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Showing Protein Sodium-coupled neutral amino acid transporter 2 (HMDBP03335)

IdentificationBiological propertiesGene propertiesProtein propertiesExternal linksReferencesXMLShow 1 metabolite
Identification
HMDB Protein ID HMDBP03335
Secondary Accession Numbers
  • 8923
Name Sodium-coupled neutral amino acid transporter 2
Synonyms
  1. Amino acid transporter A2
  2. Protein 40-9-1
  3. Solute carrier family 38 member 2
  4. System A amino acid transporter 2
  5. System A transporter 1
  6. System N amino acid transporter 2
Gene Name SLC38A2
Protein Type Unknown
Biological Properties
General Function Amino acid transport and metabolism
Specific 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
Pathways Not Available
Reactions Not Available
GO Classification Not Available
Cellular Location
  1. Cell membrane
  2. Multi-pass membrane protein
Gene Properties
Chromosome Location Chromosome:1
Locus 12q
SNPs SLC38A2
Gene Sequence 
>1521 bp
ATGAAGAAGGCCGAAATGGGACGATTCAGTATTTCCCCGGATGAAGACAGCAGCAGCTAC
AGTTCCAACAGCGACTTCAACTACTCCTACCCCACCAAGCAAGCTGCTCTGAAAAGCCAT
TATGCAGATGTAGATCCTGAAAACCAGAACTTTTTACTTGAATCGAATTTGGGGAAGAAG
AAGTATGAAACAGAATTTCATCCAGGTACTACTTCCTTTGGAATGTCAGTATTTAATCTG
AGCAATGCGATTGTGGGCAGTGGAATCCTTGGGCTTTCTTATGCCATGGCTAATACTGGA
ATTGCTCTTTTTATAATTCTCTTGACATTTGTGTCAATATTTTCCCTGTATTCTGTTCAT
CTCCTTTTGAAGACTGCCAATGAAGGAGGGTCTTTATTATATGAACAATTGGGATATAAG
GCATTTGGATTAGTTGGAAAGCTTGCAGCATCTGGATCAATTACAATGCAGAACATTGGA
GCTATGTCAAGCTACCTCTTCATAGTGAAATATGAGTTGCCTTTGGTGATCCAGGCATTA
ACGAACATTGAAGATAAAACTGGATTGTGGTATCTGAACGGGAACTATTTGGTTCTGTTG
GTGTCATTGGTGGTCATTCTTCCTTTGTCGCTGTTTAGAAATTTAGGATATTTGGGATAT
ACCAGTGGCCTTTCCTTGTTGTGTATGGTGTTCTTTCTGATTGTGGTCATTTGCAAGAAA
TTTCAGGTTCCGTGTCCTGTGGAAGCTGCTTTGATAATTAACGAAACAATAAACACCACC
TTAACACAGCCAACAGCTCTTGTACCTGCTTTGTCACATAACGTGACTGAAAATGACTCT
TGCAGACCTCACTATTTTATTTTCAACTCACAGACTGTCTATGCTGTGCCAATTCTGATC
TTTTCATTTGTCTGTCATCCTGCTGTTCTTCCCATCTATGAAGAACTGAAAGACCGCAGC
CGTAGAAGAATGATGAATGTGTCCAAGATTTCATTTTTTGCTATGTTTCTCATGTATCTG
CTTGCCGCCCTCTTTGGATACCTAACATTTTACGAACATGTTGAGTCAGAATTGCTTCAT
ACCTACTCTTCTATCTTGGGAACTGATATTCTTCTTCTCATTGTCCGTCTGGCTGTGTTA
ATGGCTGTGACCCTGACAGTACCAGTAGTTATTTTCCCAATCCGGAGTTCTGTAACTCAC
TTGTTGTGTGCATCAAAAGATTTCAGTTGGTGGCGTCATAGTCTCATTACAGTGTCTATC
TTGGCATTTACCAATTTACTTGTCATCTTTGTCCCAACTATTAGGGATATCTTTGGTTTT
ATTGGTGCATCTGCAGCTTCTATGTTGATTTTTATTCTTCCTTCTGCCTTCTATATCAAG
TTGGTGAAGAAAGAACCTATGAAATCTGTACAAAAGATTGGGGCTTTGTTCTTCCTGTTA
AGTGGTGTACTGGTGATGACCGGAAGCATGGCCTTGATTGTTTTGGATTGGGTACACAAT
GCACCTGGAGGTGGCCATTAA
Protein Properties
Number of Residues 506
Molecular Weight 56025.4
Theoretical pI 8.12
Pfam Domain Function
Signals
  • None
Transmembrane Regions
  • 77-97
  • 103-123
  • 159-179
  • 189-209
  • 218-238
  • 293-313
  • 330-350
  • 372-392
  • 414-434
  • 437-457
  • 475-495
Protein Sequence 
>Sodium-coupled neutral amino acid transporter 2
MKKAEMGRFSISPDEDSSSYSSNSDFNYSYPTKQAALKSHYADVDPENQNFLLESNLGKK
KYETEFHPGTTSFGMSVFNLSNAIVGSGILGLSYAMANTGIALFIILLTFVSIFSLYSVH
LLLKTANEGGSLLYEQLGYKAFGLVGKLAASGSITMQNIGAMSSYLFIVKYELPLVIQAL
TNIEDKTGLWYLNGNYLVLLVSLVVILPLSLFRNLGYLGYTSGLSLLCMVFFLIVVICKK
FQVPCPVEAALIINETINTTLTQPTALVPALSHNVTENDSCRPHYFIFNSQTVYAVPILI
FSFVCHPAVLPIYEELKDRSRRRMMNVSKISFFAMFLMYLLAALFGYLTFYEHVESELLH
TYSSILGTDILLLIVRLAVLMAVTLTVPVVIFPIRSSVTHLLCASKDFSWWRHSLITVSI
LAFTNLLVIFVPTIRDIFGFIGASAASMLIFILPSAFYIKLVKKEPMKSVQKIGALFFLL
SGVLVMTGSMALIVLDWVHNAPGGGH
GenBank ID Protein Not Available
UniProtKB/Swiss-Prot ID Q96QD8
UniProtKB/Swiss-Prot Entry Name S38A2_HUMAN
PDB IDs Not Available
GenBank Gene ID AF259799
GeneCard ID SLC38A2
GenAtlas ID SLC38A2
HGNC ID HGNC:13448
References
General References
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  3. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. doi: 10.1073/pnas.0805139105. Epub 2008 Jul 31. [PubMed:18669648 ]
  4. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. doi: 10.1126/scisignal.2000007. [PubMed:19690332 ]
  5. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed:17081983 ]
  6. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. doi: 10.1021/ac9004309. [PubMed:19413330 ]
  7. Rikova K, Guo A, Zeng Q, Possemato A, Yu J, Haack H, Nardone J, Lee K, Reeves C, Li Y, Hu Y, Tan Z, Stokes M, Sullivan L, Mitchell J, Wetzel R, Macneill J, Ren JM, Yuan J, Bakalarski CE, Villen J, Kornhauser JM, Smith B, Li D, Zhou X, Gygi SP, Gu TL, Polakiewicz RD, Rush J, Comb MJ: Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer. Cell. 2007 Dec 14;131(6):1190-203. [PubMed:18083107 ]
  8. Nakajima D, Okazaki N, Yamakawa H, Kikuno R, Ohara O, Nagase T: Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones. DNA Res. 2002 Jun 30;9(3):99-106. [PubMed:12168954 ]
  9. Zhang Y, Wolf-Yadlin A, Ross PL, Pappin DJ, Rush J, Lauffenburger DA, White FM: Time-resolved mass spectrometry of tyrosine phosphorylation sites in the epidermal growth factor receptor signaling network reveals dynamic modules. Mol Cell Proteomics. 2005 Sep;4(9):1240-50. Epub 2005 Jun 11. [PubMed:15951569 ]
  10. Heibeck TH, Ding SJ, Opresko LK, Zhao R, Schepmoes AA, Yang F, Tolmachev AV, Monroe ME, Camp DG 2nd, Smith RD, Wiley HS, Qian WJ: An extensive survey of tyrosine phosphorylation revealing new sites in human mammary epithelial cells. J Proteome Res. 2009 Aug;8(8):3852-61. doi: 10.1021/pr900044c. [PubMed:19534553 ]
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  13. Hatanaka T, Huang W, Wang H, Sugawara M, Prasad PD, Leibach FH, Ganapathy V: Primary structure, functional characteristics and tissue expression pattern of human ATA2, a subtype of amino acid transport system A. Biochim Biophys Acta. 2000 Jul 31;1467(1):1-6. [PubMed:10930503 ]
  14. Palii SS, Chen H, Kilberg MS: Transcriptional control of the human sodium-coupled neutral amino acid transporter system A gene by amino acid availability is mediated by an intronic element. J Biol Chem. 2004 Jan 30;279(5):3463-71. Epub 2003 Nov 17. [PubMed:14623874 ]
  15. Bevilacqua E, Bussolati O, Dall'Asta V, Gaccioli F, Sala R, Gazzola GC, Franchi-Gazzola R: SNAT2 silencing prevents the osmotic induction of transport system A and hinders cell recovery from hypertonic stress. FEBS Lett. 2005 Jun 20;579(16):3376-80. [PubMed:15922329 ]
  16. Gonzalez-Gonzalez IM, Cubelos B, Gimenez C, Zafra F: Immunohistochemical localization of the amino acid transporter SNAT2 in the rat brain. Neuroscience. 2005;130(1):61-73. [PubMed:15561425 ]
  17. Gaccioli F, Huang CC, Wang C, Bevilacqua E, Franchi-Gazzola R, Gazzola GC, Bussolati O, Snider MD, Hatzoglou M: Amino acid starvation induces the SNAT2 neutral amino acid transporter by a mechanism that involves eukaryotic initiation factor 2alpha phosphorylation and cap-independent translation. J Biol Chem. 2006 Jun 30;281(26):17929-40. Epub 2006 Apr 18. [PubMed:16621798 ]
  18. Melone M, Varoqui H, Erickson JD, Conti F: Localization of the Na(+)-coupled neutral amino acid transporter 2 in the cerebral cortex. Neuroscience. 2006 Jun 19;140(1):281-92. Epub 2006 Apr 17. [PubMed:16616430 ]