VGLU1_XENLA
ID VGLU1_XENLA Reviewed; 576 AA.
AC Q6INC8;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Vesicular glutamate transporter 1 {ECO:0000250|UniProtKB:Q3TXX4};
DE Short=VGluT1 {ECO:0000250|UniProtKB:Q3TXX4};
DE AltName: Full=Solute carrier family 17 member 7;
GN Name=slc17a7 {ECO:0000250|UniProtKB:Q3TXX4}; Synonyms=vglut1;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Multifunctional transporter that transports L-glutamate as
CC well as multiple ions such as chloride, proton, potassium, sodium and
CC phosphate. At the synaptic vesicle membrane, mainly functions as an
CC 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. 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. In addition, functions as a chloride channel that allows a
CC chloride permeation through the synaptic vesicle membrane that affects
CC the proton electrochemical gradient and promotes synaptic vesicles
CC acidification. Moreover, may function as a K(+)/H(+) antiport allowing
CC to maintain the electrical gradient and to decrease chemical gradient
CC and therefore sustain vesicular glutamate uptake. The vesicular
CC K(+)/H(+) antiport activity is electroneutral. At the plasma membrane,
CC following exocytosis, functions as a symporter of Na(+) and phosphate
CC from the extracellular space to the cytoplasm allowing synaptic
CC phosphate homeostasis regulation. The symporter activity is driven by
CC an inside negative membrane potential and is electrogenic (By
CC similarity). Is necessary for synaptic signaling of visual-evoked
CC responses from photoreceptors (By similarity).
CC {ECO:0000250|UniProtKB:Q3TXX4, ECO:0000250|UniProtKB:Q62634}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-glutamate(out) = L-glutamate(in); Xref=Rhea:RHEA:66336,
CC ChEBI:CHEBI:29985; Evidence={ECO:0000250|UniProtKB:Q62634};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=chloride(in) = chloride(out); Xref=Rhea:RHEA:29823,
CC ChEBI:CHEBI:17996; Evidence={ECO:0000250|UniProtKB:Q62634};
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:0000250|UniProtKB:Q62634};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=phosphate(in) = phosphate(out); Xref=Rhea:RHEA:32823,
CC ChEBI:CHEBI:43474; Evidence={ECO:0000250|UniProtKB:Q62634};
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 -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic
CC vesicle membrane {ECO:0000250|UniProtKB:Q62634}. Cell membrane
CC {ECO:0000250|UniProtKB:Q62634}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q62634}. Synapse, synaptosome
CC {ECO:0000250|UniProtKB:Q62634}.
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 (By similarity). However, according to
CC Eriksen J. et al., H(+) is an allosteric activator (By similarity).
CC {ECO:0000250|UniProtKB:Q3TXX4, ECO:0000250|UniProtKB:Q62634}.
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DR EMBL; BC072355; AAH72355.1; -; mRNA.
DR RefSeq; NP_001085081.1; NM_001091612.1.
DR AlphaFoldDB; Q6INC8; -.
DR SMR; Q6INC8; -.
DR DNASU; 432152; -.
DR GeneID; 432152; -.
DR CTD; 432152; -.
DR Xenbase; XB-GENE-6493995; slc17a7.S.
DR OMA; FACVICV; -.
DR OrthoDB; 497052at2759; -.
DR Proteomes; UP000186698; Genome assembly.
DR Bgee; 432152; Expressed in brain and 5 other tissues.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043005; C:neuron projection; IEA:UniProtKB-KW.
DR GO; GO:0030672; C:synaptic vesicle membrane; ISS:UniProtKB.
DR GO; GO:0005254; F:chloride channel activity; ISS:UniProtKB.
DR GO; GO:0005313; F:L-glutamate transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0015386; F:potassium:proton antiporter activity; ISS:UniProtKB.
DR GO; GO:0005436; F:sodium:phosphate symporter activity; ISS:UniProtKB.
DR GO; GO:0015813; P:L-glutamate transmembrane transport; ISS:UniProtKB.
DR GO; GO:0006836; P:neurotransmitter transport; IEA:UniProtKB-KW.
DR GO; GO:0044341; P:sodium-dependent phosphate transport; ISS:UniProtKB.
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 2: Evidence at transcript level;
KW Antiport; Cell membrane; Chloride; Chloride channel; Cytoplasmic vesicle;
KW Glycoprotein; Ion channel; Ion transport; Membrane;
KW Neurotransmitter transport; Phosphate transport; Reference proteome;
KW Sodium; Sodium transport; Symport; Synapse; Synaptosome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..576
FT /note="Vesicular glutamate transporter 1"
FT /id="PRO_0000318174"
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="Vesicular"
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..168
FT /note="Vesicular"
FT /evidence="ECO:0000255"
FT TRANSMEM 169..189
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 190..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="Vesicular"
FT /evidence="ECO:0000255"
FT TRANSMEM 237..257
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 258..297
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 298..320
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 321..341
FT /note="Vesicular"
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="Vesicular"
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="Vesicular"
FT /evidence="ECO:0000255"
FT TRANSMEM 470..490
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 491..576
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 517..552
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 525..547
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 93
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 576 AA; 63906 MW; 93C2157CFB15CB62 CRC64;
MEFRKEEFKK LAGNTLGHLH RILEKKQKNG ETIELTEEGQ PVVKEEKHQP VVDCTCFGLP
RRYIIAIMSG LGFCISFGIR CNLGVAIVSM VNNNTVYKGN KLVIEQAQFN WDPETVGMIH
GSFFWGYIVT QIPGGYICQK FAANRVFGFA IVATSTLNML IPSAARVHFA CVICVRILQG
LVEGVTYPAC HGIWSKWAPP LERSRLATTA FCGSYAGAVV AMPLAGVLVQ YSGWSSVFYV
YGSFGITWYM FWILVSYESP AQHPTISEEE RKYIEESIGE STGFMNPMAK FKAPWRKFFT
SMPVYAIIVA NFCRSWTFYL LLISQPAYFE EVFGFAISKV GLLSALPHLV MTIIVPIGGQ
IADFLRTKRI MSTTNVRKMM NCGGFGMEAT LLLVVGYSHS RGVAISFLVL AVGFSGFAIS
GFNVNHLDIA PRYASILMGI SNGVGTLSGM VCPLIVGAMT KHKTREEWQY VFLIASLVHY
GGVVFYGIFA SGEKQPWAEP EETSDEKCGF IHEDELADES EEQTQAHGGY GSYGATQTTS
QQNGGWATDW EKKDEFIQDQ GKDPYLYGTV AERDLS
