VGLU2_BOVIN
ID VGLU2_BOVIN Reviewed; 582 AA.
AC A6QLI1;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Vesicular glutamate transporter 2 {ECO:0000250|UniProtKB:Q9P2U8};
DE Short=VGluT2 {ECO:0000250|UniProtKB:Q9P2U8};
DE AltName: Full=Solute carrier family 17 member 6;
GN Name=SLC17A6 {ECO:0000250|UniProtKB:Q9P2U8}; Synonyms=VGLUT2;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Thalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2007) 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 a
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 therefore
CC affects the proton electrochemical gradient and promotes synaptic
CC vesicles acidification. Moreover, functions as a vesicular K(+)/H(+)
CC antiport allowing to maintain the electrical gradient and to decrease
CC chemical gradient and therefore sustain vesicular L-glutamate uptake.
CC The vesicular H(+)/H(+) antiport activity is electroneutral. At the
CC plasma membrane, following exocytosis, functions as a symporter of
CC Na(+) and phosphate from the extracellular space to the cytoplasm
CC allowing synaptic phosphate homeostasis regulation. The symporter
CC activity is driven by an inside negative membrane potential and is
CC electrogenic (By similarity). Also involved in the regulation of
CC retinal hyaloid vessel regression during postnatal development (By
CC similarity). May also play a role in the endocrine L-glutamatergic
CC system of other tissues such as pineal gland and pancreas (By
CC similarity). {ECO:0000250|UniProtKB:Q8BLE7,
CC ECO:0000250|UniProtKB:Q9JI12}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-glutamate(out) = L-glutamate(in); Xref=Rhea:RHEA:66336,
CC ChEBI:CHEBI:29985; Evidence={ECO:0000250|UniProtKB:Q9JI12};
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:Q9JI12};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=phosphate(in) = phosphate(out); Xref=Rhea:RHEA:32823,
CC ChEBI:CHEBI:43474; Evidence={ECO:0000250|UniProtKB:Q9JI12};
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:Q9JI12};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=chloride(in) = chloride(out); Xref=Rhea:RHEA:29823,
CC ChEBI:CHEBI:17996; Evidence={ECO:0000250|UniProtKB:Q9JI12};
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 requirement for
CC H(+) efficiently prevents non-vesicular efflux across the plasma
CC membrane. The L-glutamate uniporter activity exhibits a biphasic
CC dependence on chloride concentration. {ECO:0000250|UniProtKB:Q9JI12}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic
CC vesicle membrane {ECO:0000250|UniProtKB:Q8BLE7}; Multi-pass membrane
CC protein {ECO:0000255}. Synapse, synaptosome
CC {ECO:0000250|UniProtKB:Q8BLE7}. Cell membrane
CC {ECO:0000250|UniProtKB:Q8BLE7}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. Sodium/anion
CC cotransporter family. VGLUT 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; BC147973; AAI47974.1; -; mRNA.
DR RefSeq; NP_001096580.1; NM_001103110.1.
DR AlphaFoldDB; A6QLI1; -.
DR SMR; A6QLI1; -.
DR STRING; 9913.ENSBTAP00000007935; -.
DR PaxDb; A6QLI1; -.
DR PRIDE; A6QLI1; -.
DR Ensembl; ENSBTAT00000007935; ENSBTAP00000007935; ENSBTAG00000038347.
DR GeneID; 100125225; -.
DR KEGG; bta:100125225; -.
DR CTD; 57084; -.
DR VEuPathDB; HostDB:ENSBTAG00000038347; -.
DR VGNC; VGNC:34701; SLC17A6.
DR eggNOG; KOG2532; Eukaryota.
DR GeneTree; ENSGT00940000155891; -.
DR HOGENOM; CLU_001265_5_0_1; -.
DR InParanoid; A6QLI1; -.
DR OMA; YNEQSQM; -.
DR OrthoDB; 497052at2759; -.
DR TreeFam; TF313535; -.
DR Reactome; R-BTA-428643; Organic anion transporters.
DR Proteomes; UP000009136; Chromosome 29.
DR Bgee; ENSBTAG00000038347; Expressed in midbrain and 19 other tissues.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0060076; C:excitatory synapse; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0030285; C:integral component of synaptic vesicle membrane; IBA:GO_Central.
DR GO; GO:0043005; C:neuron projection; ISS:UniProtKB.
DR GO; GO:0008021; C:synaptic vesicle; ISS:UniProtKB.
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:0022810; F:membrane potential driven uniporter activity; ISS: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:0005436; F:sodium:phosphate symporter activity; ISS: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:1990384; P:hyaloid vascular plexus regression; ISS:UniProtKB.
DR GO; GO:0051938; P:L-glutamate import; ISS:UniProtKB.
DR GO; GO:0015813; P:L-glutamate transmembrane transport; ISS:UniProtKB.
DR GO; GO:0098700; P:neurotransmitter loading into synaptic vesicle; IBA:GO_Central.
DR GO; GO:0055062; P:phosphate ion homeostasis; ISS:UniProtKB.
DR GO; GO:0050803; P:regulation of synapse structure or activity; IBA:GO_Central.
DR GO; GO:0044341; P:sodium-dependent phosphate transport; ISS:UniProtKB.
DR GO; GO:0035249; P:synaptic transmission, glutamatergic; IBA:GO_Central.
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..582
FT /note="Vesicular glutamate transporter 2"
FT /id="PRO_0000318168"
FT TOPO_DOM 1..71
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 72..92
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 93..125
FT /note="Vesicular"
FT /evidence="ECO:0000255"
FT TRANSMEM 126..146
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 147..148
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 149..169
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 170..177
FT /note="Vesicular"
FT /evidence="ECO:0000255"
FT TRANSMEM 178..198
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 199..216
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 217..237
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 238..244
FT /note="Vesicular"
FT /evidence="ECO:0000255"
FT TRANSMEM 245..265
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 266..310
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 311..331
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 332..349
FT /note="Vesicular"
FT /evidence="ECO:0000255"
FT TRANSMEM 350..370
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 371..386
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 387..407
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 408..409
FT /note="Vesicular"
FT /evidence="ECO:0000255"
FT TRANSMEM 410..430
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 431..443
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 444..464
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 465..477
FT /note="Vesicular"
FT /evidence="ECO:0000255"
FT TRANSMEM 478..498
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 499..582
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 100
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 101
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 470
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 582 AA; 64546 MW; B3D6FAE6E7B7BD9C CRC64;
MESVKQRILT PGKEGLKNFA GKSLGQIYRV LEKKQDAGET IELTEDGKPL EVPEKKAPLC
DCTCFGLPRR YIIAIMSGLG FCISFGIRCN LGVAIVDMVN NSTIHRGGKV IKEKAKFNWD
PETVGMIHGS FFWGYIITQI PGGYIASRLA ANRVFGAAIL LTSTLNMLIP SAARVHYGCV
IFVRILQGLV EGVTYPACHG IWSKWAPPLE RSRLATTSFC GSYAGAVIAM PLAGILVQYT
GWSSVFYVYG SFGMIWYMFW LLVSYESPAK HPTITDEERR YIEESIGESA NLLGAMEKFK
TPWRKFFTSM PVYAIIVANF CRSWTFYLLL ISQPAYFEEV FGFEISKVGM LSAVPHLVMT
IIVPIGGQIA DFLRSKQILS TTTVRKIMNC GGFGMEATLL LVVGYSHTRG VAISFLVLAV
GFSGFAISGF NVNHLDIAPR YASILMGISN GVGTLSGMVC PIIVGAMTKN KSREEWQYVF
LIAALVHYGG VIFYAIFASG EKQPWADPEE TSEEKCGFIH EDELDEETGD ITQNYINYGT
TKSYGATTQA NGGWPNGWEK KEEFVQEEVQ NSYNYKDRDD YS
