Close

MFSD5 Membrane Protein Introduction

Introduction of MFSD5

Tejada-Jiménez reported a molybdate transporter different from the molybdate transporter type 1 (MOT1) family, which is encoded by the Chlamydomonas reinhardtii gene MOT2 (CrMoT2) and is also present in animals including humans (HsMOT2 ). HsMOT2 gene is mapped to the chromosome 12 position 12q13.3 and has been named as major facilitator superfamily domain-containing protein 5 (MFSD5). MFSD5 knockdown leads to a lack of uptake activity of molybdate. MFSD5 is composed of 450 amino acids and shows the typical hydrophobicity pattern of a membrane protein. With 12 transmembrane regions, MFSD5 transcripts are detected in many tissues and cell types, with higher transcript accumulation in the cervix, stomach, nerves, and skin.

Basic Information of MFSD5
Protein Name Molybdate-anion transporter
Gene Name MFSD5
Aliases Molybdate transporter 2 homolog, HsMOT2
Organism Homo sapiens (Human)
UniProt ID Q6N075
Transmembrane Times 12
Length (aa) 450
Sequence MLVTAYLAFVGLLASCLGLELSRCRAKPPGRACSNPSFLRFQLDFYQVYFLALAADWLQAPYLYKLYQHYYFLEGQIAILYVCGLASTVLFGLVASSLVDWLGRKNSCVLFSLTYSLCCLTKLSQDYFVLLVGRALGGLSTALLFSAFEAWYIHEHVERHDFPAEWIPATFARAAFWNHVLAVVAGVAAEAVASWIGLGPVAPFVAAIPLLALAGALALRNWGENYDRQRAFSRTCAGGLRCLLSDRRVLLLGTIQALFESVIFIFVFLWTPVLDPHGAPLGIIFSSFMAASLLGSSLYRIATSKRYHLQPMHLLSLAVLIVVFSLFMLTFSTSPGQESPVESFIAFLLIELACGLYFPSMSFLRRKVIPETEQAGVLNWFRVPLHSLACLGLLVLHDSDRKTGTRNMFSICSAVMVMALLAVVGLFTVVRHDAELRVPSPTEEPYAPEL

Function of MFSD5 Membrane Protein

Almost all living organisms need to get molybdenum (Mo) from the external environment to achieve the basic physiological processes of life. In these processes, some important enzymes (such as sulfite oxidase, aldehyde oxidase, etc.) are required, and they play important roles strictly depending on the presence of Mo. The cells absorb Mo in the form of molybdate oxide, which requires a molybdenum transporter. MOT1 is the first molybdate transporter identified in plant eukaryotes, but it does not exist in the animal genome. MFSD5 transcription is activated under conditions of low Mo availability and is partially inhibited by the presence of ammonium as a nitrogen source; in contrast to MoT1, the presence of nitrate has no effect on the expression of MFSD5. Although MOT1 is related to nitrate assimilation requirements, MFSD5 may help to ensure that molybdate is provided in the scarcity of the anion. Since animals do not absorb nitrate, the molybdate transporters in these organisms are not related to nitrate metabolism.

Analysis of the MOT2 protein. Fig.1 Analysis of the MOT2 protein. (Tejada-Jiménez, 2011)

Application of MFSD5 Membrane Protein in Literature

  1. Gao J.S., et al. A putative molybdate transporter LjMOT1 is required for molybdenum transport in Lotus japonicus. Physiologia Plantarum. 2016, 158(3): 331-340. PubMed ID: 27535112

    This study indicates that LjMOT1 may be involved in the transport of Mo, which lays a theoretical foundation for further understanding of the Mo transport mechanism of higher plants.

  2. Tejada-Jiménez M., et al. Algae and humans share a molybdate transporter. Proceedings of the National Academy of Sciences of the United States of America. 2011, 108(16): 6420-5. PubMed ID: 21464289

    This article reports a molybdate transporter different from the MOT1 family, encoded by the Chlamydomonas reinhardtii gene MoT2, which opens the way for understanding molybdate transport as part of dynamic molybdenum homeostasis and molybdenum biosynthesis.

  3. Ide Y., et al. Effects of molybdenum deficiency and defects in molybdate transporter MOT1 on transcript accumulation and nitrogen/sulphur metabolism in Arabidopsis thaliana. Journal of Experimental Botany. 2011, 62(4): 1483-97. PubMed ID: 21131548

    This paper investigates the effects of molybdenum deficiency and molybdate transporter mutation (MOT1) on nitrogen and sulfur metabolism in Arabidopsis and is the first survey of the effects of Mo nutrition and MOT1 on plant gene expression and metabolism.

  4. Baxter I., et al. Variation in molybdenum content across broadly distributed populations of Arabidopsis thaliana is controlled by a mitochondrial molybdenum transporter (MOT1). Plos Genetics. 2008, 4(2): e1000004. PubMed ID: 18454190

    This paper demonstrates that the natural variation in Mo content in Arabidopsis germplasm branches is controlled by the variation of the molybdenum transporter 1-MOT1, which belongs to the sulfate transporter superfamily, providing insights into the regulation of Mo accumulation in plants.

  5. Fitzpatrick K.L., et al. Molybdate transport through the plant sulfate transporter SHST1. Febs Letters. 2008, 582(10): 1508-13. PubMed ID: 18396170

    This article shows that the sulfate transporter SHST1 increases the uptake of molybdate into cells at the nM concentration, but molybdate reduces the sulfate transport of SHST1.

MFSD5 Preparation Options

Membrane protein studies have advanced significantly over the past few years. Based on our versatile Magic™ membrane protein production platform, we could offer a series of membrane protein preparation services for worldwide customers in reconstitution forms as well as multiple active formats. Aided by our versatile Magic™ anti-membrane protein antibody discovery platform, we also provide customized anti-MFSD5 antibody development services.


During the past years, Creative Biolabs has successfully generated many functional membrane proteins for our global customers. We are happy to accelerate the development of our clients’ programs with our one-stop, custom-oriented service. For more detailed information, please feel free to contact us.

Reference

  1. Tejada-Jiménez M, et al. (2011). Algae and humans share a molybdate transporter. Proceedings of the National Academy of Sciences of the United States of America. 108(16): 6420-5.

Online Inquiry

Verification code
Click image to refresh the verification code.

CONTACT US

45-1 Ramsey Road, Shirley, NY 11967, USA
Call us at:
USA: 1-631-381-2994
Europe: 44-207-097-1828
Fax: 1-631-207-8356
Email:
Our customer service representatives are available 24 hours a day, 7 days a week. Contact Us