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Multidrug and toxin extrusion protein 2

Protein-coding gene in the species Homo sapiens

SLC47A2
Identifiers
Aliases	SLC47A2, MATE2, MATE2-B, MATE2-K, MATE2K, solute carrier family 47 member 2
External IDs	OMIM: 609833; HomoloGene: 135027; GeneCards: SLC47A2; OMA:SLC47A2 - orthologs
Gene location (Human) Chr. Chromosome 17 (human)[1] Band 17p11.2 Start 19,678,288 bp[1] End 19,718,979 bp[1]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in right uterine tube gums caput epididymis human kidney gingival epithelium skin of limb skin of leg skin of abdomen hypothalamus C1 segment n/a More reference expression data BioGPS n/a
Gene ontology Molecular function antiporter activity xenobiotic transmembrane transporter activity Cellular component integral component of membrane plasma membrane membrane Biological process transmembrane transport xenobiotic export xenobiotic transmembrane transport xenobiotic transport Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 146802 n/a Ensembl ENSG00000180638 n/a UniProt Q86VL8 n/a RefSeq (mRNA) NM_001099646 NM_001256663 NM_152908 n/a RefSeq (protein) NP_001093116 NP_001243592 NP_690872 n/a Location (UCSC) Chr 17: 19.68 – 19.72 Mb n/a PubMed search [2] n/a
Wikidata
View/Edit Human

Multidrug and toxin extrusion protein 2 is a protein which in humans is encoded by the SLC47A2 gene.^[3]

This gene encodes a protein belonging to a family of transporters involved in the excretion of toxic electrolytes, both endogenous and exogenous, through urine and bile. This transporter family shares homology with the bacterial MATE (multi antimicrobial extrusion protein or multidrug and toxic compound extrusion) protein family responsible for drug resistance.^[4] This gene is one of two members of the MATE transporter family located near each other on chromosome 17. Alternatively, spliced transcript variants encoding different isoforms have been identified for this gene.^[3]

The multidrug efflux transporter NorM from V. parahaemolyticus, which mediates resistance to multiple antimicrobial agents (norfloxacin, kanamycin, ethidium bromide etc.), and its homologue from E. coli were identified in 1998.^[4] NorM seems to function as a drug/sodium antiporter, which is the first example of Na⁺-coupled multidrug efflux transporter discovered.^[5] NorM is a prototype of a new transporter family, and Brown et al. named it the multidrug and toxic compound extrusion family.^[6] The X-ray structure of the NorM was determined to be 3.65 Å, revealing an outward-facing conformation with two portals open to the outer leaflet of the membrane and a unique topology of the predicted 12 transmembrane helices distinct from any other known multidrug resistance transporter.^[7]

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