PLP2 Membrane Protein Introduction

Introduction of PLP2

Proteolipid protein 2, also known as Differentiation-dependent protein A4 or Intestinal membrane A4 protein, is a membrance protein which is encoded by the PLP2 gene in humans. Differential screening of a subtractive cDNA library of a particular ht29-18-c1 sequence is a highly differentiated daughter clone of ht29-18, resulting in a differentially-dependent cDNA clone, PLP2. The complete clone encoding PLP2 was obtained and sorted. It is 945 bp in length and contains an open reading frame (ORF) of 456 bp. The amino acid sequence deduced from the ORF revealed a 152 amino acid polypeptide with a predicted molecular mass of 17,000 Da, which is confirmed by in vitro transcription and translation by a full-length PLP2 cDNA. This polypeptide contains four potential membrane-producing domains, as well as consensus sequences for n-chain glycosylation, as well as phosphorylation sites for protein kinase C and casein kinase II.

Basic Information of PLP2
Protein Name	Proteolipid protein 2
Gene Name	PLP2
Aliases	Differentiation-dependent protein A4, Intestinal membrane A4 protein
Organism	Homo sapiens (Human)
UniProt ID	Q04941
Transmembrane Times	4
Length (aa)	152
Sequence	MADSERLSAPGCWAACTNFSRTRKGILLFAEIILCLVILICFSASTPGYSSLSVIEMILAAIFFVVYMCDLHTKIPFINWPWSDFFRTLIAAILYLITSIVVLVERGNHSKIVAGVLGLIATCLFGYDAYVTFPVRQPRHTAAPTDPADGPV

Function of PLP2 Membrane Protein

Proteolipid protein 2 is a colonic epithelial fortification protein that is restricted to the endoplasmic reticulum, similar to other proteins. The protein doubled and exhibited ion channel characteristics. PLP2 may play a role in intestinal epithelial cell differentiation. PLP2 mRNAs were detected in various cells such as U-937, HL-60, HEK293, and Stanley cells. Overexpression of PLP2 stimulated twice the migration of ho/CCR1 cells by agonists, suggesting a role for PLP2 in chemotaxis through CCR1.

PLP2 Membrane Protein Introduction Fig.1 The structure of Proteolipid protein 2.

Application of PLP2 Membrane Protein in Literature

Timms R. T., et al. Haploid Genetic Screens Identify an Essential Role for PLP2 in the Downregulation of Novel Plasma Membrane Targets by Viral E3 Ubiquitin Ligases. PLoS Pathogens. 2013, 9 (11): e1003772. PubMed ID: 24278019

This study links a key function to the PLP2 gene to obtain the ligation enzyme activity of the virus and highlights the power of non-fatal haploid gene screens in human cells to identify pathogen-operated genes in the host immune system.
Chen Y.F., et al. X-Ray Structural and Functional Studies of the Three Tandemly Linked Domains of Non-Structural Protein 3 (nsp3) from Murine Hepatitis Virus Reveal Conserved Functions. The Journal of Biological Chemistry. 2015, 290 (42): 25293–25306. PubMed ID: 26296883

This article proposed a computational derivation model of MHV PLP2 combined with ubiquitin. The on-site directed mutagenesis revealed the potential interaction of ubiquitin and PLP2.
Wang G., et al. PLP2 of Mouse Hepatitis Virus A59 (MHV-A59) Targets TBK1 to Negatively Regulate Cellular Type I Interferon Signaling Pathway. PLoS ONE. 2011, 6 (2): e17192. PubMed ID: 21364999

These results indicate that PLP2 inhibits IRF3 nuclear translocation, thus inhibiting transcriptional activation of IFN.
Van K., et al. Deubiquitinase Function of Arterivirus Papain-like Protease 2 Suppresses the Innate Immune Response in Infected Host Cells. Proceedings of the National Academy of Sciences of the United States of America. 2013, 110 (9): E838-E847. PubMed ID: 23401522

This result demonstrates the important role of PLP2 in the escape of arterial virus and provides new possibilities for the development of improved attenuated virus vaccines against economically important arterial viruses and other codes encoding similar bispecific proteases.
Chen X.J., et al. Coronavirus Membrane-Associated Papain-like Proteases Induce Autophagy through Interacting with Beclin1 to Negatively Regulate Antiviral Innate Immunity. Protein & Cell. 2014, 5 (12): 912-927. PubMed ID: 25311841

These results indicate that coronavirus PLP2, by interacting with Behrin-1, results in incomplete autophagy, which in turn regulates coronavirus replication and antiviral innate immunity.

PLP2 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-PLP2 antibody development services.

Creative Biolabs' skillful scientists are glad to leverage our expertise and advanced technologies to help you with the member protein research. If you are interested, please feel free to contact us for more details.

All listed services and products are For Research Use Only. Do Not use in any diagnostic or therapeutic applications.

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