ID EAA2_RAT Reviewed; 573 AA. AC P31596; DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1993, sequence version 2. DT 04-MAR-2015, entry version 125. DE RecName: Full=Excitatory amino acid transporter 2; DE AltName: Full=GLT-1; DE AltName: Full=Sodium-dependent glutamate/aspartate transporter 2; DE Short=GLUT-R; DE AltName: Full=Solute carrier family 1 member 2; GN Name=Slc1a2; Synonyms=Eaat2, Glt1; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Brain; RX PubMed=1448170; DOI=10.1038/360464a0; RA Pines G., Danbolt N.C., Bjoeraas M., Zhang Y., Bendahan A., Eide L., RA Koepsell H., Storm-Mathisen J., Seeberg E., Kanner B.I.; RT "Cloning and expression of a rat brain L-glutamate transporter."; RL Nature 360:464-467(1992). RN [2] RP ERRATUM. RA Pines G., Danbolt N.C., Bjoeraas M., Zhang Y., Bendahan A., Eide L., RA Koepsell H., Storm-Mathisen J., Seeberg E., Kanner B.I.; RL Nature 360:768-768(1992). RN [3] RP SEQUENCE REVISION TO 260-289. RX PubMed=8099882; DOI=10.1016/0014-5793(93)81421-U; RA Kanner B.I.; RT "Glutamate transporters from brain. A novel neurotransmitter RT transporter family."; RL FEBS Lett. 325:95-99(1993). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Forebrain; RA Roginski R.S., Choudhury K., Meiners S., Marone M., Basma A.N., RA Geller H.M.; RL Submitted (MAR-1995) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM GLT-1A). RC TISSUE=Hepatoma; RX PubMed=11068035; DOI=10.1016/S0014-5793(00)02114-1; RA Pollard M., McGivan J.; RT "The rat hepatoma cell line H4-II-E-C3 expresses high activities of RT the high-affinity glutamate transporter GLT-1A."; RL FEBS Lett. 484:74-76(2000). RN [6] RP PROTEIN SEQUENCE OF 158-173, AND IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=Sprague-Dawley; TISSUE=Brain; RA Lubec G., Kang S.U.; RL Submitted (JUL-2007) to UniProtKB. RN [7] RP MUTAGENESIS OF LYS-298 AND HIS-326. RX PubMed=7913472; RA Zhang Y., Pines G., Kanner B.I.; RT "Histidine 326 is critical for the function of GLT-1, a (Na+ + K+)- RT coupled glutamate transporter from rat brain."; RL J. Biol. Chem. 269:19573-19577(1994). RN [8] RP INTERACTION WITH AJUBA. RX PubMed=11860269; DOI=10.1006/mcne.2001.1066; RA Marie H., Billups D., Bedford F.K., Dumoulin A., Goyal R.K., RA Longmore G.D., Moss S.J., Attwell D.; RT "The amino terminus of the glial glutamate transporter GLT-1 interacts RT with the LIM protein Ajuba."; RL Mol. Cell. Neurosci. 19:152-164(2002). CC -!- FUNCTION: Transports L-glutamate and also L- and D-aspartate. CC Essential for terminating the postsynaptic action of glutamate by CC rapidly removing released glutamate from the synaptic cleft. Acts CC as a symport by cotransporting sodium. CC -!- SUBUNIT: Homotrimer (By similarity). Interacts with AJUBA. CC {ECO:0000250, ECO:0000269|PubMed:11860269}. CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=Glt1; CC IsoId=P31596-1; Sequence=Displayed; CC Name=Glt-1A; CC IsoId=P31596-2; Sequence=VSP_006266; CC -!- TISSUE SPECIFICITY: Localized in brain and is highly enriched in CC the Purkinje cell layer in cerebellum. CC -!- PTM: Glycosylated. CC -!- PTM: Palmitoylation at Cys-38 is not required for correct CC subcellular localization, but is important for glutamate uptake CC activity. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the sodium:dicarboxylate (SDF) symporter CC (TC 2.A.23) family. SLC1A2 subfamily. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAA93062.1; Type=Erroneous initiation; Evidence={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; X67857; CAA48042.1; ALT_SEQ; mRNA. DR EMBL; U15098; AAA93061.1; -; mRNA. DR EMBL; U15098; AAA93062.1; ALT_INIT; mRNA. DR EMBL; AF297648; AAG13411.1; -; mRNA. DR PIR; S28901; S28901. DR RefSeq; NP_001289018.1; NM_001302089.1. DR RefSeq; NP_058911.2; NM_017215.2. DR UniGene; Rn.10240; -. DR ProteinModelPortal; P31596; -. DR BioGrid; 248124; 1. DR IntAct; P31596; 1. DR ChEMBL; CHEMBL2900; -. DR GuidetoPHARMACOLOGY; 869; -. DR TCDB; 2.A.23.2.2; the dicarboxylate/amino acid:cation (na(+) or h(+)) symporter (daacs) family. DR PhosphoSite; P31596; -. DR PaxDb; P31596; -. DR PRIDE; P31596; -. DR GeneID; 29482; -. DR KEGG; rno:29482; -. DR UCSC; RGD:3697; rat. [P31596-1] DR CTD; 6506; -. DR RGD; 3697; Slc1a2. DR eggNOG; COG1301; -. DR HOGENOM; HOG000208776; -. DR HOVERGEN; HBG000080; -. DR InParanoid; P31596; -. DR KO; K05613; -. DR PhylomeDB; P31596; -. DR TreeFam; TF315206; -. DR NextBio; 609336; -. DR PRO; PR:P31596; -. DR Proteomes; UP000002494; Unplaced. DR Genevestigator; P31596; -. DR GO; GO:0043198; C:dendritic shaft; IDA:RGD. DR GO; GO:0043197; C:dendritic spine; IDA:RGD. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0043005; C:neuron projection; IDA:RGD. DR GO; GO:0005886; C:plasma membrane; IDA:RGD. DR GO; GO:0042734; C:presynaptic membrane; IDA:RGD. DR GO; GO:0045202; C:synapse; IDA:RGD. DR GO; GO:0005314; F:high-affinity glutamate transmembrane transporter activity; IMP:RGD. DR GO; GO:0017153; F:sodium:dicarboxylate symporter activity; IEA:InterPro. DR GO; GO:0089711; P:L-glutamate transmembrane transport; IMP:GOC. DR GO; GO:0015813; P:L-glutamate transport; IMP:RGD. DR GO; GO:0006836; P:neurotransmitter transport; TAS:RGD. DR Gene3D; 1.10.3860.10; -; 2. DR InterPro; IPR001991; Na-dicarboxylate_symporter. DR InterPro; IPR018107; Na-dicarboxylate_symporter_CS. DR PANTHER; PTHR11958; PTHR11958; 1. DR Pfam; PF00375; SDF; 1. DR PRINTS; PR00173; EDTRNSPORT. DR SUPFAM; SSF118215; SSF118215; 2. DR PROSITE; PS00713; NA_DICARBOXYL_SYMP_1; 1. DR PROSITE; PS00714; NA_DICARBOXYL_SYMP_2; 1. PE 1: Evidence at protein level; KW Alternative splicing; Complete proteome; Direct protein sequencing; KW Glycoprotein; Lipoprotein; Membrane; Palmitate; Phosphoprotein; KW Reference proteome; Symport; Transmembrane; Transmembrane helix; KW Transport. FT CHAIN 1 573 Excitatory amino acid transporter 2. FT /FTId=PRO_0000202063. FT TOPO_DOM 1 44 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 45 64 Helical. {ECO:0000255}. FT TRANSMEM 88 108 Helical. {ECO:0000255}. FT TRANSMEM 121 142 Helical. {ECO:0000255}. FT TOPO_DOM 143 238 Extracellular. {ECO:0000255}. FT TRANSMEM 239 258 Helical. {ECO:0000255}. FT TRANSMEM 279 300 Helical. {ECO:0000255}. FT TRANSMEM 316 338 Helical. {ECO:0000255}. FT TRANSMEM 405 429 Helical. {ECO:0000255}. FT TRANSMEM 436 458 Helical. {ECO:0000255}. FT MOD_RES 538 538 Phosphotyrosine. FT {ECO:0000250|UniProtKB:P43006}. FT LIPID 38 38 S-palmitoyl cysteine. {ECO:0000250}. FT CARBOHYD 205 205 N-linked (GlcNAc...). {ECO:0000255}. FT CARBOHYD 215 215 N-linked (GlcNAc...). {ECO:0000255}. FT VAR_SEQ 1 6 MASTEG -> MVS (in isoform Glt-1A). FT {ECO:0000303|PubMed:11068035}. FT /FTId=VSP_006266. FT MUTAGEN 298 298 K->H,R: Normal transporter activity. FT {ECO:0000269|PubMed:7913472}. FT MUTAGEN 298 298 K->N,T: Reduced transporter activity. FT {ECO:0000269|PubMed:7913472}. FT MUTAGEN 326 326 H->N,T,K,R: No transporter activity. FT {ECO:0000269|PubMed:7913472}. FT CONFLICT 521 521 V -> I (in Ref. 4; AAA93061/AAA93062). FT {ECO:0000305}. SQ SEQUENCE 573 AA; 62106 MW; 8C51D30954E00E7F CRC64; MASTEGANNM PKQVEVRMHD SHLSSEEPKH RNLGMRMCDK LGKNLLLSLT VFGVILGAVC GGLLRLAAPI HPDVVMLIAF PGDILMRMLK MLILPLIISS LITGLSGLDA KASGRLGTRA MVYYMSTTII AAVLGVILVL AIHPGNPKLK KQLGPGKKND EVSSLDAFLD LIRNLFPENL VQACFQQIQT VTKKVLVAPP SEEANTTKAV ISLLNETMNE APEETKIVIK KGLEFKDGMN VLGLIGFFIA FGIAMGKMGE QAKLMVEFFN ILNEIVMKLV IMIMWYSPLG IACLICGKII AIKDLEVVAR QLGMYMITVI VGLIIHGGIF LPLIYFVVTR KNPFSFFAGI FQAWITALGT ASSAGTLPVT FRCLEDNLGI DKRVTRFVLP VGATINMDGT ALYEAVAAIF IAQMNGVILD GGQIVTVSLT ATLASIGAAS IPSAGLVTML LILTAVGLPT EDISLLVAVD WLLDRMRTSV NVVGDSFGAG IVYHLSKSEL DTIDSQHRMH EDIEMTKTQS VYDDTKNHRE SNSNQCVYAA HNSVVIDECK VTLAANGKSA DCSVEEEPWK REK //