MOT2_RAT
ID MOT2_RAT Reviewed; 489 AA.
AC Q63344; Q63649;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Monocarboxylate transporter 2;
DE Short=MCT 2;
DE AltName: Full=Solute carrier family 16 member 7;
GN Name=Slc16a7; Synonyms=Mct2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION.
RC STRAIN=Sprague-Dawley; TISSUE=Testis;
RX PubMed=9182702; DOI=10.1042/bj3240447;
RA Jackson V.N., Price N.T., Carpenter L., Halestrap A.P.;
RT "Cloning of the monocarboxylate transporter isoform MCT2 from rat testis
RT provides evidence that expression in tissues is species-specific and may
RT involve post-transcriptional regulation.";
RL Biochem. J. 324:447-453(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=Wistar; TISSUE=Brain;
RX PubMed=9482213;
RX DOI=10.1002/(sici)1098-1136(199803)22:3<272::aid-glia6>3.0.co;2-7;
RA Gerhart D.Z., Enerson B.E., Zhdankina O.Y., Leino R.L., Drewes L.R.;
RT "Expression of the monocarboxylate transporter MCT2 by rat brain glia.";
RL Glia 22:272-281(1998).
RN [3]
RP INTERACTION WITH EMB, AND SUBCELLULAR LOCATION.
RX PubMed=15917240; DOI=10.1074/jbc.m411950200;
RA Wilson M.C., Meredith D., Fox J.E., Manoharan C., Davies A.J.,
RA Halestrap A.P.;
RT "Basigin (CD147) is the target for organomercurial inhibition of
RT monocarboxylate transporter isoforms 1 and 4: the ancillary protein for the
RT insensitive MCT2 is EMBIGIN (gp70).";
RL J. Biol. Chem. 280:27213-27221(2005).
RN [4]
RP INTERACTION WITH EMB, SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=20695846; DOI=10.1042/bj20100890;
RA Ovens M.J., Manoharan C., Wilson M.C., Murray C.M., Halestrap A.P.;
RT "The inhibition of monocarboxylate transporter 2 (MCT2) by AR-C155858 is
RT modulated by the associated ancillary protein.";
RL Biochem. J. 431:217-225(2010).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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. Functions as high-affinity pyruvate
CC transporter. {ECO:0000269|PubMed:20695846}.
CC -!- SUBUNIT: Interacts with GRID2IP and with isoform 2 of BSG (By
CC similarity). Interacts with EMB (PubMed:15917240, PubMed:20695846).
CC {ECO:0000250|UniProtKB:O70451, ECO:0000269|PubMed:15917240,
CC ECO:0000269|PubMed:20695846}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15917240,
CC ECO:0000269|PubMed:20695846, ECO:0000269|PubMed:9182702,
CC ECO:0000269|PubMed:9482213}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:15917240, ECO:0000269|PubMed:20695846,
CC ECO:0000269|PubMed:9182702, ECO:0000269|PubMed:9482213}.
CC -!- TISSUE SPECIFICITY: Detected in brain and kidney (at protein level).
CC {ECO:0000269|PubMed:9482213}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily.
CC Monocarboxylate porter (TC 2.A.1.13) family. {ECO:0000305}.
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DR EMBL; X97445; CAA66074.1; -; mRNA.
DR EMBL; U62316; AAB04023.1; -; mRNA.
DR AlphaFoldDB; Q63344; -.
DR SMR; Q63344; -.
DR STRING; 10116.ENSRNOP00000054845; -.
DR iPTMnet; Q63344; -.
DR PhosphoSitePlus; Q63344; -.
DR PaxDb; Q63344; -.
DR PRIDE; Q63344; -.
DR RGD; 3691; Slc16a7.
DR eggNOG; KOG2504; Eukaryota.
DR InParanoid; Q63344; -.
DR PhylomeDB; Q63344; -.
DR Reactome; R-RNO-433692; Proton-coupled monocarboxylate transport.
DR PRO; PR:Q63344; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0098686; C:hippocampal mossy fiber to CA3 synapse; IDA:SynGO.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0099061; C:integral component of postsynaptic density membrane; IDA:SynGO.
DR GO; GO:0098688; C:parallel fiber to Purkinje cell synapse; IDA:SynGO.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IDA:SynGO.
DR GO; GO:0015129; F:lactate transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0008028; F:monocarboxylic acid transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0050833; F:pyruvate transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0015293; F:symporter activity; IEA:UniProtKB-KW.
DR GO; GO:0035873; P:lactate transmembrane transport; ISS:UniProtKB.
DR GO; GO:0015718; P:monocarboxylic acid transport; IBA:GO_Central.
DR GO; GO:0035879; P:plasma membrane lactate transport; IDA:RGD.
DR GO; GO:1901475; P:pyruvate transmembrane transport; ISS:UniProtKB.
DR Gene3D; 1.20.1250.20; -; 1.
DR InterPro; IPR004743; MCT.
DR InterPro; IPR027178; MCT2.
DR InterPro; IPR011701; MFS.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR036259; MFS_trans_sf.
DR PANTHER; PTHR11360:SF25; PTHR11360:SF25; 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 Cell membrane; Membrane; Reference proteome; Symport; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..489
FT /note="Monocarboxylate transporter 2"
FT /id="PRO_0000211389"
FT TOPO_DOM 1..21
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 22..42
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 43..65
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 66..86
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 87..95
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 96..116
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 117..121
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 122..142
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 143..154
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 155..175
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 176..179
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 180..200
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 201..250
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 251..271
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 272..286
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 287..307
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 308..316
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 317..337
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 338..342
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 343..363
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 364..377
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 378..398
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 399..410
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 411..431
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 432..489
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 206..227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 441..489
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 450..466
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 95
FT /note="L -> V (in Ref. 2; AAB04023)"
FT /evidence="ECO:0000305"
FT CONFLICT 392
FT /note="F -> P (in Ref. 2; AAB04023)"
FT /evidence="ECO:0000305"
SQ 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
