GRIK2_MOUSE
ID GRIK2_MOUSE Reviewed; 908 AA.
AC P39087; Q60933;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 202.
DE RecName: Full=Glutamate receptor ionotropic, kainate 2;
DE Short=GluK2;
DE AltName: Full=Glutamate receptor 6;
DE Short=GluR-6;
DE Short=GluR6;
DE AltName: Full=Glutamate receptor beta-2;
DE Short=GluR beta-2;
DE Flags: Precursor;
GN Name=Grik2; Synonyms=Glur6;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM GLUR6-2).
RC STRAIN=BALB/cJ; TISSUE=Brain;
RX PubMed=8260617; DOI=10.1097/00001756-199309150-00014;
RA Gregor P., O'Hara B.F., Yang X., Uhl G.R.;
RT "Expression and novel subunit isoforms of glutamate receptor genes GluR5
RT and GluR6.";
RL NeuroReport 4:1343-1346(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-864 (ISOFORM GLUR6-2).
RX PubMed=1379666; DOI=10.1016/0169-328x(92)90023-5;
RA Morita T., Sakimura K., Kushiya E., Yamazaki M., Meguro H., Araki K.,
RA Abe T., Mori K.J., Mishina M.;
RT "Cloning and functional expression of a cDNA encoding the mouse beta 2
RT subunit of the kainate-selective glutamate receptor channel.";
RL Brain Res. Mol. Brain Res. 14:143-146(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 584-695, AND RNA EDITING OF POSITION
RP 621.
RC STRAIN=BALB/cJ;
RX PubMed=8700852; DOI=10.1073/pnas.93.5.1875;
RA Herb A., Higuchi M., Sprengel R., Seeburg P.H.;
RT "Q/R site editing in kainate receptor GluR5 and GluR6 pre-mRNAs requires
RT distant intronic sequences.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:1875-1880(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 560-585, AND RNA EDITING OF POSITIONS 567;
RP 571 AND 621.
RC TISSUE=Brain;
RX PubMed=7681676; DOI=10.1016/0896-6273(93)90336-p;
RA Koehler M., Burnashev N., Sakmann B., Seeburg P.H.;
RT "Determinants of Ca2+ permeability in both TM1 and TM2 of high affinity
RT kainate receptor channels: diversity by RNA editing.";
RL Neuron 10:491-500(1993).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 855-908.
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [7]
RP FUNCTION, AND INTERACTION WITH NETO2.
RX PubMed=19217376; DOI=10.1016/j.neuron.2008.12.014;
RA Zhang W., St-Gelais F., Grabner C.P., Trinidad J.C., Sumioka A.,
RA Morimoto-Tomita M., Kim K.S., Straub C., Burlingame A.L., Howe J.R.,
RA Tomita S.;
RT "A transmembrane accessory subunit that modulates kainate-type glutamate
RT receptors.";
RL Neuron 61:385-396(2009).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [9]
RP FUNCTION, ACTIVITY REGULATION, TISSUE SPECIFICITY, AND MUTAGENESIS OF
RP PRO-151; MET-620 AND GLN-622.
RX PubMed=31474366; DOI=10.1016/j.cell.2019.07.034;
RA Gong J., Liu J., Ronan E.A., He F., Cai W., Fatima M., Zhang W., Lee H.,
RA Li Z., Kim G.H., Pipe K.P., Duan B., Liu J., Xu X.Z.S.;
RT "A Cold-Sensing Receptor Encoded by a Glutamate Receptor Gene.";
RL Cell 178:1375-1386.e11(2019).
CC -!- FUNCTION: Ionotropic glutamate receptor (PubMed:19217376,
CC PubMed:31474366). L-glutamate acts as an excitatory neurotransmitter at
CC many synapses in the central nervous system. Binding of the excitatory
CC neurotransmitter L-glutamate induces a conformation change, leading to
CC the opening of the cation channel, and thereby converts the chemical
CC signal to an electrical impulse. The receptor then desensitizes rapidly
CC and enters a transient inactive state, characterized by the presence of
CC bound agonist. Modulates cell surface expression of NETO2
CC (PubMed:19217376). {ECO:0000269|PubMed:19217376,
CC ECO:0000269|PubMed:31474366}.
CC -!- FUNCTION: Independent of its ionotropic glutamate receptor activity,
CC acts as a thermoreceptor conferring sensitivity to cold temperatures
CC (PubMed:31474366). Functions in dorsal root ganglion neurons
CC (PubMed:31474366). {ECO:0000269|PubMed:31474366}.
CC -!- ACTIVITY REGULATION: Cold receptor activity activated by temperatures
CC between 10-19 degrees Celsius. {ECO:0000269|PubMed:31474366}.
CC -!- SUBUNIT: Homotetramer or heterotetramer of pore-forming glutamate
CC receptor subunits. Tetramers may be formed by the dimerization of
CC dimers (Probable). Assembles into a kainate-gated homomeric channel
CC that does not bind AMPA. GRIK2 associated to GRIK5 forms functional
CC channels that can be gated by AMPA. Interacts with DLG4 (By
CC similarity). Interacts (via C-terminus) with KLHL17 (via kelch
CC repeats); the interaction targets GRIK2 for degradation via ubiquitin-
CC proteasome pathway (By similarity). Interacts with NETO2. {ECO:0000250,
CC ECO:0000269|PubMed:19217376, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC Postsynaptic cell membrane; Multi-pass membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=GluR6 Beta2;
CC IsoId=P39087-1; Sequence=Displayed;
CC Name=GluR6-2;
CC IsoId=P39087-2; Sequence=VSP_000133;
CC -!- TISSUE SPECIFICITY: Most abundant in the cerebellum and the
CC hypothalamus. Expressed in a proportion of dorsal root ganglion (DRG)
CC neurons (13.6%); predominantly small diameter DRG neurons (75%) with
CC the remainder expressed in medium diameter DRG neurons
CC (PubMed:31474366). {ECO:0000269|PubMed:31474366}.
CC -!- DEVELOPMENTAL STAGE: Expressed during brain development. Expression
CC drops in the adult.
CC -!- PTM: Sumoylation mediates kainate receptor-mediated endocytosis and
CC regulates synaptic transmission. Sumoylation is enhanced by PIAS3 and
CC desumoylated by SENP1 (By similarity). {ECO:0000250}.
CC -!- PTM: Ubiquitinated. Ubiquitination regulates the GRIK2 levels at the
CC synapse by leading kainate receptor degradation through proteasome (By
CC similarity). {ECO:0000250}.
CC -!- PTM: Phosphorylated by PKC at Ser-868 upon agonist activation, this
CC directly enhance sumoylation. {ECO:0000250}.
CC -!- RNA EDITING: Modified_positions=567 {ECO:0000269|PubMed:7681676}, 571
CC {ECO:0000269|PubMed:7681676}, 621 {ECO:0000269|PubMed:7681676,
CC ECO:0000269|PubMed:8700852}; Note=Partially edited. The presence of Gln
CC at position 621 (non-edited) determines channels with low calcium
CC permeability, whereas Arg (edited) determines a higher calcium
CC permeability especially if the preceding sites are fully edited (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 domoate > kainate > quisqualate > 6-
CC cyano-7-nitroquinoxaline-2,3-dione > L-glutamate = 6,7-
CC dinitroquinoxaline-2,3-dione > dihydrokainate (By similarity).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glutamate-gated ion channel (TC 1.A.10.1)
CC family. GRIK2 subfamily. {ECO:0000305}.
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DR EMBL; X66117; CAA46907.1; -; mRNA.
DR EMBL; D10054; BAA00943.1; -; mRNA.
DR EMBL; U31443; AAA85221.1; -; Genomic_DNA.
DR EMBL; AC113305; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS23830.1; -. [P39087-2]
DR CCDS; CCDS48554.1; -. [P39087-1]
DR PIR; A43954; A43954.
DR PIR; S35792; S35792.
DR RefSeq; XP_017169293.1; XM_017313804.1.
DR AlphaFoldDB; P39087; -.
DR SMR; P39087; -.
DR BioGRID; 200064; 8.
DR CORUM; P39087; -.
DR IntAct; P39087; 6.
DR MINT; P39087; -.
DR STRING; 10090.ENSMUSP00000101127; -.
DR GlyConnect; 2347; 5 N-Linked glycans (3 sites).
DR GlyGen; P39087; 9 sites, 5 N-linked glycans (3 sites).
DR iPTMnet; P39087; -.
DR PhosphoSitePlus; P39087; -.
DR SwissPalm; P39087; -.
DR MaxQB; P39087; -.
DR PaxDb; P39087; -.
DR PeptideAtlas; P39087; -.
DR PRIDE; P39087; -.
DR ProteomicsDB; 269832; -. [P39087-1]
DR ProteomicsDB; 269833; -. [P39087-2]
DR Antibodypedia; 3038; 353 antibodies from 36 providers.
DR Ensembl; ENSMUST00000079751; ENSMUSP00000078687; ENSMUSG00000056073. [P39087-2]
DR Ensembl; ENSMUST00000105484; ENSMUSP00000101124; ENSMUSG00000056073. [P39087-1]
DR Ensembl; ENSMUST00000218441; ENSMUSP00000151671; ENSMUSG00000056073. [P39087-2]
DR Ensembl; ENSMUST00000218823; ENSMUSP00000151921; ENSMUSG00000056073. [P39087-1]
DR MGI; MGI:95815; Grik2.
DR VEuPathDB; HostDB:ENSMUSG00000056073; -.
DR eggNOG; KOG1052; Eukaryota.
DR GeneTree; ENSGT00940000155610; -.
DR HOGENOM; CLU_007257_1_1_1; -.
DR InParanoid; P39087; -.
DR OMA; VFAFDSV; -.
DR OrthoDB; 188544at2759; -.
DR PhylomeDB; P39087; -.
DR TreeFam; TF334668; -.
DR Reactome; R-MMU-451307; Activation of Na-permeable kainate receptors.
DR Reactome; R-MMU-451308; Activation of Ca-permeable Kainate Receptor.
DR BioGRID-ORCS; 14806; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Grik2; mouse.
DR PRO; PR:P39087; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; P39087; protein.
DR Bgee; ENSMUSG00000056073; Expressed in dentate gyrus of hippocampal formation granule cell and 102 other tissues.
DR ExpressionAtlas; P39087; baseline and differential.
DR Genevisible; P39087; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; ISO:MGI.
DR GO; GO:0030425; C:dendrite; ISO:MGI.
DR GO; GO:0032839; C:dendrite cytoplasm; ISO:MGI.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0098686; C:hippocampal mossy fiber to CA3 synapse; IDA:SynGO.
DR GO; GO:0005887; C:integral component of plasma membrane; ISO:MGI.
DR GO; GO:0008328; C:ionotropic glutamate receptor complex; ISO:MGI.
DR GO; GO:0032983; C:kainate selective glutamate receptor complex; IPI:MGI.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0043025; C:neuronal cell body; IDA:MGI.
DR GO; GO:0043204; C:perikaryon; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0014069; C:postsynaptic density; IDA:MGI.
DR GO; GO:0045211; C:postsynaptic membrane; IDA:MGI.
DR GO; GO:0042734; C:presynaptic membrane; IDA:MGI.
DR GO; GO:0045202; C:synapse; IDA:MGI.
DR GO; GO:0043195; C:terminal bouton; ISO:MGI.
DR GO; GO:0005234; F:extracellularly glutamate-gated ion channel activity; ISS:UniProtKB.
DR GO; GO:0008066; F:glutamate receptor activity; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0004970; F:ionotropic glutamate receptor activity; IDA:UniProtKB.
DR GO; GO:0015277; F:kainate selective glutamate receptor activity; IDA:MGI.
DR GO; GO:0015276; F:ligand-gated ion channel activity; IBA:GO_Central.
DR GO; GO:0099507; F:ligand-gated ion channel activity involved in regulation of presynaptic membrane potential; IDA:SynGO.
DR GO; GO:0030165; F:PDZ domain binding; ISO:MGI.
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; IDA:SynGO.
DR GO; GO:0031624; F:ubiquitin conjugating enzyme binding; ISO:MGI.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
DR GO; GO:0001662; P:behavioral fear response; IMP:MGI.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; IMP:MGI.
DR GO; GO:0007268; P:chemical synaptic transmission; IMP:MGI.
DR GO; GO:0120169; P:detection of cold stimulus involved in thermoception; IMP:UniProtKB.
DR GO; GO:0060079; P:excitatory postsynaptic potential; IMP:MGI.
DR GO; GO:0060080; P:inhibitory postsynaptic potential; IMP:MGI.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; ISO:MGI.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; IGI:MGI.
DR GO; GO:0051967; P:negative regulation of synaptic transmission, glutamatergic; IGI:MGI.
DR GO; GO:0051402; P:neuron apoptotic process; IGI:MGI.
DR GO; GO:0019228; P:neuronal action potential; IMP:MGI.
DR GO; GO:0043525; P:positive regulation of neuron apoptotic process; ISO:MGI.
DR GO; GO:0050806; P:positive regulation of synaptic transmission; ISO:MGI.
DR GO; GO:0099171; P:presynaptic modulation of chemical synaptic transmission; IGI:MGI.
DR GO; GO:0043113; P:receptor clustering; ISO:MGI.
DR GO; GO:0046328; P:regulation of JNK cascade; ISO:MGI.
DR GO; GO:0048169; P:regulation of long-term neuronal synaptic plasticity; IMP:MGI.
DR GO; GO:0042391; P:regulation of membrane potential; IDA:MGI.
DR GO; GO:0048172; P:regulation of short-term neuronal synaptic plasticity; IMP:MGI.
DR GO; GO:0035249; P:synaptic transmission, glutamatergic; IMP:MGI.
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; Disulfide bond; Glycoprotein;
KW Ion channel; Ion transport; Isopeptide bond; Ligand-gated ion channel;
KW Membrane; Phosphoprotein; Postsynaptic cell membrane; Receptor;
KW Reference proteome; RNA editing; Signal; Synapse; Transmembrane;
KW Transmembrane helix; Transport; Ubl conjugation.
FT SIGNAL 1..31
FT /evidence="ECO:0000255"
FT CHAIN 32..908
FT /note="Glutamate receptor ionotropic, kainate 2"
FT /id="PRO_0000011545"
FT TOPO_DOM 32..561
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 562..582
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 583..638
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 639..659
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 660..819
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 820..840
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 841..908
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT BINDING 516..518
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:P42260"
FT BINDING 523
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:P42260"
FT BINDING 689..690
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:P42260"
FT BINDING 738
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:P42260"
FT MOD_RES 846
FT /note="Phosphoserine; by PKC"
FT /evidence="ECO:0000250|UniProtKB:Q13002"
FT MOD_RES 868
FT /note="Phosphoserine; by PKC"
FT /evidence="ECO:0000250|UniProtKB:Q13002"
FT CARBOHYD 67
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 73
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 275
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 378
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 412
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 423
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 430
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 546
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 751
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 96..347
FT /evidence="ECO:0000250|UniProtKB:P42260"
FT CROSSLNK 886
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1)"
FT /evidence="ECO:0000250|UniProtKB:Q13002"
FT VAR_SEQ 855..908
FT /note="RSFCSAMVEELRMSLKCQRRLKHKPQAPVIVKTEEVINMHTFNDRRLPGKET
FT MA -> ESSIWLVPPYHPDTV (in isoform GluR6-2)"
FT /evidence="ECO:0000303|PubMed:1379666,
FT ECO:0000303|PubMed:8260617"
FT /id="VSP_000133"
FT VARIANT 567
FT /note="I -> V (in RNA edited version)"
FT VARIANT 571
FT /note="Y -> C (in RNA edited version)"
FT VARIANT 621
FT /note="Q -> R (in RNA edited version)"
FT MUTAGEN 151
FT /note="P->L: Abolishes cold receptor activity, no effect on
FT ionotropic glutamate receptor activity."
FT /evidence="ECO:0000269|PubMed:31474366"
FT MUTAGEN 620
FT /note="M->R: Abolishes ionotropic glutamate receptor
FT activity, no effect on cold receptor activity."
FT /evidence="ECO:0000269|PubMed:31474366"
FT MUTAGEN 622
FT /note="Q->R: Abolishes ionotropic glutamate receptor
FT activity, no effect on cold receptor activity."
FT /evidence="ECO:0000269|PubMed:31474366"
FT CONFLICT 611
FT /note="S -> G (in Ref. 1; CAA46907)"
FT /evidence="ECO:0000305"
FT CONFLICT 849..864
FT /note="NAQLEKRSFCSAMVEE -> TLNWKRGPSVAPWWKN (in Ref. 2;
FT BAA00943)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 908 AA; 102486 MW; EF430E2D8E0A87D4 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 KIGTWDPSSG 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
