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SLC45A3 Membrane Protein Introduction

Introduction of SLC45A3

SLC45A3 is encoded by the SLC45A3 gene which is located on chromosome 1 at the WI-9641 locus between q32 and q42, and the gene probably functions in prostate cancer malignancy. SLC45A3 mRNA has been proved to uniquely expressed in normal and cancerous prostate tissues. It belongs to the glycoside-pentoside-hexuronide (GPH) cation symporter transporter (TC 2.A.2) family. The molecular mass of SLC45A3 is about 59 KDa. Besides, SLC45A3 is a type IIIa plasma membrane protein with 11 transmembrane-spanning regions and a cleavable signal peptide.

Basic Information of SLC45A3
Protein Name Solute carrier family 45 member 3
Gene Name SLC45A3
Aliases Prostate cancer-associated protein 6, Prostein
Organism Homo sapiens (Human)
UniProt ID Q96JT2
Transmembrane Times Multi-pass membrane
Length (aa) 553
Sequence MVQRLWVSRLLRHRKAQLLLVNLLTFGLEVCLAAGITYVPPLLLEVGVEEKFMTMVLGIGPVLGLVCVPLLGSASDHWRGRYGRRRPFIWALSLGILLSLFLIPRAGWLAGLLCPDPRPLELALLILGVGLLDFCGQVCFTPLEALLSDLFRDPDHCRQAYSVYAFMISLGGCLGYLLPAIDWDTSALAPYLGTQEECLFGLLTLIFLTCVAATLLVAEEAALGPTEPAEGLSAPSLSPHCCPCRARLAFRNLGALLPRLHQLCCRMPRTLRRLFVAELCSWMALMTFTLFYTDFVGEGLYQGVPRAEPGTEARRHYDEGVRMGSLGLFLQCAISLVFSLVMDRLVQRFGTRAVYLASVAAFPVAAGATCLSHSVAVVTASAALTGFTFSALQILPYTLASLYHREKQVFLPKYRGDTGGASSEDSLMTSFLPGPKPGAPFPNGHVGAGGSGLLPPPPALCGASACDVSVRVVVGEPTEARVVPGRGICLDLAILDSAFLLSQVAPSLFMGSIVQLSQSVTAYMVSAAGLGLVAIYFATQVVFDKSDLAKYSA

Function of SLC45A3 Membrane Protein

SLC45A3 has sugar transmembrane transporter activity and sucrose: proton symporter activity. It also takes part in positive regulation of fatty acid biosynthetic process, positive regulation of glucose metabolic process, regulation of oligodendrocyte differentiation and some other important biological processes in human. It is worth mentioning that SLC45A3 is specifically expressed in prostate tissues both at the plasma membrane and in the cytoplasm. Besides, it can be detected in normal and cancerous prostates, and the expression of SLC45A3 is responsive to androgen, which can up-regulate SLC45A3 message and protein expression levels. Overall, SLC45A3 is a prostate-specific marker which may function in the diagnosis and treatment of prostate cancer. What’ s more, CD8 T cells specific for SLC45A3 has been identified, which promotes the development of SLC45A3 in vaccination strategies against prostate cancer. SLC45A3 may act as a target antigen for prostate carcinomas-directed cytotoxic T-cell lymphocytes. Beyond that, miR-32 and its target SLC45A3 are important in myelin maintenance which modulate glucose and lipid metabolism and myelin protein expression in oligodendrocytes. And SLC45A3 is identified as a novel sugar transporter in the kidney.

SLC45A3 Membrane Protein Preparation Fig.1 miR-32 and SLC45A3 function in the regulation of myelin lipid metabolism (Shin, 2012).

Application of SLC45A3 Membrane Protein in Literature

  1. Qin F., et al. SLC45A3-ELK4 functions as a long non-coding chimeric RNA. Cancer Letters. 2017, 404:53-61. PubMed ID: 28716526

    Authors of this article focus a fusion RNA, SLC45A3-ELK4 which is generated by cis-splicing between neighboring genes. They reveal that SLC45A3-ELK4 function in cancer cell proliferation by its transcript, not translated protein.

  2. Hernández-Llodrà S., et al. ERG overexpression plus SLC45A3 (prostein) and PTEN expression loss: Strong association of the triple hit phenotype with an aggressive pathway of prostate cancer progression. Oncotarget. 2017, 8(43):74106-74118. PubMed ID: 29088771

    Authors of this article intend to validate some previous results about SLC45A3 and TMPRSS2 by immunohistochemistry in a large cohort of tumors. In the end, they reveal that SLC45A3 and other markers can be used to improve patient stratification, treatment, and follow-up.

  3. Vitavska O., et al. Putative role of the H (+)/sucrose symporter SLC45A3 as an osmolyte transporter in the kidney. Pflugers Arch. 2016, 468(8):1-10. PubMed ID: 27228996

    Authors in this group want to explore the physiological functions of SLC45A3. They find that SLC45A3 can be detected in the kidney and is highly expressed in the medullary collecting duct. And they conclude that SLC45A3 is a novel sugar transporter in the kidney.

  4. Kumarsinha C., et al. SLC45A3-ELK4 Chimera in Prostate Cancer: Spotlight on Cis-Splicing. Cancer Discovery. 2012, 2(7):582. PubMed ID: 22787087

    This article reveals that SLC45A3-ELK4, prostate cancer RNA chimera, is generated by cis-splicing between the two adjacent genes, there is no DNA rearrangements or trans-splicing. And the chimera expression is induced by androgen treatment.

  5. Sven P., et al. Loss of SLC45A3 protein (prostein) expression in prostate cancer is associated with SLC45A3-ERG, gene rearrangement and an unfavorable clinical course †[J]. International Journal of Cancer. 2013, 132(4):807-812. PubMed ID: 22821757

    Authors of this study want to quantify the protein expression of ERG, TMPRSS2, and SLC45A3 in prostate cancer to assess for diagnostic or prognostic utility. This article suggests that the expression of SLC45A3 protein is down-regulated through SLC45A3-ERG fusion in prostate cancer.

SLC45A3 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-SLC45A3 antibody development services.


As a forward-looking research institute as well as a leading custom service provider in the field of membrane protein, Creative Biolabs has won a 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. Shin D., et al. (2012). Mir-32, and its target slc45a3 regulate the lipid metabolism of oligodendrocytes and myelin. Neuroscience. 213(2), 29-37.

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