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Monocarboxylate transporter 2 (MCT 2) (Solute carrier family 16 member 7)

 MOT2_RAT                Reviewed;         489 AA.
Q63344; Q63649;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
05-JUL-2017, entry version 115.
RecName: Full=Monocarboxylate transporter 2;
Short=MCT 2;
AltName: Full=Solute carrier family 16 member 7;
Name=Slc16a7; Synonyms=Mct2;
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], AND SUBCELLULAR LOCATION.
STRAIN=Sprague-Dawley; TISSUE=Testis;
PubMed=9182702; DOI=10.1042/bj3240447;
Jackson V.N., Price N.T., Carpenter L., Halestrap A.P.;
"Cloning of the monocarboxylate transporter isoform MCT2 from rat
testis provides evidence that expression in tissues is species-
specific and may involve post-transcriptional regulation.";
Biochem. J. 324:447-453(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND TISSUE
SPECIFICITY.
STRAIN=Wistar; TISSUE=Brain;
PubMed=9482213;
DOI=10.1002/(SICI)1098-1136(199803)22:3<272::AID-GLIA6>3.3.CO;2-T;
Gerhart D.Z., Enerson B.E., Zhdankina O.Y., Leino R.L., Drewes L.R.;
"Expression of the monocarboxylate transporter MCT2 by rat brain
glia.";
Glia 22:272-281(1998).
[3]
INTERACTION WITH EMB, AND SUBCELLULAR LOCATION.
PubMed=15917240; DOI=10.1074/jbc.M411950200;
Wilson M.C., Meredith D., Fox J.E., Manoharan C., Davies A.J.,
Halestrap A.P.;
"Basigin (CD147) is the target for organomercurial inhibition of
monocarboxylate transporter isoforms 1 and 4: the ancillary protein
for the insensitive MCT2 is EMBIGIN (gp70).";
J. Biol. Chem. 280:27213-27221(2005).
[4]
INTERACTION WITH EMB, SUBCELLULAR LOCATION, AND FUNCTION.
PubMed=20695846; DOI=10.1042/BJ20100890;
Ovens M.J., Manoharan C., Wilson M.C., Murray C.M., Halestrap A.P.;
"The inhibition of monocarboxylate transporter 2 (MCT2) by AR-C155858
is modulated by the associated ancillary protein.";
Biochem. J. 431:217-225(2010).
[5]
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. Functions
as high-affinity pyruvate transporter.
{ECO:0000269|PubMed:20695846}.
-!- SUBUNIT: Interacts with GRID2IP (By similarity). Interacts with
EMB. {ECO:0000250, ECO:0000269|PubMed:15917240,
ECO:0000269|PubMed:20695846}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15917240,
ECO:0000269|PubMed:20695846, ECO:0000269|PubMed:9182702,
ECO:0000269|PubMed:9482213}; Multi-pass membrane protein
{ECO:0000269|PubMed:15917240, ECO:0000269|PubMed:20695846,
ECO:0000269|PubMed:9182702, ECO:0000269|PubMed:9482213}.
-!- TISSUE SPECIFICITY: Detected in brain and kidney (at protein
level). {ECO:0000269|PubMed:9482213}.
-!- SIMILARITY: Belongs to the major facilitator superfamily.
Monocarboxylate porter (TC 2.A.1.13) family. {ECO:0000305}.
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EMBL; X97445; CAA66074.1; -; mRNA.
EMBL; U62316; AAB04023.1; -; mRNA.
UniGene; Rn.10524; -.
UniGene; Rn.217495; -.
ProteinModelPortal; Q63344; -.
STRING; 10116.ENSRNOP00000054845; -.
iPTMnet; Q63344; -.
PhosphoSitePlus; Q63344; -.
PaxDb; Q63344; -.
PRIDE; Q63344; -.
RGD; 3691; Slc16a7.
eggNOG; KOG2504; Eukaryota.
eggNOG; COG0477; LUCA.
HOGENOM; HOG000280688; -.
HOVERGEN; HBG006384; -.
InParanoid; Q63344; -.
PhylomeDB; Q63344; -.
PRO; PR:Q63344; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0005737; C:cytoplasm; IDA:RGD.
GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:RGD.
GO; GO:0015129; F:lactate transmembrane transporter activity; ISS:UniProtKB.
GO; GO:0008028; F:monocarboxylic acid transmembrane transporter activity; TAS:RGD.
GO; GO:0050833; F:pyruvate transmembrane transporter activity; ISS:UniProtKB.
GO; GO:0015293; F:symporter activity; IEA:UniProtKB-KW.
GO; GO:0035873; P:lactate transmembrane transport; ISS:UniProtKB.
GO; GO:0035879; P:plasma membrane lactate transport; IDA:RGD.
GO; GO:1901475; P:pyruvate transmembrane transport; ISS:UniProtKB.
CDD; cd06174; MFS; 1.
InterPro; IPR004743; MCT.
InterPro; IPR027178; MCT2.
InterPro; IPR011701; MFS.
InterPro; IPR020846; MFS_dom.
PANTHER; PTHR11360:SF198; PTHR11360:SF198; 1.
Pfam; PF07690; MFS_1; 1.
SUPFAM; SSF103473; SSF103473; 1.
TIGRFAMs; TIGR00892; 2A0113; 1.
PROSITE; PS50850; MFS; 1.
1: Evidence at protein level;
Cell membrane; Complete proteome; Membrane; Reference proteome;
Symport; Transmembrane; Transmembrane helix; Transport.
CHAIN 1 489 Monocarboxylate transporter 2.
/FTId=PRO_0000211389.
TOPO_DOM 1 21 Cytoplasmic. {ECO:0000255}.
TRANSMEM 22 42 Helical. {ECO:0000255}.
TOPO_DOM 43 65 Extracellular. {ECO:0000255}.
TRANSMEM 66 86 Helical. {ECO:0000255}.
TOPO_DOM 87 95 Cytoplasmic. {ECO:0000255}.
TRANSMEM 96 116 Helical. {ECO:0000255}.
TOPO_DOM 117 121 Extracellular. {ECO:0000255}.
TRANSMEM 122 142 Helical. {ECO:0000255}.
TOPO_DOM 143 154 Cytoplasmic. {ECO:0000255}.
TRANSMEM 155 175 Helical. {ECO:0000255}.
TOPO_DOM 176 179 Extracellular. {ECO:0000255}.
TRANSMEM 180 200 Helical. {ECO:0000255}.
TOPO_DOM 201 250 Cytoplasmic. {ECO:0000255}.
TRANSMEM 251 271 Helical. {ECO:0000255}.
TOPO_DOM 272 286 Extracellular. {ECO:0000255}.
TRANSMEM 287 307 Helical. {ECO:0000255}.
TOPO_DOM 308 316 Cytoplasmic. {ECO:0000255}.
TRANSMEM 317 337 Helical. {ECO:0000255}.
TOPO_DOM 338 342 Extracellular. {ECO:0000255}.
TRANSMEM 343 363 Helical. {ECO:0000255}.
TOPO_DOM 364 377 Cytoplasmic. {ECO:0000255}.
TRANSMEM 378 398 Helical. {ECO:0000255}.
TOPO_DOM 399 410 Extracellular. {ECO:0000255}.
TRANSMEM 411 431 Helical. {ECO:0000255}.
TOPO_DOM 432 489 Cytoplasmic. {ECO:0000255}.
CONFLICT 95 95 L -> V (in Ref. 2; AAB04023).
{ECO:0000305}.
CONFLICT 392 392 F -> P (in Ref. 2; AAB04023).
{ECO:0000305}.
SEQUENCE 489 AA; 53057 MW; 447E1CE2D707044B CRC64;
MPSESSVKAT AAPPPFPLPP DGGWGWVVVC ASFISIGFSY AFPKAVTVFF NDIKDIFKTT
SSQIAWISSI MLAVMYAGGP ISSVLVNNYG SRPVLIVGGL LCCTGMILAS FSSSVIELYL
TVGFIGGLGL AFNLQPALTI IGKYFYRKRP LANGFAMAGS PVFLSTLAPF NQFLFNSYGW
KGSFLILGAI FLHSCVAGCL MRPVGPSPRA AKSKSKVGSR QDSSTKRLSK VSTAEKINRF
LDFGLFTHRG FLIYLSGNVV LFLGMFAPII FLAPYAKDKG VDDYNSAFLL SVMAFTDMFA
RPSVGLIANT SLIRPRIQYL FSVAIMFTGI CHLLCPLAHS YTALVVYVIF FGIGFGSISS
LLFECLMDQV GASRFSSAVG LVTIVECCPV LFGPPLAGKL LDITGQYKYL YIASGIVVLS
SGIYLLICNA INYRLLEKER KREKARRKKS ASQASKEMEA LSRSKQDDVT VKVSNTHNPP
SDRDKESSI


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