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Protein

Monocarboxylate transporter 1

Gene

Slc16a1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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. Depending on the tissue and on cicumstances, mediates the import or export of lactic acid and ketone bodies. Required for normal nutrient assimilation, increase of white adipose tissue and body weight gain when on a high-fat diet. Plays a role in cellular responses to a high-fat diet by modulating the cellular levels of lactate and pyruvate, small molecules that contribute to the regulation of central metabolic pathways and insulin secretion, with concomitant effects on plasma insulin levels and blood glucose homeostasis.5 Publications

Enzyme regulationi

Inhibited by stilbene disulfonates, such as di-isothiocyanostilbene disulfonate(DIDS), a cross-linking reagent that forms covalent linkages with lysine groups.1 Publication

GO - Molecular functioni

  1. lactate transmembrane transporter activity Source: GO_Central
  2. organic cyclic compound binding Source: RGD
  3. protein homodimerization activity Source: RGD
  4. secondary active monocarboxylate transmembrane transporter activity Source: InterPro
  5. symporter activity Source: UniProtKB-KW

GO - Biological processi

  1. behavioral response to nutrient Source: Ensembl
  2. cellular response to organic cyclic compound Source: RGD
  3. centrosome organization Source: Ensembl
  4. glucose homeostasis Source: Ensembl
  5. lactate transmembrane transport Source: RGD
  6. lipid metabolic process Source: Ensembl
  7. plasma membrane lactate transport Source: UniProtKB
  8. regulation of insulin secretion Source: Ensembl
  9. response to food Source: Ensembl
Complete GO annotation...

Keywords - Biological processi

Symport, Transport

Enzyme and pathway databases

ReactomeiREACT_203088. Pyruvate metabolism.
REACT_245266. Basigin interactions.
REACT_252207. Proton-coupled monocarboxylate transport.
SABIO-RKP53987.

Names & Taxonomyi

Protein namesi
Recommended name:
Monocarboxylate transporter 1
Short name:
MCT 1
Alternative name(s):
Solute carrier family 16 member 1
Gene namesi
Name:Slc16a1
Synonyms:Mct1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Chromosome 2

Organism-specific databases

RGDi3690. Slc16a1.

Subcellular locationi

Cell membrane 6 Publications; Multi-pass membrane protein 6 Publications

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1515CytoplasmicCuratedAdd
BLAST
Transmembranei16 – 3621HelicalSequence AnalysisAdd
BLAST
Topological domaini37 – 5923ExtracellularCuratedAdd
BLAST
Transmembranei60 – 8021HelicalSequence AnalysisAdd
BLAST
Topological domaini81 – 866CytoplasmicSequence Analysis
Transmembranei87 – 10721HelicalSequence AnalysisAdd
BLAST
Topological domaini108 – 1114ExtracellularSequence Analysis
Transmembranei112 – 13221HelicalSequence AnalysisAdd
BLAST
Topological domaini133 – 14311CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei144 – 16421HelicalSequence AnalysisAdd
BLAST
Topological domaini165 – 1662ExtracellularSequence Analysis
Transmembranei167 – 18721HelicalSequence AnalysisAdd
BLAST
Topological domaini188 – 25568CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei256 – 27621HelicalSequence AnalysisAdd
BLAST
Topological domaini277 – 29115ExtracellularCuratedAdd
BLAST
Transmembranei292 – 31221HelicalSequence AnalysisAdd
BLAST
Topological domaini313 – 3219CytoplasmicSequence Analysis
Transmembranei322 – 34221HelicalSequence AnalysisAdd
BLAST
Topological domaini343 – 3464ExtracellularSequence Analysis
Transmembranei347 – 36721HelicalSequence AnalysisAdd
BLAST
Topological domaini368 – 38215CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei383 – 40321HelicalSequence AnalysisAdd
BLAST
Topological domaini404 – 41512ExtracellularCuratedAdd
BLAST
Transmembranei416 – 43621HelicalSequence AnalysisAdd
BLAST
Topological domaini437 – 49458CytoplasmicCuratedAdd
BLAST

GO - Cellular componenti

  1. centrosome Source: Ensembl
  2. extracellular vesicular exosome Source: Ensembl
  3. integral component of plasma membrane Source: UniProtKB
  4. mitochondrion Source: Ensembl
  5. plasma membrane Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi38 – 381K → Q or R: No effect on expression at the cell membrane, but abolishes lactate transport across the cell membrane. 1 Publication
Mutagenesisi45 – 451K → Q or R: No effect on expression at the cell membrane. No effect on lactate transport across the cell membrane. 1 Publication
Mutagenesisi86 – 861R → E or Q: No effect on expression at the cell membrane. No effect on lactate transport across the cell membrane. 1 Publication
Mutagenesisi196 – 1961R → E or Q: No effect on expression at the cell membrane. No effect on lactate transport across the cell membrane. 1 Publication
Mutagenesisi282 – 2821K → Q or R: No effect on expression at the cell membrane. No effect on lactate transport across the cell membrane. 1 Publication
Mutagenesisi284 – 2841K → Q or R: No effect on expression at the cell membrane. No effect on lactate transport across the cell membrane. 1 Publication
Mutagenesisi290 – 2901K → Q or R: No effect on expression at the cell membrane. No effect on lactate transport across the cell membrane. 1 Publication
Mutagenesisi302 – 3021D → R: Abolishes expression at the cell membrane. Abolishes lactate transport across the cell membrane without affecting expression at the cell membrane; when associated with E-306. 1 Publication
Mutagenesisi306 – 3061R → E: Abolishes expression at the cell membrane. Abolishes lactate transport across the cell membrane without affecting expression at the cell membrane; when associated with R-302. 1 Publication
Mutagenesisi306 – 3061R → K: No effect on expression at the cell membrane, but abolishes lactate transport across the cell membrane. 1 Publication
Mutagenesisi413 – 4131K → Q or R: No effect on expression at the cell membrane. No effect on lactate transport across the cell membrane. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 494494Monocarboxylate transporter 1PRO_0000211384Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei210 – 2101PhosphoserineBy similarity
Modified residuei213 – 2131Phosphoserine1 Publication
Modified residuei224 – 2241PhosphothreonineBy similarity
Modified residuei230 – 2301PhosphoserineBy similarity
Modified residuei459 – 4591PhosphothreonineBy similarity
Modified residuei460 – 4601PhosphoserineBy similarity
Modified residuei461 – 4611PhosphothreonineBy similarity
Modified residuei476 – 4761PhosphoserineBy similarity
Modified residuei492 – 4921PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP53987.
PRIDEiP53987.

PTM databases

PhosphoSiteiP53987.

Expressioni

Tissue specificityi

Detected in erythrocytes (at protein level). Detected in brain, heart, kidney, lung, muscle, jejunum enterocytes and brain capillaries.4 Publications

Gene expression databases

GenevestigatoriP53987.

Interactioni

Subunit structurei

Interacts with BSG. Interacts with EMB. Interaction with either BSG or EMB is required for expression at the cell membrane.4 Publications

Protein-protein interaction databases

BioGridi247107. 1 interaction.
STRINGi10116.ENSRNOP00000027234.

Structurei

3D structure databases

ProteinModelPortaliP53987.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0477.
GeneTreeiENSGT00760000118926.
HOGENOMiHOG000280688.
HOVERGENiHBG006384.
InParanoidiP53987.
KOiK08179.
OMAiQYFFAIS.
OrthoDBiEOG7W9RTN.
PhylomeDBiP53987.
TreeFamiTF313792.

Family and domain databases

InterProiIPR011701. MFS.
IPR020846. MFS_dom.
IPR004743. Monocarb_transpt.
[Graphical view]
PfamiPF07690. MFS_1. 1 hit.
[Graphical view]
SUPFAMiSSF103473. SSF103473. 2 hits.
TIGRFAMsiTIGR00892. 2A0113. 1 hit.
PROSITEiPS50850. MFS. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P53987-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MPPAIGGPVG YTPPDGGWGW AVVVGAFISI GFSYAFPKSI TVFFKEIEII
60 70 80 90 100
FSATTSEVSW ISSIMLAVMY AGGPISSILV NKYGSRPVMI AGGCLSGCGL
110 120 130 140 150
IAASFCNTVQ ELYFCIGVIG GLGLAFNLNP ALTMIGKYFY KKRPLANGLA
160 170 180 190 200
MAGSPVFLST LAPLNQAFFG IFGWRGSFLI LGGLLLNCCV AGSLMRPIGP
210 220 230 240 250
QQGKVEKLKS KESLQEAGKS DANTDLIGGS PKGEKLSVFQ TVNKFLDLSL
260 270 280 290 300
FTHRGFLLYL SGNVVMFFGL FTPLVFLSNY GKSKHFSSEK SAFLLSILAF
310 320 330 340 350
VDMVARPSMG LAANTRWIRP RVQYFFAASV VANGVCHLLA PLSTTYVGFC
360 370 380 390 400
IYAGVFGFAF GWLSSVLFET LMDLVGPQRF SSAVGLVTIV ECCPVLLGPP
410 420 430 440 450
LLGRLNDMYG DYKYTYWACG VILIIAGLYL FIGMGINYRL VAKEQKAEEK
460 470 480 490
KRDGKEDETS TDVDEKPKKT MKETQSPAPL QNSSGDPAEE ESPV
Length:494
Mass (Da):53,238
Last modified:October 1, 1996 - v1
Checksum:iCF82F8794CDBF057
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D63834 mRNA. Translation: BAA09894.1.
X86216 mRNA. Translation: CAA60116.1.
BC078877 mRNA. Translation: AAH78877.1.
AJ236865 mRNA. Translation: CAB37948.1.
PIRiJC4399.
RefSeqiNP_036848.1. NM_012716.2.
UniGeneiRn.6085.

Genome annotation databases

EnsembliENSRNOT00000027234; ENSRNOP00000027234; ENSRNOG00000019996.
GeneIDi25027.
KEGGirno:25027.
UCSCiRGD:3690. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D63834 mRNA. Translation: BAA09894.1.
X86216 mRNA. Translation: CAA60116.1.
BC078877 mRNA. Translation: AAH78877.1.
AJ236865 mRNA. Translation: CAB37948.1.
PIRiJC4399.
RefSeqiNP_036848.1. NM_012716.2.
UniGeneiRn.6085.

3D structure databases

ProteinModelPortaliP53987.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi247107. 1 interaction.
STRINGi10116.ENSRNOP00000027234.

Chemistry

BindingDBiP53987.
ChEMBLiCHEMBL2073709.

PTM databases

PhosphoSiteiP53987.

Proteomic databases

PaxDbiP53987.
PRIDEiP53987.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000027234; ENSRNOP00000027234; ENSRNOG00000019996.
GeneIDi25027.
KEGGirno:25027.
UCSCiRGD:3690. rat.

Organism-specific databases

CTDi6566.
RGDi3690. Slc16a1.

Phylogenomic databases

eggNOGiCOG0477.
GeneTreeiENSGT00760000118926.
HOGENOMiHOG000280688.
HOVERGENiHBG006384.
InParanoidiP53987.
KOiK08179.
OMAiQYFFAIS.
OrthoDBiEOG7W9RTN.
PhylomeDBiP53987.
TreeFamiTF313792.

Enzyme and pathway databases

ReactomeiREACT_203088. Pyruvate metabolism.
REACT_245266. Basigin interactions.
REACT_252207. Proton-coupled monocarboxylate transport.
SABIO-RKP53987.

Miscellaneous databases

NextBioi605163.
PROiP53987.

Gene expression databases

GenevestigatoriP53987.

Family and domain databases

InterProiIPR011701. MFS.
IPR020846. MFS_dom.
IPR004743. Monocarb_transpt.
[Graphical view]
PfamiPF07690. MFS_1. 1 hit.
[Graphical view]
SUPFAMiSSF103473. SSF103473. 2 hits.
TIGRFAMsiTIGR00892. 2A0113. 1 hit.
PROSITEiPS50850. MFS. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "cDNA cloning and functional characterization of rat intestinal monocarboxylate transporter."
    Takanaga H., Tamai I., Inaba S., Sai Y., Higashida H., Yamamoto H., Tsuji A.
    Biochem. Biophys. Res. Commun. 217:370-377(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
    Strain: Wistar.
    Tissue: Small intestine.
  2. "cDNA cloning of MCT1, a monocarboxylate transporter from rat skeletal muscle."
    Jackson V.N., Price N.T., Halestrap A.P.
    Biochim. Biophys. Acta 1238:193-196(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Wistar.
    Tissue: Skeletal muscle.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Lung.
  4. "A monocarboxylate transporter MCT1 is located at the basolateral pole of rat jejunum."
    Orsenigo M.N., Tosco M., Bazzini C., Laforenza U., Faelli A.
    Exp. Physiol. 84:1033-1042(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 264-472, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    Tissue: Jejunal epithelium.
  5. "Interaction of the erythrocyte lactate transporter (monocarboxylate transporter 1) with an integral 70-kDa membrane glycoprotein of the immunoglobulin superfamily."
    Poole R.C., Halestrap A.P.
    J. Biol. Chem. 272:14624-14628(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH EMB, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
  6. "Fluorescence resonance energy transfer studies on the interaction between the lactate transporter MCT1 and CD147 provide information on the topology and stoichiometry of the complex in situ."
    Wilson M.C., Meredith D., Halestrap A.P.
    J. Biol. Chem. 277:3666-3672(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH BSG, FUNCTION, SUBCELLULAR LOCATION.
  7. "Phosphoproteomic analysis of rat liver by high capacity IMAC and LC-MS/MS."
    Moser K., White F.M.
    J. Proteome Res. 5:98-104(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-213, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "The role of charged residues in the transmembrane helices of monocarboxylate transporter 1 and its ancillary protein basigin in determining plasma membrane expression and catalytic activity."
    Manoharan C., Wilson M.C., Sessions R.B., Halestrap A.P.
    Mol. Membr. Biol. 23:486-498(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH BSG, TOPOLOGY, 3D-STRUCTURE MODELING, MUTAGENESIS OF ARG-86; ARG-196; ASP-302 AND ARG-306.
  9. "Studies on the DIDS-binding site of monocarboxylate transporter 1 suggest a homology model of the open conformation and a plausible translocation cycle."
    Wilson M.C., Meredith D., Bunnun C., Sessions R.B., Halestrap A.P.
    J. Biol. Chem. 284:20011-20021(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH EMB, SUBCELLULAR LOCATION, TOPOLOGY, 3D-STRUCTURE MODELING, MUTAGENESIS OF LYS-38; LYS-45; LYS-282; LYS-284; LYS-290 AND LYS-413, ENZYME REGULATION, TISSUE SPECIFICITY.

Entry informationi

Entry nameiMOT1_RAT
AccessioniPrimary (citable) accession number: P53987
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: February 4, 2015
This is version 117 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.