Q03064 · MOT1_CRILO

Function

function

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 (By similarity).
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:1429658).
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).

Catalytic activity

  • (S)-lactate(in) + H+(in) = (S)-lactate(out) + H+(out)
    This reaction proceeds in the forward
    and the backward
    directions.
  • acetate(out) + H+(out) = acetate(in) + H+(in)
    This reaction proceeds in the forward
    and the backward
    directions.
  • acetoacetate(out) + H+(out) = acetoacetate(in) + H+(in)
    This reaction proceeds in the forward
    and the backward
    directions.
  • H+(out) + pyruvate(out) = H+(in) + pyruvate(in)
  • (R)-3-hydroxybutanoate(out) + H+(out) = (R)-3-hydroxybutanoate(in) + H+(in)
    This reaction proceeds in the forward
    and the backward
    directions.
  • 3-methyl-2-oxobutanoate(out) + H+(out) = 3-methyl-2-oxobutanoate(in) + H+(in)
  • 4-methyl-2-oxopentanoate(out) + H+(out) = 4-methyl-2-oxopentanoate(in) + H+(in)
  • 2 H+(in) + succinate(in) = 2 H+(out) + succinate(out)
    This reaction proceeds in the forward direction.

Features

Showing features for binding site, site.

TypeIDPosition(s)Description
Binding site38(S)-lactate (UniProtKB | ChEBI)
Site52Not glycosylated
Binding site302H+ (UniProtKB | ChEBI)
Binding site306(S)-lactate (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentapical plasma membrane
Cellular Componentbasolateral plasma membrane
Cellular Componentplasma membrane
Molecular Functionlactate transmembrane transporter activity
Molecular Functionlactate:proton symporter activity
Molecular Functionsolute:proton symporter activity
Molecular Functionsuccinate transmembrane transporter activity
Biological Processplasma membrane lactate transport
Biological Processpyruvate transmembrane transport
Biological Processsuccinate transmembrane transport

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Monocarboxylate transporter 1
  • Short names
    MCT 1
  • Alternative names
    • Solute carrier family 16 member 1

Gene names

    • Name
      SLC16A1
    • Synonyms
      MCT1, MEV

Organism names

Accessions

  • Primary accession
    Q03064

Subcellular Location

Cell membrane
; Multi-pass membrane protein
Basolateral cell membrane
; Multi-pass membrane protein
Apical cell membrane
; Multi-pass membrane protein
Note: Expression at the cell surface requires the ancillary protein BSN.

Features

Showing features for topological domain, transmembrane.

TypeIDPosition(s)Description
Topological domain1-22Cytoplasmic
Transmembrane23-44Helical; Name=1
Topological domain45-55Extracellular
Transmembrane56-80Helical; Name=2
Topological domain81-84Cytoplasmic
Transmembrane85-105Helical; Name=3
Topological domain106-109Extracellular
Transmembrane110-132Helical; Name=4
Topological domain133-146Cytoplasmic
Transmembrane147-169Helical; Name=5
Topological domain170-174Extracellular
Transmembrane175-194Helical; Name=6
Topological domain195-254Cytoplasmic
Transmembrane255-281Helical; Name=7
Topological domain282-288Extracellular
Transmembrane289-310Helical; Name=8
Topological domain311-321Cytoplasmic
Transmembrane322-342Helical; Name=9
Topological domain343-346Extracellular
Transmembrane347-368Helical; Name=10
Topological domain369-382Cytoplasmic
Transmembrane383-403Helical; Name=11
Topological domain404-414Extracellular
Transmembrane415-436Helical; Name=12
Topological domain437-494Cytoplasmic

Keywords

Phenotypes & Variants

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis360Gain of function as mevalonate transporter.

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_00002113801-494Monocarboxylate transporter 1
Modified residue210Phosphoserine
Modified residue213Phosphoserine
Modified residue220Phosphoserine
Modified residue224Phosphothreonine
Modified residue230Phosphoserine
Modified residue461Phosphothreonine
Modified residue462Phosphoserine
Modified residue463Phosphothreonine
Modified residue478Phosphoserine
Modified residue483Phosphoserine
Modified residue484Phosphoserine
Modified residue492Phosphoserine

Post-translational modification

Not glycosylated.

Keywords

Expression

Tissue specificity

Expressed at abundant levels in erythrocytes, cardiac muscle, basolateral intestinal epithelium, skeletal muscle myocytes, testis and at low levels in liver. In the stomach and in the proximal tubules of the kidney, present on the basolateral surfaces of epithelial cells. Expressed on sperm heads in the testis and proximal epididymis. In the distal epididymis, it disappeared from sperm and appeared on the microvillar surface of the lining epithelium. Also expressed in lung, cecum and eye.

Interaction

Subunit

Interacts with BSG; interaction mediates SLC16A1 targeting to the plasma membrane (By similarity).
Interacts with EMB; interaction mediates SLC16A1 targeting to the plasma membrane (By similarity).

Structure

Family & Domains

Features

Showing features for compositional bias, region.

TypeIDPosition(s)Description
Compositional bias447-474Basic and acidic residues
Region447-494Disordered
Compositional bias475-494Polar residues

Sequence similarities

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    494
  • Mass (Da)
    53,173
  • Last updated
    1994-06-01 v1
  • Checksum
    D77C4A4023684318
MPPAIGGPVGYTPPDGGWGWAVVVGAFISIGFSYAFPKSITVFFKEIEGIFNATTSEVSWISSIMLAVMYAGGPISSVLVNKYGSRPVMIAGGCLSGCGLIAASFCNTVQELYLCIGVIGGLGLAFNLNPALTMIGKYFYKKRPLANGLAMAGSPVFLSTLAPLNQAFFGIFGWRGSFLILGGLLLNCCVAGSLMRPIGPKPGKIEKLKSKESLQEAGKSEANTDLMGGSPKGEKRSVLQTINKFLDLSLFAHRGFLLYLSGNVVMFFGLFTPLVFLSNYGKSQHYSSEKSAFLLSILAFVDMVARPSMGLAANTKWIRPRIQYFFAASVVANGVCHLLAPLSTSYIGFCIYAGVFGFAFGWLSSVLFETLMDLVGPQRFSSAVGLVTIVECCPVLLGPPLLGRLNDMYGDYKYTYWACGVILIIAGIYLFIGMGINYRLVAKEQKAEEKQKQEEGKEDDTSTDVDEKPKELTKATESPQQNSSGDPAEEESPV

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias447-474Basic and acidic residues
Compositional bias475-494Polar residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
M97382
EMBL· GenBank· DDBJ
AAB59630.1
EMBL· GenBank· DDBJ
mRNA
L25842
EMBL· GenBank· DDBJ
AAB59731.1
EMBL· GenBank· DDBJ
mRNA

Similar Proteins

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