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FLVCR1 Membrane Protein Introduction

Introduction of FLVCR1

FLVCR1 is encoded by the FLVCR1 gene which is located at 1q32.3. FLVCR1 belongs to the major facilitator superfamily which can facilitate movement of small solutes across cell membranes in response to chemiosmotic gradients. The mutations of the gene can cause posterior column ataxia with retinitis pigmentosa (PCARP) which is a neurodegenerative syndrome beginning in infancy with areflexia and retinitis pigmentosa. At the same time, defects in FLVCR1 are associated with a sensory neuropathy resulting in pain insensitivity.

Basic Information of FLVCR1
Protein Name Feline leukemia virus subgroup C receptor-related protein 1
Gene Name FLVCR1
Aliases Feline leukemia virus subgroup C receptor, hFLVCR
Organism Homo sapiens (Human)
UniProt ID Q9Y5Y0
Transmembrane Times Multi-pass membrane
Length (aa) 555
Sequence MARPDDEEGAAVAPGHPLAKGYLPLPRGAPVGKESVELQNGPKAGTFPVNGAPRDSLAAASGVLGGPQTPLAPEEETQARLLPAGAGAETPGAESSPLPLTALSPRRFVVLLIFSLYSLVNAFQWIQYSIISNVFEGFYGVTLLHIDWLSMVYMLAYVPLIFPATWLLDTRGLRLTALLGSGLNCLGAWIKCGSVQQHLFWVTMLGQCLCSVAQVFILGLPSRIASVWFGPKEVSTACATAVLGNQLGTAVGFLLPPVLVPNTQNDTNLLACNISTMFYGTSAVATLLFILTAIAFKEKPRYPPSQAQAALQDSPPEEYSYKKSIRNLFKNIPFVLLLITYGIMTGAFYSVSTLLNQMILTYYEGEEVNAGRIGLTLVVAGMVGSILCGLWLDYTKTYKQTTLIVYILSFIGMVIFTFTLDLRYIIIVFVTGGVLGFFMTGYLPLGFEFAVEITYPESEGTSSGLLNASAQIFGILFTLAQGKLTSDYGPKAGNIFLCVWMFIGIILTALIKSDLRRHNINIGITNVDVKAIPADSPTDQEPKTVMLSKQSESAI

Function of FLVCR1 Membrane Protein

FLVCR1 is a heme transporter that exports cytoplasmic heme. It is expressed in all hematopoietic tissues including peripheral blood lymphocytes. Besides, it is also found in pancreas and kidney and is abundant in fetal live. The expression will be downregulated in haemopoietic progenitor cells undergoing differentiation and hemoglobinization. FLVCR1 plays an important role in blood vessel development, cellular iron ion homeostasis, embryonic skeletal system morphogenesis, in utero embryonic development, spleen development, and many other biological processes. Accordingly, FLVCR1 will export two kinds of intermediate products in the heme biosynthetic pathway, coproporphyrin, and protoporphyrin IX. FLVCR1 has the ability to prevent heme accumulation in several cell lines and primary cells. In addition, FLVCR1 regulates differentiation and expansion of committed erythroid progenitors by controlling the intracellular heme pool size. FLVCR1 is essential for erythroid cell survival and macrophage heme Fe recycling. The further study reveals that hemopexin directly interacts with FLVCR to assure systemic iron balance.

FLVCR1-Membrane-Protein-PreparationFig.1 Ribbon diagram of structure model of human FLVCR1 transporter (Shaibani, 2015).

Application of FLVCR1 Membrane Protein in Literature

  1. Mercurio S., et al. The heme exporter Flvcr1 regulates expansion and differentiation of committed erythroid progenitors by controlling intracellular heme accumulation. Haematologica. 2015, 100(6):720-9. PubMed ID: 25795718

    Authors in this passage identify the role of FLVCR1 during erythropoiesis. FLVCR1a is required for the expansion of committed erythroid progenitors but cannot drive their terminal differentiation in mice and zebrafish, while FLVCR1b contributes to the expansion phase and is required for differentiation.

  2. Chiabrando D., et al. Mutations in the Heme Exporter FLVCR1 Cause Sensory Neurodegeneration with Loss of Pain Perception. Plos Genetics. 2016, 12(12): e1006461. PubMed ID: 27923065

    Authors in this article identify bi-allelic mutations in the FLVCR1. They find that FLVCR1-mutations can enhance oxidative stress, reduce heme export activity and increase sensitivity to programmed cell death. The date link heme metabolism to sensory neuron maintenance and suggest that intracellular heme overload causes early-onset degeneration of pain-sensing neurons in humans.

  3. Cao C., et al. Placental heme receptor LRP1 correlates with the heme exporter FLVCR1 and neonatal iron status. Reproduction. 2014, 148(3):295-302. PubMed ID: 24947444

    In this article, significant associations are found between placental LRP1 protein with cord hepcidin (r = − 0.29, P = 0.03) and placental heme exporter FLVCR1 (r = 0.34, P = 0.03). The passage suggests a role for placental heme iron utilization in supporting fetal iron demands.

  4. Ishiura H., et al. Posterior column ataxia with retinitis pigmentosa in a Japanese family with a novel mutation in FLVCR1. Neurogenetics. 2011, 12(2):117-121. PubMed ID: 21267618

    Authors in this article study a Japanese consanguineous family with posterior column ataxia with retinitis pigmentosa (PCARP). Their study confirms that PCARP is caused by mutations in FLVCR1.

  5. Shalev Z., et al. Identification of a feline leukemia virus variant that can use THTR1, FLVCR1, and FLVCR2 for infection. Journal of Virology. 2009, 83(13):6706-6716. PubMed ID: 19369334

    This article reveals that FY981 can use both the FeLV-C (pathogenic subgroup C feline leukemia virus) receptor FLVCR1 and the feline FeLV-A receptor THTR1 for infection. In fact, FY981 FeLV uses FLVCR1, FLVCR2, and THTR1 as receptors.

FLVCR1 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. Aided by our versatile Magic™ anti-membrane protein antibody discovery platform, we also provide customized anti-FLVCR1 antibody development services.


As a forward-looking research institute as well as a leading customer service provider in the field of membrane protein, Creative Biolabs has won good reputation among our worldwide customers for successfully accomplishing numerous challenging projects including generation of many functional membrane proteins. Please feel free to contact us for more information.

Reference

  1. Shaibani A., et al. (2015). Autosomal recessive posterior column ataxia with retinitis pigmentosa caused by novel mutations in the flvcr1 gene. International Journal of Neuroscience, 125(1), 43-49.

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