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2.A.23.2.4 Aspartate/taurine (not glutamate):Na⁺ symporter, dEAAT2 (mediates both uptake and heteroexchange of its two substrates, both dependent on external Na⁺ (with taurine outside and Asp inside)); L-glutamate is transported with low affinity and efficiency (Besson et al., 2005).
Accession Number:	Q8T0S9
Protein Name:	dEaat2 aka CG3159-PB, isoform B
Length:	371
Molecular Weight:	40806.00
Species:	Drosophila melanogaster (Fruit fly) [7227]
Number of TMSs:	4
Location¹ / Topology² / Orientation³:	Cell membrane¹ / Multi-pass membrane protein²
Substrate	sodium(1+), L-glutamate(1-), taurine, aspartate(2-)

Pfam:	PF00375
Gene Ontology GO:0016020 C:membrane GO:0015183 F:L-aspartate transmembrane transporter activity GO:0017153 F:sodium:dicarboxylate symporter activity GO:0005369 F:taurine:sodium symporter activity GO:0006835 P:dicarboxylic acid transport GO:0015734 P:taurine transport
References (2) [1] “The genome sequence of Drosophila melanogaster.” Adams M.D.et.al. 10731132 [2] “Annotation of the Drosophila melanogaster euchromatic genome: a systematic review.” Misra S.et.al. 12537572

UniProt (Universal Protein Resource)
CDD Search (Conserved Domain Database)

Predict TMSs (Predict number of transmembrane segments)

FASTA formatted sequence

1:	MEMEKSGKFS DYLFAKMGPP TSTELPPKTT ECSDAPVELT GYRRWLSENL MLLVTLSGVL 
61:	
LGVILGLS LRPLNLHGDS IMLISYPGEL FMRVLKLMIL PLVISSLIAG SASLNAKMNG 
121:	KI
ALRTLV YFASTSFFNA ALGIALVLLI HPGNPDLHNA DDRSTDRRAV NLLDSLLDLG 
181:	RNVF
PDNL FQASIQQAHT VYLPKPSILH VFNETMNDTL ASGSEAQRLS EDLTEDVVLV 
241:	RDIQYR
SG TNTLGIVFFC LVFGTFLGTI GQKGQVVVDF FAAIFEVIMK MVTCVMWLTP 
301:	VGISSVIA
 GKILSVGDLG LVMSQLMWFI VTVAIGVFIY QFVVMQAIYF VVVRRNPFKF 
361:	YAGLIQAMLT 
AFATASTA AALPITFRCM NEKLKVDPRI TRFVLPIGCN INMDGTALYI 
421:	AVASIFIAQM SG
MVLGFG ELLTVLLTST AASMSSASVP SAALVLLLVV LTAIDAPVQD 
481:	VTLLFAVDWF VDRI
RTTN NMLGDCYTAA VVEELSRKEL MALDAASVNY QDMPAGTPNG 
541:	HGHGHGHHDG GLLEGQ
TE LETSSKCVMT MTDSVVVDIS AVMNNVNLQQ EHCNRRV

2.A.23.2.4
Aspartate/taurine (not glutamate):Na⁺ symporter, dEAAT2 (mediates both uptake and heteroexchange of its two substrates, both dependent on external Na⁺ (with taurine outside and Asp inside)); L-glutamate is transported with low affinity and efficiency (Besson et al., 2005).

Cross database links:

Gene Ontology

References (2)

External Searches:

Analyze:

2.A.23.2.4Aspartate/taurine (not glutamate):Na+ symporter, dEAAT2 (mediates both uptake and heteroexchange of its two substrates, both dependent on external Na+ (with taurine outside and Asp inside)); L-glutamate is transported with low affinity and efficiency (Besson et al., 2005).

Cross database links:

Gene Ontology

References (2)

External Searches:

Analyze:

2.A.23.2.4
Aspartate/taurine (not glutamate):Na⁺ symporter, dEAAT2 (mediates both uptake and heteroexchange of its two substrates, both dependent on external Na⁺ (with taurine outside and Asp inside)); L-glutamate is transported with low affinity and efficiency (Besson et al., 2005).