Large neutral amino acids transporter small subunit 3 (SLC43A1)
The protein contains 559 amino acids for an estimated molecular weight of 61477 Da.
Sodium-independent, high affinity transport of large neutral amino acids. Has narrower substrate selectivity compared to SLC7A5 and SLC7A8 and mainly transports branched-chain amino acids and phenylalanine. Plays a role in the development of human prostate cancer, from prostatic intraepithelial neoplasia to invasive prostate cancer. (updated: March 4, 2015)
Protein identification was indicated in the following studies:
- Goodman and co-workers. (2013) The proteomics and interactomics of human erythrocytes. Exp Biol Med (Maywood) 238(5), 509-518.
- Lange and co-workers. (2014) Annotating N termini for the human proteome project: N termini and Nα-acetylation status differentiate stable cleaved protein species from degradation remnants in the human erythrocyte proteome. J Proteome Res. 13(4), 2028-2044.
- Hegedűs and co-workers. (2015) Inconsistencies in the red blood cell membrane proteome analysis: generation of a database for research and diagnostic applications. Database (Oxford) 1-8.
- Wilson and co-workers. (2016) Comparison of the Proteome of Adult and Cord Erythroid Cells, and Changes in the Proteome Following Reticulocyte Maturation. Mol Cell Proteomics. 15(6), 1938-1946.
- Bryk and co-workers. (2017) Quantitative Analysis of Human Red Blood Cell Proteome. J Proteome Res. 16(8), 2752-2761.
- D'Alessandro and co-workers. (2017) Red blood cell proteomics update: is there more to discover? Blood Transfus. 15(2), 182-187.
- Chu and co-workers. (2018) Quantitative mass spectrometry of human reticulocytes reveal proteome-wide modifications during maturation. Br J Haematol. 180(1), 118-133.
Methods
The following articles were analysed to gather the proteome content of erythrocytes.
The gene or protein list provided in the studies were processed using the ID mapping API of Uniprot in September 2018. The number of proteins identified and mapped without ambiguity in these studies is indicated below.
Only Swiss-Prot entries (reviewed) were considered for protein evidence assignation.
| Publication | Identification 1 | Uniprot mapping 2 | Not mapped / Obsolete | TrEMBL | Swiss-Prot |
|---|---|---|---|---|---|
| Goodman (2013) | 2289 (gene list) | 2278 | 53 | 20599 | 2269 |
| Lange (2014) | 1234 | 1234 | 7 | 28 | 1224 |
| Hegedus (2015) | 2638 | 2622 | 0 | 235 | 2387 |
| Wilson (2016) | 1658 | 1528 | 170 | 291 | 1068 |
| d'Alessandro (2017) | 1826 | 1817 | 2 | 0 | 1815 |
| Bryk (2017) | 2090 | 2060 | 10 | 108 | 1942 |
| Chu (2018) | 1853 | 1804 | 55 | 362 | 1387 |
1 as available in the article and/or in supplementary material
2 uniprot mapping returns all protein isoforms as one entry
The compilation of older studies can be retrieved from the Red Blood Cell Collection database.
The data and differentiation stages presented below come from the proteomic study and analysis performed by our partners of the GReX consortium, more details are available in their published work.
This protein is annotated as membranous in Gene Ontology, is predicted to be membranous by TOPCONS.
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| Variant | Description |
|---|---|
| dbSNP:rs17151933 | |
| dbSNP:rs34746107 |
No binding partner found
The reference OMIM entry for this protein is 603733
Solute carrier family 43 (l-type amino acid transporter), member 1; slc43a1
L-type amino acid transporter 3; lat3
Prostate cancer overexpressed gene 1; pov1
DESCRIPTION
SLC43A1 belongs to the system L family of plasma membrane carrier proteins that transports large neutral amino acids (Babu et al., 2003).CLONING
To assess prostate cancer-associated gene expression in vivo, Chuaqui et al. (1997) performed RT-PCR-differential display, using zinc finger-directed primers, on RNA extracted from microdissected normal prostatic epithelium and the corresponding invasive prostatic tumor. The authors cloned POV1, which they called R00504, as a cDNA that appeared selectively in the tumor samples. Northern blot analysis detected a 2.6-kb POV1 transcript in a variety of fetal tissues, with the highest level in fetal liver. Cole et al. (1998) cloned a full-length cDNA corresponding to POV1, which they called PB39. The deduced 559-amino acid POV1 protein contains a putative secretory signal peptide and a leucine zipper motif. Northern blot analysis of adult tissues detected highest POV1 expression in pancreas. Analysis of POV1 expression in human tissues by EST database searching and by RT-PCR analysis demonstrated the presence of a unique POV1 splice variant mRNA that is primarily associated with fetal tissues and tumors. By screening a human hepatocarcinoma cell line cDNA library for cDNAs that increased the uptake of radioactive leucine into Xenopus oocytes, Babu et al. (2003) cloned SLC43A1, which they called LAT3. The deduced 559-amino acid protein contains 12 transmembrane domains and a leucine zipper motif. A long intracellular loop between transmembrane domains 1 and 2 contains 2 N-glycosylation sites, and 2 other intracellular loops contain putative phosphorylation sites. Northern blot analysis of human tissues detected a 2.5-kb transcript highly expressed in pancreas, liver, skeletal muscle, and fetal liver. Expression was weaker in heart, placenta, lung, kidney, spleen, prostate, testis, ovary, small intestine, colon, lymph node, and bone marrow, and no expression was detected in other tissues examined. Pancreas contained an additional message of 4.4 kb.GENE FUNCTION
Chuaqui et al. (1997) found that prostate carcinoma samples from 5 of 10 patients showed substantial overexpression of POV1. Although the clinical parameters of the tumors varied, they found no correlation between POV1 expression and the clinical features of the tumors. Babu et al. (2003) found that LAT3 increased the transport of neutral amino acids such as L-leucine, L-isoleucine, L-valine, and L-phenylalanine following expression in Xenopus oocytes. Transport was concentration-dependent, Na(+)-independent, and inhibited by a system L transport inhibitor. In contrast to the other system L transporters, LAT1 (SLC7A5; 600182) and LAT2 (SLC7A8; 604235), LAT3 transport activity did not require formation of a heterodimeric complex with 4F2 heavy chain (SLC3A2; 158070). In addition to amino acid substrates, LAT3 recognized amino acid alcohols. The transport of L-leucine was electroneutral and mediated by a facilitated diffusion. In contrast, L-leucinol, L-valinol, and L-phenylalinol, which have net positive charge, induced inward currents under voltage clamp. LAT3-mediated transport was inhibited by pretreatment with the thiol reagent N-ethylmaleimide.MAPPING
Cole et al. (1998) mapped the SLC43A1 gene to chromosome 11p11.2-p11.1 by fluorescence in situ hybridization. ... More on the omim web site
Feb. 2, 2018: Protein entry updated
Automatic update: Uniprot description updated
Dec. 19, 2017: Protein entry updated
Automatic update: Uniprot description updated
Nov. 23, 2017: Protein entry updated
Automatic update: Uniprot description updated
March 16, 2016: Protein entry updated
Automatic update: OMIM entry 603733 was added.