {ECO:0000244|PDB:3G3K}.
HELIX 713 716 {ECO:0000244|PDB:3G3K}.
STRAND 717 720 {ECO:0000244|PDB:3G3K}.
HELIX 721 730 {ECO:0000244|PDB:3G3K}.
STRAND 731 738 {ECO:0000244|PDB:3G3K}.
HELIX 739 748 {ECO:0000244|PDB:3G3K}.
STRAND 752 757 {ECO:0000244|PDB:3G3K}.
STRAND 762 764 {ECO:0000244|PDB:3G3K}.
STRAND 767 769 {ECO:0000244|PDB:3G3K}.
HELIX 774 787 {ECO:0000244|PDB:3G3K}.
HELIX 790 799 {ECO:0000244|PDB:3G3K}.
SEQUENCE 908 AA; 102470 MW; 7F430E2D8B2E982B CRC64;
MKIISPVLSN LVFSRSIKVL LCLLWIGYSQ GTTHVLRFGG IFEYVESGPM GAEELAFRFA
VNTINRNRTL LPNTTLTYDT QKINLYDSFE ASKKACDQLS LGVAAIFGPS HSSSANAVQS
ICNALGVPHI QTRWKHQVSD NKDSFYVSLY PDFSSLSRAI LDLVQFFKWK TVTVVYDDST
GLIRLQELIK APSRYNLRLK IRQLPADTKD AKPLLKEMKR GKEFHVIFDC SHEMAAGILK
QALAMGMMTE YYHYIFTTLD LFALDVEPYR YSGVNMTGFR ILNTENTQVS SIIEKWSMER
LQAPPKPDSG LLDGFMTTDA ALMYDAVHVV SVAVQQFPQM TVSSLQCNRH KPWRFGTRFM
SLIKEAHWEG LTGRITFNKT NGLRTDFDLD VISLKEEGLE KIGTWDPASG LNMTESQKGK
PANITDSLSN RSLIVTTILE EPYVLFKKSD KPLYGNDRFE GYCIDLLREL STILGFTYEI
RLVEDGKYGA QDDVNGQWNG MVRELIDHKA DLAVAPLAIT YVREKVIDFS KPFMTLGISI
LYRKPNGTNP GVFSFLNPLS PDIWMYILLA YLGVSCVLFV IARFSPYEWY NPHPCNPDSD
VVENNFTLLN SFWFGVGALM QQGSELMPKA LSTRIVGGIW WFFTLIIISS YTANLAAFLT
VERMESPIDS ADDLAKQTKI EYGAVEDGAT MTFFKKSKIS TYDKMWAFMS SRRQSVLVKS
NEEGIQRVLT SDYAFLMEST TIEFVTQRNC NLTQIGGLID SKGYGVGTPM GSPYRDKITI
AILQLQEEGK LHMMKEKWWR GNGCPEEESK EASALGVQNI GGIFIVLAAG LVLSVFVAVG
EFLYKSKKNA QLEKRSFCSA MVEELRMSLK CQRRLKHKPQ APVIVKTEEV INMHTFNDRR
LPGKETMA


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