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 04-NOV-2026, entry version 196. 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:28032905, PubMed:7903437). 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=K(+)(in) + L-glutamate(out) + 3 Na(+)(out) + H(+)(out) = CC K(+)(out) + L-glutamate(in) + 3 Na(+)(in) + H(+)(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=K(+)(in) + L-aspartate(out) + 3 Na(+)(out) + H(+)(out) = CC K(+)(out) + L-aspartate(in) + 3 Na(+)(in) + H(+)(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) + K(+)(in) + 3 Na(+)(out) + H(+)(out) = D- CC aspartate(in) + K(+)(out) + 3 Na(+)(in) + H(+)(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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 16. DR FunCoup; P56564; 433. DR IntAct; P56564; 5. DR STRING; 10090.ENSMUSP00000005493; -. DR GlyCosmos; P56564; 2 sites, 2 glycans. DR GlyGen; P56564; 3 sites, 2 N-linked glycans (2 sites), 1 O-linked glycan (1 site). DR iPTMnet; P56564; -. DR MetOSite; P56564; -. DR PhosphoSitePlus; P56564; -. DR SwissPalm; P56564; -. DR jPOST; P56564; -. DR PaxDb; 10090-ENSMUSP00000005493; -. DR PeptideAtlas; P56564; -. DR ProteomicsDB; 275425; -. DR Pumba; P56564; -. DR Antibodypedia; 22936; 517 antibodies from 42 providers. DR DNASU; 20512; -. DR Ensembl; ENSMPUT00000015172; ENSMPUP00000014935; ENSMPUG00000015046. DR Ensembl; ENSMUST00000005493.14; ENSMUSP00000005493.8; ENSMUSG00000005360.15. DR GeneID; 20512; -. DR KEGG; mmu:20512; -. DR UCSC; uc007vex.1; mouse. DR AGR; MGI:99917; -. 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; AAWEHDI; -. DR OrthoDB; 5877963at2759; -. DR PhylomeDB; P56564; -. DR Reactome; R-MMU-210455; Astrocytic Glutamate-Glutamine Uptake And Metabolism. DR Reactome; R-MMU-210500; Glutamate Neurotransmitter Release Cycle. DR Reactome; R-MMU-9958863; SLC-mediated transport of amino acids. DR BioGRID-ORCS; 20512; 1 hit in 78 CRISPR screens. DR CD-CODE; CE726F99; Postsynaptic density. DR PRO; PR:P56564; -. DR Proteomes; UP000000589; Chromosome 15. DR RNAct; P56564; protein. DR Bgee; ENSMUSG00000005360; Expressed in cerebellum lobe and 261 other cell types or tissues. DR ExpressionAtlas; P56564; baseline and differential. DR GO; GO:0009925; C:basal plasma membrane; ISO:GO_Central. DR GO; GO:0016323; C:basolateral plasma membrane; ISO:GO_Central. DR GO; GO:0071944; C:cell periphery; IDA:MGI. DR GO; GO:0009986; C:cell surface; IDA:MGI. DR GO; GO:0043197; C:dendritic spine; ISO:GO_Central. DR GO; GO:0098796; C:membrane protein complex; ISO:GO_Central. DR GO; GO:0005743; C:mitochondrial inner membrane; ISO:GO_Central. 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:UniProtKB. 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; IMP:MGI. DR GO; GO:0015175; F:neutral L-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: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:0006883; P:intracellular sodium ion homeostasis; 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:GO_Central. 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: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 FunFam; 1.10.3860.10:FF:000002; Amino acid transporter; 1. DR Gene3D; 1.10.3860.10; Sodium:dicarboxylate symporter; 1. DR InterPro; IPR050746; DAACS. DR InterPro; IPR001991; Na-dicarboxylate_symporter. DR InterPro; IPR018107; Na-dicarboxylate_symporter_CS. DR InterPro; IPR036458; Na:dicarbo_symporter_sf. DR PANTHER; PTHR11958:SF24; EXCITATORY AMINO ACID TRANSPORTER 1; 1. DR PANTHER; PTHR11958; SODIUM/DICARBOXYLATE SYMPORTER-RELATED; 1. DR Pfam; PF00375; SDF; 1. DR PRINTS; PR00173; EDTRNSPORT. DR SUPFAM; SSF118215; Proton glutamate symport protein; 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 COMPBIAS 531..543 FT /note="Basic and acidic residues" 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 //