VGLU1_RAT
ID VGLU1_RAT Reviewed; 560 AA.
AC Q62634; A9LRT0;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Vesicular glutamate transporter 1 {ECO:0000303|PubMed:16987242};
DE Short=VGluT1 {ECO:0000303|PubMed:16987242};
DE AltName: Full=Brain-specific Na(+)-dependent inorganic phosphate cotransporter {ECO:0000303|PubMed:8202535};
DE AltName: Full=Solute carrier family 17 member 7;
GN Name=Slc17a7 {ECO:0000312|RGD:620101}; Synonyms=Bnpi, Vglut1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, AND
RP INDUCTION.
RX PubMed=8202535; DOI=10.1073/pnas.91.12.5607;
RA Ni B., Rosteck P.R. Jr., Nadi N.S., Paul S.M.;
RT "Cloning and expression of a cDNA encoding a brain-specific Na(+)-dependent
RT inorganic phosphate cotransporter.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:5607-5611(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC STRAIN=Sprague-Dawley;
RX PubMed=16987242; DOI=10.1111/j.1471-4159.2006.04049.x;
RA Nogami H., Ogasawara K., Mimura Y., Mogi K., Shutoh F., Hisano S.;
RT "Developmentally-regulated expression of tissue-specific splice variant of
RT rat vesicular glutamate transporter 1 in retina and pineal gland.";
RL J. Neurochem. 99:142-153(2006).
RN [3]
RP PROTEIN SEQUENCE OF 99-106; 197-203 AND 291-196, FUNCTION, AND SUBCELLULAR
RP LOCATION.
RX PubMed=11001057; DOI=10.1038/35025070;
RA Takamori S., Rhee J.S., Rosenmund C., Jahn R.;
RT "Identification of a vesicular glutamate transporter that defines a
RT glutamatergic phenotype in neurons.";
RL Nature 407:189-194(2000).
RN [4]
RP FUNCTION, TRANSPORTER ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=10938000; DOI=10.1126/science.289.5481.957;
RA Bellocchio E.E., Reimer R.J., Fremeau R.T. Jr., Edwards R.H.;
RT "Uptake of glutamate into synaptic vesicles by an inorganic phosphate
RT transporter.";
RL Science 289:957-960(2000).
RN [5]
RP FUNCTION, TRANSPORTER ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=11698619; DOI=10.1523/jneurosci.21-22-j0001.2001;
RA Herzog E., Bellenchi G.C., Gras C., Bernard V., Ravassard P., Bedet C.,
RA Gasnier B., Giros B., El Mestikawy S.;
RT "The existence of a second vesicular glutamate transporter specifies
RT subpopulations of glutamatergic neurons.";
RL J. Neurosci. 21:RC181-RC181(2001).
RN [6]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=11698620; DOI=10.1523/jneurosci.21-22-j0002.2001;
RA Takamori S., Rhee J.S., Rosenmund C., Jahn R.;
RT "Identification of differentiation-associated brain-specific phosphate
RT transporter as a second vesicular glutamate transporter (VGLUT2).";
RL J. Neurosci. 21:RC182-RC182(2001).
RN [7]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=11502256; DOI=10.1016/s0896-6273(01)00344-0;
RA Fremeau R.T. Jr., Troyer M.D., Pahner I., Nygaard G.O., Tran C.H.,
RA Reimer R.J., Bellocchio E.E., Fortin D., Storm-Mathisen J., Edwards R.H.;
RT "The expression of vesicular glutamate transporters defines two classes of
RT excitatory synapse.";
RL Neuron 31:247-260(2001).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=18278042; DOI=10.1038/nn2052;
RA Gras C., Amilhon B., Lepicard E.M., Poirel O., Vinatier J., Herbin M.,
RA Dumas S., Tzavara E.T., Wade M.R., Nomikos G.G., Hanoun N., Saurini F.,
RA Kemel M.-L., Gasnier B., Giros B., Mestikawy S.E.;
RT "The vesicular glutamate transporter VGLUT3 synergizes striatal
RT acetylcholine tone.";
RL Nat. Neurosci. 11:292-300(2008).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=17110340; DOI=10.1016/j.cell.2006.10.030;
RA Takamori S., Holt M., Stenius K., Lemke E.A., Groenborg M., Riedel D.,
RA Urlaub H., Schenck S., Bruegger B., Ringler P., Mueller S.A., Rammner B.,
RA Graeter F., Hub J.S., De Groot B.L., Mieskes G., Moriyama Y., Klingauf J.,
RA Grubmueller H., Heuser J., Wieland F., Jahn R.;
RT "Molecular anatomy of a trafficking organelle.";
RL Cell 127:831-846(2006).
RN [10]
RP FUNCTION, AND TRANSPORTER ACTIVITY.
RX PubMed=18080752; DOI=10.1007/s11064-007-9546-z;
RA Mackenzie B., Illing A.C., Morris M.E.K., Varoqui H., Erickson J.D.;
RT "Analysis of a vesicular glutamate transporter (VGLUT2) supports a cell-
RT leakage mode in addition to vesicular packaging.";
RL Neurochem. Res. 33:238-247(2008).
RN [11]
RP FUNCTION, TRANSPORTER ACTIVITY, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RX PubMed=19169251; DOI=10.1038/nn.2248;
RA Schenck S., Wojcik S.M., Brose N., Takamori S.;
RT "A chloride conductance in VGLUT1 underlies maximal glutamate loading into
RT synaptic vesicles.";
RL Nat. Neurosci. 12:156-162(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-504, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [13]
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 [14]
RP ACTIVITY REGULATION.
RX PubMed=27133463; DOI=10.1016/j.neuron.2016.03.026;
RA Eriksen J., Chang R., McGregor M., Silm K., Suzuki T., Edwards R.H.;
RT "Protons Regulate Vesicular Glutamate Transporters through an Allosteric
RT Mechanism.";
RL Neuron 90:768-780(2016).
RN [15]
RP FUNCTION, TRANSPORTER ACTIVITY, AND 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 [16]
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:11001057, PubMed:10938000, PubMed:18080752,
CC PubMed:19169251, PubMed:8202535, PubMed:27133463, PubMed:25433636,
CC PubMed:33440152, PubMed:29642010, PubMed:11698619). At the synaptic
CC vesicle membrane, mainly functions as an uniporter which transports
CC preferentially L-glutamate but also phosphate from the cytoplasm into
CC synaptic vesicles at presynaptic nerve terminals of excitatory neural
CC cells (PubMed:29642010, PubMed:11001057, PubMed:10938000,
CC PubMed:11698619, PubMed:18080752). The L-glutamate or phosphate
CC uniporter activity is electrogenic and is driven by the proton
CC electrochemical gradient, mainly by the electrical gradient established
CC by the vacuolar H(+)-ATPase across the synaptic vesicle membrane
CC (PubMed:29642010). In addition, functions as a chloride channel that
CC allows a chloride permeation through the synaptic vesicle membrane that
CC affects the proton electrochemical gradient and promotes synaptic
CC vesicles acidification (PubMed:10938000, PubMed:27133463,
CC PubMed:25433636, PubMed:29642010, PubMed:19169251). Moreover, may
CC function as a K(+)/H(+) antiport allowing to maintain the electrical
CC gradient and to decrease chemical gradient and therefore sustain
CC vesicular glutamate uptake (PubMed:25433636). The vesicular K(+)/H(+)
CC antiport activity is electroneutral (PubMed:25433636). At the plasma
CC membrane, following exocytosis, functions as a symporter of Na(+) and
CC phosphate from the extracellular space to the cytoplasm allowing
CC synaptic phosphate homeostasis regulation (PubMed:33440152,
CC PubMed:8202535, PubMed:29642010). The symporter activity is driven by
CC an inside negative membrane potential and is electrogenic
CC (PubMed:29642010). Is necessary for synaptic signaling of visual-evoked
CC responses from photoreceptors (By similarity).
CC {ECO:0000250|UniProtKB:Q3TXX4, ECO:0000269|PubMed:10938000,
CC ECO:0000269|PubMed:11001057, ECO:0000269|PubMed:11698619,
CC ECO:0000269|PubMed:18080752, ECO:0000269|PubMed:19169251,
CC ECO:0000269|PubMed:25433636, ECO:0000269|PubMed:27133463,
CC ECO:0000269|PubMed:29642010, ECO:0000269|PubMed:33440152,
CC ECO:0000269|PubMed:8202535}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-glutamate(out) = L-glutamate(in); Xref=Rhea:RHEA:66336,
CC ChEBI:CHEBI:29985; Evidence={ECO:0000269|PubMed:10938000,
CC ECO:0000269|PubMed:11698619, ECO:0000269|PubMed:18080752,
CC ECO:0000269|PubMed:19169251, ECO:0000269|PubMed:29642010};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=chloride(in) = chloride(out); Xref=Rhea:RHEA:29823,
CC ChEBI:CHEBI:17996; Evidence={ECO:0000269|PubMed:19169251,
CC ECO:0000305|PubMed:10938000};
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=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:0000269|PubMed:25433636};
CC -!- ACTIVITY REGULATION: Chloride channel activity is allosterically
CC activated by lumenal H(+) and Cl(-) leading to synaptic vesicles
CC acidification (PubMed:27133463). The L-glutamate transport activity is
CC allosterically activated by lumenal H(+) and Cl(-) (PubMed:27133463,
CC PubMed:19169251). The allosteric activation by H(+) efficiently
CC prevents non-vesicular efflux across the plasma membrane, thereby
CC restricting L-glutamate transport activity to acidic membranes such as
CC synaptic vesicles (PubMed:27133463). {ECO:0000269|PubMed:19169251,
CC ECO:0000269|PubMed:27133463}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.36 mM for L-glutamate (for gluconate-loaded liposomes)
CC {ECO:0000269|PubMed:19169251};
CC KM=1.86 mM for L-glutamate (for Cl(-)-loaded liposomes)
CC {ECO:0000269|PubMed:19169251};
CC KM=2 mM for L-glutamate {ECO:0000269|PubMed:10938000};
CC KM=3.4 mM for L-glutamate {ECO:0000269|PubMed:11698619};
CC Vmax=23.41 nmol/min/mg enzyme toward L-glutamate(for gluconate-loaded
CC liposomes) {ECO:0000269|PubMed:19169251};
CC Vmax=76.89 nmol/min/mg enzyme toward L-glutamate(for Cl(-)-loaded
CC liposomes) {ECO:0000269|PubMed:19169251};
CC Vmax=500 pmol/min/mg enzyme toward L-glutamate
CC {ECO:0000269|PubMed:11698619};
CC -!- SUBUNIT: Interacts with SHANK3. {ECO:0000250|UniProtKB:Q3TXX4}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic
CC vesicle membrane {ECO:0000269|PubMed:11001057,
CC ECO:0000269|PubMed:11698619}. Cell membrane
CC {ECO:0000305|PubMed:29642010}; Multi-pass membrane protein
CC {ECO:0000305}. Synapse, synaptosome {ECO:0000269|PubMed:11698619}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q62634-1; Sequence=Displayed;
CC Name=2; Synonyms=Vglut1v;
CC IsoId=Q62634-2; Sequence=VSP_033264;
CC -!- TISSUE SPECIFICITY: Expressed in the cerebellum, cerberal cortex and
CC hippocampus. Isoform 2 is expressed specifically in retina.
CC {ECO:0000269|PubMed:11502256, ECO:0000269|PubMed:11698619,
CC ECO:0000269|PubMed:11698620, ECO:0000269|PubMed:16987242,
CC ECO:0000269|PubMed:8202535}.
CC -!- DEVELOPMENTAL STAGE: Expression of isoform 2 increases sharply during
CC the first ten days of postnatal life, and also increases with
CC increasing numbers of rhodopsin cells in the retina.
CC {ECO:0000269|PubMed:16987242}.
CC -!- INDUCTION: Induced within cerebellar granule cells by exposure to N-
CC methyl-D-aspartate (NMDA). {ECO:0000269|PubMed:8202535}.
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 (PubMed:27133463).
CC {ECO:0000250|UniProtKB:Q3TXX4, ECO:0000269|PubMed:27133463}.
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DR EMBL; U07609; AAA19646.1; -; mRNA.
DR EMBL; EU253553; ABX55782.1; -; mRNA.
DR PIR; I59302; I59302.
DR RefSeq; NP_446311.1; NM_053859.2. [Q62634-1]
DR AlphaFoldDB; Q62634; -.
DR SMR; Q62634; -.
DR BioGRID; 250523; 3.
DR IntAct; Q62634; 6.
DR MINT; Q62634; -.
DR STRING; 10116.ENSRNOP00000063604; -.
DR TCDB; 2.A.1.14.13; the major facilitator superfamily (mfs).
DR iPTMnet; Q62634; -.
DR PhosphoSitePlus; Q62634; -.
DR SwissPalm; Q62634; -.
DR PaxDb; Q62634; -.
DR PRIDE; Q62634; -.
DR ABCD; Q62634; 12 sequenced antibodies.
DR Ensembl; ENSRNOT00000028064; ENSRNOP00000028064; ENSRNOG00000020650. [Q62634-1]
DR Ensembl; ENSRNOT00000064184; ENSRNOP00000063604; ENSRNOG00000020650. [Q62634-2]
DR GeneID; 116638; -.
DR KEGG; rno:116638; -.
DR UCSC; RGD:620101; rat. [Q62634-1]
DR CTD; 57030; -.
DR RGD; 620101; Slc17a7.
DR eggNOG; KOG2532; Eukaryota.
DR GeneTree; ENSGT00940000159110; -.
DR HOGENOM; CLU_001265_5_0_1; -.
DR InParanoid; Q62634; -.
DR OMA; WFPAYLV; -.
DR OrthoDB; 497052at2759; -.
DR PhylomeDB; Q62634; -.
DR TreeFam; TF313535; -.
DR Reactome; R-RNO-210500; Glutamate Neurotransmitter Release Cycle.
DR Reactome; R-RNO-428643; Organic anion transporters.
DR PRO; PR:Q62634; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000020650; Expressed in frontal cortex and 9 other tissues.
DR Genevisible; Q62634; RN.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0044300; C:cerebellar mossy fiber; ISO:RGD.
DR GO; GO:0060076; C:excitatory synapse; IDA:BHF-UCL.
DR GO; GO:0016021; C:integral component of membrane; IDA:RGD.
DR GO; GO:0030285; C:integral component of synaptic vesicle membrane; IDA:SynGO.
DR GO; GO:0043229; C:intracellular organelle; IDA:RGD.
DR GO; GO:0098794; C:postsynapse; IEA:GOC.
DR GO; GO:0048786; C:presynaptic active zone; IDA:MGI.
DR GO; GO:0045202; C:synapse; IDA:MGI.
DR GO; GO:0008021; C:synaptic vesicle; ISO:RGD.
DR GO; GO:0030672; C:synaptic vesicle membrane; IDA:UniProtKB.
DR GO; GO:0005254; F:chloride channel activity; IDA:UniProtKB.
DR GO; GO:0008068; F:extracellularly glutamate-gated chloride channel activity; ISO:RGD.
DR GO; GO:0005315; F:inorganic phosphate transmembrane transporter activity; IDA:RGD.
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; IDA:UniProtKB.
DR GO; GO:0015319; F:sodium:inorganic phosphate symporter activity; ISO:RGD.
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:0007420; P:brain development; IEP:RGD.
DR GO; GO:0007268; P:chemical synaptic transmission; ISO:RGD.
DR GO; GO:0060079; P:excitatory postsynaptic potential; ISO:RGD.
DR GO; GO:0051938; P:L-glutamate import; ISO:RGD.
DR GO; GO:0015813; P:L-glutamate transmembrane transport; IDA:UniProtKB.
DR GO; GO:0007616; P:long-term memory; ISO:RGD.
DR GO; GO:0003407; P:neural retina development; IEP:RGD.
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:0006817; P:phosphate ion transport; IDA:RGD.
DR GO; GO:0050803; P:regulation of synapse structure or activity; IBA:GO_Central.
DR GO; GO:1900242; P:regulation of synaptic vesicle endocytosis; IMP:RGD.
DR GO; GO:0042137; P:sequestering of neurotransmitter; ISO:RGD.
DR GO; GO:0044341; P:sodium-dependent phosphate transport; IDA:UniProtKB.
DR GO; GO:0035249; P:synaptic transmission, glutamatergic; ISO:RGD.
DR GO; GO:0097401; P:synaptic vesicle lumen acidification; ISO:RGD.
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 Alternative splicing; Antiport; Cell membrane; Chloride; Chloride channel;
KW Cytoplasmic vesicle; Direct protein sequencing; Ion channel; Ion transport;
KW Membrane; Neurotransmitter transport; Phosphate transport; Phosphoprotein;
KW Reference proteome; Sodium; Sodium transport; Symport; Synapse;
KW Synaptosome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..560
FT /note="Vesicular glutamate transporter 1"
FT /id="PRO_0000331613"
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:0007744|PubMed:22673903"
FT VAR_SEQ 105
FT /note="Q -> QTPYRSVHKQEAVTPTVGDIQGGDTE (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16987242"
FT /id="VSP_033264"
SQ SEQUENCE 560 AA; 61665 MW; F686889F606B8305 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 ESEMEDEVEP PGAPPAPPPS
YGATHSTVQP PRPPPPVRDY
