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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_MOUSE             Reviewed;         504 AA.
Q8CFE6; Q3TEX3; Q6PFR1; Q6ZPS7; Q810U9; Q8CC66; Q8CD21;
13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
01-MAR-2003, sequence version 1.
07-JUN-2017, entry version 101.
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, Kiaa1382, Sat2, Snat2;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Embryonic tail;
PubMed=14621295; DOI=10.1093/dnares/10.4.167;
Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
Saga Y., Nagase T., Ohara O., Koga H.;
"Prediction of the coding sequences of mouse homologues of KIAA gene:
III. The complete nucleotide sequences of 500 mouse KIAA-homologous
cDNAs identified by screening of terminal sequences of cDNA clones
randomly sampled from size-fractionated libraries.";
DNA Res. 10:167-180(2003).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Epididymis, Kidney, and Testis;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J, and Czech II; TISSUE=Brain, and Mammary tumor;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
INDUCTION.
PubMed=14623874; DOI=10.1074/jbc.M310483200;
Palii S.S., Chen H., Kilberg M.S.;
"Transcriptional control of the human sodium-coupled neutral amino
acid transporter system A gene by amino acid availability is mediated
by an intronic element.";
J. Biol. Chem. 279:3463-3471(2004).
[5]
TISSUE SPECIFICITY.
PubMed=12971909; DOI=10.1016/S0197-0186(03)00123-2;
Dolinska M., Zablocka B., Sonnewald U., Albrecht J.;
"Glutamine uptake and expression of mRNA's of glutamine transporting
proteins in mouse cerebellar and cerebral cortical astrocytes and
neurons.";
Neurochem. Int. 44:75-81(2004).
[6]
FUNCTION.
PubMed=16365304; DOI=10.1073/pnas.0504468103;
Constancia M., Angiolini E., Sandovici I., Smith P., Smith R.,
Kelsey G., Dean W., Ferguson-Smith A., Sibley C.P., Reik W.,
Fowden A.;
"Adaptation of nutrient supply to fetal demand in the mouse involves
interaction between the Igf2 gene and placental transporter systems.";
Proc. Natl. Acad. Sci. U.S.A. 102:19219-19224(2005).
[7]
SUBCELLULAR LOCATION, AND UBIQUITINATION BY NEDD4L.
PubMed=17003038; DOI=10.1074/jbc.M606577200;
Hatanaka T., Hatanaka Y., Setou M.;
"Regulation of amino acid transporter ATA2 by ubiquitin ligase Nedd4-
2.";
J. Biol. Chem. 281:35922-35930(2006).
[8]
SUBCELLULAR LOCATION.
PubMed=17050538; DOI=10.1074/jbc.M604534200;
Hatanaka T., Hatanaka Y., Tsuchida J., Ganapathy V., Setou M.;
"Amino acid transporter ATA2 is stored at the trans-Golgi network and
released by insulin stimulus in adipocytes.";
J. Biol. Chem. 281:39273-39284(2006).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
PubMed=18034455; DOI=10.1021/pr0701254;
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
"Large-scale identification and evolution indexing of tyrosine
phosphorylation sites from murine brain.";
J. Proteome Res. 7:311-318(2008).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-55, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
Thibault P.;
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Immunity 30:143-154(2009).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic fibroblast;
PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
"Large scale localization of protein phosphorylation by use of
electron capture dissociation mass spectrometry.";
Mol. Cell. Proteomics 8:904-912(2009).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Pancreas, and Spleen;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- 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:16365304}.
-!- ENZYME REGULATION: Inhibited by N-methyl-D-glucamine and choline.
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17003038,
ECO:0000269|PubMed:17050538}; Multi-pass membrane protein
{ECO:0000269|PubMed:17003038, ECO:0000269|PubMed:17050538}.
Note=Insulin promotes recruitment to the plasma membrane from a
pool localized in the trans-Golgi network or endosomes. 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: Expressed in cerebral and cerebellar
astrocytes and neurons. {ECO:0000269|PubMed:12971909}.
-!- INDUCTION: Up-regulated upon amino acid deprivation.
{ECO:0000269|PubMed:14623874}.
-!- PTM: Polyubiquitination by NEDD4L regulates the degradation and
the activity of SLC38A2. {ECO:0000269|PubMed:17003038}.
-!- SIMILARITY: Belongs to the amino acid/polyamine transporter 2
family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAC98152.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AK129342; BAC98152.1; ALT_INIT; mRNA.
EMBL; AK031615; BAC27479.1; -; mRNA.
EMBL; AK033812; BAC28483.1; -; mRNA.
EMBL; AK169378; BAE41125.1; -; mRNA.
EMBL; BC041108; AAH41108.1; -; mRNA.
EMBL; BC048178; AAH48178.1; -; mRNA.
EMBL; BC049271; AAH49271.1; -; mRNA.
EMBL; BC057454; AAH57454.1; -; mRNA.
CCDS; CCDS27778.1; -.
RefSeq; NP_780330.2; NM_175121.3.
UniGene; Mm.46754; -.
ProteinModelPortal; Q8CFE6; -.
BioGrid; 212424; 2.
STRING; 10090.ENSMUSP00000023099; -.
iPTMnet; Q8CFE6; -.
PhosphoSitePlus; Q8CFE6; -.
SwissPalm; Q8CFE6; -.
EPD; Q8CFE6; -.
MaxQB; Q8CFE6; -.
PaxDb; Q8CFE6; -.
PeptideAtlas; Q8CFE6; -.
PRIDE; Q8CFE6; -.
Ensembl; ENSMUST00000023099; ENSMUSP00000023099; ENSMUSG00000022462.
GeneID; 67760; -.
KEGG; mmu:67760; -.
UCSC; uc007xkm.1; mouse.
CTD; 54407; -.
MGI; MGI:1915010; Slc38a2.
eggNOG; KOG1305; Eukaryota.
eggNOG; COG0814; LUCA.
GeneTree; ENSGT00760000119147; -.
HOVERGEN; HBG059571; -.
InParanoid; Q8CFE6; -.
KO; K14207; -.
OMA; FAYTCHQ; -.
OrthoDB; EOG091G0GP8; -.
PhylomeDB; Q8CFE6; -.
TreeFam; TF328787; -.
Reactome; R-MMU-210500; Glutamate Neurotransmitter Release Cycle.
Reactome; R-MMU-352230; Amino acid transport across the plasma membrane.
PRO; PR:Q8CFE6; -.
Proteomes; UP000000589; Chromosome 15.
Bgee; ENSMUSG00000022462; -.
CleanEx; MM_SAT2; -.
CleanEx; MM_SLC38A2; -.
Genevisible; Q8CFE6; MM.
GO; GO:0030424; C:axon; IEA:Ensembl.
GO; GO:0005903; C:brush border; IEA:Ensembl.
GO; GO:0030425; C:dendrite; IEA:Ensembl.
GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
GO; GO:0005886; C:plasma membrane; IDA:MGI.
GO; GO:0042383; C:sarcolemma; IEA:Ensembl.
GO; GO:0015171; F:amino acid transmembrane transporter activity; IDA:MGI.
GO; GO:0015293; F:symporter activity; IEA:UniProtKB-KW.
GO; GO:0032328; P:alanine transport; IEA:Ensembl.
GO; GO:0006865; P:amino acid transport; IDA:MGI.
GO; GO:0034198; P:cellular response to amino acid starvation; IEA:Ensembl.
GO; GO:0071260; P:cellular response to mechanical stimulus; IEA:Ensembl.
GO; GO:0021987; P:cerebral cortex development; IEA:Ensembl.
GO; GO:0007565; P:female pregnancy; IEA:Ensembl.
GO; GO:0031460; P:glycine betaine transport; IEA:Ensembl.
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_0000311370.
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 239 289 Extracellular. {ECO:0000255}.
TRANSMEM 290 310 Helical. {ECO:0000255}.
TOPO_DOM 311 326 Cytoplasmic. {ECO:0000255}.
TRANSMEM 327 347 Helical. {ECO:0000255}.
TOPO_DOM 348 368 Extracellular. {ECO:0000255}.
TRANSMEM 369 389 Helical. {ECO:0000255}.
TOPO_DOM 390 410 Cytoplasmic. {ECO:0000255}.
TRANSMEM 411 431 Helical. {ECO:0000255}.
TOPO_DOM 432 433 Extracellular. {ECO:0000255}.
TRANSMEM 434 454 Helical. {ECO:0000255}.
TOPO_DOM 455 471 Cytoplasmic. {ECO:0000255}.
TRANSMEM 472 492 Helical. {ECO:0000255}.
TOPO_DOM 493 504 Extracellular. {ECO:0000255}.
REGION 1 96 Regulates protein turnover upon amino
acid deprivation. {ECO:0000250}.
MOD_RES 12 12 Phosphoserine.
{ECO:0000250|UniProtKB:Q96QD8}.
MOD_RES 21 21 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 22 22 Phosphoserine.
{ECO:0000250|UniProtKB:Q96QD8}.
MOD_RES 55 55 Phosphoserine.
{ECO:0000244|PubMed:19144319}.
CARBOHYD 254 254 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 258 258 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CONFLICT 245 245 C -> R (in Ref. 2; BAC27479).
{ECO:0000305}.
SEQUENCE 504 AA; 55503 MW; E69A497E350B5AEF CRC64;
MKKTEMGRFN ISPDEDSSSY SSNSDFNYSY PTKQAALKSH YADVDPENQN FLLESNLGKK
KYETDFHPGT TSFGMSVFNL SNAIVGSGIL GLSYAMANTG IALFIILLTF VSIFSLYSVH
LLLKTANEGG SLLYEQLGHK AYGLAGKLAA SGSITMQNIG AMSSYLFIVK YELPLVIKAL
MNIEDTNGLW YLNGDYLVLL VSLVLILPLS LLRNLGYLGY TSGLSLLCMI FFLIVVICKK
FQIPCPVEAA LVANETVNGT FTQAALALAF NSTADDACRP RYFIFNSQTV YAVPILTFSF
VCHPAVLPIY EELKSRSRRR MMNVSKISFF AMFLMYLLAA LFGYLTFYGH VESELLHTYS
EIVGTDILLL VVRLAVLVAV TLTVPVVIFP IRSSVTHLLC PTKEFSWLRH SIITVTILSF
TNLLVIFVPT IRDIFGFIGA SAAAMLIFIL PSAFYIKLVK KEPMRSVQKI GALCFLLSGI
VVMIGSMGLI VLDWVHDASA AGGH


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