4F2 cell-surface antigen heavy chain is a protein that in humans is encoded by the SLC3A2 (solute carrier family 3 member 2) gene.[5][6]
SLC3A2 | |||||||||||||||||||||||||||||||||||||||||||||||||||
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Identifiers | |||||||||||||||||||||||||||||||||||||||||||||||||||
Aliases | SLC3A2, 4F2, 4F2HC, 4T2HC, CD98, CD98HC, MDU1, NACAE, solute carrier family 3 member 2 | ||||||||||||||||||||||||||||||||||||||||||||||||||
External IDs | OMIM: 158070; MGI: 96955; HomoloGene: 1795; GeneCards: SLC3A2; OMA:SLC3A2 - orthologs | ||||||||||||||||||||||||||||||||||||||||||||||||||
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SLC3A2 comprises the heavy subunit of the large neutral amino acid transporter (LAT1) that is also known as CD98 (cluster of differentiation 98).[7][8]
Function
SLC3A2 is a member of the solute carrier family and encodes a cell surface, transmembrane protein with an alpha-amylase domain. The protein exists as the heavy chain of a heterodimer, covalently bound through di-sulfide bonds to one of several possible light chains. It associates with integrins and mediates integrin-dependent signaling related to normal cell growth and tumorigenesis. Alternate transcriptional splice variants, encoding different isoforms, have been characterized.[6]
LAT1 is a heterodimeric membrane transport protein that preferentially transports neutral branched (valine, leucine, isoleucine) and aromatic (tryptophan, tyrosine, phenylalanine) amino acids.[9] LAT is highly expressed in brain capillaries (which form the blood brain barrier) relative to other tissues.[9]
A functional LAT1 transporter is composed of two proteins encoded by two distinct genes:
Interactions
SLC3A2 has been shown to interact with SLC7A7.[12]
Additionally, SLC3A2 is a constituent member of the system xc- cystine/glutamate antiporter, complexing with SLC7A11.
See also
References
Further reading
External links
- Large+Neutral+Amino+Acid-Transporter+1 at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
- Amino+Acid+Transport+System+L at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
This article incorporates text from the United States National Library of Medicine, which is in the public domain.