Introduction of FXYD1
FXYD1 belongs to the FXYD family of which members share a 35-amino acid signature sequence domain, beginning with the amino acid sequence PFXYD. FXYD1 is a single-pass type I membrane protein, with its N-terminus on the extracellular side of the membrane and removal of its signal sequence. FXYD1 is encoded by the FXYD1 gene which is located at 19q13.1. The molecular mass of FXYD1 is about 10 KDa.
|Basic Information of FXYD1|
|Aliases||FXYD domain-containing ion transport regulator 1, Sodium/potassium-transporting ATPase subunit FXYD1|
|Organism||Homo sapiens (Human)|
|Transmembrane Times||Single-pass membrane|
Function of FXYD1 Membrane Protein
FXYD1 plays a role in several biological functions, such as chloride channel activity, ion channel binding and sodium channel regulator activity. It is wildly expressed in all kinds of tissues in human, especially in skeletal muscle and heart where it is the main substrate for protein kinase A and C. Besides, its expression is relatively high in brain, placenta, lung, liver, pancreas, uterus, bladder, prostate, small intestine, and colon with mucosal lining. FXYD1 can switch among different conformations with different selectivities for cations and anions. Besides, FXYD1 is able to induce hyperpolarization-activated Cl-selective currents. It has been identified as a tissue-speciﬁc regulator of Na, K-ATPase (NKA). FXYDI will inhibit NKA activity when it’s unphosphorylated and stimulate activity when phosphorylated. In addition, the interaction between FXYD1 and NKA causes a small decrease in the external K+ afﬁnity of α1–β1 and α2–β1 isozymes and a nearly 2-fold decrease in the internal Na+ afﬁnity. Beyond that, FXYD1 is associated with female sexual development. It also plays a role in the water channel aquaporin 2 (AQP2) trafficking.
Fig.1 Structural model of the α/β/FXYD1 Na, K-ATPase complex (Peter, 2009)
Application of FXYD1 Membrane Protein in Literature
This article reveals that FXYD1 functions in regulating the water channel aquaporin 2 (AQP2) retention in the apical membrane, and that this involves transfers between raft-like membrane domains in endosomes and plasma membranes.
Authors in this article study the effect of intensive training in combination with a marked reduction in training volume on phospholemman (FXYD1) expression and phosphorylation at rest and during exercise. They find that a period of high-intensity training with reduced training volume increases expression and phosphorylation levels of FXYD1.
Authors in this group find increased expression of FXYD1, FXYD3, and FXYD5 in the lungs of acute respiratory distress syndrome (ARDS) patients. They suspect that FXYD1 overexpression in ARDS patient lungs may limit Na (+)/K (+)-ATPase activity, and contribute to edema persistence.
This article reveals a previously undescribed phosphorylation site in FXYD1, threonine 69 (T69). Acute T69 phosphorylation elicits stimulation of the sodium pump additional to that induced by S63 and S68 phosphorylation.
This research reports the three-dimensional structure of the FXYD1/Na, K-ATPase complex. It is essential for understanding the function of FXYD1 and the role of FXYD1 phosphorylation. The article also presents the α/β/FXYD1 structural model and the data.
FXYD1 Preparation Options
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