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2.A.18.6.4
Plasma membrane System A-like neutral amino acid transporter, SA1, SAT2 or SNAT2 (transports small, neutral aliphatic amino acids including α-(methylamino)isobutyrate, mAIB with Na+ (1:1 stoichiometry; Km = 200-500 μM)). Asparagine 82 controls the interaction of Na+ with the transporter (Zhang and Grewer, 2007). The C-terminal domain regulates transport activity through a voltage-dependent process (Zhang et al., 2011).

Accession Number:Q9JHE5
Protein Name:SAT2
Length:504
Molecular Weight:55554.00
Species:Rattus norvegicus (Rat) [10116]
Number of TMSs:12
Location1 / Topology2 / Orientation3: Cell membrane1 / Multi-pass membrane protein2
Substrate Neutral amino acids, Na+

Cross database links:

Genevestigator: Q9JHE5
eggNOG: roNOG11799
RefSeq: NP_851604.1   
Entrez Gene ID: 29642   
Pfam: PF01490   
KEGG: rno:29642   

Gene Ontology

GO:0016021 C:integral to membrane
GO:0005886 C:plasma membrane
GO:0015293 F:symporter activity
GO:0006865 P:amino acid transport
GO:0006814 P:sodium ion transport

References (12)

[1] “Cloning of an amino acid transporter with functional characteristics and tissue expression pattern identical to that of system A.”  Sugawara M.et.al.   10747860
[2] “A novel system A isoform mediating Na+/neutral amino acid cotransport.”  Yao D.et.al.   10811809
[3] “Amino acid transport system A resembles system N in sequence but differs in mechanism.”  Reimer R.J.et.al.   10859363
[4] “Subcellular localization and adaptive up-regulation of the system A (SAT2) amino acid transporter in skeletal-muscle cells and adipocytes.”  Hyde R.et.al.   11311116
[5] “Transforming growth factor-beta 1 stimulates vascular smooth muscle cell L-proline transport by inducing system A amino acid transporter 2 (SAT2) gene expression.”  Ensenat D.et.al.   11716780
[6] “ATA2-mediated amino acid uptake following partial hepatectomy is regulated by redistribution to the plasma membrane.”  Freeman T.L.et.al.   12054432
[7] “Insulin promotes the cell surface recruitment of the SAT2/ATA2 system A amino acid transporter from an endosomal compartment in skeletal muscle cells.”  Hyde R.et.al.   11834730
[8] “Glutamine uptake by neurons: interaction of protons with system a transporters.”  Chaudhry F.A.et.al.   11756489
[9] “ATA2 is predominantly expressed as system A at the blood-brain barrier and acts as brain-to-blood efflux transport for L-proline.”  Takanaga H.et.al.   12021389
[10] “Evidence for allosteric regulation of pH-sensitive System A (SNAT2) and System N (SNAT5) amino acid transporter activity involving a conserved histidine residue.”  Baird F.E.et.al.   16629640
[11] “Localization of the Na(+)-coupled neutral amino acid transporter 2 in the cerebral cortex.”  Melone M.et.al.   16616430
[12] “Distinct sensor pathways in the hierarchical control of SNAT2, a putative amino acid transceptor, by amino acid availability.”  Hyde R.et.al.   17488712

External Searches:

  • Search: DB with
  • BLAST ExPASy (Swiss Institute of Bioinformatics (SIB) BLAST)
  • CDD Search (Conserved Domain Database)
  • Search COGs (Clusters of Orthologous Groups of proteins)
  • 2° Structure (Network Protein Sequence Analysis)

Analyze:

Predict TMSs (Predict number of transmembrane segments)
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FASTA formatted sequence
1:	MKKTEMGRFN ISPDEDSSSY SSNGDFNYSY PTKQAALKSH YVDVDPENQN FLLESNLGKK 
61:	KYETDFHPGT TSFGMSVFNL SNAIVGSGIL GLSYAMANTG IALFIILLTF VSIFSLYSVH 
121:	LLLKTANEGG SLLYEQLGHK AYGLAGKLAA SGSITMQNIG AMSSYLFIVK YELPLVIKAL 
181:	MNIEDTNGLW YLNGDYLVLL VSFVLILPLS LLRNLGYLGY TSGLSLLCMI FFLIVVICKK 
241:	FQIPCPVEVA LMANETVNGT FTQVALAALA SNSTAADTCR PRYFIFNSQT VYAVPILTFS 
301:	FVCHPAVLPI YEELKSRSRR RMMNVSKISF FAMFLMYLLA ALFGYLTFYE HVESELLHTY 
361:	SAIVGTDILL LVVRLAVLVA VTLTVPVVIF PIRSSVTHLL CPTKEFSWFR HSVITVTILA 
421:	FTNLLVIFVP TIRDIFGFIG ASAAAMLIFI LPSAFYIKLV KKEPMRSVQK IGALCFLLSG 
481:	VVVMIGSMGL IVLDWVHDAS AGGH