Search Results

Overview

Uniprot IDP53985
Protein NameMonocarboxylate transporter 1
Gene NameSLC16A1
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
224 AGKSGVKKDLHDANT

Function

Bidirectional proton-coupled monocarboxylate transporter (PubMed:12946269, PubMed:32946811, PubMed:33333023). 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 (PubMed:12946269, PubMed:33333023). The transport direction is determined by the proton motive force and the concentration gradient of the substrate monocarboxylate. MCT1 is a major lactate exporter (By similarity). 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 (PubMed:32946811). Functions via alternate outward- and inward-open conformation states. Protonation and deprotonation of 309-Asp is essential for the conformational transition (PubMed:33333023)

Protein Sequence

10 MPPAVGGPVG 20 YTPPDGGWGW 30 AVVIGAFISI 40 GFSYAFPKSI 50 TVFFKEIEGI 60 FHATTSEVSW 70 ISSIMLAVMY 80 GGGPISSILV 90 NKYGSRIVMI 100 VGGCLSGCGL 110 IAASFCNTVQ 120 QLYVCIGVIG 130 GLGLAFNLNP 140 ALTMIGKYFY 150 KRRPLANGLA 160 MAGSPVFLCT 170 LAPLNQVFFG 180 IFGWRGSFLI 190 LGGLLLNCCV 200 AGALMRPIGP 210 KPTKAGKDKS 220 KASLEKAGKS 230 GVKKDLHDAN 240 TDLIGRHPKQ 250 EKRSVFQTIN 260 QFLDLTLFTH 270 RGFLLYLSGN 280 VIMFFGLFAP 290 LVFLSSYGKS 300 QHYSSEKSAF 310 LLSILAFVDM 320 VARPSMGLVA 330 NTKPIRPRIQ 340 YFFAASVVAN 350 GVCHMLAPLS 360 TTYVGFCVYA 370 GFFGFAFGWL 380 SSVLFETLMD 390 LVGPQRFSSA 400 VGLVTIVECC 410 PVLLGPPLLG 420 RLNDMYGDYK 430 YTYWACGVVL 440 IISGIYLFIG 450 MGINYRLLAK 460 EQKANEQKKE 470 SKEEETSIDV 480 AGKPNEVTKA 490 AESPDQKDTD 500 GGPKEEESPV

Gene Ontology

Classification GO ID Description
Cellular Component GO:0016324 apical plasma membrane
Biological Process GO:0032094 response to food
Biological Process GO:0071422 succinate transmembrane transport
Biological Process GO:0150104 transport across blood-brain barrier
Cellular Component GO:0009925 basal plasma membrane
Cellular Component GO:0016323 basolateral plasma membrane
Cellular Component GO:0030054 cell junction
Cellular Component GO:0005813 centrosome
Cellular Component GO:0070062 extracellular exosome
Cellular Component GO:0016328 lateral plasma membrane
Cellular Component GO:0016020 membrane
Cellular Component GO:0005886 plasma membrane
Cellular Component GO:0045202 synapse
Molecular Function GO:0046943 carboxylic acid transmembrane transporter activity
Molecular Function GO:0042802 identical protein binding
Molecular Function GO:0015129 lactate transmembrane transporter activity
Molecular Function GO:0015650 lactate:proton symporter activity
Molecular Function GO:0015130 mevalonate transmembrane transporter activity
Molecular Function GO:0008028 monocarboxylic acid transmembrane transporter activity
Molecular Function GO:0015141 succinate transmembrane transporter activity
Biological Process GO:0051780 behavioral response to nutrient
Biological Process GO:1905039 carboxylic acid transmembrane transport
Biological Process GO:0007098 centrosome cycle
Biological Process GO:0042593 glucose homeostasis
Biological Process GO:0006629 lipid metabolic process
Biological Process GO:0015728 mevalonate transport
Biological Process GO:0015718 monocarboxylic acid transport
Biological Process GO:0035879 plasma membrane lactate transport
Biological Process GO:0042867 pyruvate catabolic process
Biological Process GO:1901475 pyruvate transmembrane transport
Biological Process GO:0050796 regulation of insulin secretion

Reference

[1] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.

[2] He C, Zhang J, Bai X, Lu C, Zhang K. Lysine lactylation-based insight to understanding the characterization of cervical cancer.. Biochim Biophys Acta Mol Basis Dis 1870(7):167356. 2024 Oct. PMID: 39025375.

[3] Wu Q, Li Z, Gong T, Zheng X, Zhou X et al.. Porphyromonas gingivalis infection induces lysine lactylation reprogramming in human umbilical vein endothelial cells.. Front Cell Infect Microbiol 16:1706727. 2026. PMID: 41696360.