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Q9DCP2 (S38A3_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 98. 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 3
Alternative name(s):
N-system amino acid transporter 1
Na(+)-coupled neutral amino acid transporter 3
Solute carrier family 38 member 3
Short name=mNAT
System N amino acid transporter 1
Gene names
Name:Slc38a3
Synonyms:Sn1, Snat3
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length505 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Sodium-dependent amino acid/proton antiporter. Mediates electrogenic cotransport of glutamine and sodium ions in exchange for protons. Also recognizes histidine, asparagine and alanine. May mediate amino acid transport in either direction under physiological conditions. May play a role in nitrogen metabolism and synaptic transmission. Ref.1 UniProtKB Q9JHZ9

Subcellular location

Cell membrane; Multi-pass membrane protein Ref.1.

Tissue specificity

Expressed predominantly in liver, moderately expressed in kidney and brain, and barely detectable in heart and muscle. Within liver, expressed in hepatocytes. Not detected in testis. Ref.1

Sequence similarities

Belongs to the amino acid/polyamine transporter 2 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 505505Sodium-coupled neutral amino acid transporter 3
PRO_0000093829

Regions

Transmembrane82 – 10221Helical; Potential
Transmembrane105 – 12521Helical; Potential
Transmembrane143 – 16321Helical; Potential
Transmembrane186 – 20621Helical; Potential
Transmembrane212 – 23221Helical; Potential
Transmembrane288 – 30821Helical; Potential
Transmembrane325 – 34521Helical; Potential
Transmembrane367 – 38721Helical; Potential
Transmembrane409 – 42921Helical; Potential
Transmembrane432 – 45221Helical; Potential
Transmembrane472 – 49221Helical; Potential

Amino acid modifications

Glycosylation731N-linked (GlcNAc...) Potential
Glycosylation2471N-linked (GlcNAc...) Potential
Glycosylation2511N-linked (GlcNAc...) Potential
Glycosylation3241N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict1101S → N in BAC28963. Ref.2
Sequence conflict1301Q → R in BAC28963. Ref.2
Sequence conflict2701T → A in AAF61849. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9DCP2 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 368DBB87F1BB248A

FASTA50555,592
        10         20         30         40         50         60 
MEIPRQTEMV ELVPNGKHLE GLLPVGVPTT DTQRTEDTQH CGEGKGFLQK SPSKEPHFTD 

        70         80         90        100        110        120 
FEGKTSFGMS VFNLSNAIMG SGILGLAYAM ANTGIILFLF LLTAVALLSS YSIHLLLKSS 

       130        140        150        160        170        180 
GIVGIRAYEQ LGYRAFGTPG KLAAALAITL QNIGAMSSYL YIIKSELPLV IQTFLNLEKP 

       190        200        210        220        230        240 
ASVWYMDGNY LVILVSVTII LPLALMRQLG YLGYSSGFSL SCMVFFLIAV IYKKFQVPCP 

       250        260        270        280        290        300 
LAHNLANATG NFSHMVVAEE KAQLQGEPDT AAEAFCTPSY FTLNSQTAYT IPIMAFAFVC 

       310        320        330        340        350        360 
HPEVLPIYTE LKDPSKRKMQ HISNLSIAVM YVMYFLAALF GYLTFYDGVE SELLHTYSKV 

       370        380        390        400        410        420 
DPFDVLILCV RVAVLIAVTL TVPIVLFPVR RAIQQMLFQN QEFSWLRHVL IATGLLTCIN 

       430        440        450        460        470        480 
LLVIFAPNIL GIFGIIGATS APCLIFIFPA IFYFRIMPTD KEPARSTPKI LALCFAAVGF 

       490        500 
LLMTMSLSFI IIDWVSGTSQ HGGNH 

« Hide

References

« Hide 'large scale' references
[1]"Identification and characterization of an amino acid transporter expressed differentially in liver."
Gu S., Roderick H.L., Camacho P., Jiang J.X.
Proc. Natl. Acad. Sci. U.S.A. 97:3230-3235(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
Tissue: Brain, Kidney and Liver.
[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: Embryo and Kidney.
[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.
Tissue: Brain and Retina.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF159856 mRNA. Translation: AAF61849.1.
AK002607 mRNA. Translation: BAB22226.1.
AK035155 mRNA. Translation: BAC28963.1.
BC054846 mRNA. Translation: AAH54846.1.
BC055339 mRNA. Translation: AAH55339.1.
CCDSCCDS23503.1.
RefSeqNP_001186146.1. NM_001199217.1.
NP_001186147.1. NM_001199218.1.
NP_076294.2. NM_023805.3.
XP_006511909.1. XM_006511846.1.
UniGeneMm.296560.

3D structure databases

ProteinModelPortalQ9DCP2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid218051. 1 interaction.
IntActQ9DCP2. 2 interactions.
MINTMINT-1837264.
STRING10090.ENSMUSP00000010208.

Protein family/group databases

TCDB2.A.18.6.2. the amino acid/auxin permease (aaap) family.

PTM databases

PhosphoSiteQ9DCP2.

Proteomic databases

MaxQBQ9DCP2.
PaxDbQ9DCP2.
PRIDEQ9DCP2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000010208; ENSMUSP00000010208; ENSMUSG00000010064.
ENSMUST00000167868; ENSMUSP00000130414; ENSMUSG00000010064.
ENSMUST00000177567; ENSMUSP00000137561; ENSMUSG00000010064.
GeneID76257.
KEGGmmu:76257.
UCSCuc009rmn.1. mouse.

Organism-specific databases

CTD10991.
MGIMGI:1923507. Slc38a3.

Phylogenomic databases

eggNOGCOG0814.
GeneTreeENSGT00650000093166.
HOGENOMHOG000013088.
HOVERGENHBG059571.
InParanoidQ9DCP2.
KOK13576.
OMAIGHSATH.
OrthoDBEOG7WHH9J.
PhylomeDBQ9DCP2.
TreeFamTF328787.

Gene expression databases

BgeeQ9DCP2.
CleanExMM_SLC38A3.
GenevestigatorQ9DCP2.

Family and domain databases

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

Other

ChiTaRSSLC38A3. mouse.
NextBio344865.
PROQ9DCP2.
SOURCESearch...

Entry information

Entry nameS38A3_MOUSE
AccessionPrimary (citable) accession number: Q9DCP2
Secondary accession number(s): Q8BS53, Q9JLL8
Entry history
Integrated into UniProtKB/Swiss-Prot: September 27, 2004
Last sequence update: June 1, 2001
Last modified: July 9, 2014
This is version 98 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