SLC20A1 Membrane Protein Introduction

Introduction of SLC20A1

Sodium-dependent phosphate transporter 1, also known as Gibbon ape leukemia virus receptor 1 (GLVR-1), is a transmembrane protein encoded by the SLC20A1 gene in humans. Retroviral receptors allow infection of human and mouse cells by various retroviruses. CD4 cells of human immunodeficiency virus, Rec1 of the ecological virus of mice, and GLVR1 of the Yoshimoto leukemia virus belong to the receptors recognized at the molecular level. These three proteins have no homology at the DNA or protein level.

Basic Information of SLC20A1
Protein Name	Sodium-dependent phosphate transporter 1
Gene Name	SLC20A1
Aliases	Gibbon ape leukemia virus receptor 1 (GLVR-1), Leukemia virus receptor 1 homolog, Phosphate transporter 1 (PiT-1), Solute carrier family 20 member 1
Organism	Homo sapiens (Human)
UniProt ID	Q8WUM9
Transmembrane Times	10
Length (aa)	679
Sequence	MATLITSTTAATAASGPLVDYLWMLILGFIIAFVLAFSVGANDVANSFGTAVGSGVVTLKQACILASIFETVGSVLLGAKVSETIRKGLIDVEMYNSTQGLLMAGSVSAMFGSAVWQLVASFLKLPISGTHCIVGATIGFSLVAKGQEGVKWSELIKIVMSWFVSPLLSGIMSGILFFLVRAFILHKADPVPNGLRALPVFYACTVGINLFSIMYTGAPLLGFDKLPLWGTILISVGCAVFCALIVWFFVCPRMKRKIEREIKCSPSESPLMEKKNSLKEDHEETKLSVGDIENKHPVSEVGPATVPLQAVVEERTVSFKLGDLEEAPERERLPSVDLKEETSIDSTVNGAVQLPNGNLVQFSQAVSNQINSSGHYQYHTVHKDSGLYKELLHKLHLAKVGDCMGDSGDKPLRRNNSYTSYTMAICGMPLDSFRAKEGEQKGEEMEKLTWPNADSKKRIRMDSYTSYCNAVSDLHSASEIDMSVKAEMGLGDRKGSNGSLEEWYDQDKPEVSLLFQFLQILTACFGSFAHGGNDVSNAIGPLVALYLVYDTGDVSSKVATPIWLLLYGGVGICVGLWVWGRRVIQTMGKDLTPITPSSGFSIELASALTVVIASNIGLPISTTHCKVGSVVSVGWLRSKKAVDWRLFRNIFMAWFVTVPISGVISAAIMAIFRYVILRM

Function of SLC20A1 Membrane Protein

The structure of SLC20A1 was initially predicted to contain 10 transmembrane helices (TMHs), with both the N and C termini positioned intracellularly. The predicted structure of SLC20A1 has since been modified, based on experimental data that showed both ends of the protein are extracellular and that the protein contains an N-linked glycosylation site; however, the number and positions of the extracellular regions (ECRs) and transmembrane helices (TMHs) remain not experimentally validated.

SLC20A1 is a sodium-dependent phosphate symporter. It is ubiquitously expressed and plays a major role in the housekeeping process of maintaining cell P_i homeostasis in transporting monovalent H₂PO₄ forms of P_i. This P_i transporter is important for chondroblastic and osteoblastic mineralization and vascular calcification.

SLC20A1 Membrance Protein Introduction Fig.1 The structure of Sodium-dependent phosphate transporter 1.

Application of SLC20A1 Membrane Protein in Literature

El H.D., et al. High Expression of the Pi-Transporter SLC20A1/Pit1 in Calcific Aortic Valve Disease Promotes Mineralization through Regulation of Akt-1. PLoS ONE. 2013, 8 (1): e53393. PubMed ID: 23308213

These results strongly suggest that apoptosis and mineralization are promoted by the overexpression of SLC20A1 which utilizes the altering to the level of Akt-1.
Keasey M.P., et al. Vitamin-D Receptor Agonist Calcitriol Reduces Calcification in Vitro through Selective Upregulation of SLC20A2 but Not SLC20A1 or XPR1. Scientific Reports. 2016, (6): 25802. PubMed ID: 27184385

This study reveals that neither SLC20A1 nor XPR1 were affected by calcitriol treatment and remained suppressed.
Farrell K.B., Tusnady GE, Eiden MV. New Structural Arrangement of the Extracellular Regions of the Phosphate Transporter SLC20A1, the Receptor for Gibbon Ape Leukemia Virus. The Journal of Biological Chemistry. 2009, 284(43):29979-29987. PubMed ID: 19717569

The authors propose a comprehensive topological model for SLC20A1, a transmembrane protein with 12 transmembrane helices and 7 extracellular regions, that varies from previous models and should permit approaches that define both virus interaction and transport function.
Liu Li., et al. Mice Lacking the Sodium-Dependent Phosphate Import Protein, PiT1 (SLC20A1), Have a Severe Defect in Terminal Erythroid Differentiation and Early B Cell Development. Experimental hematology. 2013, 41 (5): 432-43. PubMed ID: 23376999

The severity of the anemia and block in terminal erythroid differentiation and B cell lympho-penia are striking and suggest that PiT1 serves a fundamental and nonredundant role in murine terminal erythroid differentiation and B cell development.
Salaün C., et al. Identification of a Novel Transport-Independent Function of PiT1/SLC20A1 in the Regulation of TNF-Induced Apoptosis. The Journal of Biological Chemistry. 2010, 285 (45): 34408-34418. PubMed ID: 20817733

The results show that the re-expression of a Pi uptake mutant of PiT1 in PiT1^−/− mouse embryonic fibroblasts delays apoptosis as efficiently as the WT protein, showing that this function of PiT1 is unrelated to its transport activity.

SLC20A1 Preparation Options

To obtain the soluble and functional target protein, the versatile Magic™ membrane protein production platform in Creative Biolabs enables many flexible options, from which you can always find a better match for your particular project. Besides, aided by our versatile Magic™ anti-membrane protein antibody discovery platform, we also provide customized anti-SLC20A1 antibody development services.

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