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 24-JAN-2024, entry version 153. 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}. 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; 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; 10116-ENSRNOP00000063604; -. DR ABCD; Q62634; 12 sequenced antibodies. DR Ensembl; ENSRNOT00000028064.6; ENSRNOP00000028064.1; ENSRNOG00000020650.8. [Q62634-1] DR Ensembl; ENSRNOT00000064184.5; ENSRNOP00000063604.1; ENSRNOG00000020650.8. [Q62634-2] DR Ensembl; ENSRNOT00055009185; ENSRNOP00055007026; ENSRNOG00055005694. [Q62634-1] DR Ensembl; ENSRNOT00060014013; ENSRNOP00060010717; ENSRNOG00060008397. [Q62634-1] DR Ensembl; ENSRNOT00065049662; ENSRNOP00065040770; ENSRNOG00065028761. [Q62634-1] DR GeneID; 116638; -. DR KEGG; rno:116638; -. DR UCSC; RGD:620101; rat. [Q62634-1] DR AGR; RGD:620101; -. 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; 2685946at2759; -. 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 cell types or tissues. DR GO; GO:0044300; C:cerebellar mossy fiber; ISO:RGD. DR GO; GO:0034707; C:chloride channel complex; IEA:UniProtKB-KW. DR GO; GO:0060076; C:excitatory synapse; IDA:BHF-UCL. DR GO; GO:0016020; C:membrane; ISO:RGD. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. 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:0140788; F:L-glutamate uniporter activity; IDA:UniProtKB. DR GO; GO:0005326; F:neurotransmitter transmembrane transporter activity; IBA:GO_Central. DR GO; GO:0140787; F:phosphate ion uniporter activity; IDA:UniProtKB. 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:0007268; P:chemical synaptic transmission; ISO:RGD. DR GO; GO:0006821; P:chloride transport; IDA:UniProtKB. DR GO; GO:0051649; P:establishment of localization in cell; 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:0051651; P:maintenance of location in cell; ISO:RGD. DR GO; GO:0006820; P:monoatomic anion transport; IBA:GO_Central. 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:0035435; P:phosphate ion transmembrane transport; ISO:RGD. DR GO; GO:0006817; P:phosphate ion transport; IDA:UniProtKB. DR GO; GO:0006813; P:potassium ion transport; IDA:UniProtKB. 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 CDD; cd17382; MFS_SLC17A6_7_8_VGluT; 1. DR Gene3D; 1.20.1250.20; MFS general substrate transporter like domains; 2. DR InterPro; IPR011701; MFS. DR InterPro; IPR020846; MFS_dom. DR InterPro; IPR036259; MFS_trans_sf. DR PANTHER; PTHR11662; SOLUTE CARRIER FAMILY 17; 1. DR PANTHER; PTHR11662:SF29; VESICULAR GLUTAMATE TRANSPORTER 1; 1. DR Pfam; PF07690; MFS_1; 1. DR SUPFAM; SSF103473; MFS general substrate transporter; 1. DR PROSITE; PS50850; MFS; 1. DR Genevisible; Q62634; RN. 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 //