ID MOT1_RAT Reviewed; 494 AA. AC P53987; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 27-MAR-2024, entry version 173. DE RecName: Full=Monocarboxylate transporter 1; DE Short=MCT 1; DE AltName: Full=Solute carrier family 16 member 1; GN Name=Slc16a1; Synonyms=Mct1; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TRANSPORTER ACTIVITY, TISSUE RP SPECIFICITY, AND SUBCELLULAR LOCATION. RC STRAIN=Wistar; TISSUE=Small intestine; RX PubMed=8526936; DOI=10.1006/bbrc.1995.2786; RA Takanaga H., Tamai I., Inaba S., Sai Y., Higashida H., Yamamoto H., RA Tsuji A.; RT "cDNA cloning and functional characterization of rat intestinal RT monocarboxylate transporter."; RL Biochem. Biophys. Res. Commun. 217:370-377(1995). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=Wistar; TISSUE=Skeletal muscle; RX PubMed=7548134; DOI=10.1016/0005-2736(95)00160-5; RA Jackson V.N., Price N.T., Halestrap A.P.; RT "cDNA cloning of MCT1, a monocarboxylate transporter from rat skeletal RT muscle."; RL Biochim. Biophys. Acta 1238:193-196(1995). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Lung; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] OF 264-472, FUNCTION, TRANSPORTER ACTIVITY, RP TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION. RC TISSUE=Jejunal epithelium; RX PubMed=10564700; DOI=10.1111/j.1469-445x.1999.01918.x; RA Orsenigo M.N., Tosco M., Bazzini C., Laforenza U., Faelli A.; RT "A monocarboxylate transporter MCT1 is located at the basolateral pole of RT rat jejunum."; RL Exp. Physiol. 84:1033-1042(1999). RN [5] RP INTERACTION WITH EMB, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION. RX PubMed=9169423; DOI=10.1074/jbc.272.23.14624; RA Poole R.C., Halestrap A.P.; RT "Interaction of the erythrocyte lactate transporter (monocarboxylate RT transporter 1) with an integral 70-kDa membrane glycoprotein of the RT immunoglobulin superfamily."; RL J. Biol. Chem. 272:14624-14628(1997). RN [6] RP FUNCTION, AND TRANSPORTER ACTIVITY. RX PubMed=9374487; DOI=10.1074/jbc.272.48.30096; RA Broeer S., Rahman B., Pellegri G., Pellerin L., Martin J.L., RA Verleysdonk S., Hamprecht B., Magistretti P.J.; RT "Comparison of lactate transport in astroglial cells and monocarboxylate RT transporter 1 (MCT 1) expressing Xenopus laevis oocytes. Expression of two RT different monocarboxylate transporters in astroglial cells and neurons."; RL J. Biol. Chem. 272:30096-30102(1997). RN [7] RP FUNCTION, TRANSPORTER ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=9639576; DOI=10.1042/bj3330167; RA Broeer S., Schneider H.P., Broeer A., Rahman B., Hamprecht B., RA Deitmer J.W.; RT "Characterization of the monocarboxylate transporter 1 expressed in Xenopus RT laevis oocytes by changes in cytosolic pH."; RL Biochem. J. 333:167-174(1998). RN [8] RP FUNCTION, TRANSPORTER ACTIVITY, AND ACTIVITY REGULATION. RX PubMed=10417314; DOI=10.1042/0264-6021:3410529; RA Broeer S., Broeer A., Schneider H.P., Stegen C., Halestrap A.P., RA Deitmer J.W.; RT "Characterization of the high-affinity monocarboxylate transporter MCT2 in RT Xenopus laevis oocytes."; RL Biochem. J. 341:529-535(1999). RN [9] RP INTERACTION WITH BSG, FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=11719518; DOI=10.1074/jbc.m109658200; RA Wilson M.C., Meredith D., Halestrap A.P.; RT "Fluorescence resonance energy transfer studies on the interaction between RT the lactate transporter MCT1 and CD147 provide information on the topology RT and stoichiometry of the complex in situ."; RL J. Biol. Chem. 277:3666-3672(2002). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-213, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=16396499; DOI=10.1021/pr0503073; RA Moser K., White F.M.; RT "Phosphoproteomic analysis of rat liver by high capacity IMAC and LC- RT MS/MS."; RL J. Proteome Res. 5:98-104(2006). RN [11] RP FUNCTION, TRANSPORTER ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR RP LOCATION, INTERACTION WITH BSG, 3D-STRUCTURE MODELING, AND MUTAGENESIS OF RP ARG-86; ARG-196; ASP-302 AND ARG-306. RX PubMed=17127621; DOI=10.1080/09687860600841967; RA Manoharan C., Wilson M.C., Sessions R.B., Halestrap A.P.; RT "The role of charged residues in the transmembrane helices of RT monocarboxylate transporter 1 and its ancillary protein basigin in RT determining plasma membrane expression and catalytic activity."; RL Mol. Membr. Biol. 23:486-498(2006). RN [12] RP FUNCTION, TRANSPORTER ACTIVITY, INTERACTION WITH EMB, SUBCELLULAR LOCATION, RP TOPOLOGY, 3D-STRUCTURE MODELING, MUTAGENESIS OF LYS-38; LYS-45; LYS-282; RP LYS-284; LYS-290 AND LYS-413, ACTIVITY REGULATION, AND TISSUE SPECIFICITY. RX PubMed=19473976; DOI=10.1074/jbc.m109.014217; RA Wilson M.C., Meredith D., Bunnun C., Sessions R.B., Halestrap A.P.; RT "Studies on the DIDS-binding site of monocarboxylate transporter 1 suggest RT a homology model of the open conformation and a plausible translocation RT cycle."; RL J. Biol. Chem. 284:20011-20021(2009). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-210; SER-213; SER-220; RP SER-230; SER-460 AND SER-492, AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=22673903; DOI=10.1038/ncomms1871; RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., RA Olsen J.V.; RT "Quantitative maps of protein phosphorylation sites across 14 different rat RT organs and tissues."; RL Nat. Commun. 3:876-876(2012). CC -!- FUNCTION: Bidirectional proton-coupled monocarboxylate transporter. CC Catalyzes the rapid transport across the plasma membrane of many CC monocarboxylates such as lactate, pyruvate, acetate and the ketone CC bodies acetoacetate and beta-hydroxybutyrate, and thus contributes to CC the maintenance of intracellular pH. The transport direction is CC determined by the proton motive force and the concentration gradient of CC the substrate monocarboxylate. MCT1 is a major lactate exporter CC (PubMed:9374487, PubMed:9639576, PubMed:10417314, PubMed:19473976, CC PubMed:8526936, PubMed:10564700, PubMed:11719518, PubMed:17127621). CC Plays a role in cellular responses to a high-fat diet by modulating the CC cellular levels of lactate and pyruvate that contribute to the CC regulation of central metabolic pathways and insulin secretion, with CC concomitant effects on plasma insulin levels and blood glucose CC homeostasis (By similarity). Facilitates the protonated monocarboxylate CC form of succinate export, that its transient protonation upon muscle CC cell acidification in exercising muscle and ischemic heart. Functions CC via alternate outward- and inward-open conformation states. Protonation CC and deprotonation of 302-Asp is essential for the conformational CC transition (By similarity). {ECO:0000250|UniProtKB:P53985, CC ECO:0000250|UniProtKB:P53986, ECO:0000269|PubMed:10417314, CC ECO:0000269|PubMed:10564700, ECO:0000269|PubMed:11719518, CC ECO:0000269|PubMed:17127621, ECO:0000269|PubMed:19473976, CC ECO:0000269|PubMed:8526936, ECO:0000269|PubMed:9374487, CC ECO:0000269|PubMed:9639576}. CC -!- CATALYTIC ACTIVITY: CC Reaction=(S)-lactate(in) + H(+)(in) = (S)-lactate(out) + H(+)(out); CC Xref=Rhea:RHEA:29415, ChEBI:CHEBI:15378, ChEBI:CHEBI:16651; CC Evidence={ECO:0000269|PubMed:10417314, ECO:0000269|PubMed:10564700, CC ECO:0000269|PubMed:17127621, ECO:0000269|PubMed:19473976, CC ECO:0000269|PubMed:8526936, ECO:0000269|PubMed:9374487, CC ECO:0000269|PubMed:9639576}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:29416; CC Evidence={ECO:0000305|PubMed:9639576}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:29417; CC Evidence={ECO:0000305|PubMed:9639576}; CC -!- CATALYTIC ACTIVITY: CC Reaction=H(+)(out) + pyruvate(out) = H(+)(in) + pyruvate(in); CC Xref=Rhea:RHEA:64720, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378; CC Evidence={ECO:0000269|PubMed:10417314, ECO:0000269|PubMed:9374487, CC ECO:0000269|PubMed:9639576}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64721; CC Evidence={ECO:0000305|PubMed:9639576}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:64722; CC Evidence={ECO:0000305|PubMed:9639576}; CC -!- CATALYTIC ACTIVITY: CC Reaction=acetoacetate(out) + H(+)(out) = acetoacetate(in) + H(+)(in); CC Xref=Rhea:RHEA:71775, ChEBI:CHEBI:13705, ChEBI:CHEBI:15378; CC Evidence={ECO:0000269|PubMed:10417314, ECO:0000269|PubMed:9639576}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71776; CC Evidence={ECO:0000305|PubMed:9639576}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:71777; CC Evidence={ECO:0000305|PubMed:9639576}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(S)-3-hydroxybutanoate(out) + H(+)(out) = (S)-3- CC hydroxybutanoate(in) + H(+)(in); Xref=Rhea:RHEA:71871, CC ChEBI:CHEBI:11047, ChEBI:CHEBI:15378; CC Evidence={ECO:0000269|PubMed:10417314, ECO:0000269|PubMed:9639576}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71872; CC Evidence={ECO:0000305|PubMed:9639576}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:71873; CC Evidence={ECO:0000305|PubMed:9639576}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(R)-3-hydroxybutanoate(out) + H(+)(out) = (R)-3- CC hydroxybutanoate(in) + H(+)(in); Xref=Rhea:RHEA:71795, CC ChEBI:CHEBI:10983, ChEBI:CHEBI:15378; CC Evidence={ECO:0000269|PubMed:10417314, ECO:0000305|PubMed:9639576}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71796; CC Evidence={ECO:0000305|PubMed:9639576}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:71797; CC Evidence={ECO:0000305|PubMed:9639576}; CC -!- CATALYTIC ACTIVITY: CC Reaction=3-methyl-2-oxobutanoate(out) + H(+)(out) = 3-methyl-2- CC oxobutanoate(in) + H(+)(in); Xref=Rhea:RHEA:71783, ChEBI:CHEBI:11851, CC ChEBI:CHEBI:15378; Evidence={ECO:0000269|PubMed:10417314}; CC -!- CATALYTIC ACTIVITY: CC Reaction=4-methyl-2-oxopentanoate(out) + H(+)(out) = 4-methyl-2- CC oxopentanoate(in) + H(+)(in); Xref=Rhea:RHEA:71779, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17865; CC Evidence={ECO:0000269|PubMed:10417314}; CC -!- ACTIVITY REGULATION: Inhibited by stilbene disulfonates, such as di- CC isothiocyanostilbene disulfonate(DIDS), a cross-linking reagent that CC forms covalent linkages with lysine groups. CC {ECO:0000269|PubMed:19473976}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=3.5 mM for (S)-lactate {ECO:0000269|PubMed:17127621, CC ECO:0000269|PubMed:9639576}; CC KM=1.25 mM for pyruvate {ECO:0000269|PubMed:9639576}; CC -!- SUBUNIT: Interacts with BSG. Interacts with EMB. Interaction with CC either BSG or EMB is required for expression at the cell membrane. CC {ECO:0000269|PubMed:11719518, ECO:0000269|PubMed:17127621, CC ECO:0000269|PubMed:19473976, ECO:0000269|PubMed:9169423}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11719518, CC ECO:0000269|PubMed:17127621, ECO:0000269|PubMed:19473976, CC ECO:0000269|PubMed:8526936, ECO:0000269|PubMed:9169423}; Multi-pass CC membrane protein {ECO:0000250|UniProtKB:P53985}. Basolateral cell CC membrane {ECO:0000269|PubMed:10564700}; Multi-pass membrane protein CC {ECO:0000250|UniProtKB:P53985}. Apical cell membrane CC {ECO:0000250|UniProtKB:P53985}; Multi-pass membrane protein CC {ECO:0000250|UniProtKB:P53985}. Note=Expression at the cell surface CC requires the ancillary proteins BSG and EMB. CC {ECO:0000250|UniProtKB:P53985}. CC -!- TISSUE SPECIFICITY: Detected in erythrocytes (at protein level). CC Detected in brain, heart, kidney, lung, muscle, jejunum enterocytes and CC brain capillaries. {ECO:0000269|PubMed:10564700, CC ECO:0000269|PubMed:19473976, ECO:0000269|PubMed:8526936, CC ECO:0000269|PubMed:9169423}. CC -!- SIMILARITY: Belongs to the major facilitator superfamily. CC Monocarboxylate porter (TC 2.A.1.13) family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; D63834; BAA09894.1; -; mRNA. DR EMBL; X86216; CAA60116.1; -; mRNA. DR EMBL; BC078877; AAH78877.1; -; mRNA. DR EMBL; AJ236865; CAB37948.1; -; mRNA. DR PIR; JC4399; JC4399. DR RefSeq; NP_036848.1; NM_012716.2. DR RefSeq; XP_017446125.1; XM_017590636.1. DR AlphaFoldDB; P53987; -. DR SMR; P53987; -. DR BioGRID; 247107; 2. DR IntAct; P53987; 1. DR STRING; 10116.ENSRNOP00000027234; -. DR BindingDB; P53987; -. DR ChEMBL; CHEMBL2073709; -. DR iPTMnet; P53987; -. DR PhosphoSitePlus; P53987; -. DR jPOST; P53987; -. DR PaxDb; 10116-ENSRNOP00000027234; -. DR Ensembl; ENSRNOT00000027234.6; ENSRNOP00000027234.3; ENSRNOG00000019996.6. DR Ensembl; ENSRNOT00055032820; ENSRNOP00055026573; ENSRNOG00055019230. DR Ensembl; ENSRNOT00060044679; ENSRNOP00060037031; ENSRNOG00060025806. DR Ensembl; ENSRNOT00065055810; ENSRNOP00065045972; ENSRNOG00065032425. DR GeneID; 25027; -. DR KEGG; rno:25027; -. DR UCSC; RGD:3690; rat. DR AGR; RGD:3690; -. DR CTD; 6566; -. DR RGD; 3690; Slc16a1. DR eggNOG; KOG2504; Eukaryota. DR GeneTree; ENSGT00940000154955; -. DR HOGENOM; CLU_001265_59_1_1; -. DR InParanoid; P53987; -. DR OMA; LFMWGMF; -. DR OrthoDB; 2917104at2759; -. DR PhylomeDB; P53987; -. DR TreeFam; TF313792; -. DR SABIO-RK; P53987; -. DR PRO; PR:P53987; -. DR Proteomes; UP000002494; Chromosome 2. DR Bgee; ENSRNOG00000019996; Expressed in heart and 19 other cell types or tissues. DR GO; GO:0016324; C:apical plasma membrane; IDA:ARUK-UCL. DR GO; GO:0009925; C:basal plasma membrane; ISO:RGD. DR GO; GO:0016323; C:basolateral plasma membrane; IDA:UniProtKB. DR GO; GO:0005813; C:centrosome; ISO:RGD. DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IEA:Ensembl. DR GO; GO:0016328; C:lateral plasma membrane; ISO:RGD. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0045202; C:synapse; ISO:RGD. DR GO; GO:0046943; F:carboxylic acid transmembrane transporter activity; IMP:ARUK-UCL. DR GO; GO:0042802; F:identical protein binding; IPI:RGD. DR GO; GO:0015129; F:lactate transmembrane transporter activity; ISO:RGD. DR GO; GO:0015650; F:lactate:proton symporter activity; IDA:UniProtKB. DR GO; GO:0008028; F:monocarboxylic acid transmembrane transporter activity; IDA:ARUK-UCL. DR GO; GO:0097159; F:organic cyclic compound binding; IMP:RGD. DR GO; GO:0015295; F:solute:proton symporter activity; IDA:UniProtKB. DR GO; GO:0015141; F:succinate transmembrane transporter activity; ISS:UniProtKB. DR GO; GO:0051780; P:behavioral response to nutrient; ISO:RGD. DR GO; GO:1905039; P:carboxylic acid transmembrane transport; IMP:ARUK-UCL. DR GO; GO:0071407; P:cellular response to organic cyclic compound; IMP:RGD. DR GO; GO:0007098; P:centrosome cycle; ISO:RGD. DR GO; GO:0042593; P:glucose homeostasis; ISO:RGD. DR GO; GO:0035873; P:lactate transmembrane transport; IDA:RGD. DR GO; GO:0006629; P:lipid metabolic process; ISO:RGD. DR GO; GO:0015718; P:monocarboxylic acid transport; IDA:ARUK-UCL. DR GO; GO:0035879; P:plasma membrane lactate transport; IDA:RGD. DR GO; GO:0042867; P:pyruvate catabolic process; ISO:RGD. DR GO; GO:1901475; P:pyruvate transmembrane transport; IDA:UniProtKB. DR GO; GO:0050796; P:regulation of insulin secretion; ISO:RGD. DR GO; GO:0032094; P:response to food; ISO:RGD. DR GO; GO:0071422; P:succinate transmembrane transport; ISS:UniProtKB. DR CDD; cd17426; MFS_MCT1; 1. DR Gene3D; 1.20.1250.20; MFS general substrate transporter like domains; 1. DR InterPro; IPR004743; MCT. DR InterPro; IPR011701; MFS. DR InterPro; IPR020846; MFS_dom. DR InterPro; IPR036259; MFS_trans_sf. DR NCBIfam; TIGR00892; 2A0113; 1. DR PANTHER; PTHR11360; MONOCARBOXYLATE TRANSPORTER; 1. DR PANTHER; PTHR11360:SF24; MONOCARBOXYLATE TRANSPORTER 1; 1. DR Pfam; PF07690; MFS_1; 1. DR SUPFAM; SSF103473; MFS general substrate transporter; 1. DR PROSITE; PS50850; MFS; 1. DR Genevisible; P53987; RN. PE 1: Evidence at protein level; KW Cell membrane; Membrane; Phosphoprotein; Reference proteome; Symport; KW Transmembrane; Transmembrane helix; Transport. FT CHAIN 1..494 FT /note="Monocarboxylate transporter 1" FT /id="PRO_0000211384" FT TOPO_DOM 1..22 FT /note="Cytoplasmic" FT /evidence="ECO:0000305" FT TRANSMEM 23..44 FT /note="Helical; Name=1" FT /evidence="ECO:0000250|UniProtKB:P53985" FT TOPO_DOM 45..55 FT /note="Extracellular" FT /evidence="ECO:0000305" FT TRANSMEM 56..80 FT /note="Helical; Name=2" FT /evidence="ECO:0000250|UniProtKB:P53985" FT TOPO_DOM 81..84 FT /note="Cytoplasmic" FT /evidence="ECO:0000305" FT TRANSMEM 85..105 FT /note="Helical; Name=3" FT /evidence="ECO:0000250|UniProtKB:P53985" FT TOPO_DOM 106..109 FT /note="Extracellular" FT /evidence="ECO:0000305" FT TRANSMEM 110..132 FT /note="Helical; Name=4" FT /evidence="ECO:0000250|UniProtKB:P53985" FT TOPO_DOM 133..146 FT /note="Cytoplasmic" FT /evidence="ECO:0000305" FT TRANSMEM 147..169 FT /note="Helical; Name=5" FT /evidence="ECO:0000250|UniProtKB:P53985" FT TOPO_DOM 170..174 FT /note="Extracellular" FT /evidence="ECO:0000305" FT TRANSMEM 175..194 FT /note="Helical; Name=6" FT /evidence="ECO:0000250|UniProtKB:P53985" FT TOPO_DOM 195..254 FT /note="Cytoplasmic" FT /evidence="ECO:0000305" FT TRANSMEM 255..281 FT /note="Helical; Name=7" FT /evidence="ECO:0000250|UniProtKB:P53985" FT TOPO_DOM 282..288 FT /note="Extracellular" FT /evidence="ECO:0000305" FT TRANSMEM 289..310 FT /note="Helical; Name=8" FT /evidence="ECO:0000250|UniProtKB:P53985" FT TOPO_DOM 311..321 FT /note="Cytoplasmic" FT /evidence="ECO:0000305" FT TRANSMEM 322..342 FT /note="Helical; Name=9" FT /evidence="ECO:0000250|UniProtKB:P53985" FT TOPO_DOM 343..346 FT /note="Extracellular" FT /evidence="ECO:0000305" FT TRANSMEM 347..368 FT /note="Helical; Name=10" FT /evidence="ECO:0000250|UniProtKB:P53985" FT TOPO_DOM 369..382 FT /note="Cytoplasmic" FT /evidence="ECO:0000305" FT TRANSMEM 383..403 FT /note="Helical; Name=11" FT /evidence="ECO:0000250|UniProtKB:P53985" FT TOPO_DOM 404..414 FT /note="Extracellular" FT /evidence="ECO:0000305" FT TRANSMEM 415..436 FT /note="Helical; Name=12" FT /evidence="ECO:0000250|UniProtKB:P53985" FT TOPO_DOM 437..494 FT /note="Cytoplasmic" FT /evidence="ECO:0000305" FT REGION 446..494 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 446..472 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 474..494 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 38 FT /ligand="(S)-lactate" FT /ligand_id="ChEBI:CHEBI:16651" FT /evidence="ECO:0000250|UniProtKB:P53985" FT BINDING 302 FT /ligand="H(+)" FT /ligand_id="ChEBI:CHEBI:15378" FT /evidence="ECO:0000250|UniProtKB:P53985" FT BINDING 306 FT /ligand="(S)-lactate" FT /ligand_id="ChEBI:CHEBI:16651" FT /evidence="ECO:0000250|UniProtKB:P53985" FT MOD_RES 210 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:22673903" FT MOD_RES 213 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:16396499, FT ECO:0007744|PubMed:22673903" FT MOD_RES 220 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:22673903" FT MOD_RES 224 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P53986" FT MOD_RES 230 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:22673903" FT MOD_RES 459 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P53985" FT MOD_RES 460 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:22673903" FT MOD_RES 461 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P53986" FT MOD_RES 476 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P53985" FT MOD_RES 483 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P53986" FT MOD_RES 484 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P53986" FT MOD_RES 492 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:22673903" FT MUTAGEN 38 FT /note="K->Q,R: No effect on expression at the cell FT membrane, but abolishes lactate transport across the cell FT membrane." FT /evidence="ECO:0000269|PubMed:19473976" FT MUTAGEN 45 FT /note="K->Q,R: No effect on expression at the cell FT membrane. No effect on lactate transport across the cell FT membrane." FT /evidence="ECO:0000269|PubMed:19473976" FT MUTAGEN 86 FT /note="R->E,Q: No effect on expression at the cell FT membrane. No effect on lactate transport across the cell FT membrane." FT /evidence="ECO:0000269|PubMed:17127621" FT MUTAGEN 196 FT /note="R->E,Q: No effect on expression at the cell FT membrane. No effect on lactate transport across the cell FT membrane." FT /evidence="ECO:0000269|PubMed:17127621" FT MUTAGEN 282 FT /note="K->Q,R: No effect on expression at the cell FT membrane. No effect on lactate transport across the cell FT membrane." FT /evidence="ECO:0000269|PubMed:19473976" FT MUTAGEN 284 FT /note="K->Q,R: No effect on expression at the cell FT membrane. No effect on lactate transport across the cell FT membrane." FT /evidence="ECO:0000269|PubMed:19473976" FT MUTAGEN 290 FT /note="K->Q,R: No effect on expression at the cell FT membrane. No effect on lactate transport across the cell FT membrane." FT /evidence="ECO:0000269|PubMed:19473976" FT MUTAGEN 302 FT /note="D->R: Abolishes expression at the cell membrane. FT Abolishes lactate transport across the cell membrane FT without affecting expression at the cell membrane; when FT associated with E-306." FT /evidence="ECO:0000269|PubMed:17127621" FT MUTAGEN 306 FT /note="R->E: Abolishes expression at the cell membrane. FT Abolishes lactate transport across the cell membrane FT without affecting expression at the cell membrane; when FT associated with R-302." FT /evidence="ECO:0000269|PubMed:17127621" FT MUTAGEN 306 FT /note="R->K: No effect on expression at the cell membrane, FT but abolishes lactate transport across the cell membrane." FT /evidence="ECO:0000269|PubMed:17127621" FT MUTAGEN 413 FT /note="K->Q,R: No effect on expression at the cell FT membrane. No effect on lactate transport across the cell FT membrane." FT /evidence="ECO:0000269|PubMed:19473976" SQ SEQUENCE 494 AA; 53238 MW; CF82F8794CDBF057 CRC64; MPPAIGGPVG YTPPDGGWGW AVVVGAFISI GFSYAFPKSI TVFFKEIEII FSATTSEVSW ISSIMLAVMY AGGPISSILV NKYGSRPVMI AGGCLSGCGL IAASFCNTVQ ELYFCIGVIG GLGLAFNLNP ALTMIGKYFY KKRPLANGLA MAGSPVFLST LAPLNQAFFG IFGWRGSFLI LGGLLLNCCV AGSLMRPIGP QQGKVEKLKS KESLQEAGKS DANTDLIGGS PKGEKLSVFQ TVNKFLDLSL FTHRGFLLYL SGNVVMFFGL FTPLVFLSNY GKSKHFSSEK SAFLLSILAF VDMVARPSMG LAANTRWIRP RVQYFFAASV VANGVCHLLA PLSTTYVGFC IYAGVFGFAF GWLSSVLFET LMDLVGPQRF SSAVGLVTIV ECCPVLLGPP LLGRLNDMYG DYKYTYWACG VILIIAGLYL FIGMGINYRL VAKEQKAEEK KRDGKEDETS TDVDEKPKKT MKETQSPAPL QNSSGDPAEE ESPV //