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Monocarboxylate transporter 1 (MCT 1) (Solute carrier family 16 member 1)

 MOT1_RAT                Reviewed;         494 AA.
P53987;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 1.
12-SEP-2018, entry version 143.
RecName: Full=Monocarboxylate transporter 1;
Short=MCT 1;
AltName: Full=Solute carrier family 16 member 1;
Name=Slc16a1; Synonyms=Mct1;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND
SUBCELLULAR LOCATION.
STRAIN=Wistar; TISSUE=Small intestine;
PubMed=8526936; DOI=10.1006/bbrc.1995.2786;
Takanaga H., Tamai I., Inaba S., Sai Y., Higashida H., Yamamoto H.,
Tsuji A.;
"cDNA cloning and functional characterization of rat intestinal
monocarboxylate transporter.";
Biochem. Biophys. Res. Commun. 217:370-377(1995).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Wistar; TISSUE=Skeletal muscle;
PubMed=7548134; DOI=10.1016/0005-2736(95)00160-5;
Jackson V.N., Price N.T., Halestrap A.P.;
"cDNA cloning of MCT1, a monocarboxylate transporter from rat skeletal
muscle.";
Biochim. Biophys. Acta 1238:193-196(1995).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lung;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 264-472, FUNCTION, SUBCELLULAR LOCATION,
AND TISSUE SPECIFICITY.
TISSUE=Jejunal epithelium;
PubMed=10564700; DOI=10.1017/S0958067099019181;
Orsenigo M.N., Tosco M., Bazzini C., Laforenza U., Faelli A.;
"A monocarboxylate transporter MCT1 is located at the basolateral pole
of rat jejunum.";
Exp. Physiol. 84:1033-1042(1999).
[5]
INTERACTION WITH EMB, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
PubMed=9169423; DOI=10.1074/jbc.272.23.14624;
Poole R.C., Halestrap A.P.;
"Interaction of the erythrocyte lactate transporter (monocarboxylate
transporter 1) with an integral 70-kDa membrane glycoprotein of the
immunoglobulin superfamily.";
J. Biol. Chem. 272:14624-14628(1997).
[6]
INTERACTION WITH BSG, FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=11719518; DOI=10.1074/jbc.M109658200;
Wilson M.C., Meredith D., Halestrap A.P.;
"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.";
J. Biol. Chem. 277:3666-3672(2002).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-213, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=16396499; DOI=10.1021/pr0503073;
Moser K., White F.M.;
"Phosphoproteomic analysis of rat liver by high capacity IMAC and LC-
MS/MS.";
J. Proteome Res. 5:98-104(2006).
[8]
FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH BSG, TOPOLOGY,
3D-STRUCTURE MODELING, AND MUTAGENESIS OF ARG-86; ARG-196; ASP-302 AND
ARG-306.
PubMed=17127621; DOI=10.1080/09687860600841967;
Manoharan C., Wilson M.C., Sessions R.B., Halestrap A.P.;
"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.";
Mol. Membr. Biol. 23:486-498(2006).
[9]
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, ACTIVITY REGULATION, AND TISSUE
SPECIFICITY.
PubMed=19473976; DOI=10.1074/jbc.M109.014217;
Wilson M.C., Meredith D., Bunnun C., Sessions R.B., Halestrap A.P.;
"Studies on the DIDS-binding site of monocarboxylate transporter 1
suggest a homology model of the open conformation and a plausible
translocation cycle.";
J. Biol. Chem. 284:20011-20021(2009).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-210; SER-213; SER-220;
SER-230; SER-460 AND SER-492, AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- 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.
{ECO:0000269|PubMed:10564700, ECO:0000269|PubMed:11719518,
ECO:0000269|PubMed:17127621, ECO:0000269|PubMed:19473976,
ECO:0000269|PubMed:8526936}.
-!- ACTIVITY REGULATION: Inhibited by stilbene disulfonates, such as
di-isothiocyanostilbene disulfonate(DIDS), a cross-linking reagent
that forms covalent linkages with lysine groups.
{ECO:0000269|PubMed:19473976}.
-!- SUBUNIT: Interacts with BSG. Interacts with EMB. Interaction with
either BSG or EMB is required for expression at the cell membrane.
{ECO:0000269|PubMed:11719518, ECO:0000269|PubMed:17127621,
ECO:0000269|PubMed:19473976, ECO:0000269|PubMed:9169423}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10564700,
ECO:0000269|PubMed:11719518, ECO:0000269|PubMed:17127621,
ECO:0000269|PubMed:19473976, ECO:0000269|PubMed:8526936,
ECO:0000269|PubMed:9169423}; Multi-pass membrane protein
{ECO:0000269|PubMed:10564700, ECO:0000269|PubMed:11719518,
ECO:0000269|PubMed:17127621, ECO:0000269|PubMed:19473976,
ECO:0000269|PubMed:8526936, ECO:0000269|PubMed:9169423}.
-!- TISSUE SPECIFICITY: Detected in erythrocytes (at protein level).
Detected in brain, heart, kidney, lung, muscle, jejunum
enterocytes and brain capillaries. {ECO:0000269|PubMed:10564700,
ECO:0000269|PubMed:19473976, ECO:0000269|PubMed:8526936,
ECO:0000269|PubMed:9169423}.
-!- SIMILARITY: Belongs to the major facilitator superfamily.
Monocarboxylate porter (TC 2.A.1.13) family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; D63834; BAA09894.1; -; mRNA.
EMBL; X86216; CAA60116.1; -; mRNA.
EMBL; BC078877; AAH78877.1; -; mRNA.
EMBL; AJ236865; CAB37948.1; -; mRNA.
PIR; JC4399; JC4399.
RefSeq; NP_036848.1; NM_012716.2.
RefSeq; XP_017446125.1; XM_017590636.1.
UniGene; Rn.6085; -.
ProteinModelPortal; P53987; -.
BioGrid; 247107; 1.
STRING; 10116.ENSRNOP00000027234; -.
BindingDB; P53987; -.
ChEMBL; CHEMBL2073709; -.
iPTMnet; P53987; -.
PhosphoSitePlus; P53987; -.
PaxDb; P53987; -.
PRIDE; P53987; -.
Ensembl; ENSRNOT00000027234; ENSRNOP00000027234; ENSRNOG00000019996.
GeneID; 25027; -.
KEGG; rno:25027; -.
UCSC; RGD:3690; rat.
CTD; 6566; -.
RGD; 3690; Slc16a1.
eggNOG; ENOG410IMVV; Eukaryota.
eggNOG; ENOG41116NW; LUCA.
GeneTree; ENSGT00760000118926; -.
HOGENOM; HOG000280688; -.
HOVERGEN; HBG006384; -.
InParanoid; P53987; -.
KO; K08179; -.
OMA; RPFVGMF; -.
OrthoDB; EOG091G05SW; -.
PhylomeDB; P53987; -.
TreeFam; TF313792; -.
Reactome; R-RNO-210991; Basigin interactions.
Reactome; R-RNO-433692; Proton-coupled monocarboxylate transport.
Reactome; R-RNO-70268; Pyruvate metabolism.
SABIO-RK; P53987; -.
PRO; PR:P53987; -.
Proteomes; UP000002494; Chromosome 2.
Bgee; ENSRNOG00000019996; Expressed in 10 organ(s), highest expression level in heart.
Genevisible; P53987; RN.
GO; GO:0030054; C:cell junction; IEA:Ensembl.
GO; GO:0005813; C:centrosome; IEA:Ensembl.
GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IEA:Ensembl.
GO; GO:0005886; C:plasma membrane; IDA:RGD.
GO; GO:0015129; F:lactate transmembrane transporter activity; IEA:InterPro.
GO; GO:0008028; F:monocarboxylic acid transmembrane transporter activity; IBA:GO_Central.
GO; GO:0097159; F:organic cyclic compound binding; IMP:RGD.
GO; GO:0042803; F:protein homodimerization activity; IDA:RGD.
GO; GO:0015293; F:symporter activity; IEA:UniProtKB-KW.
GO; GO:0051780; P:behavioral response to nutrient; IEA:Ensembl.
GO; GO:0071407; P:cellular response to organic cyclic compound; IMP:RGD.
GO; GO:0007098; P:centrosome cycle; IEA:Ensembl.
GO; GO:0042593; P:glucose homeostasis; IEA:Ensembl.
GO; GO:0035873; P:lactate transmembrane transport; IDA:RGD.
GO; GO:0006629; P:lipid metabolic process; IEA:Ensembl.
GO; GO:0035879; P:plasma membrane lactate transport; IDA:RGD.
GO; GO:0050796; P:regulation of insulin secretion; IEA:Ensembl.
GO; GO:0032094; P:response to food; IEA:Ensembl.
CDD; cd06174; MFS; 1.
InterPro; IPR004743; MCT.
InterPro; IPR030757; MCT1.
InterPro; IPR011701; MFS.
InterPro; IPR020846; MFS_dom.
InterPro; IPR036259; MFS_trans_sf.
PANTHER; PTHR11360:SF24; PTHR11360:SF24; 1.
Pfam; PF07690; MFS_1; 1.
SUPFAM; SSF103473; SSF103473; 2.
TIGRFAMs; TIGR00892; 2A0113; 1.
PROSITE; PS50850; MFS; 1.
1: Evidence at protein level;
Cell membrane; Complete proteome; Membrane; Phosphoprotein;
Reference proteome; Symport; Transmembrane; Transmembrane helix;
Transport.
CHAIN 1 494 Monocarboxylate transporter 1.
/FTId=PRO_0000211384.
TOPO_DOM 1 15 Cytoplasmic. {ECO:0000305}.
TRANSMEM 16 36 Helical. {ECO:0000255}.
TOPO_DOM 37 59 Extracellular. {ECO:0000305}.
TRANSMEM 60 80 Helical. {ECO:0000255}.
TOPO_DOM 81 86 Cytoplasmic. {ECO:0000255}.
TRANSMEM 87 107 Helical. {ECO:0000255}.
TOPO_DOM 108 111 Extracellular. {ECO:0000255}.
TRANSMEM 112 132 Helical. {ECO:0000255}.
TOPO_DOM 133 143 Cytoplasmic. {ECO:0000255}.
TRANSMEM 144 164 Helical. {ECO:0000255}.
TOPO_DOM 165 166 Extracellular. {ECO:0000255}.
TRANSMEM 167 187 Helical. {ECO:0000255}.
TOPO_DOM 188 255 Cytoplasmic. {ECO:0000255}.
TRANSMEM 256 276 Helical. {ECO:0000255}.
TOPO_DOM 277 291 Extracellular. {ECO:0000305}.
TRANSMEM 292 312 Helical. {ECO:0000255}.
TOPO_DOM 313 321 Cytoplasmic. {ECO:0000255}.
TRANSMEM 322 342 Helical. {ECO:0000255}.
TOPO_DOM 343 346 Extracellular. {ECO:0000255}.
TRANSMEM 347 367 Helical. {ECO:0000255}.
TOPO_DOM 368 382 Cytoplasmic. {ECO:0000255}.
TRANSMEM 383 403 Helical. {ECO:0000255}.
TOPO_DOM 404 415 Extracellular. {ECO:0000305}.
TRANSMEM 416 436 Helical. {ECO:0000255}.
TOPO_DOM 437 494 Cytoplasmic. {ECO:0000305}.
MOD_RES 210 210 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 213 213 Phosphoserine.
{ECO:0000244|PubMed:16396499,
ECO:0000244|PubMed:22673903}.
MOD_RES 220 220 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 224 224 Phosphothreonine.
{ECO:0000250|UniProtKB:P53986}.
MOD_RES 230 230 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 459 459 Phosphothreonine.
{ECO:0000250|UniProtKB:P53985}.
MOD_RES 460 460 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 461 461 Phosphothreonine.
{ECO:0000250|UniProtKB:P53986}.
MOD_RES 476 476 Phosphoserine.
{ECO:0000250|UniProtKB:P53985}.
MOD_RES 483 483 Phosphoserine.
{ECO:0000250|UniProtKB:P53986}.
MOD_RES 484 484 Phosphoserine.
{ECO:0000250|UniProtKB:P53986}.
MOD_RES 492 492 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MUTAGEN 38 38 K->Q,R: No effect on expression at the
cell membrane, but abolishes lactate
transport across the cell membrane.
{ECO:0000269|PubMed:19473976}.
MUTAGEN 45 45 K->Q,R: No effect on expression at the
cell membrane. No effect on lactate
transport across the cell membrane.
{ECO:0000269|PubMed:19473976}.
MUTAGEN 86 86 R->E,Q: No effect on expression at the
cell membrane. No effect on lactate
transport across the cell membrane.
{ECO:0000269|PubMed:17127621}.
MUTAGEN 196 196 R->E,Q: No effect on expression at the
cell membrane. No effect on lactate
transport across the cell membrane.
{ECO:0000269|PubMed:17127621}.
MUTAGEN 282 282 K->Q,R: No effect on expression at the
cell membrane. No effect on lactate
transport across the cell membrane.
{ECO:0000269|PubMed:19473976}.
MUTAGEN 284 284 K->Q,R: No effect on expression at the
cell membrane. No effect on lactate
transport across the cell membrane.
{ECO:0000269|PubMed:19473976}.
MUTAGEN 290 290 K->Q,R: No effect on expression at the
cell membrane. No effect on lactate
transport across the cell membrane.
{ECO:0000269|PubMed:19473976}.
MUTAGEN 302 302 D->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.
{ECO:0000269|PubMed:17127621}.
MUTAGEN 306 306 R->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.
{ECO:0000269|PubMed:17127621}.
MUTAGEN 306 306 R->K: No effect on expression at the cell
membrane, but abolishes lactate transport
across the cell membrane.
{ECO:0000269|PubMed:17127621}.
MUTAGEN 413 413 K->Q,R: No effect on expression at the
cell membrane. No effect on lactate
transport across the cell membrane.
{ECO:0000269|PubMed:19473976}.
SEQUENCE 494 AA; 53238 MW; CF82F8794CDBF057 CRC64;
MPPAIGGPVG YTPPDGGWGW AVVVGAFISI GFSYAFPKSI TVFFKEIEII FSATTSEVSW
ISSIMLAVMY AGGPISSILV NKYGSRPVMI AGGCLSGCGL IAASFCNTVQ ELYFCIGVIG
GLGLAFNLNP ALTMIGKYFY KKRPLANGLA MAGSPVFLST LAPLNQAFFG IFGWRGSFLI
LGGLLLNCCV AGSLMRPIGP QQGKVEKLKS KESLQEAGKS DANTDLIGGS PKGEKLSVFQ
TVNKFLDLSL FTHRGFLLYL SGNVVMFFGL FTPLVFLSNY GKSKHFSSEK SAFLLSILAF
VDMVARPSMG LAANTRWIRP RVQYFFAASV VANGVCHLLA PLSTTYVGFC IYAGVFGFAF
GWLSSVLFET LMDLVGPQRF SSAVGLVTIV ECCPVLLGPP LLGRLNDMYG DYKYTYWACG
VILIIAGLYL FIGMGINYRL VAKEQKAEEK KRDGKEDETS TDVDEKPKKT MKETQSPAPL
QNSSGDPAEE ESPV


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