GRIA3_MOUSE
ID GRIA3_MOUSE Reviewed; 888 AA.
AC Q9Z2W9; A2VDF4; Q5DTJ0;
DT 11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 168.
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, Kiaa4184;
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].
RC STRAIN=C57BL/6J;
RA Sakimura K., Yamazaki M.;
RT "Mouse glutamate receptor channel alpha3 subunit.";
RL Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=ddY; TISSUE=Spinal cord;
RA Doi Y., Nishizawa M., Minami T., Ito S.;
RT "Expression of AMPA-selective glutamate receptors in mouse spinal cord.";
RL Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=ILS, and ISS;
RX PubMed=11471062; DOI=10.1007/s00335-001-1001-x;
RA Ehringer M.A., Thompson J., Conroy O., Xu Y., Yang F., Canniff J.,
RA Beeson M., Gordon L., Bennett B., Johnson T.E., Sikela J.M.;
RT "High-throughput sequence identification of gene coding variants within
RT alcohol-related QTLs.";
RL Mamm. Genome 12:657-663(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RA Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene. The
RT complete nucleotide sequences of mouse KIAA-homologous cDNAs identified by
RT screening of terminal sequences of cDNA clones randomly sampled from size-
RT fractionated libraries.";
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP PALMITOYLATION AT CYS-841.
RX PubMed=16129400; DOI=10.1016/j.neuron.2005.06.035;
RA Hayashi T., Rumbaugh G., Huganir R.L.;
RT "Differential regulation of AMPA receptor subunit trafficking by
RT palmitoylation of two distinct sites.";
RL Neuron 47:709-723(2005).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-871 AND TYR-881, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=18034455; DOI=10.1021/pr0701254;
RA Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT "Large-scale identification and evolution indexing of tyrosine
RT phosphorylation sites from murine brain.";
RL J. Proteome Res. 7:311-318(2008).
RN [10]
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 [11]
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 658-799 IN COMPLEX WITH
RP GLUTAMATE, SUBUNIT, AND DISULFIDE BOND.
RX PubMed=20163115; DOI=10.1021/jm901905j;
RA Ahmed A.H., Oswald R.E.;
RT "Piracetam defines a new binding site for allosteric modulators of alpha-
RT amino-3-hydroxy-5-methyl-4-isoxazole-propionic acid (AMPA) receptors.";
RL J. Med. Chem. 53:2197-2203(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 -!- 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 (By similarity). Found
CC in a complex with GRIA1, GRIA2, GRIA4, CNIH2, CNIH3, CACNG2, CACNG3,
CC CACNG4, CACNG5, CACNG7 and CACNG8. Interacts with CACNG5 (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}. Postsynaptic cell membrane {ECO:0000250}; Multi-
CC pass membrane protein {ECO:0000250}. Note=Interaction with CNIH2 and
CC CNIH3 promotes cell surface expression. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Flip;
CC IsoId=Q9Z2W9-1; Sequence=Displayed;
CC Name=Flop;
CC IsoId=Q9Z2W9-2; Sequence=Not described;
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD90527.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB022342; BAA37124.1; -; mRNA.
DR EMBL; AB079072; BAE06153.1; -; mRNA.
DR EMBL; AF483494; AAL90768.1; -; mRNA.
DR EMBL; AF483495; AAL90769.1; -; mRNA.
DR EMBL; AK220530; BAD90527.1; ALT_INIT; mRNA.
DR EMBL; CH466570; EDL29035.1; -; Genomic_DNA.
DR EMBL; AL672232; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL672290; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC129855; AAI29856.1; -; mRNA.
DR CCDS; CCDS30097.1; -. [Q9Z2W9-1]
DR RefSeq; NP_001268858.1; NM_001281929.1. [Q9Z2W9-1]
DR RefSeq; NP_058582.3; NM_016886.4. [Q9Z2W9-1]
DR RefSeq; XP_006541583.1; XM_006541520.3.
DR RefSeq; XP_017174034.1; XM_017318545.1. [Q9Z2W9-1]
DR PDB; 3LSW; X-ray; 1.75 A; A=658-799.
DR PDB; 3LSX; X-ray; 2.01 A; A=658-799.
DR PDBsum; 3LSW; -.
DR PDBsum; 3LSX; -.
DR AlphaFoldDB; Q9Z2W9; -.
DR SMR; Q9Z2W9; -.
DR BioGRID; 207340; 10.
DR IntAct; Q9Z2W9; 6.
DR MINT; Q9Z2W9; -.
DR STRING; 10090.ENSMUSP00000075687; -.
DR ChEMBL; CHEMBL2096617; -.
DR GlyConnect; 2343; 7 N-Linked glycans (2 sites).
DR GlyGen; Q9Z2W9; 5 sites, 7 N-linked glycans (2 sites).
DR iPTMnet; Q9Z2W9; -.
DR PhosphoSitePlus; Q9Z2W9; -.
DR SwissPalm; Q9Z2W9; -.
DR MaxQB; Q9Z2W9; -.
DR PaxDb; Q9Z2W9; -.
DR PeptideAtlas; Q9Z2W9; -.
DR PRIDE; Q9Z2W9; -.
DR ProteomicsDB; 271162; -. [Q9Z2W9-1]
DR Antibodypedia; 29962; 346 antibodies from 30 providers.
DR DNASU; 53623; -.
DR Ensembl; ENSMUST00000076349; ENSMUSP00000075687; ENSMUSG00000001986. [Q9Z2W9-1]
DR GeneID; 53623; -.
DR KEGG; mmu:53623; -.
DR UCSC; uc009tal.3; mouse. [Q9Z2W9-1]
DR CTD; 2892; -.
DR MGI; MGI:95810; Gria3.
DR VEuPathDB; HostDB:ENSMUSG00000001986; -.
DR eggNOG; KOG1054; Eukaryota.
DR GeneTree; ENSGT00940000156123; -.
DR InParanoid; Q9Z2W9; -.
DR TreeFam; TF315232; -.
DR Reactome; R-MMU-399710; Activation of AMPA receptors.
DR Reactome; R-MMU-416993; Trafficking of GluR2-containing AMPA receptors.
DR Reactome; R-MMU-438066; Unblocking of NMDA receptors, glutamate binding and activation.
DR Reactome; R-MMU-8849932; Synaptic adhesion-like molecules.
DR BioGRID-ORCS; 53623; 2 hits in 74 CRISPR screens.
DR ChiTaRS; Gria3; mouse.
DR EvolutionaryTrace; Q9Z2W9; -.
DR PRO; PR:Q9Z2W9; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q9Z2W9; protein.
DR Bgee; ENSMUSG00000001986; Expressed in subiculum and 196 other tissues.
DR ExpressionAtlas; Q9Z2W9; baseline and differential.
DR Genevisible; Q9Z2W9; MM.
DR GO; GO:0032281; C:AMPA glutamate receptor complex; IDA:MGI.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0032279; C:asymmetric synapse; ISO:MGI.
DR GO; GO:0030425; C:dendrite; ISO:MGI.
DR GO; GO:0043198; C:dendritic shaft; ISO:MGI.
DR GO; GO:0043197; C:dendritic spine; ISO:MGI.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
DR GO; GO:0099061; C:integral component of postsynaptic density membrane; ISO:MGI.
DR GO; GO:0099055; C:integral component of postsynaptic membrane; ISO:MGI.
DR GO; GO:0099056; C:integral component of presynaptic membrane; ISO:MGI.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0098688; C:parallel fiber to Purkinje cell synapse; IDA:SynGO.
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; ISO:MGI.
DR GO; GO:0045211; C:postsynaptic membrane; IDA:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0043083; C:synaptic cleft; ISO:MGI.
DR GO; GO:0043195; C:terminal bouton; ISO:MGI.
DR GO; GO:0004971; F:AMPA glutamate receptor activity; ISS:UniProtKB.
DR GO; GO:0001540; F:amyloid-beta binding; ISO:MGI.
DR GO; GO:0004970; F:ionotropic glutamate receptor activity; ISO:MGI.
DR GO; GO:0015276; F:ligand-gated ion channel activity; IBA:GO_Central.
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:0001919; P:regulation of receptor recycling; ISO: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 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_0000042230"
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:20163115"
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:20163115"
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:20163115"
FT MOD_RES 871
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:18034455"
FT MOD_RES 881
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:18034455"
FT LIPID 615
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 841
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000269|PubMed:16129400"
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:0000255"
FT CARBOHYD 374
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
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 /evidence="ECO:0000250"
FT DISULFID 744..799
FT /evidence="ECO:0000269|PubMed:20163115"
FT CONFLICT 300
FT /note="T -> I (in Ref. 4; BAD90527)"
FT /evidence="ECO:0000305"
FT CONFLICT 769
FT /note="R -> G (in Ref. 1; BAA37124/BAE06153, 3; AAL90768/
FT AAL90769 and 4; BAD90527)"
FT /evidence="ECO:0000305"
FT STRAND 418..423
FT /evidence="ECO:0007829|PDB:3LSW"
FT TURN 427..429
FT /evidence="ECO:0007829|PDB:3LSW"
FT STRAND 430..432
FT /evidence="ECO:0007829|PDB:3LSW"
FT HELIX 436..438
FT /evidence="ECO:0007829|PDB:3LSW"
FT HELIX 441..444
FT /evidence="ECO:0007829|PDB:3LSW"
FT STRAND 445..447
FT /evidence="ECO:0007829|PDB:3LSW"
FT HELIX 448..460
FT /evidence="ECO:0007829|PDB:3LSW"
FT STRAND 463..468
FT /evidence="ECO:0007829|PDB:3LSW"
FT TURN 479..481
FT /evidence="ECO:0007829|PDB:3LSW"
FT HELIX 486..492
FT /evidence="ECO:0007829|PDB:3LSW"
FT STRAND 497..499
FT /evidence="ECO:0007829|PDB:3LSW"
FT HELIX 507..510
FT /evidence="ECO:0007829|PDB:3LSW"
FT STRAND 513..515
FT /evidence="ECO:0007829|PDB:3LSW"
FT STRAND 519..522
FT /evidence="ECO:0007829|PDB:3LSW"
FT STRAND 524..529
FT /evidence="ECO:0007829|PDB:3LSW"
FT HELIX 662..666
FT /evidence="ECO:0007829|PDB:3LSW"
FT STRAND 669..676
FT /evidence="ECO:0007829|PDB:3LSW"
FT HELIX 680..687
FT /evidence="ECO:0007829|PDB:3LSW"
FT HELIX 691..702
FT /evidence="ECO:0007829|PDB:3LSW"
FT STRAND 708..711
FT /evidence="ECO:0007829|PDB:3LSW"
FT HELIX 712..721
FT /evidence="ECO:0007829|PDB:3LSW"
FT TURN 722..724
FT /evidence="ECO:0007829|PDB:3LSW"
FT STRAND 725..731
FT /evidence="ECO:0007829|PDB:3LSW"
FT HELIX 732..739
FT /evidence="ECO:0007829|PDB:3LSW"
FT STRAND 746..750
FT /evidence="ECO:0007829|PDB:3LSW"
FT STRAND 756..758
FT /evidence="ECO:0007829|PDB:3LSW"
FT STRAND 761..763
FT /evidence="ECO:0007829|PDB:3LSW"
FT HELIX 770..781
FT /evidence="ECO:0007829|PDB:3LSW"
FT HELIX 784..793
FT /evidence="ECO:0007829|PDB:3LSW"
FT TURN 794..796
FT /evidence="ECO:0007829|PDB:3LSW"
SQ SEQUENCE 888 AA; 100527 MW; 9F68C5D80E81DC02 CRC64;
MGQSVLRAVF FLVLGLLGHS HGGFPNTISI GGLFMRNTVQ EHSAFRFAVQ LYNTNQNTTE
KPFHLNYHVD HLDSSNSFSV TNAFCSQFSR GVYAIFGFYD QMSMNTLTSF CGALHTSFVT
PSFPTDADVQ FVIQMRPALK GAILSLLGYY KWEKFVYLYD TERGFSILQA IMEAAVQNNW
QVTARSVGNI KDIQEFRRII EEMDRRQEKR YLIDCEVERI NTILEQVVIL GKHSRGYHYM
LANLGFTDIV 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 ATPKGSALRT PVNLAVLKLS
EQGILDKLKN KWWYDKGECG AKDSGSKDKT SALSLSNVAG VFYILVGGLG LAMMVALIEF
CYKSRAESKR MKLTKNTQNF KPAPATNTQN YATYREGYNV YGTESVKI
