TCDB is operated by the Saier Lab Bioinformatics Group
« See all members of the family


2.A.1.13.1
The proton-linked monocarboxylate (lactate, pyruvate, mevalonate, branched chain oxo acids, β-hydroxybutyrate, γ-hydroxybutyrate, butyrate, acetoacetate acetate and formate) uptake/efflux porter (Moschen et al. 2012). Also transports anti-tumor agents, 3-bromopyruvate and dichloroacetate (Cooper et al. 1989; Su et al. 2016). Activity is stimulated by direct interaction with carbonic anhydrase isoform II (Becker et al., 2005). This transporter interacts physically with the chaperone protein Basigin (CD147; TC #8.A.23.1.1) which is required both for targetting to the plasma membrane and for activity. Mct-2 uses a different chaperone protein, GP70. Mct-1 also transports the methionine hydroxy analogue 2-hydroxy (4-methylthio) butanate (Martin-Venegas et al., 2007; Becker and Deitmer, 2008). MCT1, 3 and 4 require the ancillary protein, basigin (P35613; 8.A.23.1.1) for plasma membrane localization (Ovens et al., 2010).  Partially localizes to the peroxysomal membrane (Visser et al. 2007). MCT1 is regulated by CD147 proteins, and this association is important for lactate export and cell proliferation in certain cancer cells (Walters et al. 2013).  Upregulated in some cancers and maintains the metabolic phenotype of these cancer cells by mediating lactate efflux together with a proton, promoting pH homeostasis (PMID 24921258). 

Accession Number:P53985
Protein Name:MOT1 aka Mct-1 aka SLC16A1 aka MCT1
Length:500
Molecular Weight:53958.00
Species:Homo sapiens (Human) [9606]
Number of TMSs:12
Location1 / Topology2 / Orientation3: Cell membrane1 / Multi-pass membrane protein2
Substrate Monocarboxylates

Cross database links:

Genevestigator: P53985 P53985
eggNOG: prNOG08079 NOG314865
HEGENOM: HBG444740 HOG000280688
RefSeq: NP_001159968.1    NP_003042.3   
Entrez Gene ID: 6566   
Pfam: PF07690   
Drugbank: Drugbank Link   
OMIM: 156575  phenotype
245340  phenotype
600682  gene
610021  phenotype
KEGG: hsa:6566    hsa:6566   

Gene Ontology

GO:0016021 C:integral to membrane
GO:0005624 C:membrane fraction
GO:0005886 C:plasma membrane
GO:0015130 F:mevalonate transmembrane transporter activity
GO:0005515 F:protein binding
GO:0015355 F:secondary active monocarboxylate transmembr...
GO:0015293 F:symporter activity
GO:0015728 P:mevalonate transport
GO:0015711 P:organic anion transport
GO:0055085 P:transmembrane transport
GO:0005739 C:mitochondrion
GO:0015355 F:secondary active monocarboxylate transmembrane transporter activity
GO:0007596 P:blood coagulation
GO:0050900 P:leukocyte migration
GO:0006090 P:pyruvate metabolic process

References (25)

[1] “cDNA cloning of the human monocarboxylate transporter 1 and chromosomal localization of the SLC16A1 locus to 1p13.2-p12.”  Garcia C.K.et.al.   7835905
[2] “The full-ORF clone resource of the German cDNA consortium.”  Bechtel S.et.al.   17974005
[3] “The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).”  The MGC Project Teamet.al.   15489334
[4] “Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.”  Olsen J.V.et.al.   17081983
[5] “Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis.”  Wang B.et.al.   19007248
[6] “Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle.”  Daub H.et.al.   18691976
[7] “A quantitative atlas of mitotic phosphorylation.”  Dephoure N.et.al.   18669648
[8] “Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.”  Gauci S.et.al.   19413330
[9] “Large-scale proteomics analysis of the human kinome.”  Oppermann F.S.et.al.   19369195
[10] “Mutations in MCT1 cDNA in patients with symptomatic deficiency in lactate transport.”  Merezhinskaya N.et.al.   10590411
[11] “Physical exercise-induced hypoglycemia caused by failed silencing of monocarboxylate transporter 1 in pancreatic beta cells.”  Otonkoski T.et.al.   17701893
[12] “cDNA cloning of the human monocarboxylate transporter 1 and chromosomal localization of the SLC16A1 locus to 1p13.2-p12.”  Garcia C.K.et.al.   7835905
[13] “The human monocarboxylate transporter, MCT1: genomic organization and promoter analysis.”  Cuff M.A.et.al.   11944921
[14] “The full-ORF clone resource of the German cDNA consortium.”  Bechtel S.et.al.   17974005
[15] “The DNA sequence and biological annotation of human chromosome 1.”  Gregory S.G.et.al.   16710414
[16] “The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).”  The MGC Project Teamet.al.   15489334
[17] “Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.”  Olsen J.V.et.al.   17081983
[18] “Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis.”  Wang B.et.al.   19007248
[19] “Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle.”  Daub H.et.al.   18691976
[20] “A quantitative atlas of mitotic phosphorylation.”  Dephoure N.et.al.   18669648
[21] “Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.”  Gauci S.et.al.   19413330
[22] “Large-scale proteomics analysis of the human kinome.”  Oppermann F.S.et.al.   19369195
[23] “Initial characterization of the human central proteome.”  Burkard T.R.et.al.   21269460
[24] “Mutations in MCT1 cDNA in patients with symptomatic deficiency in lactate transport.”  Merezhinskaya N.et.al.   10590411
[25] “Physical exercise-induced hypoglycemia caused by failed silencing of monocarboxylate transporter 1 in pancreatic beta cells.”  Otonkoski T.et.al.   17701893

External Searches:

  • Search: DB with
  • BLAST ExPASy (Swiss Institute of Bioinformatics (SIB) BLAST)
  • CDD Search (Conserved Domain Database)
  • Search COGs (Clusters of Orthologous Groups of proteins)
  • 2° Structure (Network Protein Sequence Analysis)

Analyze:

Predict TMSs (Predict number of transmembrane segments)
Window Size: Angle:  
Window Size: Angle:  
FASTA formatted sequence
1:	MPPAVGGPVG YTPPDGGWGW AVVIGAFISI GFSYAFPKSI TVFFKEIEGI FHATTSEVSW 
61:	ISSIMLAVMY GGGPISSILV NKYGSRIVMI VGGCLSGCGL IAASFCNTVQ QLYVCIGVIG 
121:	GLGLAFNLNP ALTMIGKYFY KRRPLANGLA MAGSPVFLCT LAPLNQVFFG IFGWRGSFLI 
181:	LGGLLLNCCV AGALMRPIGP KPTKAGKDKS KASLEKAGKS GVKKDLHDAN TDLIGRHPKQ 
241:	EKRSVFQTIN QFLDLTLFTH RGFLLYLSGN VIMFFGLFAP LVFLSSYGKS QHYSSEKSAF 
301:	LLSILAFVDM VARPSMGLVA NTKPIRPRIQ YFFAASVVAN GVCHMLAPLS TTYVGFCVYA 
361:	GFFGFAFGWL SSVLFETLMD LVGPQRFSSA VGLVTIVECC PVLLGPPLLG RLNDMYGDYK 
421:	YTYWACGVVL IISGIYLFIG MGINYRLLAK EQKANEQKKE SKEEETSIDV AGKPNEVTKA 
481:	AESPDQKDTE GGPKEEESPV