Q03064 · MOT1_CRILO
- ProteinMonocarboxylate transporter 1
- GeneSLC16A1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids494 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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).
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.(S)-lactate (in)CHEBI:16651
+ H+ (in)CHEBI:15378= (S)-lactate (out)CHEBI:16651+ H+ (out)CHEBI:15378 - 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.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | apical plasma membrane | |
Cellular Component | basolateral plasma membrane | |
Cellular Component | plasma membrane | |
Molecular Function | lactate transmembrane transporter activity | |
Molecular Function | lactate:proton symporter activity | |
Molecular Function | solute:proton symporter activity | |
Molecular Function | succinate transmembrane transporter activity | |
Biological Process | plasma membrane lactate transport | |
Biological Process | pyruvate transmembrane transport | |
Biological Process | succinate transmembrane transport |
Keywords
- Biological process
Names & Taxonomy
Protein names
- Recommended nameMonocarboxylate transporter 1
- Short namesMCT 1
- Alternative names
Gene names
Organism names
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Cricetidae > Cricetinae > Cricetulus
Accessions
- Primary accessionQ03064
Subcellular Location
UniProt Annotation
GO Annotation
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.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-22 | Cytoplasmic | ||||
Sequence: MPPAIGGPVGYTPPDGGWGWAV | ||||||
Transmembrane | 23-44 | Helical; Name=1 | ||||
Sequence: VVGAFISIGFSYAFPKSITVFF | ||||||
Topological domain | 45-55 | Extracellular | ||||
Sequence: KEIEGIFNATT | ||||||
Transmembrane | 56-80 | Helical; Name=2 | ||||
Sequence: SEVSWISSIMLAVMYAGGPISSVLV | ||||||
Topological domain | 81-84 | Cytoplasmic | ||||
Sequence: NKYG | ||||||
Transmembrane | 85-105 | Helical; Name=3 | ||||
Sequence: SRPVMIAGGCLSGCGLIAASF | ||||||
Topological domain | 106-109 | Extracellular | ||||
Sequence: CNTV | ||||||
Transmembrane | 110-132 | Helical; Name=4 | ||||
Sequence: QELYLCIGVIGGLGLAFNLNPAL | ||||||
Topological domain | 133-146 | Cytoplasmic | ||||
Sequence: TMIGKYFYKKRPLA | ||||||
Transmembrane | 147-169 | Helical; Name=5 | ||||
Sequence: NGLAMAGSPVFLSTLAPLNQAFF | ||||||
Topological domain | 170-174 | Extracellular | ||||
Sequence: GIFGW | ||||||
Transmembrane | 175-194 | Helical; Name=6 | ||||
Sequence: RGSFLILGGLLLNCCVAGSL | ||||||
Topological domain | 195-254 | Cytoplasmic | ||||
Sequence: MRPIGPKPGKIEKLKSKESLQEAGKSEANTDLMGGSPKGEKRSVLQTINKFLDLSLFAHR | ||||||
Transmembrane | 255-281 | Helical; Name=7 | ||||
Sequence: GFLLYLSGNVVMFFGLFTPLVFLSNYG | ||||||
Topological domain | 282-288 | Extracellular | ||||
Sequence: KSQHYSS | ||||||
Transmembrane | 289-310 | Helical; Name=8 | ||||
Sequence: EKSAFLLSILAFVDMVARPSMG | ||||||
Topological domain | 311-321 | Cytoplasmic | ||||
Sequence: LAANTKWIRPR | ||||||
Transmembrane | 322-342 | Helical; Name=9 | ||||
Sequence: IQYFFAASVVANGVCHLLAPL | ||||||
Topological domain | 343-346 | Extracellular | ||||
Sequence: STSY | ||||||
Transmembrane | 347-368 | Helical; Name=10 | ||||
Sequence: IGFCIYAGVFGFAFGWLSSVLF | ||||||
Topological domain | 369-382 | Cytoplasmic | ||||
Sequence: ETLMDLVGPQRFSS | ||||||
Transmembrane | 383-403 | Helical; Name=11 | ||||
Sequence: AVGLVTIVECCPVLLGPPLLG | ||||||
Topological domain | 404-414 | Extracellular | ||||
Sequence: RLNDMYGDYKY | ||||||
Transmembrane | 415-436 | Helical; Name=12 | ||||
Sequence: TYWACGVILIIAGIYLFIGMGI | ||||||
Topological domain | 437-494 | Cytoplasmic | ||||
Sequence: NYRLVAKEQKAEEKQKQEEGKEDDTSTDVDEKPKELTKATESPQQNSSGDPAEEESPV |
Keywords
- Cellular component
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 360 | Gain of function as mevalonate transporter. | ||||
Sequence: F → C |
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000211380 | 1-494 | Monocarboxylate transporter 1 | |||
Sequence: MPPAIGGPVGYTPPDGGWGWAVVVGAFISIGFSYAFPKSITVFFKEIEGIFNATTSEVSWISSIMLAVMYAGGPISSVLVNKYGSRPVMIAGGCLSGCGLIAASFCNTVQELYLCIGVIGGLGLAFNLNPALTMIGKYFYKKRPLANGLAMAGSPVFLSTLAPLNQAFFGIFGWRGSFLILGGLLLNCCVAGSLMRPIGPKPGKIEKLKSKESLQEAGKSEANTDLMGGSPKGEKRSVLQTINKFLDLSLFAHRGFLLYLSGNVVMFFGLFTPLVFLSNYGKSQHYSSEKSAFLLSILAFVDMVARPSMGLAANTKWIRPRIQYFFAASVVANGVCHLLAPLSTSYIGFCIYAGVFGFAFGWLSSVLFETLMDLVGPQRFSSAVGLVTIVECCPVLLGPPLLGRLNDMYGDYKYTYWACGVILIIAGIYLFIGMGINYRLVAKEQKAEEKQKQEEGKEDDTSTDVDEKPKELTKATESPQQNSSGDPAEEESPV | ||||||
Modified residue | 210 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 213 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 220 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 224 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 230 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 461 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 462 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 463 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 478 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 483 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 484 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 492 | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Not glycosylated.
Keywords
- PTM
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).
Interacts with EMB; interaction mediates SLC16A1 targeting to the plasma membrane (By similarity).
Structure
Family & Domains
Features
Showing features for compositional bias, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 447-474 | Basic and acidic residues | ||||
Sequence: AEEKQKQEEGKEDDTSTDVDEKPKELTK | ||||||
Region | 447-494 | Disordered | ||||
Sequence: AEEKQKQEEGKEDDTSTDVDEKPKELTKATESPQQNSSGDPAEEESPV | ||||||
Compositional bias | 475-494 | Polar residues | ||||
Sequence: ATESPQQNSSGDPAEEESPV |
Sequence similarities
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Length494
- Mass (Da)53,173
- Last updated1994-06-01 v1
- ChecksumD77C4A4023684318
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 447-474 | Basic and acidic residues | ||||
Sequence: AEEKQKQEEGKEDDTSTDVDEKPKELTK | ||||||
Compositional bias | 475-494 | Polar residues | ||||
Sequence: ATESPQQNSSGDPAEEESPV |