Pho1 family

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The Pho1 phosphate permease family (TC# 2.A.94) is a family of phosphate transporters belonging to the ion transporter (IT) superfamily. [1] Representative members of the Pho1 family include the putative phosphate transporter PHO1 of Arabidopsis thaliana (TC# 2.A.94.1.1), and the xenotropic and polytropic murine-leukemia virus receptor Xpr1 of Metazoa, such as Homo sapein , [2] [3] Drosophila, [4] and Culex pipiens (TC# 2.A.94.1.2).

Contents

Pho1

Pho1 of A. thaliana is a member of the PHO1 family (11 paralogues in A. thaliana). This protein is 782 amino acyl residues in length and possesses 7 transmembrane segments (TMSs). It functions in inorganic phosphate transport and homeostasis. Pho1 catalyzes efflux of phosphate from epidermal and cortical cells into the xylem. [5] [6] The SPX superfamily domain is an N-terminal soluble domain. These proteins belong to the EXS (Erd1/Xpr1/Syg1) superfamily.

The generalized reaction catalyzed by Pho1 is: [7]

Pi (cells) → Pi (xylem)

See also

Further reading

Related Research Articles

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4
:HCO
3
exchange, or more generally, anion:anion antiport. For example, the mouse homologue, SLC26A6, can transport sulfate, formate, oxalate, chloride and bicarbonate, exchanging any one of these anions for another. A cyanobacterial homologue can transport nitrate. Some members can function as channels. SLC26A3 and SLC26A6 can function as carriers or channels, depending on the transported anion. In these porters, mutating a glutamate, also involved in transport in the CIC family, created a channel out of the carrier. It also changed the stoichiometry from 2Cl/HCO
3
to 1Cl/HCO
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.

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References

  1. Prakash, Shraddha; Cooper, Garret; Singhi, Soumya; Saier, Milton H. (2003-12-03). "The ion transporter superfamily". Biochimica et Biophysica Acta (BBA) - Biomembranes. 1618 (1): 79–92. doi:10.1016/j.bbamem.2003.10.010. ISSN   0006-3002. PMID   14643936.
  2. Giovannini, Donatella; Touhami, Jawida; Charnet, Pierre; Sitbon, Marc; Battini, Jean-Luc (2013). "Inorganic Phosphate Export by the Retrovirus Receptor XPR1 in Metazoans". Cell Reports . 3 (6): 1866–1873. doi:10.1016/j.celrep.2013.05.035.
  3. Lu, Yi; Yue, Chen-Xi; Zhang, Li; Yao, Deqiang; Xia, Ying; Zhang, Qing; Zhang, Xinchen; Li, Shaobai; Shen, Yafeng; Cao, Mi; Guo, Chang-Run; Qin, An; Zhao, Jie; Zhou, Lu; Yu, Ye (2024). "Structural basis for inositol pyrophosphate gating of the phosphate channel XPR1". Science. doi:10.1126/science.adp3252. ISSN   0036-8075.
  4. Xu, Chiwei; Xu, Jun; Tang, Hong-Wen; Ericsson, Maria; Weng, Jui-Hsia; DiRusso, Jonathan; Hu, Yanhui; Ma, Wenzhe; Asara, John M.; Perrimon, Norbert (2023). "A phosphate-sensing organelle regulates phosphate and tissue homeostasis". Nature . 617 (7962): 798–806. doi:10.1038/s41586-023-06039-y. ISSN   1476-4687. PMC   10443203 .
  5. Quaghebeur, Mieke; Rengel, Zed (2004-02-01). "Arsenic uptake, translocation and speciation in pho1 and pho2 mutants of Arabidopsis thaliana". Physiologia Plantarum. 120 (2): 280–286. doi:10.1111/j.0031-9317.2004.0240.x. ISSN   1399-3054. PMID   15032863.
  6. Stefanovic, Aleksandra; Ribot, Cécile; Rouached, Hatem; Wang, Yong; Chong, Julie; Belbahri, Lassaad; Delessert, Syndie; Poirier, Yves (2007-06-01). "Members of the PHO1 gene family show limited functional redundancy in phosphate transfer to the shoot, and are regulated by phosphate deficiency via distinct pathways". The Plant Journal. 50 (6): 982–994. doi:10.1111/j.1365-313X.2007.03108.x. ISSN   0960-7412. PMID   17461783.
  7. "2.A.94 The Phosphate Permease (Pho1) Family". Transporter Classification Database. Retrieved 2016-03-03.