ID   S38A5_RAT               Reviewed;         479 AA.
AC   A2VCW5; Q91XR7;
DT   04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT   20-MAR-2007, sequence version 1.
DT   27-MAR-2024, entry version 99.
DE   RecName: Full=Sodium-coupled neutral amino acid transporter 5 {ECO:0000305};
DE   AltName: Full=Solute carrier family 38 member 5;
DE   AltName: Full=System N transporter 2;
GN   Name=Slc38a5 {ECO:0000312|RGD:620702};
GN   Synonyms=Sn2 {ECO:0000303|PubMed:11698233}, Snat5
GN   {ECO:0000303|PubMed:15218073};
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 2), FUNCTION, TRANSPORTER ACTIVITY, AND
RP   TISSUE SPECIFICITY.
RC   TISSUE=Brain;
RX   PubMed=11698233; DOI=10.1152/ajpcell.2001.281.6.c1757;
RA   Nakanishi T., Kekuda R., Fei Y.J., Hatanaka T., Sugawara M.,
RA   Martindale R.G., Leibach F.H., Prasad P.D., Ganapathy V.;
RT   "Cloning and functional characterization of a new subtype of the amino acid
RT   transport system N.";
RL   Am. J. Physiol. 281:C1757-C1768(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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).
RN   [3]
RP   FUNCTION, TRANSPORTER ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE
RP   SPECIFICITY.
RX   PubMed=15218073; DOI=10.1113/jphysiol.2003.060293;
RA   Baird F.E., Beattie K.J., Hyde A.R., Ganapathy V., Rennie M.J.,
RA   Taylor P.M.;
RT   "Bidirectional substrate fluxes through the system N (SNAT5) glutamine
RT   transporter may determine net glutamine flux in rat liver.";
RL   J. Physiol. (Lond.) 559:367-381(2004).
RN   [4]
RP   TOPOLOGY, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=15390093; DOI=10.1002/glia.20106;
RA   Cubelos B., Gonzalez-Gonzalez I.M., Gimenez C., Zafra F.;
RT   "Amino acid transporter SNAT5 localizes to glial cells in the rat brain.";
RL   Glia 49:230-244(2005).
RN   [5]
RP   FUNCTION, TRANSPORTER ACTIVITY, TISSUE SPECIFICITY, AND BIOPHYSICOCHEMICAL
RP   PROPERTIES.
RX   PubMed=16249471; DOI=10.1167/iovs.05-0488;
RA   Umapathy N.S., Li W., Mysona B.A., Smith S.B., Ganapathy V.;
RT   "Expression and function of glutamine transporters SN1 (SNAT3) and SN2
RT   (SNAT5) in retinal Mueller cells.";
RL   Invest. Ophthalmol. Vis. Sci. 46:3980-3987(2005).
RN   [6]
RP   FUNCTION, TRANSPORTER ACTIVITY, MUTAGENESIS OF HIS-479, BIOPHYSICOCHEMICAL
RP   PROPERTIES, AND ACTIVITY REGULATION.
RX   PubMed=16629640; DOI=10.1042/bj20060026;
RA   Baird F.E., Pinilla-Tenas J.J., Ogilvie W.L.J., Ganapathy V., Hundal H.S.,
RA   Taylor P.M.;
RT   "Evidence for allosteric regulation of pH-sensitive System A (SNAT2) and
RT   System N (SNAT5) amino acid transporter activity involving a conserved
RT   histidine residue.";
RL   Biochem. J. 397:369-375(2006).
RN   [7]
RP   FUNCTION, TRANSPORTER ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR
RP   LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=22821889; DOI=10.1002/glia.22386;
RA   Hamdani E.H., Gudbrandsen M., Bjoerkmo M., Chaudhry F.A.;
RT   "The system N transporter SN2 doubles as a transmitter precursor furnisher
RT   and a potential regulator of NMDA receptors.";
RL   Glia 60:1671-1683(2012).
RN   [8]
RP   TISSUE SPECIFICITY.
RX   PubMed=24333324; DOI=10.1016/j.neuint.2013.11.011;
RA   Rodriguez A., Ortega A., Berumen L.C., Garcia-Alcocer M.G., Gimenez C.,
RA   Zafra F.;
RT   "Expression of the System N transporter (SNAT5/SN2) during development
RT   indicates its plausible role in glutamatergic neurotransmission.";
RL   Neurochem. Int. 73:166-171(2014).
CC   -!- FUNCTION: Symporter that cotransports neutral amino acids and sodium
CC       ions, coupled to an H(+) antiporter activity (PubMed:11698233,
CC       PubMed:16629640, PubMed:15218073, PubMed:22821889, PubMed:16249471).
CC       Releases L-glutamine and glycine from astroglial cells and may
CC       participate in the glutamate/GABA-glutamine cycle and the NMDA
CC       receptors activation (PubMed:22821889). In addition contributes
CC       significantly to L-glutamine uptake in retina, namely in ganglion and
CC       Mueller cells and, therefore participates in the retinal glutamate-
CC       glutamine cycle (PubMed:16249471). The transport activity is pH
CC       sensitive (PubMed:22821889, PubMed:15218073, PubMed:11698233), Li(+)
CC       tolerant (PubMed:22821889, PubMed:15218073, PubMed:11698233),
CC       bidirectional (PubMed:22821889, PubMed:15218073) and associated with
CC       large uncoupled fluxes of protons (PubMed:22821889, PubMed:15218073,
CC       PubMed:11698233). The transport is electroneutral coupled to the
CC       cotransport of 1 Na(+) and the antiport of 1 H(+) (PubMed:22821889).
CC       May have particular importance for modulation of net hepatic glutamine
CC       flux (PubMed:15218073). {ECO:0000269|PubMed:11698233,
CC       ECO:0000269|PubMed:15218073, ECO:0000269|PubMed:16249471,
CC       ECO:0000269|PubMed:16629640, ECO:0000269|PubMed:22821889}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+)(in) + L-serine(out) + Na(+)(out) = H(+)(out) + L-
CC         serine(in) + Na(+)(in); Xref=Rhea:RHEA:71159, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:29101, ChEBI:CHEBI:33384;
CC         Evidence={ECO:0000269|PubMed:11698233, ECO:0000269|PubMed:15218073,
CC         ECO:0000269|PubMed:16629640, ECO:0000269|PubMed:22821889};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71160;
CC         Evidence={ECO:0000269|PubMed:11698233, ECO:0000305|PubMed:15218073,
CC         ECO:0000305|PubMed:16629640};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:71161;
CC         Evidence={ECO:0000305|PubMed:15218073};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+)(in) + L-alanine(out) + Na(+)(out) = H(+)(out) + L-
CC         alanine(in) + Na(+)(in); Xref=Rhea:RHEA:71163, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:29101, ChEBI:CHEBI:57972;
CC         Evidence={ECO:0000269|PubMed:11698233, ECO:0000269|PubMed:22821889};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71164;
CC         Evidence={ECO:0000269|PubMed:11698233};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:71165;
CC         Evidence={ECO:0000305|PubMed:15218073};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=glycine(out) + H(+)(in) + Na(+)(out) = glycine(in) + H(+)(out)
CC         + Na(+)(in); Xref=Rhea:RHEA:71167, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:29101, ChEBI:CHEBI:57305;
CC         Evidence={ECO:0000269|PubMed:11698233, ECO:0000269|PubMed:22821889};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71168;
CC         Evidence={ECO:0000269|PubMed:11698233, ECO:0000269|PubMed:22821889};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:71169;
CC         Evidence={ECO:0000269|PubMed:22821889, ECO:0000305|PubMed:15218073};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+)(in) + L-glutamine(out) + Na(+)(out) = H(+)(out) + L-
CC         glutamine(in) + Na(+)(in); Xref=Rhea:RHEA:71127, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:29101, ChEBI:CHEBI:58359;
CC         Evidence={ECO:0000269|PubMed:11698233, ECO:0000269|PubMed:15218073,
CC         ECO:0000269|PubMed:16249471, ECO:0000269|PubMed:22821889};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71128;
CC         Evidence={ECO:0000269|PubMed:11698233, ECO:0000269|PubMed:15218073,
CC         ECO:0000269|PubMed:22821889};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:71129;
CC         Evidence={ECO:0000269|PubMed:15218073, ECO:0000269|PubMed:22821889};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+)(in) + L-asparagine(out) + Na(+)(out) = H(+)(out) + L-
CC         asparagine(in) + Na(+)(in); Xref=Rhea:RHEA:71131, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:29101, ChEBI:CHEBI:58048;
CC         Evidence={ECO:0000269|PubMed:11698233, ECO:0000269|PubMed:22821889};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71132;
CC         Evidence={ECO:0000269|PubMed:11698233};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:71133;
CC         Evidence={ECO:0000305|PubMed:15218073};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+)(in) + L-histidine(out) + Na(+)(out) = H(+)(out) + L-
CC         histidine(in) + Na(+)(in); Xref=Rhea:RHEA:71135, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:29101, ChEBI:CHEBI:57595;
CC         Evidence={ECO:0000269|PubMed:11698233, ECO:0000269|PubMed:15218073};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71136;
CC         Evidence={ECO:0000269|PubMed:11698233, ECO:0000305|PubMed:15218073};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:71137;
CC         Evidence={ECO:0000305|PubMed:15218073};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+)(in) + L-cysteine(out) + Na(+)(out) = H(+)(out) + L-
CC         cysteine(in) + Na(+)(in); Xref=Rhea:RHEA:71171, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:29101, ChEBI:CHEBI:35235;
CC         Evidence={ECO:0000269|PubMed:22821889};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71172;
CC         Evidence={ECO:0000269|PubMed:22821889};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:71173;
CC         Evidence={ECO:0000305|PubMed:22821889};
CC   -!- ACTIVITY REGULATION: Not inhibited by lithium (By similarity). Partial
CC       allosteric regulation on ions sodium binding (PubMed:16629640).
CC       {ECO:0000250|UniProtKB:Q8WUX1, ECO:0000269|PubMed:16629640}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.92 mM for L-serine (at pH 8.0) {ECO:0000269|PubMed:16629640};
CC         KM=0.99 mM for L-glutamine influx (at pH 8.0)
CC         {ECO:0000269|PubMed:15218073};
CC         KM=0.73 mM for L-serine (at pH 8.0) {ECO:0000269|PubMed:15218073};
CC         KM=0.21 mM for L-histidine (at pH 8.0) {ECO:0000269|PubMed:15218073};
CC         KM=1.2 mM for L-glutamine efflux (at pH 8.0)
CC         {ECO:0000269|PubMed:15218073};
CC         KM=7.1 mM for glycine {ECO:0000269|PubMed:22821889};
CC         KM=1.2 mM for L-glutamine {ECO:0000269|PubMed:22821889};
CC         KM=76.7 mM for sodium ion {ECO:0000269|PubMed:22821889};
CC         Vmax=192 nmol/min/mg enzyme toward glycine (at (-) 80 mV)
CC         {ECO:0000269|PubMed:22821889};
CC         Vmax=87 nmol/min/mg enzyme toward L-glutamine (at (-) 80 mV)
CC         {ECO:0000269|PubMed:22821889};
CC       pH dependence:
CC         Optimum pH is 8.0. {ECO:0000269|PubMed:15218073,
CC         ECO:0000269|PubMed:16249471};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15390093,
CC       ECO:0000269|PubMed:22821889}; Multi-pass membrane protein
CC       {ECO:0000255}. Note=Localized at astroglial membrane.
CC       {ECO:0000269|PubMed:22821889}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=A2VCW5-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=A2VCW5-2; Sequence=VSP_029704;
CC   -!- TISSUE SPECIFICITY: Highly expressed in neocortex, hippocampus,
CC       striatum and spinal cord by astrocytes (at protein level)
CC       (PubMed:15390093). Expressed in brain, lung, stomach, kidney, spleen
CC       and testis (PubMed:11698233). Expressed in the cerebral cortex between
CC       the second and third postnatal week, where expressed exclusively in
CC       glial cells from postnatal day 14 to adulthood (at protein level)
CC       (PubMed:24333324). Expressed in the cerebellum at post natal day 12
CC       (P12) (PubMed:24333324). Expressed in liver (PubMed:15218073,
CC       PubMed:11698233). Expressed inside the cell body of the astrocytes
CC       (PubMed:22821889). {ECO:0000269|PubMed:11698233,
CC       ECO:0000269|PubMed:15218073, ECO:0000269|PubMed:15390093,
CC       ECO:0000269|PubMed:22821889, ECO:0000269|PubMed:24333324}.
CC   -!- SIMILARITY: Belongs to the amino acid/polyamine transporter 2 family.
CC       {ECO:0000305}.
CC   -!- CAUTION: Nakanishi et al (PubMed:11698233) shows that the transport
CC       process is electrogenic, contrary to the conclusions of Hamdani et al
CC       (PubMed:22821889) who finds that the transport is electroneutral with a
CC       Na(+):L-glutamine stoichiometry of 1:1 (PubMed:22821889,
CC       PubMed:11698233). Hamdani et al. shows that this electrogenic transport
CC       describes by Nakanishi et al. would correspond to large uncoupled
CC       fluxes of protons (PubMed:22821889, PubMed:11698233).
CC       {ECO:0000269|PubMed:11698233, ECO:0000269|PubMed:22821889}.
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DR   EMBL; AF276870; AAK69075.1; -; mRNA.
DR   EMBL; BC128725; AAI28726.1; -; mRNA.
DR   RefSeq; NP_620209.1; NM_138854.1. [A2VCW5-2]
DR   RefSeq; XP_008771290.1; XM_008773068.2. [A2VCW5-1]
DR   AlphaFoldDB; A2VCW5; -.
DR   SMR; A2VCW5; -.
DR   STRING; 10116.ENSRNOP00000038781; -.
DR   TCDB; 2.A.18.6.8; the amino acid/auxin permease (aaap) family.
DR   GlyCosmos; A2VCW5; 1 site, No reported glycans.
DR   GlyGen; A2VCW5; 1 site.
DR   iPTMnet; A2VCW5; -.
DR   PhosphoSitePlus; A2VCW5; -.
DR   PaxDb; 10116-ENSRNOP00000038781; -.
DR   PeptideAtlas; A2VCW5; -.
DR   Ensembl; ENSRNOT00000038068.6; ENSRNOP00000038781.5; ENSRNOG00000027767.6. [A2VCW5-1]
DR   Ensembl; ENSRNOT00000079664.2; ENSRNOP00000073818.1; ENSRNOG00000027767.6. [A2VCW5-2]
DR   Ensembl; ENSRNOT00055038402; ENSRNOP00055031259; ENSRNOG00055022355. [A2VCW5-1]
DR   Ensembl; ENSRNOT00060038574; ENSRNOP00060031833; ENSRNOG00060022262. [A2VCW5-1]
DR   Ensembl; ENSRNOT00065019140; ENSRNOP00065014643; ENSRNOG00065011778. [A2VCW5-1]
DR   GeneID; 192208; -.
DR   KEGG; rno:192208; -.
DR   UCSC; RGD:620702; rat. [A2VCW5-1]
DR   AGR; RGD:620702; -.
DR   CTD; 92745; -.
DR   RGD; 620702; Slc38a5.
DR   eggNOG; KOG1305; Eukaryota.
DR   GeneTree; ENSGT00940000161233; -.
DR   InParanoid; A2VCW5; -.
DR   OMA; MEVAGEM; -.
DR   OrthoDB; 935269at2759; -.
DR   PhylomeDB; A2VCW5; -.
DR   TreeFam; TF328787; -.
DR   Reactome; R-RNO-352230; Amino acid transport across the plasma membrane.
DR   SABIO-RK; A2VCW5; -.
DR   PRO; PR:A2VCW5; -.
DR   Proteomes; UP000002494; Chromosome X.
DR   Bgee; ENSRNOG00000027767; Expressed in pancreas and 15 other cell types or tissues.
DR   ExpressionAtlas; A2VCW5; baseline and differential.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0022858; F:alanine transmembrane transporter activity; ISO:RGD.
DR   GO; GO:0015171; F:amino acid transmembrane transporter activity; IDA:RGD.
DR   GO; GO:0015187; F:glycine transmembrane transporter activity; IDA:RGD.
DR   GO; GO:0015182; F:L-asparagine transmembrane transporter activity; ISO:RGD.
DR   GO; GO:0015186; F:L-glutamine transmembrane transporter activity; IDA:ARUK-UCL.
DR   GO; GO:0140830; F:L-glutamine, sodium:proton antiporter activity; IDA:UniProtKB.
DR   GO; GO:0005290; F:L-histidine transmembrane transporter activity; IDA:ARUK-UCL.
DR   GO; GO:0015194; F:L-serine transmembrane transporter activity; IDA:ARUK-UCL.
DR   GO; GO:0140893; F:neutral amino acid, sodium:proton antiporter activity; IDA:UniProtKB.
DR   GO; GO:0015175; F:neutral L-amino acid transmembrane transporter activity; IDA:RGD.
DR   GO; GO:0032973; P:amino acid export across plasma membrane; IDA:UniProtKB.
DR   GO; GO:0089718; P:amino acid import across plasma membrane; IDA:UniProtKB.
DR   GO; GO:1903713; P:asparagine transmembrane transport; ISO:RGD.
DR   GO; GO:0006868; P:glutamine transport; IDA:ARUK-UCL.
DR   GO; GO:0015816; P:glycine transport; IDA:RGD.
DR   GO; GO:1904557; P:L-alanine transmembrane transport; ISO:RGD.
DR   GO; GO:1903803; P:L-glutamine import across plasma membrane; IDA:UniProtKB.
DR   GO; GO:0089709; P:L-histidine transmembrane transport; IDA:ARUK-UCL.
DR   GO; GO:1903812; P:L-serine import across plasma membrane; IDA:UniProtKB.
DR   GO; GO:0015825; P:L-serine transport; IDA:ARUK-UCL.
DR   GO; GO:0015804; P:neutral amino acid transport; IDA:UniProtKB.
DR   GO; GO:0032329; P:serine transport; ISO:RGD.
DR   InterPro; IPR013057; AA_transpt_TM.
DR   PANTHER; PTHR22950; AMINO ACID TRANSPORTER; 1.
DR   PANTHER; PTHR22950:SF74; SODIUM-COUPLED NEUTRAL AMINO ACID TRANSPORTER 5; 1.
DR   Pfam; PF01490; Aa_trans; 1.
DR   Genevisible; A2VCW5; RN.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell membrane; Disulfide bond; Glycoprotein;
KW   Membrane; Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..479
FT                   /note="Sodium-coupled neutral amino acid transporter 5"
FT                   /id="PRO_0000312117"
FT   TOPO_DOM        1..58
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255, ECO:0000305|PubMed:15390093"
FT   TRANSMEM        59..81
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        82..97
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        98..118
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        119..135
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        136..156
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        157..176
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        177..197
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        198..202
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        203..223
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        224..264
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        265..285
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        286..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..383
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        384..404
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        405..406
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        407..427
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        428..446
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        447..467
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        468..479
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   SITE            471
FT                   /note="Involved in pH-sensing to the transport activity
FT                   regulation"
FT                   /evidence="ECO:0000269|PubMed:16629640"
FT   CARBOHYD        236
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        231..254
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   VAR_SEQ         1..8
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:11698233"
FT                   /id="VSP_029704"
FT   MUTAGEN         479
FT                   /note="H->A: Modifies the transporter pH-sensitivity."
FT                   /evidence="ECO:0000269|PubMed:16629640"
FT   CONFLICT        392
FT                   /note="I -> N (in Ref. 1; AAK69075)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   479 AA;  52436 MW;  DC172C28CB7F5EDC CRC64;
     MAISCAVGME MQEPKMNGTL STGAAAGYRQ EREGFLPTTH GPAPGRKPVQ FLDFEGKTSF
     GMSVFNLSNA IMGSGILGLA YAMAHTGVIF FLALLLCIAL LSSYSIHLLL TCASVVGIRA
     YEQLGQRAFG PAGKVVVAII ICLHNVGAMS SYLFIIKSEL PLVIGTFLHM DPEGDWFLKG
     NLLIILVSLL IILPLALMKH LGYLGYTSSL SLTCMLFFLI SVIYKKFQLG CVVSHNDTVV
     ESEPAPLQAF NSSCEAKLFT VDSQMSYTVP IMAFAFVCHP EVLPIYTELC CPTQRRMQAV
     ANMSIGAMFI MYGLTATFGY LTFYSTVKAE MLEMYTQEDL LILCVRLAVL LAVTLTVPVV
     LFPIRRALQQ LLFPSKAFSW PRHVAIALIL LILVNILVIC VPTIRDIFGF IGSTSAPSLI
     FILPSVFYLR IVPADMEPLF SWPKIQALCF GVLGVLFMAI SLGFMFANWA TGQSRMSGH
//