EAA1_MOUSE
ID EAA1_MOUSE Reviewed; 543 AA.
AC P56564; Q99P53;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 05-MAR-2002, sequence version 2.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Excitatory amino acid transporter 1;
DE AltName: Full=Glial high affinity glutamate transporter;
DE AltName: Full=High-affinity neuronal glutamate transporter;
DE Short=GluT-1 {ECO:0000303|PubMed:7903437};
DE AltName: Full=Sodium-dependent glutamate/aspartate transporter 1;
DE Short=GLAST-1;
DE AltName: Full=Solute carrier family 1 member 3;
GN Name=Slc1a3; Synonyms=Eaat1, Gmt1;
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], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=7903437; DOI=10.1016/0304-3940(93)90829-a;
RA Tanaka K.;
RT "Cloning and expression of a glutamate transporter from mouse brain.";
RL Neurosci. Lett. 159:183-186(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain, and Neural stem cell;
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 [3]
RP PROTEIN SEQUENCE OF 80-114; 161-175; 189-196; 269-280 AND 480-499, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [4]
RP DISRUPTION PHENOTYPE, FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=15363892; DOI=10.1016/j.molbrainres.2004.06.026;
RA Stoffel W., Koerner R., Wachtmann D., Keller B.U.;
RT "Functional analysis of glutamate transporters in excitatory synaptic
RT transmission of GLAST1 and GLAST1/EAAC1 deficient mice.";
RL Brain Res. Mol. Brain Res. 128:170-181(2004).
RN [5]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=15390100; DOI=10.1002/glia.20097;
RA Sarthy V.P., Pignataro L., Pannicke T., Weick M., Reichenbach A.,
RA Harada T., Tanaka K., Marc R.;
RT "Glutamate transport by retinal Muller cells in glutamate/aspartate
RT transporter-knockout mice.";
RL Glia 49:184-196(2005).
RN [6]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=16880397; DOI=10.1073/pnas.0509144103;
RA Matsugami T.R., Tanemura K., Mieda M., Nakatomi R., Yamada K., Kondo T.,
RA Ogawa M., Obata K., Watanabe M., Hashikawa T., Tanaka K.;
RT "Indispensability of the glutamate transporters GLAST and GLT1 to brain
RT development.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:12161-12166(2006).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain cortex;
RX PubMed=17114649; DOI=10.1074/mcp.m600046-mcp200;
RA Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B.,
RA Panse C., Schlapbach R., Mansuy I.M.;
RT "Qualitative and quantitative analyses of protein phosphorylation in naive
RT and stimulated mouse synaptosomal preparations.";
RL Mol. Cell. Proteomics 6:283-293(2007).
RN [8]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-206 AND ASN-216.
RC TISSUE=Myoblast;
RX PubMed=19656770; DOI=10.1074/mcp.m900195-mcp200;
RA Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I., Bausch-Fluck D.,
RA Elliott S.T., Boheler K.R., Van Eyk J.E., Wollscheid B.;
RT "The mouse C2C12 myoblast cell surface N-linked glycoproteome:
RT identification, glycosite occupancy, and membrane orientation.";
RL Mol. Cell. Proteomics 8:2555-2569(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-512, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Liver, and Lung;
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 [10]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=28032905; DOI=10.1002/1873-3468.12549;
RA Krycer J.R., Fazakerley D.J., Cater R.J., C Thomas K., Naghiloo S.,
RA Burchfield J.G., Humphrey S.J., Vandenberg R.J., Ryan R.M., James D.E.;
RT "The amino acid transporter, SLC1A3, is plasma membrane-localised in
RT adipocytes and its activity is insensitive to insulin.";
RL FEBS Lett. 591:322-330(2017).
CC -!- FUNCTION: Sodium-dependent, high-affinity amino acid transporter that
CC mediates the uptake of L-glutamate and also L-aspartate and D-aspartate
CC (PubMed:7903437, PubMed:28032905). Functions as a symporter that
CC transports one amino acid molecule together with two or three Na(+)
CC ions and one proton, in parallel with the counter-transport of one K(+)
CC ion (By similarity). Plays a redundant role in the rapid removal of
CC released glutamate from the synaptic cleft, which is essential for
CC terminating the postsynaptic action of glutamate (PubMed:15363892,
CC PubMed:15390100,PubMed:16880397). {ECO:0000250|UniProtKB:O57321,
CC ECO:0000269|PubMed:15363892, ECO:0000269|PubMed:15390100,
CC ECO:0000269|PubMed:16880397, ECO:0000269|PubMed:28032905,
CC ECO:0000269|PubMed:7903437}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+)(out) + K(+)(in) + L-glutamate(out) + 3 Na(+)(out) =
CC H(+)(in) + K(+)(out) + L-glutamate(in) + 3 Na(+)(in);
CC Xref=Rhea:RHEA:70699, ChEBI:CHEBI:15378, ChEBI:CHEBI:29101,
CC ChEBI:CHEBI:29103, ChEBI:CHEBI:29985;
CC Evidence={ECO:0000250|UniProtKB:P43003};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+)(out) + K(+)(in) + L-aspartate(out) + 3 Na(+)(out) =
CC H(+)(in) + K(+)(out) + L-aspartate(in) + 3 Na(+)(in);
CC Xref=Rhea:RHEA:70851, ChEBI:CHEBI:15378, ChEBI:CHEBI:29101,
CC ChEBI:CHEBI:29103, ChEBI:CHEBI:29991;
CC Evidence={ECO:0000250|UniProtKB:P43003};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-aspartate(out) + H(+)(out) + K(+)(in) + 3 Na(+)(out) = D-
CC aspartate(in) + H(+)(in) + K(+)(out) + 3 Na(+)(in);
CC Xref=Rhea:RHEA:71379, ChEBI:CHEBI:15378, ChEBI:CHEBI:29101,
CC ChEBI:CHEBI:29103, ChEBI:CHEBI:29990;
CC Evidence={ECO:0000250|UniProtKB:P43003};
CC -!- SUBUNIT: Homotrimer (By similarity). {ECO:0000250|UniProtKB:P43003}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:28032905,
CC ECO:0000269|PubMed:7903437}; Multi-pass membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Detected in brain, in Bergmann glia arborising into
CC the molecular layer of the cerebellum (at protein level)
CC (PubMed:15363892). Localized in brain and is highly enriched in the
CC Purkinje cell layer in cerebellum. Intermediate level in lung, low
CC level in spleen, skeletal muscle and testis.
CC {ECO:0000269|PubMed:7903437}.
CC -!- DOMAIN: Contains eight transmembrane regions plus two helical hairpins
CC that dip into the membrane. These helical hairpin structures play an
CC important role in the transport process. The first enters the membrane
CC from the cytoplasmic side, the second one from the extracellular side.
CC During the transport cycle, the regions involved in amino acid
CC transport, and especially the helical hairpins, move vertically by
CC about 15-18 Angstroms, alternating between exposure to the aqueous
CC phase and reinsertion in the lipid bilayer. In contrast, the regions
CC involved in trimerization do not move. {ECO:0000250|UniProtKB:P43003}.
CC -!- PTM: Glycosylated. {ECO:0000269|PubMed:19656770}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype (PubMed:15363892,
CC PubMed:15390100). Mutant mice display normal locomotion, motor
CC coordination and learning, and globally normal glutamate uptake in
CC brain vesicle preparations (PubMed:15363892). The decay time of
CC glutamate receptor mediated excitatory postsynaptic currents (EPSCs) in
CC cerebellar Purkinje is slightly increased (PubMed:15363892). The
CC decreased rate of glutamate uptake in retina Mueller cells from mutant
CC mice suggests that Slc1a3 accounts for about half of the glutamate
CC uptake activity in wild-type cells (PubMed:15390100). Mice deficient in
CC both Slc1a2 and Slc1a3 die at about 17 dpc (PubMed:16880397).
CC {ECO:0000269|PubMed:15363892, ECO:0000269|PubMed:15390100,
CC ECO:0000269|PubMed:16880397}.
CC -!- SIMILARITY: Belongs to the dicarboxylate/amino acid:cation symporter
CC (DAACS) (TC 2.A.23) family. SLC1A3 subfamily. {ECO:0000305}.
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DR EMBL; AF330257; AAK01708.1; -; mRNA.
DR EMBL; BC058711; AAH58711.1; -; mRNA.
DR EMBL; BC066154; AAH66154.1; -; mRNA.
DR CCDS; CCDS27373.1; -.
DR RefSeq; NP_683740.1; NM_148938.3.
DR AlphaFoldDB; P56564; -.
DR SMR; P56564; -.
DR BioGRID; 203291; 8.
DR IntAct; P56564; 5.
DR MINT; P56564; -.
DR STRING; 10090.ENSMUSP00000005493; -.
DR GlyGen; P56564; 2 sites.
DR iPTMnet; P56564; -.
DR PhosphoSitePlus; P56564; -.
DR SwissPalm; P56564; -.
DR jPOST; P56564; -.
DR PaxDb; P56564; -.
DR PeptideAtlas; P56564; -.
DR PRIDE; P56564; -.
DR ProteomicsDB; 275425; -.
DR Antibodypedia; 22936; 409 antibodies from 39 providers.
DR DNASU; 20512; -.
DR Ensembl; ENSMUST00000005493; ENSMUSP00000005493; ENSMUSG00000005360.
DR GeneID; 20512; -.
DR KEGG; mmu:20512; -.
DR UCSC; uc007vex.1; mouse.
DR CTD; 6507; -.
DR MGI; MGI:99917; Slc1a3.
DR VEuPathDB; HostDB:ENSMUSG00000005360; -.
DR eggNOG; KOG3787; Eukaryota.
DR GeneTree; ENSGT00940000155464; -.
DR HOGENOM; CLU_019375_3_2_1; -.
DR InParanoid; P56564; -.
DR OMA; GHGMNVD; -.
DR OrthoDB; 1184392at2759; -.
DR PhylomeDB; P56564; -.
DR TreeFam; TF315206; -.
DR Reactome; R-MMU-210455; Astrocytic Glutamate-Glutamine Uptake And Metabolism.
DR Reactome; R-MMU-210500; Glutamate Neurotransmitter Release Cycle.
DR Reactome; R-MMU-425393; Transport of inorganic cations/anions and amino acids/oligopeptides.
DR BioGRID-ORCS; 20512; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Slc1a3; mouse.
DR PRO; PR:P56564; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; P56564; protein.
DR Bgee; ENSMUSG00000005360; Expressed in cerebellum lobe and 259 other tissues.
DR ExpressionAtlas; P56564; baseline and differential.
DR Genevisible; P56564; MM.
DR GO; GO:0009925; C:basal plasma membrane; ISO:MGI.
DR GO; GO:0016323; C:basolateral plasma membrane; ISO:MGI.
DR GO; GO:0071944; C:cell periphery; IDA:MGI.
DR GO; GO:0042995; C:cell projection; IDA:MGI.
DR GO; GO:0009986; C:cell surface; IDA:MGI.
DR GO; GO:0043197; C:dendritic spine; ISO:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0098796; C:membrane protein complex; ISO:MGI.
DR GO; GO:0005743; C:mitochondrial inner membrane; ISO:MGI.
DR GO; GO:0043005; C:neuron projection; IDA:MGI.
DR GO; GO:0043025; C:neuronal cell body; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0045202; C:synapse; IDA:MGI.
DR GO; GO:0015172; F:acidic amino acid transmembrane transporter activity; IMP:UniProtKB.
DR GO; GO:0016597; F:amino acid binding; IDA:MGI.
DR GO; GO:0016595; F:glutamate binding; IDA:MGI.
DR GO; GO:0015501; F:glutamate:sodium symporter activity; ISS:UniProtKB.
DR GO; GO:0005314; F:high-affinity L-glutamate transmembrane transporter activity; IDA:MGI.
DR GO; GO:0005313; F:L-glutamate transmembrane transporter activity; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0015175; F:neutral amino acid transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0031223; P:auditory behavior; IMP:MGI.
DR GO; GO:0048667; P:cell morphogenesis involved in neuron differentiation; IMP:MGI.
DR GO; GO:0071314; P:cellular response to cocaine; IDA:MGI.
DR GO; GO:0006883; P:cellular sodium ion homeostasis; IMP:MGI.
DR GO; GO:1902476; P:chloride transmembrane transport; ISS:UniProtKB.
DR GO; GO:0021545; P:cranial nerve development; IMP:MGI.
DR GO; GO:0070779; P:D-aspartate import across plasma membrane; IMP:UniProtKB.
DR GO; GO:0009449; P:gamma-aminobutyric acid biosynthetic process; IMP:MGI.
DR GO; GO:0140009; P:L-aspartate import across plasma membrane; ISS:UniProtKB.
DR GO; GO:0051938; P:L-glutamate import; IMP:MGI.
DR GO; GO:0098712; P:L-glutamate import across plasma membrane; IMP:MGI.
DR GO; GO:0015813; P:L-glutamate transmembrane transport; IDA:MGI.
DR GO; GO:0043490; P:malate-aspartate shuttle; ISO:MGI.
DR GO; GO:0050885; P:neuromuscular process controlling balance; IMP:MGI.
DR GO; GO:0050806; P:positive regulation of synaptic transmission; IMP:MGI.
DR GO; GO:0071805; P:potassium ion transmembrane transport; ISS:UniProtKB.
DR GO; GO:0043200; P:response to amino acid; ISO:MGI.
DR GO; GO:0046677; P:response to antibiotic; IMP:MGI.
DR GO; GO:0010035; P:response to inorganic substance; ISO:MGI.
DR GO; GO:0009416; P:response to light stimulus; IMP:MGI.
DR GO; GO:0009611; P:response to wounding; IMP:MGI.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IMP:MGI.
DR GO; GO:0007605; P:sensory perception of sound; IMP:MGI.
DR Gene3D; 1.10.3860.10; -; 1.
DR InterPro; IPR001991; Na-dicarboxylate_symporter.
DR InterPro; IPR018107; Na-dicarboxylate_symporter_CS.
DR InterPro; IPR036458; Na:dicarbo_symporter_sf.
DR Pfam; PF00375; SDF; 1.
DR SUPFAM; SSF118215; SSF118215; 1.
DR PROSITE; PS00713; NA_DICARBOXYL_SYMP_1; 1.
DR PROSITE; PS00714; NA_DICARBOXYL_SYMP_2; 1.
PE 1: Evidence at protein level;
KW Amino-acid transport; Cell membrane; Chloride; Direct protein sequencing;
KW Glycoprotein; Membrane; Metal-binding; Phosphoprotein; Potassium;
KW Reference proteome; Sodium; Symport; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..543
FT /note="Excitatory amino acid transporter 1"
FT /id="PRO_0000202058"
FT TOPO_DOM 1..47
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P43003"
FT TRANSMEM 48..68
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250|UniProtKB:P43003"
FT TOPO_DOM 69..86
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P43003"
FT TRANSMEM 87..108
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250|UniProtKB:P43003"
FT TOPO_DOM 109..122
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P43003"
FT TRANSMEM 123..145
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250|UniProtKB:P43003"
FT TOPO_DOM 146..236
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P43003"
FT TRANSMEM 237..260
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250|UniProtKB:P43003"
FT TOPO_DOM 261..269
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P43003"
FT TRANSMEM 270..297
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250|UniProtKB:P43003"
FT TOPO_DOM 298..318
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P43003"
FT TRANSMEM 319..340
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250|UniProtKB:P43003"
FT TOPO_DOM 341..345
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P43003"
FT INTRAMEM 346..376
FT /note="Discontinuously helical"
FT /evidence="ECO:0000250|UniProtKB:P43003"
FT TOPO_DOM 377..385
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P43003"
FT TRANSMEM 386..412
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250|UniProtKB:P43003"
FT TOPO_DOM 413..425
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P43003"
FT INTRAMEM 426..459
FT /note="Discontinuously helical"
FT /evidence="ECO:0000250|UniProtKB:P43003"
FT TOPO_DOM 460..472
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P43003"
FT TRANSMEM 473..494
FT /note="Helical; Name=8"
FT /evidence="ECO:0000250|UniProtKB:P43003"
FT TOPO_DOM 495..543
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P43003"
FT REGION 522..543
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 363..365
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250|UniProtKB:O59010"
FT BINDING 394
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O59010"
FT BINDING 396
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O59010"
FT BINDING 398
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O59010"
FT BINDING 402
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250|UniProtKB:O59010"
FT BINDING 443..447
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250|UniProtKB:P43003"
FT BINDING 476
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250|UniProtKB:O59010"
FT BINDING 483
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250|UniProtKB:O59010"
FT BINDING 483
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O59010"
FT BINDING 487
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O59010"
FT MOD_RES 512
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CARBOHYD 206
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19656770"
FT CARBOHYD 216
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19656770"
SQ SEQUENCE 543 AA; 59622 MW; E0B24CBA1D5B086D CRC64;
MTKSNGEEPR MGGRMERLQQ GVRKRTLLAK KKVQSLTKED VKSYLFRNAF VLLTVTAVIV
GTILGFALRP YKMSYREVKY FSFPGELLMR MLQMLVLPLI ISSLVTGMAA LDSKASGKMG
MRAVVYYMTT TIIAVVIGII IVIIIHPGKG TKENMYREGK IVQVTAADAF LDLIRNMFPP
NLVEACFKQF KTSYEKRSFK VPIQSNETLL GAVINNVSEA METLTRIREE MVPVPGSVNG
VNALGLVVFS MCFGFVIGNM KEQGQALREF FDSLNEAIMR LVAVIMWYAP LGILFLIAGK
IVEMEDMGVI GGQLAMYTVT VIVGLLIHAV IVLPLLYFLV TRKNPWVFIG GLLQALITAL
GTSSSSATLP ITFKCLEENN GVDKRITRFV LPVGATINMD GTALYEALAA IFIAQVNNFD
LNFGQIITIS ITATAASIGA AGIPQAGLVT MVIVLTSVGL PTDDITLIIA VDWFLDRLRT
TTNVLGDSLG AGIVEHLSRH ELKNRDVEMG NSVIEENEMK KPYQLIAQDN EPEKPVADSE
TKM
