ID   VGLU1_HUMAN             Reviewed;         560 AA.
AC   Q9P2U7; B4DFR9; B4DG46; Q6PCD0;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   27-NOV-2024, entry version 170.
DE   RecName: Full=Vesicular glutamate transporter 1 {ECO:0000250|UniProtKB:Q3TXX4};
DE            Short=VGluT1 {ECO:0000250|UniProtKB:Q3TXX4};
DE   AltName: Full=Brain-specific Na(+)-dependent inorganic phosphate cotransporter {ECO:0000303|PubMed:10820226};
DE   AltName: Full=Solute carrier family 17 member 7;
GN   Name=SLC17A7 {ECO:0000312|HGNC:HGNC:16704};
GN   Synonyms=BNPI {ECO:0000303|PubMed:10820226}, VGLUT1;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND TISSUE SPECIFICITY.
RC   TISSUE=Brain;
RX   PubMed=10820226; DOI=10.1046/j.1471-4159.2000.0742622.x;
RA   Aihara Y., Mashima H., Onda H., Hisano S., Kasuya H., Hori T., Yamada S.,
RA   Tomura H., Yamada Y., Inoue I., Kojima I., Takeda J.;
RT   "Molecular cloning of a novel brain-type Na(+)-dependent inorganic
RT   phosphate cotransporter.";
RL   J. Neurochem. 74:2622-2625(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC   TISSUE=Amygdala;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15057824; DOI=10.1038/nature02399;
RA   Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA   Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA   Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA   Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA   Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA   Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA   Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA   Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA   Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA   McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA   Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA   Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA   She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA   Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA   Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA   Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA   Rubin E.M., Lucas S.M.;
RT   "The DNA sequence and biology of human chromosome 19.";
RL   Nature 428:529-535(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ARG-431.
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Multifunctional transporter that transports L-glutamate as
CC       well as multiple ions such as chloride, proton, potassium, sodium and
CC       phosphate (PubMed:10820226). At the synaptic vesicle membrane, mainly
CC       functions as an uniporter which transports preferentially L-glutamate
CC       but also phosphate from the cytoplasm into synaptic vesicles at
CC       presynaptic nerve terminals of excitatory neural cells (By similarity).
CC       The L-glutamate or phosphate uniporter activity is electrogenic and is
CC       driven by the proton electrochemical gradient, mainly by the electrical
CC       gradient established by the vacuolar H(+)-ATPase across the synaptic
CC       vesicle membrane (By similarity). 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 (By similarity). Moreover, may function
CC       as a K(+)/H(+) antiport allowing to maintain the electrical gradient
CC       and to decrease chemical gradient and therefore sustain vesicular
CC       glutamate uptake (By similarity). The vesicular K(+)/H(+) antiport
CC       activity is electroneutral (By similarity). 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 (PubMed:10820226). The symporter
CC       activity is driven by an inside negative membrane potential and is
CC       electrogenic (By similarity). Is necessary for synaptic signaling of
CC       visual-evoked responses from photoreceptors (By similarity).
CC       {ECO:0000250|UniProtKB:Q3TXX4, ECO:0000250|UniProtKB:Q62634,
CC       ECO:0000269|PubMed:10820226}.
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=K(+)(in) + H(+)(out) = K(+)(out) + H(+)(in);
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   -!- SUBUNIT: Interacts with SHANK3. {ECO:0000250|UniProtKB:Q3TXX4}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic
CC       vesicle membrane {ECO:0000250|UniProtKB:Q3TXX4}. Cell membrane
CC       {ECO:0000305|PubMed:10820226}; Multi-pass membrane protein
CC       {ECO:0000305}. Synapse, synaptosome {ECO:0000250|UniProtKB:Q3TXX4}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q9P2U7-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9P2U7-2; Sequence=VSP_056110;
CC       Name=3;
CC         IsoId=Q9P2U7-3; Sequence=VSP_056111;
CC   -!- TISSUE SPECIFICITY: Expressed in several regions of the brain including
CC       amygdala, cerebellum, cerebral cortex, hippocampus, frontal lobe,
CC       medulla, occipital lobe, putamen and temporal lobe.
CC       {ECO:0000269|PubMed:10820226}.
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; AB032436; BAA92875.1; -; mRNA.
DR   EMBL; AK294226; BAG57530.1; -; mRNA.
DR   EMBL; AK294405; BAG57657.1; -; mRNA.
DR   EMBL; AC010619; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471177; EAW52485.1; -; Genomic_DNA.
DR   EMBL; BC059379; AAH59379.1; -; mRNA.
DR   CCDS; CCDS12764.1; -. [Q9P2U7-1]
DR   RefSeq; NP_064705.1; NM_020309.3. [Q9P2U7-1]
DR   AlphaFoldDB; Q9P2U7; -.
DR   SMR; Q9P2U7; -.
DR   BioGRID; 121331; 3.
DR   IntAct; Q9P2U7; 2.
DR   STRING; 9606.ENSP00000221485; -.
DR   TCDB; 2.A.1.14.30; the major facilitator superfamily (mfs).
DR   iPTMnet; Q9P2U7; -.
DR   PhosphoSitePlus; Q9P2U7; -.
DR   SwissPalm; Q9P2U7; -.
DR   BioMuta; SLC17A7; -.
DR   DMDM; 74725387; -.
DR   MassIVE; Q9P2U7; -.
DR   PaxDb; 9606-ENSP00000221485; -.
DR   PeptideAtlas; Q9P2U7; -.
DR   ProteomicsDB; 4105; -.
DR   ProteomicsDB; 83898; -. [Q9P2U7-1]
DR   TopDownProteomics; Q9P2U7-1; -. [Q9P2U7-1]
DR   ABCD; Q9P2U7; 1 sequenced antibody.
DR   Antibodypedia; 31998; 288 antibodies from 31 providers.
DR   DNASU; 57030; -.
DR   Ensembl; ENST00000221485.8; ENSP00000221485.2; ENSG00000104888.10. [Q9P2U7-1]
DR   Ensembl; ENST00000600601.5; ENSP00000470338.1; ENSG00000104888.10. [Q9P2U7-2]
DR   GeneID; 57030; -.
DR   KEGG; hsa:57030; -.
DR   MANE-Select; ENST00000221485.8; ENSP00000221485.2; NM_020309.4; NP_064705.1.
DR   UCSC; uc002pnp.4; human. [Q9P2U7-1]
DR   AGR; HGNC:16704; -.
DR   CTD; 57030; -.
DR   DisGeNET; 57030; -.
DR   GeneCards; SLC17A7; -.
DR   HGNC; HGNC:16704; SLC17A7.
DR   HPA; ENSG00000104888; Group enriched (brain, retina).
DR   MIM; 605208; gene.
DR   neXtProt; NX_Q9P2U7; -.
DR   OpenTargets; ENSG00000104888; -.
DR   PharmGKB; PA423; -.
DR   VEuPathDB; HostDB:ENSG00000104888; -.
DR   eggNOG; KOG2532; Eukaryota.
DR   GeneTree; ENSGT00940000159110; -.
DR   HOGENOM; CLU_001265_5_0_1; -.
DR   InParanoid; Q9P2U7; -.
DR   OMA; WFPAYLV; -.
DR   OrthoDB; 2685946at2759; -.
DR   PhylomeDB; Q9P2U7; -.
DR   TreeFam; TF313535; -.
DR   PathwayCommons; Q9P2U7; -.
DR   Reactome; R-HSA-210500; Glutamate Neurotransmitter Release Cycle.
DR   Reactome; R-HSA-428643; Organic anion transporters.
DR   SignaLink; Q9P2U7; -.
DR   BioGRID-ORCS; 57030; 15 hits in 1155 CRISPR screens.
DR   ChiTaRS; SLC17A7; human.
DR   GeneWiki; Vesicular_glutamate_transporter_1; -.
DR   GenomeRNAi; 57030; -.
DR   Pharos; Q9P2U7; Tbio.
DR   PRO; PR:Q9P2U7; -.
DR   Proteomes; UP000005640; Chromosome 19.
DR   RNAct; Q9P2U7; protein.
DR   Bgee; ENSG00000104888; Expressed in right hemisphere of cerebellum and 132 other cell types or tissues.
DR   ExpressionAtlas; Q9P2U7; baseline and differential.
DR   GO; GO:0034707; C:chloride channel complex; IEA:UniProtKB-KW.
DR   GO; GO:0060203; C:clathrin-sculpted glutamate transport vesicle membrane; TAS:Reactome.
DR   GO; GO:0060076; C:excitatory synapse; IBA:GO_Central.
DR   GO; GO:0016020; C:membrane; IDA:MGI.
DR   GO; GO:0043005; C:neuron projection; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0048786; C:presynaptic active zone; IEA:Ensembl.
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; IBA:GO_Central.
DR   GO; GO:0140788; F:L-glutamate uniporter activity; ISS:UniProtKB.
DR   GO; GO:0005326; F:neurotransmitter transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0140787; F:phosphate ion uniporter activity; ISS:UniProtKB.
DR   GO; GO:0015386; F:potassium:proton antiporter activity; ISS:UniProtKB.
DR   GO; GO:0005436; F:sodium:phosphate symporter activity; IDA:MGI.
DR   GO; GO:0006821; P:chloride transport; ISS:UniProtKB.
DR   GO; GO:0015813; P:L-glutamate transmembrane transport; ISS:UniProtKB.
DR   GO; GO:0006820; P:monoatomic anion transport; IBA:GO_Central.
DR   GO; GO:0006811; P:monoatomic ion transport; TAS:Reactome.
DR   GO; GO:0003407; P:neural retina development; IEA:Ensembl.
DR   GO; GO:0098700; P:neurotransmitter loading into synaptic vesicle; IBA:GO_Central.
DR   GO; GO:0006836; P:neurotransmitter transport; TAS:Reactome.
DR   GO; GO:0055062; P:phosphate ion homeostasis; IEA:Ensembl.
DR   GO; GO:0006817; P:phosphate ion transport; ISS:UniProtKB.
DR   GO; GO:0006813; P:potassium ion transport; ISS: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; IEA:Ensembl.
DR   GO; GO:0044341; P:sodium-dependent phosphate transport; ISS:UniProtKB.
DR   GO; GO:0035249; P:synaptic transmission, glutamatergic; IBA:GO_Central.
DR   CDD; cd17382; MFS_SLC17A6_7_8_VGluT; 1.
DR   FunFam; 1.20.1250.20:FF:000004; vesicular glutamate transporter 2 isoform X1; 1.
DR   FunFam; 1.20.1250.20:FF:000005; vesicular glutamate transporter 2 isoform X1; 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; IPR050382; MFS_Na/Anion_cotransporter.
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.
PE   1: Evidence at protein level;
KW   Alternative splicing; Antiport; Cell membrane; Chloride; Chloride channel;
KW   Cytoplasmic vesicle; Ion channel; Ion transport; Membrane;
KW   Neurotransmitter transport; Phosphate transport; Phosphoprotein;
KW   Proteomics identification; Reference proteome; Sodium; Sodium transport;
KW   Symport; Synapse; Synaptosome; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN           1..560
FT                   /note="Vesicular glutamate transporter 1"
FT                   /id="PRO_0000331611"
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   VAR_SEQ         1..67
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_056110"
FT   VAR_SEQ         1..21
FT                   /note="MEFRQEEFRKLAGRALGKLHR -> MGSQLALAG (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_056111"
FT   VARIANT         431
FT                   /note="P -> R (in dbSNP:rs17855709)"
FT                   /evidence="ECO:0000269|PubMed:15489334"
FT                   /id="VAR_042904"
SQ   SEQUENCE   560 AA;  61613 MW;  C88DAFB34B6E45B6 CRC64;
     MEFRQEEFRK LAGRALGKLH RLLEKRQEGA ETLELSADGR PVTTQTRDPP VVDCTCFGLP
     RRYIIAIMSG LGFCISFGIR CNLGVAIVSM VNNSTTHRGG HVVVQKAQFS WDPETVGLIH
     GSFFWGYIVT QIPGGFICQK FAANRVFGFA IVATSTLNML IPSAARVHYG CVIFVRILQG
     LVEGVTYPAC HGIWSKWAPP LERSRLATTA FCGSYAGAVV AMPLAGVLVQ YSGWSSVFYV
     YGSFGIFWYL FWLLVSYESP ALHPSISEEE RKYIEDAIGE SAKLMNPLTK FSTPWRRFFT
     SMPVYAIIVA NFCRSWTFYL LLISQPAYFE EVFGFEISKV GLVSALPHLV MTIIVPIGGQ
     IADFLRSRRI MSTTNVRKLM NCGGFGMEAT LLLVVGYSHS KGVAISFLVL AVGFSGFAIS
     GFNVNHLDIA PRYASILMGI SNGVGTLSGM VCPIIVGAMT KHKTREEWQY VFLIASLVHY
     GGVIFYGVFA SGEKQPWAEP EEMSEEKCGF VGHDQLAGSD DSEMEDEAEP PGAPPAPPPS
     YGATHSTFQP PRPPPPVRDY
//