MPPAIGGPVGYTPPDGGWGWAVVVGAFISIGFSYAFPKSITVFFKEIEIIFSATTSEVSWISSIMLAVMYAGGPISSILVNKYGSRPVMIAGGCLSGCGLIAASFCNTVQELYFCIGVIGGLGLAFNLNPALTMIGKYFYKKRPLANGLAMAGSPVFLSTLAPLNQAFFGIFGWRGSFLILGGLLLNCCVAGSLMRPIGPQQGKVEKLKSKESLQEAGKSDANTDLIGGSPKGEKLSVFQTVNKFLDLSLFTHRGFLLYLSGNVVMFFGLFTPLVFLSNYGKSKHFSSEKSAFLLSILAFVDMVARPSMGLAANTRWIRPRVQYFFAASVVANGVCHLLAPLSTTYVGFCIYAGVFGFAFGWLSSVLFETLMDLVGPQRFSSAVGLVTIVECCPVLLGPPLLGRLNDMYGDYKYTYWACGVILIIAGLYLFIGMGINYRLVAKEQKAEEKKRDGKEDETSTDVDEKPKKTMKETQSPAPLQNSSGDPAEEESPV

Bidirectional proton-coupled monocarboxylate transporter. Catalyzes the rapid transport across the plasma membrane of many monocarboxylates such as lactate, pyruvate, acetate and the ketone bodies acetoacetate and beta-hydroxybutyrate, and thus contributes to the maintenance of intracellular pH. The transport direction is determined by the proton motive force and the concentration gradient of the substrate monocarboxylate. MCT1 is a major lactate exporter (PubMed:9374487, PubMed:9639576, PubMed:10417314, PubMed:19473976, PubMed:8526936, PubMed:10564700, PubMed:11719518, PubMed:17127621). Plays a role in cellular responses to a high-fat diet by modulating the cellular levels of lactate and pyruvate that contribute to the regulation of central metabolic pathways and insulin secretion, with concomitant effects on plasma insulin levels and blood glucose homeostasis (By similarity). Facilitates the protonated monocarboxylate form of succinate export, that its transient protonation upon muscle cell acidification in exercising muscle and ischemic heart. Functions via alternate outward- and inward-open conformation states. Protonation and deprotonation of 302-Asp is essential for the conformational transition (By similarity).