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Q8CFE6 (S38A2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 76. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:Slc38a2
Synonyms:Ata2, Kiaa1382, Sat2, Snat2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length504 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.6

Enzyme regulation

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

Subcellular location

Cell membrane; Multi-pass membrane protein. 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 By similarity. Ref.7 Ref.8

Tissue specificity

Expressed in cerebral and cerebellar astrocytes and neurons. Ref.5

Induction

Up-regulated upon amino acid deprivation. Ref.4

Post-translational modification

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

Sequence similarities

Belongs to the amino acid/polyamine transporter 2 family.

Sequence caution

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 504504Sodium-coupled neutral amino acid transporter 2
PRO_0000311370

Regions

Topological domain1 – 7676Cytoplasmic Potential
Transmembrane77 – 9721Helical; Potential
Topological domain98 – 1025Extracellular Potential
Transmembrane103 – 12321Helical; Potential
Topological domain124 – 15835Cytoplasmic Potential
Transmembrane159 – 17921Helical; Potential
Topological domain180 – 1889Extracellular Potential
Transmembrane189 – 20921Helical; Potential
Topological domain210 – 2178Cytoplasmic Potential
Transmembrane218 – 23821Helical; Potential
Topological domain239 – 28951Extracellular Potential
Transmembrane290 – 31021Helical; Potential
Topological domain311 – 32616Cytoplasmic Potential
Transmembrane327 – 34721Helical; Potential
Topological domain348 – 36821Extracellular Potential
Transmembrane369 – 38921Helical; Potential
Topological domain390 – 41021Cytoplasmic Potential
Transmembrane411 – 43121Helical; Potential
Topological domain432 – 4332Extracellular Potential
Transmembrane434 – 45421Helical; Potential
Topological domain455 – 47117Cytoplasmic Potential
Transmembrane472 – 49221Helical; Potential
Topological domain493 – 50412Extracellular Potential
Region1 – 9696Regulates protein turnover upon amino acid deprivation By similarity

Amino acid modifications

Modified residue121Phosphoserine By similarity
Modified residue221Phosphoserine By similarity
Modified residue551Phosphoserine Ref.10
Glycosylation2541N-linked (GlcNAc...) Potential
Glycosylation2581N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict2451C → R in BAC27479. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q8CFE6 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: E69A497E350B5AEF

FASTA50455,503
        10         20         30         40         50         60 
MKKTEMGRFN ISPDEDSSSY SSNSDFNYSY PTKQAALKSH YADVDPENQN FLLESNLGKK 

        70         80         90        100        110        120 
KYETDFHPGT TSFGMSVFNL SNAIVGSGIL GLSYAMANTG IALFIILLTF VSIFSLYSVH 

       130        140        150        160        170        180 
LLLKTANEGG SLLYEQLGHK AYGLAGKLAA SGSITMQNIG AMSSYLFIVK YELPLVIKAL 

       190        200        210        220        230        240 
MNIEDTNGLW YLNGDYLVLL VSLVLILPLS LLRNLGYLGY TSGLSLLCMI FFLIVVICKK 

       250        260        270        280        290        300 
FQIPCPVEAA LVANETVNGT FTQAALALAF NSTADDACRP RYFIFNSQTV YAVPILTFSF 

       310        320        330        340        350        360 
VCHPAVLPIY EELKSRSRRR MMNVSKISFF AMFLMYLLAA LFGYLTFYGH VESELLHTYS 

       370        380        390        400        410        420 
EIVGTDILLL VVRLAVLVAV TLTVPVVIFP IRSSVTHLLC PTKEFSWLRH SIITVTILSF 

       430        440        450        460        470        480 
TNLLVIFVPT IRDIFGFIGA SAAAMLIFIL PSAFYIKLVK KEPMRSVQKI GALCFLLSGI 

       490        500 
VVMIGSMGLI VLDWVHDASA AGGH 

« Hide

References

« Hide 'large scale' references
[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(2003) [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. expand/collapse author list , 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(2005) [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(2004) [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(2004) [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(2004) [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(2005) [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(2006) [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(2006) [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(2008) [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(2009) [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(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS27778.1.
RefSeqNP_780330.2. NM_175121.3.
UniGeneMm.46754.

3D structure databases

ProteinModelPortalQ8CFE6.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid212424. 1 interaction.

PTM databases

PhosphoSiteQ8CFE6.

Proteomic databases

PaxDbQ8CFE6.
PRIDEQ8CFE6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000023099; ENSMUSP00000023099; ENSMUSG00000022462.
GeneID67760.
KEGGmmu:67760.
UCSCuc007xkm.1. mouse.

Organism-specific databases

CTD54407.
MGIMGI:1915010. Slc38a2.
RougeSearch...

Phylogenomic databases

eggNOGNOG236441.
GeneTreeENSGT00650000093166.
HOVERGENHBG059571.
InParanoidQ8CFE6.
KOK14207.
OMAMFLMYLF.
OrthoDBEOG7WHH9J.
PhylomeDBQ8CFE6.
TreeFamTF328787.

Gene expression databases

BgeeQ8CFE6.
CleanExMM_SAT2.
MM_SLC38A2.
GenevestigatorQ8CFE6.

Family and domain databases

InterProIPR013057. AA_transpt_TM.
[Graphical view]
PfamPF01490. Aa_trans. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio325493.
PROQ8CFE6.
SOURCESearch...

Entry information

Entry nameS38A2_MOUSE
AccessionPrimary (citable) accession number: Q8CFE6
Secondary accession number(s): Q3TEX3 expand/collapse secondary AC list , Q6PFR1, Q6ZPS7, Q810U9, Q8CC66, Q8CD21
Entry history
Integrated into UniProtKB/Swiss-Prot: November 13, 2007
Last sequence update: March 1, 2003
Last modified: July 9, 2014
This is version 76 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot