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P53987 (MOT1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 111. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Monocarboxylate transporter 1

Short name=MCT 1
Alternative name(s):
Solute carrier family 16 member 1
Gene names
Name:Slc16a1
Synonyms:Mct1
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length494 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1 Ref.4 Ref.6 Ref.8 Ref.9

Enzyme regulation

Inhibited by stilbene disulfonates, such as di-isothiocyanostilbene disulfonate(DIDS), a cross-linking reagent that forms covalent linkages with lysine groups. Ref.9

Subunit structure

Interacts with BSG. Interacts with EMB. Interaction with either BSG or EMB is required for expression at the cell membrane. Ref.5 Ref.6 Ref.8 Ref.9

Subcellular location

Cell membrane; Multi-pass membrane protein Ref.1 Ref.4 Ref.5 Ref.6 Ref.8 Ref.9.

Tissue specificity

Detected in erythrocytes (at protein level). Detected in brain, heart, kidney, lung, muscle, jejunum enterocytes and brain capillaries. Ref.1 Ref.4 Ref.5 Ref.9

Sequence similarities

Belongs to the major facilitator superfamily. Monocarboxylate porter (TC 2.A.1.13) family. [View classification]

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 494494Monocarboxylate transporter 1
PRO_0000211384

Regions

Topological domain1 – 1515Cytoplasmic Probable
Transmembrane16 – 3621Helical; Potential
Topological domain37 – 5923Extracellular Probable
Transmembrane60 – 8021Helical; Potential
Topological domain81 – 866Cytoplasmic Potential
Transmembrane87 – 10721Helical; Potential
Topological domain108 – 1114Extracellular Potential
Transmembrane112 – 13221Helical; Potential
Topological domain133 – 14311Cytoplasmic Potential
Transmembrane144 – 16421Helical; Potential
Topological domain165 – 1662Extracellular Potential
Transmembrane167 – 18721Helical; Potential
Topological domain188 – 25568Cytoplasmic Potential
Transmembrane256 – 27621Helical; Potential
Topological domain277 – 29115Extracellular Probable
Transmembrane292 – 31221Helical; Potential
Topological domain313 – 3219Cytoplasmic Potential
Transmembrane322 – 34221Helical; Potential
Topological domain343 – 3464Extracellular Potential
Transmembrane347 – 36721Helical; Potential
Topological domain368 – 38215Cytoplasmic Potential
Transmembrane383 – 40321Helical; Potential
Topological domain404 – 41512Extracellular Probable
Transmembrane416 – 43621Helical; Potential
Topological domain437 – 49458Cytoplasmic Probable

Amino acid modifications

Modified residue2101Phosphoserine By similarity
Modified residue2131Phosphoserine Ref.7
Modified residue2241Phosphothreonine By similarity
Modified residue2301Phosphoserine By similarity
Modified residue4591Phosphothreonine By similarity
Modified residue4601Phosphoserine By similarity
Modified residue4611Phosphothreonine By similarity
Modified residue4761Phosphoserine By similarity
Modified residue4921Phosphoserine By similarity

Experimental info

Mutagenesis381K → Q or R: No effect on expression at the cell membrane, but abolishes lactate transport across the cell membrane. Ref.9
Mutagenesis451K → Q or R: No effect on expression at the cell membrane. No effect on lactate transport across the cell membrane. Ref.9
Mutagenesis861R → E or Q: No effect on expression at the cell membrane. No effect on lactate transport across the cell membrane. Ref.8
Mutagenesis1961R → E or Q: No effect on expression at the cell membrane. No effect on lactate transport across the cell membrane. Ref.8
Mutagenesis2821K → Q or R: No effect on expression at the cell membrane. No effect on lactate transport across the cell membrane. Ref.9
Mutagenesis2841K → Q or R: No effect on expression at the cell membrane. No effect on lactate transport across the cell membrane. Ref.9
Mutagenesis2901K → Q or R: No effect on expression at the cell membrane. No effect on lactate transport across the cell membrane. Ref.9
Mutagenesis3021D → 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. Ref.8
Mutagenesis3061R → 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. Ref.8
Mutagenesis3061R → K: No effect on expression at the cell membrane, but abolishes lactate transport across the cell membrane. Ref.8
Mutagenesis4131K → Q or R: No effect on expression at the cell membrane. No effect on lactate transport across the cell membrane. Ref.9

Sequences

Sequence LengthMass (Da)Tools
P53987 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: CF82F8794CDBF057

FASTA49453,238
        10         20         30         40         50         60 
MPPAIGGPVG YTPPDGGWGW AVVVGAFISI GFSYAFPKSI TVFFKEIEII FSATTSEVSW 

        70         80         90        100        110        120 
ISSIMLAVMY AGGPISSILV NKYGSRPVMI AGGCLSGCGL IAASFCNTVQ ELYFCIGVIG 

       130        140        150        160        170        180 
GLGLAFNLNP ALTMIGKYFY KKRPLANGLA MAGSPVFLST LAPLNQAFFG IFGWRGSFLI 

       190        200        210        220        230        240 
LGGLLLNCCV AGSLMRPIGP QQGKVEKLKS KESLQEAGKS DANTDLIGGS PKGEKLSVFQ 

       250        260        270        280        290        300 
TVNKFLDLSL FTHRGFLLYL SGNVVMFFGL FTPLVFLSNY GKSKHFSSEK SAFLLSILAF 

       310        320        330        340        350        360 
VDMVARPSMG LAANTRWIRP RVQYFFAASV VANGVCHLLA PLSTTYVGFC IYAGVFGFAF 

       370        380        390        400        410        420 
GWLSSVLFET LMDLVGPQRF SSAVGLVTIV ECCPVLLGPP LLGRLNDMYG DYKYTYWACG 

       430        440        450        460        470        480 
VILIIAGLYL FIGMGINYRL VAKEQKAEEK KRDGKEDETS TDVDEKPKKT MKETQSPAPL 

       490 
QNSSGDPAEE ESPV 

« Hide

References

« Hide 'large scale' references
[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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D63834 mRNA. Translation: BAA09894.1.
X86216 mRNA. Translation: CAA60116.1.
BC078877 mRNA. Translation: AAH78877.1.
AJ236865 mRNA. Translation: CAB37948.1.
PIRJC4399.
RefSeqNP_036848.1. NM_012716.2.
UniGeneRn.6085.

3D structure databases

ProteinModelPortalP53987.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid247107. 1 interaction.
STRING10116.ENSRNOP00000027234.

Chemistry

ChEMBLCHEMBL2073709.

PTM databases

PhosphoSiteP53987.

Proteomic databases

PaxDbP53987.
PRIDEP53987.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000027234; ENSRNOP00000027234; ENSRNOG00000019996.
GeneID25027.
KEGGrno:25027.
UCSCRGD:3690. rat.

Organism-specific databases

CTD6566.
RGD3690. Slc16a1.

Phylogenomic databases

eggNOGCOG0477.
GeneTreeENSGT00670000097675.
HOGENOMHOG000280688.
HOVERGENHBG006384.
InParanoidP53987.
KOK08179.
OMAQYFFAIS.
OrthoDBEOG7W9RTN.
PhylomeDBP53987.
TreeFamTF313792.

Enzyme and pathway databases

SABIO-RKP53987.

Gene expression databases

GenevestigatorP53987.

Family and domain databases

InterProIPR011701. MFS.
IPR020846. MFS_dom.
IPR016196. MFS_dom_general_subst_transpt.
IPR004743. Monocarb_transpt.
[Graphical view]
PfamPF07690. MFS_1. 1 hit.
[Graphical view]
SUPFAMSSF103473. SSF103473. 2 hits.
TIGRFAMsTIGR00892. 2A0113. 1 hit.
PROSITEPS50850. MFS. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio605163.
PROP53987.

Entry information

Entry nameMOT1_RAT
AccessionPrimary (citable) accession number: P53987
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: June 11, 2014
This is version 111 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families