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Protein

Sodium-coupled neutral amino acid transporter 2

Gene

Slc38a2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

Enzyme regulationi

Inhibited by N-methyl-D-glucamine and choline.By similarity

GO - Molecular functioni

  1. amino acid transmembrane transporter activity Source: MGI
  2. symporter activity Source: UniProtKB-KW

GO - Biological processi

  1. amino acid transmembrane transport Source: GOC
  2. amino acid transport Source: MGI
  3. sodium ion transport Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Amino-acid transport, Ion transport, Sodium transport, Symport, Transport

Keywords - Ligandi

Sodium

Enzyme and pathway databases

ReactomeiREACT_287745. Glutamate Neurotransmitter Release Cycle.
REACT_301178. Amino acid transport across the plasma membrane.

Names & Taxonomyi

Protein namesi
Recommended name:
Sodium-coupled neutral amino acid transporter 2
Alternative name(s):
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
Gene namesi
Name:Slc38a2
Synonyms:Ata2, Kiaa1382, Sat2, Snat2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 15

Organism-specific databases

MGIiMGI:1915010. Slc38a2.

Subcellular locationi

Cell membrane 2 Publications; Multi-pass membrane protein 2 Publications
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.By similarity

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 7676CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei77 – 9721HelicalSequence AnalysisAdd
BLAST
Topological domaini98 – 1025ExtracellularSequence Analysis
Transmembranei103 – 12321HelicalSequence AnalysisAdd
BLAST
Topological domaini124 – 15835CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei159 – 17921HelicalSequence AnalysisAdd
BLAST
Topological domaini180 – 1889ExtracellularSequence Analysis
Transmembranei189 – 20921HelicalSequence AnalysisAdd
BLAST
Topological domaini210 – 2178CytoplasmicSequence Analysis
Transmembranei218 – 23821HelicalSequence AnalysisAdd
BLAST
Topological domaini239 – 28951ExtracellularSequence AnalysisAdd
BLAST
Transmembranei290 – 31021HelicalSequence AnalysisAdd
BLAST
Topological domaini311 – 32616CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei327 – 34721HelicalSequence AnalysisAdd
BLAST
Topological domaini348 – 36821ExtracellularSequence AnalysisAdd
BLAST
Transmembranei369 – 38921HelicalSequence AnalysisAdd
BLAST
Topological domaini390 – 41021CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei411 – 43121HelicalSequence AnalysisAdd
BLAST
Topological domaini432 – 4332ExtracellularSequence Analysis
Transmembranei434 – 45421HelicalSequence AnalysisAdd
BLAST
Topological domaini455 – 47117CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei472 – 49221HelicalSequence AnalysisAdd
BLAST
Topological domaini493 – 50412ExtracellularSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. integral component of plasma membrane Source: GO_Central
  2. plasma membrane Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 504504Sodium-coupled neutral amino acid transporter 2PRO_0000311370Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei12 – 121PhosphoserineBy similarity
Modified residuei22 – 221PhosphoserineBy similarity
Modified residuei55 – 551Phosphoserine1 Publication
Glycosylationi254 – 2541N-linked (GlcNAc...)Sequence Analysis
Glycosylationi258 – 2581N-linked (GlcNAc...)Sequence Analysis

Post-translational modificationi

Polyubiquitination by NEDD4L regulates the degradation and the activity of SLC38A2.1 Publication

Keywords - PTMi

Glycoprotein, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ8CFE6.
PaxDbiQ8CFE6.
PRIDEiQ8CFE6.

PTM databases

PhosphoSiteiQ8CFE6.

Expressioni

Tissue specificityi

Expressed in cerebral and cerebellar astrocytes and neurons.1 Publication

Inductioni

Up-regulated upon amino acid deprivation.1 Publication

Gene expression databases

BgeeiQ8CFE6.
CleanExiMM_SAT2.
MM_SLC38A2.
GenevestigatoriQ8CFE6.

Interactioni

Protein-protein interaction databases

BioGridi212424. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliQ8CFE6.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 9696Regulates protein turnover upon amino acid deprivationBy similarityAdd
BLAST

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG236441.
GeneTreeiENSGT00760000119147.
HOVERGENiHBG059571.
InParanoidiQ8CFE6.
KOiK14207.
OMAiAIFNIST.
OrthoDBiEOG7WHH9J.
PhylomeDBiQ8CFE6.
TreeFamiTF328787.

Family and domain databases

InterProiIPR013057. AA_transpt_TM.
[Graphical view]
PfamiPF01490. Aa_trans. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8CFE6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKKTEMGRFN ISPDEDSSSY SSNSDFNYSY PTKQAALKSH YADVDPENQN
60 70 80 90 100
FLLESNLGKK KYETDFHPGT TSFGMSVFNL SNAIVGSGIL GLSYAMANTG
110 120 130 140 150
IALFIILLTF VSIFSLYSVH LLLKTANEGG SLLYEQLGHK AYGLAGKLAA
160 170 180 190 200
SGSITMQNIG AMSSYLFIVK YELPLVIKAL MNIEDTNGLW YLNGDYLVLL
210 220 230 240 250
VSLVLILPLS LLRNLGYLGY TSGLSLLCMI FFLIVVICKK FQIPCPVEAA
260 270 280 290 300
LVANETVNGT FTQAALALAF NSTADDACRP RYFIFNSQTV YAVPILTFSF
310 320 330 340 350
VCHPAVLPIY EELKSRSRRR MMNVSKISFF AMFLMYLLAA LFGYLTFYGH
360 370 380 390 400
VESELLHTYS EIVGTDILLL VVRLAVLVAV TLTVPVVIFP IRSSVTHLLC
410 420 430 440 450
PTKEFSWLRH SIITVTILSF TNLLVIFVPT IRDIFGFIGA SAAAMLIFIL
460 470 480 490 500
PSAFYIKLVK KEPMRSVQKI GALCFLLSGI VVMIGSMGLI VLDWVHDASA

AGGH
Length:504
Mass (Da):55,503
Last modified:March 1, 2003 - v1
Checksum:iE69A497E350B5AEF
GO

Sequence cautioni

The sequence BAC98152.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti245 – 2451C → R in BAC27479 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK129342 mRNA. Translation: BAC98152.1. Different initiation.
AK031615 mRNA. Translation: BAC27479.1.
AK033812 mRNA. Translation: BAC28483.1.
AK169378 mRNA. Translation: BAE41125.1.
BC041108 mRNA. Translation: AAH41108.1.
BC048178 mRNA. Translation: AAH48178.1.
BC049271 mRNA. Translation: AAH49271.1.
BC057454 mRNA. Translation: AAH57454.1.
CCDSiCCDS27778.1.
RefSeqiNP_780330.2. NM_175121.3.
UniGeneiMm.46754.

Genome annotation databases

EnsembliENSMUST00000023099; ENSMUSP00000023099; ENSMUSG00000022462.
GeneIDi67760.
KEGGimmu:67760.
UCSCiuc007xkm.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK129342 mRNA. Translation: BAC98152.1. Different initiation.
AK031615 mRNA. Translation: BAC27479.1.
AK033812 mRNA. Translation: BAC28483.1.
AK169378 mRNA. Translation: BAE41125.1.
BC041108 mRNA. Translation: AAH41108.1.
BC048178 mRNA. Translation: AAH48178.1.
BC049271 mRNA. Translation: AAH49271.1.
BC057454 mRNA. Translation: AAH57454.1.
CCDSiCCDS27778.1.
RefSeqiNP_780330.2. NM_175121.3.
UniGeneiMm.46754.

3D structure databases

ProteinModelPortaliQ8CFE6.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi212424. 1 interaction.

PTM databases

PhosphoSiteiQ8CFE6.

Proteomic databases

MaxQBiQ8CFE6.
PaxDbiQ8CFE6.
PRIDEiQ8CFE6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000023099; ENSMUSP00000023099; ENSMUSG00000022462.
GeneIDi67760.
KEGGimmu:67760.
UCSCiuc007xkm.1. mouse.

Organism-specific databases

CTDi54407.
MGIiMGI:1915010. Slc38a2.
RougeiSearch...

Phylogenomic databases

eggNOGiNOG236441.
GeneTreeiENSGT00760000119147.
HOVERGENiHBG059571.
InParanoidiQ8CFE6.
KOiK14207.
OMAiAIFNIST.
OrthoDBiEOG7WHH9J.
PhylomeDBiQ8CFE6.
TreeFamiTF328787.

Enzyme and pathway databases

ReactomeiREACT_287745. Glutamate Neurotransmitter Release Cycle.
REACT_301178. Amino acid transport across the plasma membrane.

Miscellaneous databases

NextBioi325493.
PROiQ8CFE6.
SOURCEiSearch...

Gene expression databases

BgeeiQ8CFE6.
CleanExiMM_SAT2.
MM_SLC38A2.
GenevestigatoriQ8CFE6.

Family and domain databases

InterProiIPR013057. AA_transpt_TM.
[Graphical view]
PfamiPF01490. Aa_trans. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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."
    Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Nagase T., Ohara O., Koga H.
    DNA Res. 10:167-180(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Embryonic tail.
  2. "The transcriptional landscape of the mammalian genome."
    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.
    Science 309:1559-1563(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Epididymis, Kidney and Testis.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6 and Czech II.
    Tissue: Brain and Mammary tumor.
  4. "Transcriptional control of the human sodium-coupled neutral amino acid transporter system A gene by amino acid availability is mediated by an intronic element."
    Palii S.S., Chen H., Kilberg M.S.
    J. Biol. Chem. 279:3463-3471(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  5. "Glutamine uptake and expression of mRNA's of glutamine transporting proteins in mouse cerebellar and cerebral cortical astrocytes and neurons."
    Dolinska M., Zablocka B., Sonnewald U., Albrecht J.
    Neurochem. Int. 44:75-81(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  6. "Adaptation of nutrient supply to fetal demand in the mouse involves interaction between the Igf2 gene and placental transporter systems."
    Constancia M., Angiolini E., Sandovici I., Smith P., Smith R., Kelsey G., Dean W., Ferguson-Smith A., Sibley C.P., Reik W., Fowden A.
    Proc. Natl. Acad. Sci. U.S.A. 102:19219-19224(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  7. "Regulation of amino acid transporter ATA2 by ubiquitin ligase Nedd4-2."
    Hatanaka T., Hatanaka Y., Setou M.
    J. Biol. Chem. 281:35922-35930(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, UBIQUITINATION BY NEDD4L.
  8. "Amino acid transporter ATA2 is stored at the trans-Golgi network and released by insulin stimulus in adipocytes."
    Hatanaka T., Hatanaka Y., Tsuchida J., Ganapathy V., Setou M.
    J. Biol. Chem. 281:39273-39284(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  9. "Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain."
    Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.
    J. Proteome Res. 7:311-318(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.
  10. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-55, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
    Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
    Mol. Cell. Proteomics 8:904-912(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiS38A2_MOUSE
AccessioniPrimary (citable) accession number: Q8CFE6
Secondary accession number(s): Q3TEX3
, Q6PFR1, Q6ZPS7, Q810U9, Q8CC66, Q8CD21
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 13, 2007
Last sequence update: March 1, 2003
Last modified: April 1, 2015
This is version 83 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.