VGLU1_MOUSE
ID VGLU1_MOUSE Reviewed; 560 AA.
AC Q3TXX4; E9QMT8;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Vesicular glutamate transporter 1 {ECO:0000303|PubMed:15103023};
DE Short=VGluT1 {ECO:0000303|PubMed:15103023};
DE AltName: Full=Brain-specific Na(+)-dependent inorganic phosphate cotransporter {ECO:0000250|UniProtKB:Q62634};
DE AltName: Full=Solute carrier family 17 member 7;
GN Name=Slc17a7 {ECO:0000312|MGI:MGI:1920211}; Synonyms=Bnpi, Vglut1;
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=Visual cortex;
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 DEVELOPMENTAL STAGE.
RX PubMed=12384506; DOI=10.1074/jbc.m206738200;
RA Schaefer M.K.-H., Varoqui H., Defamie N., Weihe E., Erickson J.D.;
RT "Molecular cloning and functional identification of mouse vesicular
RT glutamate transporter 3 and its expression in subsets of novel excitatory
RT neurons.";
RL J. Biol. Chem. 277:50734-50748(2002).
RN [4]
RP FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=15103023; DOI=10.1073/pnas.0401764101;
RA Wojcik S.M., Rhee J.S., Herzog E., Sigler A., Jahn R., Takamori S.,
RA Brose N., Rosenmund C.;
RT "An essential role for vesicular glutamate transporter 1 (VGLUT1) in
RT postnatal development and control of quantal size.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7158-7163(2004).
RN [5]
RP FUNCTION, DISRUPTION PHENOTYPE, AND DEVELOPMENTAL STAGE.
RX PubMed=15118123; DOI=10.1126/science.1097468;
RA Fremeau R.T. Jr., Kam K., Qureshi T., Johnson J., Copenhagen D.R.,
RA Storm-Mathisen J., Chaudhry F.A., Nicoll R.A., Edwards R.H.;
RT "Vesicular glutamate transporters 1 and 2 target to functionally distinct
RT synaptic release sites.";
RL Science 304:1815-1819(2004).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=16942593; DOI=10.1111/j.1471-4159.2006.04144.x;
RA Herzog E., Takamori S., Jahn R., Brose N., Wojcik S.M.;
RT "Synaptic and vesicular co-localization of the glutamate transporters
RT VGLUT1 and VGLUT2 in the mouse hippocampus.";
RL J. Neurochem. 99:1011-1018(2006).
RN [7]
RP INDUCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=16595674; DOI=10.1074/jbc.m600378200;
RA Yelamanchili S.V., Pendyala G., Brunk I., Darna M., Albrecht U.,
RA Ahnert-Hilger G.;
RT "Differential sorting of the vesicular glutamate transporter 1 into a
RT defined vesicular pool is regulated by light signaling involving the clock
RT gene Period2.";
RL J. Biol. Chem. 281:15671-15679(2006).
RN [8]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=17611277; DOI=10.1523/jneurosci.0815-07.2007;
RA Johnson J., Fremeau R.T. Jr., Duncan J.L., Renteria R.C., Yang H., Hua Z.,
RA Liu X., LaVail M.M., Edwards R.H., Copenhagen D.R.;
RT "Vesicular glutamate transporter 1 is required for photoreceptor synaptic
RT signaling but not for intrinsic visual functions.";
RL J. Neurosci. 27:7245-7255(2007).
RN [9]
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 [10]
RP INTERACTION WITH SHANK3, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=24153177; DOI=10.1038/nature12630;
RA Han K., Holder J.L. Jr., Schaaf C.P., Lu H., Chen H., Kang H., Tang J.,
RA Wu Z., Hao S., Cheung S.W., Yu P., Sun H., Breman A.M., Patel A., Lu H.C.,
RA Zoghbi H.Y.;
RT "SHANK3 overexpression causes manic-like behaviour with unique
RT pharmacogenetic properties.";
RL Nature 503:72-77(2013).
RN [11]
RP FUNCTION, AND TRANSPORTER ACTIVITY.
RX PubMed=25433636; DOI=10.1016/j.neuron.2014.11.008;
RA Preobraschenski J., Zander J.F., Suzuki T., Ahnert-Hilger G., Jahn R.;
RT "Vesicular glutamate transporters use flexible anion and cation binding
RT sites for efficient accumulation of neurotransmitter.";
RL Neuron 84:1287-1301(2014).
RN [12]
RP FUNCTION, TRANSPORTER ACTIVITY, ACTIVITY REGULATION, AND CAUTION.
RX PubMed=29273736; DOI=10.1038/s41467-017-02367-6;
RA Martineau M., Guzman R.E., Fahlke C., Klingauf J.;
RT "VGLUT1 functions as a glutamate/proton exchanger with chloride channel
RT activity in hippocampal glutamatergic synapses.";
RL Nat. Commun. 8:2279-2279(2017).
RN [13]
RP FUNCTION, TRANSPORTER ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP SUBCELLULAR LOCATION.
RX PubMed=29642010; DOI=10.1016/j.celrep.2018.03.055;
RA Preobraschenski J., Cheret C., Ganzella M., Zander J.F., Richter K.,
RA Schenck S., Jahn R., Ahnert-Hilger G.;
RT "Dual and Direction-Selective Mechanisms of Phosphate Transport by the
RT Vesicular Glutamate Transporter.";
RL Cell Rep. 23:535-545(2018).
RN [14]
RP FUNCTION, AND TRANSPORTER ACTIVITY.
RX PubMed=33440152; DOI=10.1016/j.celrep.2020.108623;
RA Cheret C., Ganzella M., Preobraschenski J., Jahn R., Ahnert-Hilger G.;
RT "Vesicular Glutamate Transporters (SLCA17 A6, 7, 8) Control Synaptic
RT Phosphate Levels.";
RL Cell Rep. 34:108623-108623(2021).
CC -!- FUNCTION: Multifunctional transporter that transports L-glutamate as
CC well as multiple ions such as chloride, proton, potassium, sodium and
CC phosphate (PubMed:29642010, PubMed:25433636, PubMed:33440152,
CC PubMed:29273736). At the synaptic vesicle membrane, mainly functions as
CC an uniporter which transports preferentially L-glutamate but also
CC phosphate from the cytoplasm into synaptic vesicles at presynaptic
CC nerve terminals of excitatory neural cells (PubMed:25433636,
CC PubMed:29642010, PubMed:15103023, PubMed:15118123). The L-glutamate or
CC phosphate uniporter activity is electrogenic and is driven by the
CC proton electrochemical gradient, mainly by the electrical gradient
CC established by the vacuolar H(+)-ATPase across the synaptic vesicle
CC membrane (PubMed:29642010). In addition, functions as a chloride
CC channel that allows a chloride permeation through the synaptic vesicle
CC membrane that affects the proton electrochemical gradient and promotes
CC synaptic vesicles acidification (PubMed:25433636, PubMed:29273736,
CC PubMed:29642010). Moreover, may function as a K(+)/H(+) antiport
CC allowing to maintain the electrical gradient and to decrease chemical
CC gradient and therefore sustain vesicular glutamate uptake (By
CC similarity). The vesicular K(+)/H(+) antiport activity is
CC electroneutral (By similarity). At the plasma membrane, following
CC exocytosis, functions as a symporter of Na(+) and phosphate from the
CC extracellular space to the cytoplasm allowing synaptic phosphate
CC homeostasis regulation (PubMed:33440152, PubMed:29642010). The
CC symporter activity is driven by an inside negative membrane potential
CC and is electrogenic (PubMed:29642010). Is necessary for synaptic
CC signaling of visual-evoked responses from photoreceptors
CC (PubMed:17611277). {ECO:0000250|UniProtKB:Q62634,
CC ECO:0000269|PubMed:15103023, ECO:0000269|PubMed:15118123,
CC ECO:0000269|PubMed:17611277, ECO:0000269|PubMed:25433636,
CC ECO:0000269|PubMed:29273736, ECO:0000269|PubMed:29642010,
CC ECO:0000269|PubMed:33440152}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=chloride(in) = chloride(out); Xref=Rhea:RHEA:29823,
CC ChEBI:CHEBI:17996; Evidence={ECO:0000269|PubMed:25433636,
CC ECO:0000269|PubMed:29273736};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3 Na(+)(out) + phosphate(out) = 3 Na(+)(in) + phosphate(in);
CC Xref=Rhea:RHEA:71255, ChEBI:CHEBI:29101, ChEBI:CHEBI:43474;
CC Evidence={ECO:0000269|PubMed:29642010, ECO:0000305|PubMed:33440152};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-glutamate(out) = L-glutamate(in); Xref=Rhea:RHEA:66336,
CC ChEBI:CHEBI:29985; Evidence={ECO:0000269|PubMed:25433636,
CC ECO:0000269|PubMed:29642010};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=phosphate(in) = phosphate(out); Xref=Rhea:RHEA:32823,
CC ChEBI:CHEBI:43474; Evidence={ECO:0000269|PubMed:29642010};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+)(out) + K(+)(in) = H(+)(in) + K(+)(out);
CC Xref=Rhea:RHEA:29467, ChEBI:CHEBI:15378, ChEBI:CHEBI:29103;
CC Evidence={ECO:0000250|UniProtKB:Q62634};
CC -!- ACTIVITY REGULATION: Chloride channel activity is allosterically
CC activated by lumenal H(+) and Cl(-) leading to synaptic vesicles
CC acidification. The L-glutamate transport activity is allosterically
CC activated by lumenal H(+) and Cl(-). The allosteric activation by H(+)
CC efficiently prevents non-vesicular efflux across the plasma membrane,
CC thereby restricting L-glutamate transport activity to acidic membranes
CC such as synaptic vesicles. {ECO:0000250|UniProtKB:Q62634}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.09 mM for L-glutamate {ECO:0000269|PubMed:29642010};
CC KM=1.44 mM for L-glutamate (with 300mM of inorganic phosphate)
CC {ECO:0000269|PubMed:29642010};
CC KM=4.3 mM for inorganic phosphate {ECO:0000269|PubMed:29642010};
CC Vmax=1.57 nmol/min/mg enzyme toward L-glutamate
CC {ECO:0000269|PubMed:29642010};
CC Vmax=0.58 nmol/min/mg enzyme toward L-glutamate (with 300mM of
CC inorganic phosphate) {ECO:0000269|PubMed:29642010};
CC Vmax=2.09 nmol/min/mg enzyme toward inorganic phosphate
CC {ECO:0000269|PubMed:29642010};
CC -!- SUBUNIT: Interacts with SHANK3. {ECO:0000269|PubMed:24153177}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic
CC vesicle membrane {ECO:0000269|PubMed:16942593}. Cell membrane
CC {ECO:0000305|PubMed:29642010}; Multi-pass membrane protein
CC {ECO:0000305}. Synapse, synaptosome {ECO:0000269|PubMed:16595674}.
CC -!- TISSUE SPECIFICITY: Expressed in hippocampus (at protein level).
CC Expressed in the molecular layer of the cerebellum and in retina.
CC {ECO:0000269|PubMed:15103023, ECO:0000269|PubMed:16595674,
CC ECO:0000269|PubMed:17611277, ECO:0000269|PubMed:24153177}.
CC -!- DEVELOPMENTAL STAGE: Expression in brain increases progressively from
CC four days to adulthood. {ECO:0000269|PubMed:12384506,
CC ECO:0000269|PubMed:15118123}.
CC -!- INDUCTION: Oscillates diurnally in synaptic vesicles (at protein
CC level). {ECO:0000269|PubMed:16595674}.
CC -!- DISRUPTION PHENOTYPE: Mice begin to die 3 weeks after birth. They
CC exhibit a progressive neurological phenotype including blindness, loss
CC of coordination and enhanced startle response. Glutamatergic
CC neurotransmission is drastically reduced due to a decrease in the
CC reserve pool of synaptic vesicles and reduced quantal size. Visual
CC signaling from photoreceptors to retinal output neurons is impaired
CC while photoentrainment and pupillary light responses remain intact.
CC {ECO:0000269|PubMed:15103023, ECO:0000269|PubMed:15118123,
CC ECO:0000269|PubMed:17611277}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. Sodium/anion
CC cotransporter family. VGLUT subfamily. {ECO:0000305}.
CC -!- CAUTION: Martineau M. et al. show that may function as a L-
CC glutamate/H(+) antiporter (PubMed:29273736). However, according to
CC Eriksen J. et al., H(+) is an allosteric activator (By similarity).
CC {ECO:0000250|UniProtKB:Q62634, ECO:0000269|PubMed:29273736}.
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DR EMBL; AK159064; BAE34790.1; -; mRNA.
DR EMBL; AC149868; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS52244.1; -.
DR RefSeq; NP_892038.2; NM_182993.2.
DR AlphaFoldDB; Q3TXX4; -.
DR SMR; Q3TXX4; -.
DR BioGRID; 215675; 20.
DR IntAct; Q3TXX4; 2.
DR MINT; Q3TXX4; -.
DR STRING; 10090.ENSMUSP00000082489; -.
DR iPTMnet; Q3TXX4; -.
DR PhosphoSitePlus; Q3TXX4; -.
DR SwissPalm; Q3TXX4; -.
DR MaxQB; Q3TXX4; -.
DR PaxDb; Q3TXX4; -.
DR PeptideAtlas; Q3TXX4; -.
DR PRIDE; Q3TXX4; -.
DR ProteomicsDB; 298280; -.
DR ABCD; Q3TXX4; 1 sequenced antibody.
DR Antibodypedia; 31998; 246 antibodies from 31 providers.
DR DNASU; 72961; -.
DR Ensembl; ENSMUST00000085374; ENSMUSP00000082489; ENSMUSG00000070570.
DR GeneID; 72961; -.
DR KEGG; mmu:72961; -.
DR UCSC; uc009gtx.2; mouse.
DR CTD; 57030; -.
DR MGI; MGI:1920211; Slc17a7.
DR VEuPathDB; HostDB:ENSMUSG00000070570; -.
DR eggNOG; KOG2532; Eukaryota.
DR GeneTree; ENSGT00940000159110; -.
DR HOGENOM; CLU_001265_5_0_1; -.
DR InParanoid; Q3TXX4; -.
DR OMA; WFPAYLV; -.
DR OrthoDB; 497052at2759; -.
DR PhylomeDB; Q3TXX4; -.
DR TreeFam; TF313535; -.
DR Reactome; R-MMU-210500; Glutamate Neurotransmitter Release Cycle.
DR Reactome; R-MMU-428643; Organic anion transporters.
DR BioGRID-ORCS; 72961; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Slc17a7; mouse.
DR PRO; PR:Q3TXX4; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q3TXX4; protein.
DR Bgee; ENSMUSG00000070570; Expressed in retinal neural layer and 82 other tissues.
DR ExpressionAtlas; Q3TXX4; baseline and differential.
DR Genevisible; Q3TXX4; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0044300; C:cerebellar mossy fiber; IDA:MGI.
DR GO; GO:0060076; C:excitatory synapse; IDA:MGI.
DR GO; GO:0016021; C:integral component of membrane; ISO:MGI.
DR GO; GO:0030285; C:integral component of synaptic vesicle membrane; ISO:MGI.
DR GO; GO:0043229; C:intracellular organelle; ISO:MGI.
DR GO; GO:0098794; C:postsynapse; IEA:GOC.
DR GO; GO:0048786; C:presynaptic active zone; IDA:BHF-UCL.
DR GO; GO:0045202; C:synapse; IDA:MGI.
DR GO; GO:0008021; C:synaptic vesicle; IDA:MGI.
DR GO; GO:0030672; C:synaptic vesicle membrane; IDA:MGI.
DR GO; GO:0005254; F:chloride channel activity; IDA:UniProtKB.
DR GO; GO:0008068; F:extracellularly glutamate-gated chloride channel activity; IDA:MGI.
DR GO; GO:0005315; F:inorganic phosphate transmembrane transporter activity; ISO:MGI.
DR GO; GO:0005313; F:L-glutamate transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0005326; F:neurotransmitter transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015386; F:potassium:proton antiporter activity; ISS:UniProtKB.
DR GO; GO:0015319; F:sodium:inorganic phosphate symporter activity; ISO:MGI.
DR GO; GO:0005436; F:sodium:phosphate symporter activity; IDA:UniProtKB.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0006820; P:anion transport; IBA:GO_Central.
DR GO; GO:0007268; P:chemical synaptic transmission; IMP:MGI.
DR GO; GO:0051649; P:establishment of localization in cell; IMP:MGI.
DR GO; GO:0060079; P:excitatory postsynaptic potential; IMP:MGI.
DR GO; GO:0051938; P:L-glutamate import; IDA:MGI.
DR GO; GO:0015813; P:L-glutamate transmembrane transport; IDA:UniProtKB.
DR GO; GO:0007616; P:long-term memory; IMP:MGI.
DR GO; GO:0051651; P:maintenance of location in cell; IMP:MGI.
DR GO; GO:0098700; P:neurotransmitter loading into synaptic vesicle; IDA:SynGO.
DR GO; GO:0055062; P:phosphate ion homeostasis; IDA:UniProtKB.
DR GO; GO:0035435; P:phosphate ion transmembrane transport; IDA:UniProtKB.
DR GO; GO:0006817; P:phosphate ion transport; ISO:MGI.
DR GO; GO:0050803; P:regulation of synapse structure or activity; IBA:GO_Central.
DR GO; GO:1900242; P:regulation of synaptic vesicle endocytosis; ISO:MGI.
DR GO; GO:0042137; P:sequestering of neurotransmitter; IMP:MGI.
DR GO; GO:0044341; P:sodium-dependent phosphate transport; IDA:UniProtKB.
DR GO; GO:0035249; P:synaptic transmission, glutamatergic; IMP:MGI.
DR GO; GO:0097401; P:synaptic vesicle lumen acidification; IMP:MGI.
DR Gene3D; 1.20.1250.20; -; 2.
DR InterPro; IPR011701; MFS.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR036259; MFS_trans_sf.
DR Pfam; PF07690; MFS_1; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
DR PROSITE; PS50850; MFS; 1.
PE 1: Evidence at protein level;
KW Antiport; Cell membrane; Chloride; Chloride channel; Cytoplasmic vesicle;
KW Ion channel; Ion transport; Membrane; Neurotransmitter transport;
KW Phosphate transport; Phosphoprotein; Reference proteome;
KW Sensory transduction; Sodium; Sodium transport; Symport; Synapse;
KW Synaptosome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..560
FT /note="Vesicular glutamate transporter 1"
FT /id="PRO_0000331612"
FT TOPO_DOM 1..63
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 64..84
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 85..116
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 117..137
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 138..140
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 141..161
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 162..169
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 170..190
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 191..208
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 209..229
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 230..236
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 237..257
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 258..302
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 303..323
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 324..341
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 342..362
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 363..378
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 379..399
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 400..401
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 402..422
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 423..435
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 436..456
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 457..469
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 470..490
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 491..560
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 497..560
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 504
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q62634"
FT CONFLICT 500
FT /note="P -> Q (in Ref. 1; BAE34790)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 560 AA; 61637 MW; E866668F606B8305 CRC64;
MEFRQEEFRK LAGRALGRLH RLLEKRQEGA ETLELSADGR PVTTHTRDPP VVDCTCFGLP
RRYIIAIMSG LGFCISFGIR CNLGVAIVSM VNNSTTHRGG HVVVQKAQFN WDPETVGLIH
GSFFWGYIVT QIPGGFICQK FAANRVFGFA IVATSTLNML IPSAARVHYG CVIFVRILQG
LVEGVTYPAC HGIWSKWAPP LERSRLATTA FCGSYAGAVV AMPLAGVLVQ YSGWSSVFYV
YGSFGIFWYL FWLLVSYESP ALHPSISEEE RKYIEDAIGE SAKLMNPVTK FNTPWRRFFT
SMPVYAIIVA NFCRSWTFYL LLISQPAYFE EVFGFEISKV GLVSALPHLV MTIIVPIGGQ
IADFLRSRHI MSTTNVRKLM NCGGFGMEAT LLLVVGYSHS KGVAISFLVL AVGFSGFAIS
GFNVNHLDIA PRYASILMGI SNGVGTLSGM VCPIIVGAMT KHKTREEWQY VFLIASLVHY
GGVIFYGVFA SGEKQPWAEP EEMSEEKCGF VGHDQLAGSD ESEMEDEAEP PGAPPAPPPS
YGATHSTVQP PRPPPPVRDY
