SLC2A13 Membrane Protein Introduction

Introduction of SLC2A13

Proton myo-inositol cotransporter (H(+)-myo-inositol cotransporter, Hmit), also known as H(+)-myo-inositol symporter or solute carrier family 2 member 13 (SLC2A13), is a protein that in humans is encoded by the SLC2A13 gene. It belongs to the class III GLUT family.

Basic Information of SLC2A13
Protein Name	Proton myo-inositol cotransporter
Gene Name	SLC2A13
Aliases	H(+)-myo-inositol cotransporter, Hmit, H(+)-myo-inositol symporter, solute carrier family 2 member 13
Organism	Homo sapiens (Human)
UniProt ID	Q96QE2
Transmembrane Times	12
Length (aa)	648
Sequence	MSRKASENVEYTLRSLSSLMGERRRKQPEPDAASAAGECSLLAAAESSTSLQSAGAGGGGVGDLERAARRQFQQDETPAFVYVVAVFSALGGFLFGYDTGVVSGAMLLLKRQLSLDALWQELLVSSTVGAAAVSALAGGALNGVFGRRAAILLASALFTAGSAVLAAANNKETLLAGRLVVGLGIGIASMTVPVYIAEVSPPNLRGRLVTINTLFITGGQFFASVVDGAFSYLQKDGWRYMLGLAAVPAVIQFFGFLFLPESPRWLIQKGQTQKARRILSQMRGNQTIDEEYDSIKNNIEEEEKEVGSAGPVICRMLSYPPTRRALIVGCGLQMFQQLSGINTIMYYSATILQMSGVEDDRLAIWLASVTAFTNFIFTLVGVWLVEKVGRRKLTFGSLAGTTVALIILALGFVLSAQVSPRITFKPIAPSGQNATCTRYSYCNECMLDPDCGFCYKMNKSTVIDSSCVPVNKASTNEAAWGRCENETKFKTEDIFWAYNFCPTPYSWTALLGLILYLVFFAPGMGPMPWTVNSEIYPLWARSTGNACSSGINWIFNVLVSLTFLHTAEYLTYYGAFFLYAGFAAVGLLFIYGCLPETKGKKLEEIESLFDNRLCTCGTSDSDEGRYIEYIRVKGSNYHLSDNDASDVE

Function of SLC2A13 Membrane Protein

HMIT (SLC2A13) is a member of the class III GLUT family which is restricted to an intracellular location. It is a glycosylated protein containing three conserved internalization signals: an endoplasmic reticulum (ER) retention signal in the N-terminal region, a dileucine internalization signal and a tyrosine-based internalization motif at the C-terminal. Despite low expression level in adipose tissue and kidney, HMIT is predominantly expressed in the brain, with high expression found in hippocampus, hypothalamus, cerebellum, and brainstem. Surprisingly, no sugar transport activity has been found for HMIT. Instead, HMIT has been identified as an H1-coupled myoinositol symporter with a Km of about 100 lM. More recently, HMIT has been shown to transport inositol-3-phosphate (IP3). Furthermore, studies have shown that HMIT is inhibited by the common GLUT inhibitors phloretin, phlorizin, and cytochalasin B, although at high concentrations.

Fig.1 Protein model for human SMIT1 and postulated splice variants. (Schneider, 2015)

Application SLC2A13 of Membrane Protein in Literature

G Lee D., et al. H⁺-myo-inositol transporter SLC2A13 as a potential marker for cancer stem cells in an oral squamous cell carcinoma. Current cancer drug targets. 2011, 11(8):966-75. PubMed ID: 21861841

This article aims to find new CSC markers for oral squamous cell carcinoma (OSCC). It suggests that SLC2A13 can be a potential marker for CSC in various tumors.
Uldry M., et al. Identification of a mammalian H⁺-myo-inositol symporter expressed predominantly in the brain. The EMBO Journal. 2001, 20(16):4467-77. PubMed ID: 11500374

This article investigates the functional characterization of a novel H(+)-myo-inositol co-transporter, HMIT, expressed predominantly in the brain. It indicates that HMIT has a key role in the control of myo-inositol brain metabolism.
Di Daniel E., et al. Evaluation of expression and function of the H⁺/myo-inositol transporter HMIT. BMC cell biology. 2009, 10(1):54. PubMed ID: 19607714

This article is conducted to study the expression and function of the recently identified H⁺/myo-inositol transporter (HMIT) in PIns signaling. It suggests that HMIT can transport inositol triphosphate, indicating unanticipated intracellular functions for this transporter that may be relevant to mood control.
Edamatsu M., et al. Differential localizations of the myo-inositol transporters HMIT and SMIT1 in the cochlear stria vascularis. Neuroscience letters. 2018, 674:88-93. PubMed ID: 29551423

This article investigates the protein localization of HMIT and Na⁺/myo-inositol cotransporter 1 (SMIT1) in the stria vascularis by immunohistochemistry. It suggests that HMIT is expressed in marginal cells and basal cells of the stria vascularis, indicating that HMIT may play important roles in the homeostasis of cochlear fluids, for example by participating in pH regulation and osmoregulation.

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Reference

Schneider S. (2015). Inositol transport proteins. FEBS letters. 589(10): 1049-1058.

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