MOT1_HUMAN
ID MOT1_HUMAN Reviewed; 500 AA.
AC P53985; Q49A45; Q5T8R6; Q9NSJ9;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 3.
DT 03-AUG-2022, entry version 209.
DE RecName: Full=Monocarboxylate transporter 1;
DE Short=MCT 1;
DE AltName: Full=Solute carrier family 16 member 1;
GN Name=SLC16A1; Synonyms=MCT1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT GLU-490.
RC TISSUE=Heart;
RX PubMed=7835905; DOI=10.1006/geno.1994.1532;
RA Garcia C.K., Li X., Luna J., Francke U.;
RT "cDNA cloning of the human monocarboxylate transporter 1 and chromosomal
RT localization of the SLC16A1 locus to 1p13.2-p12.";
RL Genomics 23:500-503(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Colon;
RX PubMed=11944921; DOI=10.1006/bbrc.2002.6763;
RA Cuff M.A., Shirazi-Beechey S.P.;
RT "The human monocarboxylate transporter, MCT1: genomic organization and
RT promoter analysis.";
RL Biochem. Biophys. Res. Commun. 292:1048-1056(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT GLU-490.
RC TISSUE=Melanoma;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, and Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=15505343; DOI=10.1369/jhc.4a6306.2004;
RA Merezhinskaya N., Ogunwuyi S.A., Mullick F.G., Fishbein W.N.;
RT "Presence and localization of three lactic acid transporters (MCT1, -2, and
RT -4) in separated human granulocytes, lymphocytes, and monocytes.";
RL J. Histochem. Cytochem. 52:1483-1493(2004).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-213 AND SER-498, VARIANT
RP [LARGE SCALE ANALYSIS] GLU-490, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [9]
RP INTERACTION WITH BSG, AND SUBCELLULAR LOCATION.
RX PubMed=17127621; DOI=10.1080/09687860600841967;
RA Manoharan C., Wilson M.C., Sessions R.B., Halestrap A.P.;
RT "The role of charged residues in the transmembrane helices of
RT monocarboxylate transporter 1 and its ancillary protein basigin in
RT determining plasma membrane expression and catalytic activity.";
RL Mol. Membr. Biol. 23:486-498(2006).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-461 AND SER-498, VARIANT
RP [LARGE SCALE ANALYSIS] GLU-490, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-461; SER-467; SER-483 AND
RP SER-498, VARIANT [LARGE SCALE ANALYSIS] GLU-490, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-461, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-213; SER-483 AND SER-498,
RP VARIANT [LARGE SCALE ANALYSIS] GLU-490, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-213; THR-466; SER-483 AND
RP SER-498, VARIANT [LARGE SCALE ANALYSIS] GLU-490, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [16]
RP REVIEW.
RX PubMed=22162139; DOI=10.1002/iub.572;
RA Halestrap A.P., Wilson M.C.;
RT "The monocarboxylate transporter family--role and regulation.";
RL IUBMB Life 64:109-119(2012).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-461; THR-466; SER-467;
RP SER-483 AND SER-498, VARIANT [LARGE SCALE ANALYSIS] GLU-490, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-467 AND SER-498, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [19]
RP INVOLVEMENT IN MCT1D, AND VARIANT MCT1D GLN-313.
RX PubMed=25390740; DOI=10.1056/nejmoa1407778;
RA van Hasselt P.M., Ferdinandusse S., Monroe G.R., Ruiter J.P.,
RA Turkenburg M., Geerlings M.J., Duran K., Harakalova M., van der Zwaag B.,
RA Monavari A.A., Okur I., Sharrard M.J., Cleary M., O'Connell N., Walker V.,
RA Rubio-Gozalbo M.E., de Vries M.C., Visser G., Houwen R.H.,
RA van der Smagt J.J., Verhoeven-Duif N.M., Wanders R.J., van Haaften G.;
RT "Monocarboxylate transporter 1 deficiency and ketone utilization.";
RL N. Engl. J. Med. 371:1900-1907(2014).
RN [20]
RP SUBCELLULAR LOCATION.
RX PubMed=24390345; DOI=10.1038/nature12828;
RG The SIGMA Type 2 Diabetes Consortium;
RT "Sequence variants in SLC16A11 are a common risk factor for type 2 diabetes
RT in Mexico.";
RL Nature 506:97-101(2014).
RN [21]
RP INTERACTION WITH BSG, AND SUBCELLULAR LOCATION.
RX PubMed=25957687; DOI=10.1016/j.cell.2015.03.023;
RA Ait-Ali N., Fridlich R., Millet-Puel G., Clerin E., Delalande F.,
RA Jaillard C., Blond F., Perrocheau L., Reichman S., Byrne L.C.,
RA Olivier-Bandini A., Bellalou J., Moyse E., Bouillaud F., Nicol X.,
RA Dalkara D., van Dorsselaer A., Sahel J.A., Leveillard T.;
RT "Rod-derived cone viability factor promotes cone survival by stimulating
RT aerobic glycolysis.";
RL Cell 161:817-832(2015).
RN [22]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [23]
RP VARIANTS SDLT GLU-204 AND ARG-472, AND VARIANT GLU-490.
RX PubMed=10590411;
RX DOI=10.1002/(sici)1097-4598(200001)23:1<90::aid-mus12>3.0.co;2-m;
RA Merezhinskaya N., Fishbein W.N., Davis J.I., Foellmer J.W.;
RT "Mutations in MCT1 cDNA in patients with symptomatic deficiency in lactate
RT transport.";
RL Muscle Nerve 23:90-97(2000).
RN [24]
RP INVOLVEMENT IN HHF7, AND FUNCTION.
RX PubMed=17701893; DOI=10.1086/520960;
RA Otonkoski T., Jiao H., Kaminen-Ahola N., Tapia-Paez I., Ullah M.S.,
RA Parton L.E., Schuit F., Quintens R., Sipilae I., Mayatepek E., Meissner T.,
RA Halestrap A.P., Rutter G.A., Kere J.;
RT "Physical exercise-induced hypoglycemia caused by failed silencing of
RT monocarboxylate transporter 1 in pancreatic beta cells.";
RL Am. J. Hum. Genet. 81:467-474(2007).
RN [25]
RP VARIANT [LARGE SCALE ANALYSIS] GLU-490, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Proton-coupled monocarboxylate transporter. Catalyzes the
CC rapid transport across the plasma membrane of many monocarboxylates
CC such as lactate, pyruvate, branched-chain oxo acids derived from
CC leucine, valine and isoleucine, and the ketone bodies acetoacetate,
CC beta-hydroxybutyrate and acetate. Depending on the tissue and on
CC cicumstances, mediates the import or export of lactic acid and ketone
CC bodies. Required for normal nutrient assimilation, increase of white
CC adipose tissue and body weight gain when on a high-fat diet. Plays a
CC role in cellular responses to a high-fat diet by modulating the
CC cellular levels of lactate and pyruvate, small molecules that
CC contribute to the regulation of central metabolic pathways and insulin
CC secretion, with concomitant effects on plasma insulin levels and blood
CC glucose homeostasis. {ECO:0000269|PubMed:17701893}.
CC -!- SUBUNIT: Interacts with EMB; interaction mediates SLC16A1 targeting to
CC the plasma membrane (By similarity). Interacts with isoform 2 of BSG;
CC interaction mediates SLC16A1 targeting to the plasma membrane
CC (PubMed:17127621, PubMed:25957687). {ECO:0000250|UniProtKB:P53987,
CC ECO:0000269|PubMed:17127621, ECO:0000269|PubMed:25957687}.
CC -!- INTERACTION:
CC P53985-2; Q66PJ3-4: ARL6IP4; NbExp=3; IntAct=EBI-25891616, EBI-5280499;
CC P53985-2; Q92782-2: DPF1; NbExp=3; IntAct=EBI-25891616, EBI-23669343;
CC P53985-2; Q9UH65: SWAP70; NbExp=3; IntAct=EBI-25891616, EBI-310749;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15505343,
CC ECO:0000269|PubMed:17127621, ECO:0000269|PubMed:24390345,
CC ECO:0000269|PubMed:25957687}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P53985-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P53985-2; Sequence=VSP_056191;
CC -!- TISSUE SPECIFICITY: Detected in heart and in blood lymphocytes and
CC monocytes (at protein level). Widely expressed.
CC {ECO:0000269|PubMed:15505343}.
CC -!- DISEASE: Symptomatic deficiency in lactate transport (SDLT)
CC [MIM:245340]: Deficiency of lactate transporter may result in an acidic
CC intracellular environment created by muscle activity with consequent
CC degeneration of muscle and release of myoglobin and creatine kinase.
CC This defect might compromise extreme performance in otherwise healthy
CC individuals. {ECO:0000269|PubMed:10590411}. Note=The disease is caused
CC by variants affecting the gene represented in this entry.
CC -!- DISEASE: Familial hyperinsulinemic hypoglycemia 7 (HHF7) [MIM:610021]:
CC Dominantly inherited hypoglycemic disorder characterized by
CC inappropriate insulin secretion during anaerobic exercise or on
CC pyruvate load. {ECO:0000269|PubMed:17701893}. Note=The disease is
CC caused by variants affecting the gene represented in this entry.
CC -!- DISEASE: Monocarboxylate transporter 1 deficiency (MCT1D) [MIM:616095]:
CC A metabolic disorder characterized by recurrent ketoacidosis, a
CC pathologic state due to ketone formation exceeding ketone utilization.
CC The clinical consequences of ketoacidosis are vomiting, osmotic
CC diuresis, dehydration, and Kussmaul breathing. The condition may
CC progress to decreased consciousness and, ultimately, death.
CC {ECO:0000269|PubMed:25390740}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- MISCELLANEOUS: Overexpression in pancreatic beta-cells triggers insulin
CC secretion in response to pyruvate, causing hyperinsulemia and
CC hypoglycemia during strenuous exercise.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily.
CC Monocarboxylate porter (TC 2.A.1.13) family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/SLC16A1ID44046ch1p13.html";
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DR EMBL; L31801; AAC41707.1; -; mRNA.
DR EMBL; AJ438945; CAD27707.1; -; Genomic_DNA.
DR EMBL; AL162079; CAB82412.1; -; mRNA.
DR EMBL; AL158844; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471122; EAW56552.1; -; Genomic_DNA.
DR EMBL; BC026317; AAH26317.1; -; mRNA.
DR EMBL; BC045664; AAH45664.1; -; mRNA.
DR CCDS; CCDS858.1; -. [P53985-1]
DR PIR; A55568; A55568.
DR RefSeq; NP_001159968.1; NM_001166496.1. [P53985-1]
DR RefSeq; NP_003042.3; NM_003051.3. [P53985-1]
DR RefSeq; XP_011540328.1; XM_011542026.2.
DR RefSeq; XP_011540329.1; XM_011542027.2.
DR PDB; 6LYY; EM; 3.60 A; A=1-500.
DR PDB; 6LZ0; EM; 3.60 A; A=1-500.
DR PDB; 7CKO; EM; 2.95 A; A=1-500.
DR PDB; 7CKR; EM; 3.00 A; A=1-500.
DR PDB; 7DA5; EM; 3.30 A; A=1-500.
DR PDBsum; 6LYY; -.
DR PDBsum; 6LZ0; -.
DR PDBsum; 7CKO; -.
DR PDBsum; 7CKR; -.
DR PDBsum; 7DA5; -.
DR AlphaFoldDB; P53985; -.
DR SMR; P53985; -.
DR BioGRID; 112454; 138.
DR IntAct; P53985; 59.
DR MINT; P53985; -.
DR STRING; 9606.ENSP00000441065; -.
DR BindingDB; P53985; -.
DR ChEMBL; CHEMBL4360; -.
DR DrugBank; DB03166; Acetic acid.
DR DrugBank; DB01762; Acetoacetic acid.
DR DrugBank; DB03773; alpha-D-quinovopyranose.
DR DrugBank; DB04074; alpha-Ketoisovalerate.
DR DrugBank; DB00345; Aminohippuric acid.
DR DrugBank; DB00415; Ampicillin.
DR DrugBank; DB08892; Arbaclofen Placarbil.
DR DrugBank; DB03793; Benzoic acid.
DR DrugBank; DB03066; D-Lactic acid.
DR DrugBank; DB00529; Foscarnet.
DR DrugBank; DB01440; gamma-Hydroxybutyric acid.
DR DrugBank; DB00142; Glutamic acid.
DR DrugBank; DB04398; Lactic acid.
DR DrugBank; DB09338; Mersalyl.
DR DrugBank; DB00563; Methotrexate.
DR DrugBank; DB00731; Nateglinide.
DR DrugBank; DB00627; Niacin.
DR DrugBank; DB04552; Niflumic acid.
DR DrugBank; DB00175; Pravastatin.
DR DrugBank; DB01032; Probenecid.
DR DrugBank; DB00119; Pyruvic acid.
DR DrugBank; DB04216; Quercetin.
DR DrugBank; DB00936; Salicylic acid.
DR DrugBank; DB04348; Taurocholic acid.
DR DrugBank; DB00313; Valproic acid.
DR GuidetoPHARMACOLOGY; 988; -.
DR TCDB; 2.A.1.13.1; the major facilitator superfamily (mfs).
DR GlyGen; P53985; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P53985; -.
DR PhosphoSitePlus; P53985; -.
DR SwissPalm; P53985; -.
DR BioMuta; SLC16A1; -.
DR DMDM; 313104214; -.
DR EPD; P53985; -.
DR jPOST; P53985; -.
DR MassIVE; P53985; -.
DR MaxQB; P53985; -.
DR PaxDb; P53985; -.
DR PeptideAtlas; P53985; -.
DR PRIDE; P53985; -.
DR ProteomicsDB; 56635; -. [P53985-1]
DR ProteomicsDB; 62023; -.
DR Antibodypedia; 4301; 339 antibodies from 37 providers.
DR DNASU; 6566; -.
DR Ensembl; ENST00000369626.8; ENSP00000358640.4; ENSG00000155380.13. [P53985-1]
DR Ensembl; ENST00000429288.2; ENSP00000397106.2; ENSG00000155380.13. [P53985-1]
DR Ensembl; ENST00000443580.6; ENSP00000399104.2; ENSG00000155380.13. [P53985-1]
DR Ensembl; ENST00000458229.6; ENSP00000416167.2; ENSG00000155380.13. [P53985-1]
DR Ensembl; ENST00000538576.5; ENSP00000441065.1; ENSG00000155380.13. [P53985-1]
DR Ensembl; ENST00000628110.2; ENSP00000485688.1; ENSG00000281917.4. [P53985-1]
DR Ensembl; ENST00000630362.4; ENSP00000486000.1; ENSG00000281917.4. [P53985-1]
DR Ensembl; ENST00000679803.1; ENSP00000505879.1; ENSG00000155380.13. [P53985-1]
DR GeneID; 6566; -.
DR KEGG; hsa:6566; -.
DR MANE-Select; ENST00000369626.8; ENSP00000358640.4; NM_003051.4; NP_003042.3.
DR UCSC; uc001ecx.4; human. [P53985-1]
DR CTD; 6566; -.
DR DisGeNET; 6566; -.
DR GeneCards; SLC16A1; -.
DR HGNC; HGNC:10922; SLC16A1.
DR HPA; ENSG00000155380; Low tissue specificity.
DR MalaCards; SLC16A1; -.
DR MIM; 245340; phenotype.
DR MIM; 600682; gene.
DR MIM; 610021; phenotype.
DR MIM; 616095; phenotype.
DR neXtProt; NX_P53985; -.
DR OpenTargets; ENSG00000155380; -.
DR Orphanet; 165991; Exercise-induced hyperinsulinism.
DR Orphanet; 438075; Ketoacidosis due to monocarboxylate transporter-1 deficiency.
DR Orphanet; 171690; Metabolic myopathy due to lactate transporter defect.
DR PharmGKB; PA35813; -.
DR VEuPathDB; HostDB:ENSG00000155380; -.
DR eggNOG; KOG2504; Eukaryota.
DR GeneTree; ENSGT00940000154955; -.
DR InParanoid; P53985; -.
DR OMA; TYAGFCI; -.
DR PhylomeDB; P53985; -.
DR TreeFam; TF313792; -.
DR BioCyc; MetaCyc:ENSG00000155380-MON; -.
DR PathwayCommons; P53985; -.
DR Reactome; R-HSA-210991; Basigin interactions.
DR Reactome; R-HSA-433692; Proton-coupled monocarboxylate transport.
DR Reactome; R-HSA-5619070; Defective SLC16A1 causes symptomatic deficiency in lactate transport (SDLT).
DR Reactome; R-HSA-70268; Pyruvate metabolism.
DR Reactome; R-HSA-9749641; Aspirin ADME.
DR SABIO-RK; P53985; -.
DR SignaLink; P53985; -.
DR BioGRID-ORCS; 6566; 71 hits in 1089 CRISPR screens.
DR ChiTaRS; SLC16A1; human.
DR GenomeRNAi; 6566; -.
DR Pharos; P53985; Tchem.
DR PRO; PR:P53985; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; P53985; protein.
DR Bgee; ENSG00000155380; Expressed in mucosa of transverse colon and 103 other tissues.
DR ExpressionAtlas; P53985; baseline and differential.
DR Genevisible; P53985; HS.
DR GO; GO:0016324; C:apical plasma membrane; IDA:ARUK-UCL.
DR GO; GO:0009925; C:basal plasma membrane; IDA:ARUK-UCL.
DR GO; GO:0016323; C:basolateral plasma membrane; ISS:ARUK-UCL.
DR GO; GO:0030054; C:cell junction; IDA:HPA.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0016328; C:lateral plasma membrane; IDA:ARUK-UCL.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0045202; C:synapse; IEA:Ensembl.
DR GO; GO:0046943; F:carboxylic acid transmembrane transporter activity; ISS:ARUK-UCL.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0015129; F:lactate transmembrane transporter activity; ISS:ARUK-UCL.
DR GO; GO:0015130; F:mevalonate transmembrane transporter activity; TAS:ProtInc.
DR GO; GO:0008028; F:monocarboxylic acid transmembrane transporter activity; IDA:ARUK-UCL.
DR GO; GO:0097159; F:organic cyclic compound binding; IEA:Ensembl.
DR GO; GO:0015293; F:symporter activity; IEA:UniProtKB-KW.
DR GO; GO:0051780; P:behavioral response to nutrient; IEA:Ensembl.
DR GO; GO:1905039; P:carboxylic acid transmembrane transport; ISS:ARUK-UCL.
DR GO; GO:0071407; P:cellular response to organic cyclic compound; IEA:Ensembl.
DR GO; GO:0007098; P:centrosome cycle; IMP:UniProtKB.
DR GO; GO:0042593; P:glucose homeostasis; IEA:Ensembl.
DR GO; GO:0006629; P:lipid metabolic process; IEA:Ensembl.
DR GO; GO:0015728; P:mevalonate transport; TAS:ProtInc.
DR GO; GO:0015718; P:monocarboxylic acid transport; IDA:ARUK-UCL.
DR GO; GO:0035879; P:plasma membrane lactate transport; ISS:UniProtKB.
DR GO; GO:0050796; P:regulation of insulin secretion; IEA:Ensembl.
DR GO; GO:0032094; P:response to food; IEA:Ensembl.
DR GO; GO:0150104; P:transport across blood-brain barrier; NAS:ARUK-UCL.
DR Gene3D; 1.20.1250.20; -; 1.
DR InterPro; IPR004743; MCT.
DR InterPro; IPR030757; MCT1.
DR InterPro; IPR011701; MFS.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR036259; MFS_trans_sf.
DR PANTHER; PTHR11360:SF24; PTHR11360:SF24; 1.
DR Pfam; PF07690; MFS_1; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
DR TIGRFAMs; TIGR00892; 2A0113; 1.
DR PROSITE; PS50850; MFS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Disease variant;
KW Membrane; Phosphoprotein; Reference proteome; Symport; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..500
FT /note="Monocarboxylate transporter 1"
FT /id="PRO_0000211381"
FT TOPO_DOM 1..15
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 16..36
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 37..59
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 60..80
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 81..86
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 87..107
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 108..111
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 112..132
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 133..143
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 144..164
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 165..166
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 167..187
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 188..262
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 263..283
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 284..298
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 299..319
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 320..328
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 329..349
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 350..353
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 354..374
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 375..389
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 390..410
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 411..422
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 423..443
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 444..500
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 454..500
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 454..470
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 480..500
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 210
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P53986"
FT MOD_RES 213
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692"
FT MOD_RES 231
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P53986"
FT MOD_RES 461
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 466
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 467
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 483
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 498
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT VAR_SEQ 411..500
FT /note="RLNDMYGDYKYTYWACGVVLIISGIYLFIGMGINYRLLAKEQKANEQKKESK
FT EEETSIDVAGKPNEVTKAAESPDQKDTDGGPKEEESPV -> IVYLPTNVGLLQNKHVR
FT WEC (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_056191"
FT VARIANT 85
FT /note="S -> G (in dbSNP:rs11551867)"
FT /id="VAR_054804"
FT VARIANT 204
FT /note="K -> E (in SDLT; dbSNP:rs80358222)"
FT /evidence="ECO:0000269|PubMed:10590411"
FT /id="VAR_010434"
FT VARIANT 313
FT /note="R -> Q (in MCT1D; dbSNP:rs606231302)"
FT /evidence="ECO:0000269|PubMed:25390740"
FT /id="VAR_072428"
FT VARIANT 472
FT /note="G -> R (in SDLT; dbSNP:rs72552271)"
FT /evidence="ECO:0000269|PubMed:10590411"
FT /id="VAR_010435"
FT VARIANT 490
FT /note="D -> E (in dbSNP:rs1049434)"
FT /evidence="ECO:0000269|PubMed:10590411,
FT ECO:0000269|PubMed:17974005, ECO:0000269|PubMed:7835905,
FT ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21269460, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT /id="VAR_010436"
FT CONFLICT 480
FT /note="A -> T (in Ref. 1; AAC41707)"
FT /evidence="ECO:0000305"
FT HELIX 18..39
FT /evidence="ECO:0007829|PDB:7CKO"
FT HELIX 41..43
FT /evidence="ECO:0007829|PDB:7CKO"
FT HELIX 44..51
FT /evidence="ECO:0007829|PDB:7CKO"
FT HELIX 55..83
FT /evidence="ECO:0007829|PDB:7CKO"
FT HELIX 86..103
FT /evidence="ECO:0007829|PDB:7CKO"
FT HELIX 109..138
FT /evidence="ECO:0007829|PDB:7CKO"
FT STRAND 140..142
FT /evidence="ECO:0007829|PDB:7CKO"
FT HELIX 143..171
FT /evidence="ECO:0007829|PDB:7CKO"
FT HELIX 174..191
FT /evidence="ECO:0007829|PDB:7CKO"
FT HELIX 255..258
FT /evidence="ECO:0007829|PDB:7CKR"
FT HELIX 263..275
FT /evidence="ECO:0007829|PDB:7CKO"
FT HELIX 279..290
FT /evidence="ECO:0007829|PDB:7CKO"
FT HELIX 297..320
FT /evidence="ECO:0007829|PDB:7CKO"
FT TURN 323..325
FT /evidence="ECO:0007829|PDB:7CKO"
FT HELIX 326..328
FT /evidence="ECO:0007829|PDB:7CKO"
FT HELIX 331..346
FT /evidence="ECO:0007829|PDB:7CKO"
FT HELIX 347..349
FT /evidence="ECO:0007829|PDB:7CKR"
FT STRAND 351..353
FT /evidence="ECO:0007829|PDB:7DA5"
FT HELIX 354..382
FT /evidence="ECO:0007829|PDB:7CKO"
FT STRAND 384..386
FT /evidence="ECO:0007829|PDB:7CKR"
FT HELIX 387..398
FT /evidence="ECO:0007829|PDB:7CKO"
FT HELIX 401..414
FT /evidence="ECO:0007829|PDB:7CKO"
FT TURN 415..417
FT /evidence="ECO:0007829|PDB:7DA5"
FT TURN 420..422
FT /evidence="ECO:0007829|PDB:7CKO"
FT HELIX 423..448
FT /evidence="ECO:0007829|PDB:7CKO"
SQ SEQUENCE 500 AA; 53944 MW; 3F5B048CB962ECC8 CRC64;
MPPAVGGPVG YTPPDGGWGW AVVIGAFISI GFSYAFPKSI TVFFKEIEGI FHATTSEVSW
ISSIMLAVMY GGGPISSILV NKYGSRIVMI VGGCLSGCGL IAASFCNTVQ QLYVCIGVIG
GLGLAFNLNP ALTMIGKYFY KRRPLANGLA MAGSPVFLCT LAPLNQVFFG IFGWRGSFLI
LGGLLLNCCV AGALMRPIGP KPTKAGKDKS KASLEKAGKS GVKKDLHDAN TDLIGRHPKQ
EKRSVFQTIN QFLDLTLFTH RGFLLYLSGN VIMFFGLFAP LVFLSSYGKS QHYSSEKSAF
LLSILAFVDM VARPSMGLVA NTKPIRPRIQ YFFAASVVAN GVCHMLAPLS TTYVGFCVYA
GFFGFAFGWL SSVLFETLMD LVGPQRFSSA VGLVTIVECC PVLLGPPLLG RLNDMYGDYK
YTYWACGVVL IISGIYLFIG MGINYRLLAK EQKANEQKKE SKEEETSIDV AGKPNEVTKA
AESPDQKDTD GGPKEEESPV
