Monocarboxylate transporter 2 (SLC16A7)

The protein contains 478 amino acids for an estimated molecular weight of 52200 Da.

 

Proton-coupled monocarboxylate transporter. Catalyzes the rapid transport across the plasma membrane of many monocarboxylates such as lactate, pyruvate, branched-chain oxo acids derived from leucine, valine and isoleucine, and the ketone bodies acetoacetate, beta-hydroxybutyrate and acetate. Functions as high-affinity pyruvate transporter. (updated: Oct. 10, 2018)

Protein identification was indicated in the following studies:

  1. Bryk and co-workers. (2017) Quantitative Analysis of Human Red Blood Cell Proteome. J Proteome Res. 16(8), 2752-2761.

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.

PublicationIdentification 1Uniprot mapping 2Not mapped /
Obsolete
TrEMBLSwiss-Prot
Goodman (2013)2289 (gene list)227853205992269
Lange (2014)123412347281224
Hegedus (2015)2638262202352387
Wilson (2016)165815281702911068
d'Alessandro (2017)18261817201815
Bryk (2017)20902060101081942
Chu (2018)18531804553621387

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.

No sequence conservation computed yet.

This protein is annotated as membranous in Gene Ontology, is annotated as membranous in UniProt, is predicted to be membranous by TOPCONS.


Interpro domains
Total structural coverage: 0%
Model score: 0
No model available.

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VariantDescription
dbSNP:rs3763980

No binding partner found

The reference OMIM entry for this protein is 603654

Solute carrier family 16 (monocarboxylic acid transporter), member 7; slc16a7
Monocarboxylate transporter 2; mct2

DESCRIPTION

Tissues with few or no mitochondria, such as erythrocytes and tumor cells, depend largely on glycolysis to generate ATP. The major end products of glycolysis, pyruvate and lactate, must be eliminated from these cells to enable continued glycolytic flux and prevent toxic effects. H+/monocarboxylate transporters (MCTs) mediate the transport of lactate and pyruvate. Human MCT2 has a high affinity for the transport of pyruvate (summary by Lin et al., 1998).

CLONING

Garcia et al. (1995) isolated a hamster cDNA encoding an MCT that they designated Mct2. By screening a human liver library with the hamster Mct2 cDNA, Lin et al. (1998) isolated cDNAs encoding human MCT2. The predicted 478-amino acid protein shares 77% and 49% identity to hamster Mct2 and human MCT1 (SLC16A1; 600682), respectively. Like MCT1, MCT2 contains 12 putative transmembrane domains with a lengthy hydrophilic segment between transmembrane domains 6 and 7. MCT2 is composed of 41% hydrophobic residues, which the authors suggested might account for the discrepancy between its calculated molecular mass of 52 kD and its migration as a 40-kD protein by SDS-PAGE. Northern blot analysis revealed that MCT2 is expressed as multiple transcripts in a tissue-specific pattern.

MAPPING

By analysis of somatic cell hybrids and by fluorescence in situ hybridization, Lin et al. (1998) mapped the MCT2 gene to 12q13.

GENE FUNCTION

Using Xenopus oocytes expressing MCT2, Lin et al. (1998) demonstrated that MCT2 exhibits high affinity for the transport of pyruvate, implying that it is a primary pyruvate transporter in human cells. Using immunohistochemistry in mouse testis, Mannowetz et al. (2012) showed that Bsg (109480) was expressed in elongating spermatid cytoplasm and sperm tails, whereas Emb (615669) localized in sperm tails only. Mct1 was detectable in spermatozoa tails and plasma membranes of both spermatocytes and spermatids, whereas Mct2 was present in sperm tails and cytoplasm of Sertoli cells. The distribution of Bsg, Emb, Mct1, and Mct2 differed in epididymis and epididymal sperm. Bsg colocalized with Mct1 and Mct2 in spermatozoa, but Emb did not colocalize and was detected in the principal piece and the acrosome. Immunoblot analysis showed that in epididymal sperm, Bsg was expressed as a 51-kD protein, Emb as a 40-kD protein, Mct1 as a 40- to 48-kD protein, and Mct2 as a 40-kD protein. Mct1 and Mct2 coimmunoprecipitated with Bsg, but not Emb, in cauda sperm preparations. Functional analysis showed that Mct1 and Mct2 were active and provided the cells with L-lactate. Mannowetz et al. (2012) proposed that BSG interacts with MCT1 and MCT2 to locate them properly in the membrane of spermatogenic cells and that this may enable sperm to use lactate as an energy substrate. ... More on the omim web site

Subscribe to this protein entry history

June 30, 2020: Protein entry updated
Automatic update: OMIM entry 603654 was added.

Oct. 19, 2018: Additional information
Initial protein addition to the database. This entry was referenced in Bryk and co-workers. (2017).