ID EAA5_MOUSE Reviewed; 559 AA.
AC Q8JZR4; A2A8F0;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 24-JAN-2024, entry version 140.
DE RecName: Full=Excitatory amino acid transporter 5 {ECO:0000305};
DE AltName: Full=Solute carrier family 1 member 7;
GN Name=Slc1a7 {ECO:0000312|MGI:MGI:2444087};
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Retina;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
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 [4]
RP TISSUE SPECIFICITY, SUBCELLULAR LOCATION, FUNCTION, AND TRANSPORTER
RP ACTIVITY.
RX PubMed=16973698; DOI=10.1113/jphysiol.2006.118281;
RA Wersinger E., Schwab Y., Sahel J.A., Rendon A., Pow D.V., Picaud S.,
RA Roux M.J.;
RT "The glutamate transporter EAAT5 works as a presynaptic receptor in mouse
RT rod bipolar cells.";
RL J. Physiol. (Lond.) 577:221-234(2006).
RN [5]
RP FUNCTION, TRANSPORTER ACTIVITY, AND TISSUE SPECIFICITY.
RX PubMed=32233906; DOI=10.1152/jn.00527.2019;
RA Bligard G.W., DeBrecht J., Smith R.G., Lukasiewicz P.D.;
RT "Light-evoked glutamate transporter EAAT5 activation coordinates with
RT conventional feedback inhibition to control rod bipolar cell output.";
RL J. Neurophysiol. 123:1828-1837(2020).
CC -!- FUNCTION: Sodium-dependent, high-affinity amino acid transporter that
CC mediates the uptake of L-glutamate and also L-aspartate and D-
CC aspartate. Functions as a symporter that transports one amino acid
CC molecule together with two or three Na(+) ions and one proton, in
CC parallel with the counter-transport of one K(+) ion (By similarity).
CC Acts primarily as an inhibitory glutamate-gated chloride channel being
CC a major inhibitory presynaptic receptor at mammalian rod bipolar cell
CC axon terminals. Glutamate binding gates a large Cl(-) conductance that
CC mediates inhibition, affecting visual processing in the retina
CC (PubMed:16973698, PubMed:32233906). {ECO:0000250|UniProtKB:O00341,
CC ECO:0000269|PubMed:16973698, ECO:0000269|PubMed:32233906}.
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:0000269|PubMed:16973698, ECO:0000269|PubMed:32233906};
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:O00341};
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:O00341};
CC -!- SUBUNIT: Interacts with the PDZ domains of DLG4.
CC {ECO:0000250|UniProtKB:O00341}.
CC -!- SUBCELLULAR LOCATION: Photoreceptor inner segment membrane
CC {ECO:0000269|PubMed:16973698}; Multi-pass membrane protein
CC {ECO:0000255}. Synaptic cell membrane {ECO:0000269|PubMed:16973698};
CC Multi-pass membrane protein {ECO:0000255}. Note=Located in both cone
CC and rod photoreceptor terminals and in axon terminals of rod bipolar
CC cells. {ECO:0000269|PubMed:16973698}.
CC -!- TISSUE SPECIFICITY: Expressed in retina, located in both cone and rod
CC photoreceptor terminals and in axon terminals of rod bipolar cells.
CC {ECO:0000269|PubMed:32233906}.
CC -!- SIMILARITY: Belongs to the dicarboxylate/amino acid:cation symporter
CC (DAACS) (TC 2.A.23) family. SLC1A7 subfamily. {ECO:0000305}.
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DR EMBL; AK044586; BAC31989.1; -; mRNA.
DR EMBL; AK044671; BAC32027.1; -; mRNA.
DR EMBL; AL611936; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC030400; AAH30400.1; -; mRNA.
DR CCDS; CCDS18444.3; -.
DR RefSeq; NP_666367.2; NM_146255.2.
DR AlphaFoldDB; Q8JZR4; -.
DR SMR; Q8JZR4; -.
DR STRING; 10090.ENSMUSP00000158982; -.
DR GlyCosmos; Q8JZR4; 2 sites, No reported glycans.
DR GlyGen; Q8JZR4; 2 sites.
DR iPTMnet; Q8JZR4; -.
DR PhosphoSitePlus; Q8JZR4; -.
DR PaxDb; 10090-ENSMUSP00000102324; -.
DR ProteomicsDB; 277750; -.
DR Antibodypedia; 46889; 166 antibodies from 22 providers.
DR DNASU; 242607; -.
DR Ensembl; ENSMUST00000106713.5; ENSMUSP00000102324.5; ENSMUSG00000008932.11.
DR GeneID; 242607; -.
DR KEGG; mmu:242607; -.
DR AGR; MGI:2444087; -.
DR CTD; 6512; -.
DR MGI; MGI:2444087; Slc1a7.
DR VEuPathDB; HostDB:ENSMUSG00000008932; -.
DR eggNOG; KOG3787; Eukaryota.
DR GeneTree; ENSGT00940000156073; -.
DR InParanoid; Q8JZR4; -.
DR OrthoDB; 49426at2759; -.
DR PhylomeDB; Q8JZR4; -.
DR TreeFam; TF315206; -.
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; 242607; 2 hits in 80 CRISPR screens.
DR ChiTaRS; Slc1a7; mouse.
DR PRO; PR:Q8JZR4; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q8JZR4; Protein.
DR Bgee; ENSMUSG00000008932; Expressed in retinal neural layer and 17 other cell types or tissues.
DR ExpressionAtlas; Q8JZR4; baseline and differential.
DR GO; GO:0043679; C:axon terminus; IDA:UniProtKB.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:1990796; C:photoreceptor cell terminal bouton; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0045211; C:postsynaptic membrane; IDA:SynGO.
DR GO; GO:0042734; C:presynaptic membrane; IDA:SynGO.
DR GO; GO:0008068; F:extracellularly glutamate-gated chloride channel activity; IDA:UniProtKB.
DR GO; GO:0015501; F:glutamate:sodium symporter activity; IDA:UniProtKB.
DR GO; GO:0005313; F:L-glutamate transmembrane transporter activity; IDA:MGI.
DR GO; GO:0008509; F:monoatomic anion transmembrane transporter activity; IDA:MGI.
DR GO; GO:0015175; F:neutral L-amino acid transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:1902476; P:chloride transmembrane transport; IDA:UniProtKB.
DR GO; GO:0015813; P:L-glutamate transmembrane transport; IDA:UniProtKB.
DR GO; GO:0098656; P:monoatomic anion transmembrane transport; IDA:MGI.
DR GO; GO:0001504; P:neurotransmitter uptake; ISO:MGI.
DR Gene3D; 1.10.3860.10; Sodium:dicarboxylate symporter; 1.
DR InterPro; IPR001991; Na-dicarboxylate_symporter.
DR InterPro; IPR018107; Na-dicarboxylate_symporter_CS.
DR InterPro; IPR036458; Na:dicarbo_symporter_sf.
DR PANTHER; PTHR11958:SF22; EXCITATORY AMINO ACID TRANSPORTER 5; 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 2: Evidence at transcript level;
KW Cell membrane; Glycoprotein; Membrane; Reference proteome; Symport;
KW Synapse; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..559
FT /note="Excitatory amino acid transporter 5"
FT /id="PRO_0000284451"
FT TOPO_DOM 1..16
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 17..37
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 60..80
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 94..114
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 115..215
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 216..236
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 259..279
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 298..318
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 329..349
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 371..391
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 413..433
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 456..476
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CARBOHYD 190
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 253
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 559 AA; 60106 MW; BEC713C884E27187 CRC64;
MVLDAVLARG RTVCKHNGLL ILSVLSVIVG CLLGFFLRTQ RLSPQEISYF QFPGELLMRM
LKMLILPLVV SSLMSGLASL DAKTSSRLGI LTVAYYLWTT FLAVVVGIIM VSIIHPGGAA
QKETTEQSGK PVMSSADALL DLVRNMFPAN LVEATFKQYR TKTTPVIKSP RGAAEEAPRR
IVIYGVQEDN GSRVQNFALD LTPPPEIVYK SEPGTSDGMN VLGIVIFSAT MGIMLGRMGD
SGTPLVSFCQ CLNESVMKIV AVAGWYFPFG IVFLIAGKIL EMDDPKAVGK KLGFYAVTVV
CGLVVHGLLI LPLLYFLITK KNPIVFIRGV LQALLIALAT SSSSATLPIT FKCLLENNHI
DRRIARFVLP VGATINMDGT ALYEAVAAIF IAQVNNYELD FGQIITISIT ATAASIGAAG
IPQAGLVTMV IVLTSVGLPT DDINLIIAVD WALDRFRTMI NVLGDALAAG IMAHICRKDF
AQDMGTEKLL PCETKPVTLQ EIVAAQQNGC VKSVAEASEL TLGPTCPHHI PVQVEQDEDP
AAASLDHCTI EISELETNV
//
