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Sodium-coupled neutral amino acid transporter 2 (Amino acid transporter A2) (Solute carrier family 38 member 2) (System A amino acid transporter 2) (System A transporter 1) (System N amino acid transporter 2)

 S38A2_RAT               Reviewed;         504 AA.
Q9JHE5; Q9JI88;
13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
01-OCT-2000, sequence version 1.
22-NOV-2017, entry version 96.
RecName: Full=Sodium-coupled neutral amino acid transporter 2;
AltName: Full=Amino acid transporter A2;
AltName: Full=Solute carrier family 38 member 2;
AltName: Full=System A amino acid transporter 2;
AltName: Full=System A transporter 1;
AltName: Full=System N amino acid transporter 2;
Name=Slc38a2; Synonyms=Ata2, Sa1, Sat2, Snat2;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, ENZYME REGULATION,
BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE SPECIFICITY.
STRAIN=Sprague-Dawley; TISSUE=Skeletal muscle;
PubMed=10747860; DOI=10.1074/jbc.C000205200;
Sugawara M., Nakanishi T., Fei Y.-J., Huang W., Ganapathy M.E.,
Leibach F.H., Ganapathy V.;
"Cloning of an amino acid transporter with functional characteristics
and tissue expression pattern identical to that of system A.";
J. Biol. Chem. 275:16473-16477(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, ENZYME REGULATION,
BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE SPECIFICITY.
STRAIN=Sprague-Dawley; TISSUE=Cerebellum;
PubMed=10811809; DOI=10.1074/jbc.M002965200;
Yao D., Mackenzie B., Ming H., Varoqui H., Zhu H., Hediger M.A.,
Erickson J.D.;
"A novel system A isoform mediating Na+/neutral amino acid
cotransport.";
J. Biol. Chem. 275:22790-22797(2000).
[3]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, ENZYME REGULATION,
BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, AND TISSUE
SPECIFICITY.
TISSUE=Brain;
PubMed=10859363; DOI=10.1073/pnas.140152797;
Reimer R.J., Chaudhry F.A., Gray A.T., Edwards R.H.;
"Amino acid transport system A resembles system N in sequence but
differs in mechanism.";
Proc. Natl. Acad. Sci. U.S.A. 97:7715-7720(2000).
[4]
SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INDUCTION.
PubMed=11311116;
Hyde R., Christie G.R., Litherland G.J., Hajduch E., Taylor P.M.,
Hundal H.S.;
"Subcellular localization and adaptive up-regulation of the system A
(SAT2) amino acid transporter in skeletal-muscle cells and
adipocytes.";
Biochem. J. 355:563-568(2001).
[5]
INDUCTION BY TGFB1.
PubMed=11716780; DOI=10.1042/0264-6021:3600507;
Ensenat D., Hassan S., Reyna S.V., Schafer A.I., Durante W.;
"Transforming growth factor-beta 1 stimulates vascular smooth muscle
cell L-proline transport by inducing system A amino acid transporter 2
(SAT2) gene expression.";
Biochem. J. 360:507-512(2001).
[6]
SUBCELLULAR LOCATION.
PubMed=12054432; DOI=10.1016/S0003-9861(02)00006-1;
Freeman T.L., Thiele G.M., Tuma D.J., Machu T.K., Mailliard M.E.;
"ATA2-mediated amino acid uptake following partial hepatectomy is
regulated by redistribution to the plasma membrane.";
Arch. Biochem. Biophys. 400:215-222(2002).
[7]
SUBCELLULAR LOCATION.
PubMed=11834730; DOI=10.1074/jbc.M108609200;
Hyde R., Peyrollier K., Hundal H.S.;
"Insulin promotes the cell surface recruitment of the SAT2/ATA2 system
A amino acid transporter from an endosomal compartment in skeletal
muscle cells.";
J. Biol. Chem. 277:13628-13634(2002).
[8]
FUNCTION.
PubMed=11756489;
Chaudhry F.A., Schmitz D., Reimer R.J., Larsson P., Gray A.T.,
Nicoll R., Kavanaugh M., Edwards R.H.;
"Glutamine uptake by neurons: interaction of protons with system a
transporters.";
J. Neurosci. 22:62-72(2002).
[9]
FUNCTION.
PubMed=12021389; DOI=10.1124/mol.61.6.1289;
Takanaga H., Tokuda N., Ohtsuki S., Hosoya K., Terasaki T.;
"ATA2 is predominantly expressed as system A at the blood-brain
barrier and acts as brain-to-blood efflux transport for L-proline.";
Mol. Pharmacol. 61:1289-1296(2002).
[10]
FUNCTION, MUTAGENESIS OF HIS-504, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=16629640; DOI=10.1042/BJ20060026;
Baird F.E., Pinilla-Tenas J.J., Ogilvie W.L.J., Ganapathy V.,
Hundal H.S., Taylor P.M.;
"Evidence for allosteric regulation of pH-sensitive System A (SNAT2)
and System N (SNAT5) amino acid transporter activity involving a
conserved histidine residue.";
Biochem. J. 397:369-375(2006).
[11]
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=16616430; DOI=10.1016/j.neuroscience.2006.02.042;
Melone M., Varoqui H., Erickson J.D., Conti F.;
"Localization of the Na(+)-coupled neutral amino acid transporter 2 in
the cerebral cortex.";
Neuroscience 140:281-292(2006).
[12]
TOPOLOGY, AND INDUCTION.
PubMed=17488712; DOI=10.1074/jbc.M611520200;
Hyde R., Cwiklinski E.L., MacAulay K., Taylor P.M., Hundal H.S.;
"Distinct sensor pathways in the hierarchical control of SNAT2, a
putative amino acid transceptor, by amino acid availability.";
J. Biol. Chem. 282:19788-19798(2007).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- FUNCTION: Functions as a sodium-dependent amino acid transporter.
Mediates the saturable, pH-sensitive and electrogenic cotransport
of neutral amino acids and sodium ions with a stoichiometry of
1:1. May function in the transport of amino acids at the blood-
brain barrier and in the supply of maternal nutrients to the fetus
through the placenta. {ECO:0000269|PubMed:10747860,
ECO:0000269|PubMed:10811809, ECO:0000269|PubMed:10859363,
ECO:0000269|PubMed:11756489, ECO:0000269|PubMed:12021389,
ECO:0000269|PubMed:16629640}.
-!- ENZYME REGULATION: Inhibited by N-methyl-D-glucamine and choline.
{ECO:0000269|PubMed:10747860, ECO:0000269|PubMed:10811809,
ECO:0000269|PubMed:10859363}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.53 mM for alanine (at pH 7.4) {ECO:0000269|PubMed:10747860,
ECO:0000269|PubMed:10811809, ECO:0000269|PubMed:10859363,
ECO:0000269|PubMed:16629640};
KM=1.65 mM for glutamine (at pH 7.4)
{ECO:0000269|PubMed:10747860, ECO:0000269|PubMed:10811809,
ECO:0000269|PubMed:10859363, ECO:0000269|PubMed:16629640};
KM=0.94 mM for serine (at pH 8.0) {ECO:0000269|PubMed:10747860,
ECO:0000269|PubMed:10811809, ECO:0000269|PubMed:10859363,
ECO:0000269|PubMed:16629640};
KM=0.23 mM for 2-methylamino-isobutyric acid (MeAIB) (at pH 8.0
according to PubMed:10747860) {ECO:0000269|PubMed:10747860,
ECO:0000269|PubMed:10811809, ECO:0000269|PubMed:10859363,
ECO:0000269|PubMed:16629640};
KM=0.14 mM for 2-methylamino-isobutyric acid (MeAIB) (at pH 8.0
according to PubMed:10859363) {ECO:0000269|PubMed:10747860,
ECO:0000269|PubMed:10811809, ECO:0000269|PubMed:10859363,
ECO:0000269|PubMed:16629640};
KM=0.53 mM for 2-methylamino-isobutyric acid (MeAIB) (at pH 7.4)
{ECO:0000269|PubMed:10747860, ECO:0000269|PubMed:10811809,
ECO:0000269|PubMed:10859363, ECO:0000269|PubMed:16629640};
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10859363,
ECO:0000269|PubMed:11311116, ECO:0000269|PubMed:11834730,
ECO:0000269|PubMed:12054432, ECO:0000269|PubMed:16616430}; Multi-
pass membrane protein {ECO:0000269|PubMed:10859363,
ECO:0000269|PubMed:11311116, ECO:0000269|PubMed:11834730,
ECO:0000269|PubMed:12054432, ECO:0000269|PubMed:16616430}.
Note=Insulin promotes recruitment to the plasma membrane from a
pool localized in the trans-Golgi network or endosomes (By
similarity). Enriched in the somatodendritic compartment of
neurons, it is also detected at the axonal shaft but excluded from
the nerve terminal. {ECO:0000250}.
-!- TISSUE SPECIFICITY: Widely expressed. Expressed in skeletal muscle
and adipose tissue (at protein level). Expressed by glutamatergic
and GABAergic neurons together with astrocytes and other non-
neuronal cells in the cerebral cortex (at protein level).
{ECO:0000269|PubMed:10747860, ECO:0000269|PubMed:10811809,
ECO:0000269|PubMed:10859363, ECO:0000269|PubMed:11311116,
ECO:0000269|PubMed:16616430}.
-!- INDUCTION: Up-regulation upon amino acid deprivation results from
both increased transcription and protein stabilization. Up-
regulated by TGFB1. {ECO:0000269|PubMed:11311116,
ECO:0000269|PubMed:11716780, ECO:0000269|PubMed:17488712}.
-!- PTM: Polyubiquitination by NEDD4L regulates the degradation and
the activity of SLC38A2. {ECO:0000250}.
-!- SIMILARITY: Belongs to the amino acid/polyamine transporter 2
family. {ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AF249673; AAF74195.1; -; mRNA.
EMBL; AF173682; AAF75589.2; -; mRNA.
EMBL; AF273024; AAF81796.1; -; mRNA.
RefSeq; NP_851604.1; NM_181090.2.
UniGene; Rn.16393; -.
STRING; 10116.ENSRNOP00000031532; -.
TCDB; 2.A.18.6.4; the amino acid/auxin permease (aaap) family.
iPTMnet; Q9JHE5; -.
PhosphoSitePlus; Q9JHE5; -.
PaxDb; Q9JHE5; -.
Ensembl; ENSRNOT00000039002; ENSRNOP00000031532; ENSRNOG00000006305.
GeneID; 29642; -.
KEGG; rno:29642; -.
CTD; 54407; -.
RGD; 69420; Slc38a2.
eggNOG; KOG1305; Eukaryota.
eggNOG; COG0814; LUCA.
GeneTree; ENSGT00760000119147; -.
HOGENOM; HOG000013088; -.
HOVERGEN; HBG059571; -.
InParanoid; Q9JHE5; -.
KO; K14207; -.
OMA; FAYTCHQ; -.
OrthoDB; EOG091G0GP8; -.
PhylomeDB; Q9JHE5; -.
TreeFam; TF328787; -.
Reactome; R-RNO-210500; Glutamate Neurotransmitter Release Cycle.
Reactome; R-RNO-352230; Amino acid transport across the plasma membrane.
PRO; PR:Q9JHE5; -.
Proteomes; UP000002494; Chromosome 7.
Bgee; ENSRNOG00000006305; -.
Genevisible; Q9JHE5; RN.
GO; GO:0030424; C:axon; IDA:RGD.
GO; GO:0005903; C:brush border; IDA:RGD.
GO; GO:0030425; C:dendrite; IDA:RGD.
GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
GO; GO:0043025; C:neuronal cell body; IDA:RGD.
GO; GO:0005886; C:plasma membrane; IDA:RGD.
GO; GO:0042383; C:sarcolemma; IDA:RGD.
GO; GO:0015171; F:amino acid transmembrane transporter activity; ISO:RGD.
GO; GO:0015293; F:symporter activity; IEA:UniProtKB-KW.
GO; GO:0032328; P:alanine transport; IDA:RGD.
GO; GO:0003333; P:amino acid transmembrane transport; IBA:GO_Central.
GO; GO:0006865; P:amino acid transport; ISO:RGD.
GO; GO:0034198; P:cellular response to amino acid starvation; IEP:RGD.
GO; GO:0071260; P:cellular response to mechanical stimulus; IEP:RGD.
GO; GO:0021987; P:cerebral cortex development; IEP:RGD.
GO; GO:0007565; P:female pregnancy; IEP:RGD.
GO; GO:0031460; P:glycine betaine transport; IDA:RGD.
GO; GO:0006814; P:sodium ion transport; IEA:UniProtKB-KW.
InterPro; IPR013057; AA_transpt_TM.
Pfam; PF01490; Aa_trans; 1.
1: Evidence at protein level;
Amino-acid transport; Cell membrane; Complete proteome; Glycoprotein;
Ion transport; Membrane; Phosphoprotein; Reference proteome; Sodium;
Sodium transport; Symport; Transmembrane; Transmembrane helix;
Transport; Ubl conjugation.
CHAIN 1 504 Sodium-coupled neutral amino acid
transporter 2.
/FTId=PRO_0000311372.
TOPO_DOM 1 76 Cytoplasmic. {ECO:0000255}.
TRANSMEM 77 97 Helical. {ECO:0000255}.
TOPO_DOM 98 102 Extracellular. {ECO:0000255}.
TRANSMEM 103 123 Helical. {ECO:0000255}.
TOPO_DOM 124 158 Cytoplasmic. {ECO:0000255}.
TRANSMEM 159 179 Helical. {ECO:0000255}.
TOPO_DOM 180 188 Extracellular. {ECO:0000255}.
TRANSMEM 189 209 Helical. {ECO:0000255}.
TOPO_DOM 210 217 Cytoplasmic. {ECO:0000255}.
TRANSMEM 218 238 Helical. {ECO:0000255}.
TOPO_DOM 239 290 Extracellular. {ECO:0000255}.
TRANSMEM 291 311 Helical. {ECO:0000255}.
TOPO_DOM 312 327 Cytoplasmic. {ECO:0000255}.
TRANSMEM 328 348 Helical. {ECO:0000255}.
TOPO_DOM 349 369 Extracellular. {ECO:0000255}.
TRANSMEM 370 390 Helical. {ECO:0000255}.
TOPO_DOM 391 411 Cytoplasmic. {ECO:0000255}.
TRANSMEM 412 432 Helical. {ECO:0000255}.
TOPO_DOM 433 434 Extracellular. {ECO:0000255}.
TRANSMEM 435 455 Helical. {ECO:0000255}.
TOPO_DOM 456 472 Cytoplasmic. {ECO:0000255}.
TRANSMEM 473 493 Helical. {ECO:0000255}.
TOPO_DOM 494 504 Extracellular. {ECO:0000255}.
REGION 1 96 Regulates protein turnover upon amino
acid deprivation.
MOD_RES 12 12 Phosphoserine.
{ECO:0000250|UniProtKB:Q96QD8}.
MOD_RES 21 21 Phosphoserine.
{ECO:0000250|UniProtKB:Q8CFE6}.
MOD_RES 22 22 Phosphoserine.
{ECO:0000250|UniProtKB:Q96QD8}.
MOD_RES 55 55 Phosphoserine.
{ECO:0000250|UniProtKB:Q96QD8}.
CARBOHYD 254 254 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 258 258 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
MUTAGEN 504 504 H->A: Modifies the transporter pH-
sensitivity.
{ECO:0000269|PubMed:16629640}.
CONFLICT 69 69 G -> S (in Ref. 1; AAF74195).
{ECO:0000305}.
CONFLICT 81 81 S -> T (in Ref. 1; AAF74195).
{ECO:0000305}.
CONFLICT 87 87 S -> N (in Ref. 1; AAF74195).
{ECO:0000305}.
SEQUENCE 504 AA; 55554 MW; F53022C07152648C CRC64;
MKKTEMGRFN ISPDEDSSSY SSNGDFNYSY PTKQAALKSH YVDVDPENQN FLLESNLGKK
KYETDFHPGT TSFGMSVFNL SNAIVGSGIL GLSYAMANTG IALFIILLTF VSIFSLYSVH
LLLKTANEGG SLLYEQLGHK AYGLAGKLAA SGSITMQNIG AMSSYLFIVK YELPLVIKAL
MNIEDTNGLW YLNGDYLVLL VSFVLILPLS LLRNLGYLGY TSGLSLLCMI FFLIVVICKK
FQIPCPVEVA LMANETVNGT FTQVALAALA SNSTAADTCR PRYFIFNSQT VYAVPILTFS
FVCHPAVLPI YEELKSRSRR RMMNVSKISF FAMFLMYLLA ALFGYLTFYE HVESELLHTY
SAIVGTDILL LVVRLAVLVA VTLTVPVVIF PIRSSVTHLL CPTKEFSWFR HSVITVTILA
FTNLLVIFVP TIRDIFGFIG ASAAAMLIFI LPSAFYIKLV KKEPMRSVQK IGALCFLLSG
VVVMIGSMGL IVLDWVHDAS AGGH


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