ID   MOT2_MESAU              Reviewed;         484 AA.
AC   P53988;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   25-MAY-2022, entry version 94.
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   Mesocricetus auratus (Golden hamster).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Cricetinae; Mesocricetus.
OX   NCBI_TaxID=10036;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP   SPECIFICITY.
RC   TISSUE=Liver;
RX   PubMed=7829520; DOI=10.1074/jbc.270.4.1843;
RA   Garcia C.K., Brown M.S., Pathak R.K., Goldstein J.L.;
RT   "cDNA cloning of MCT2, a second monocarboxylate transporter expressed in
RT   different cells than MCT1.";
RL   J. Biol. Chem. 270:1843-1849(1995).
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:7829520}.
CC   -!- SUBUNIT: Interacts with GRID2IP (By similarity). Interacts with EMB (By
CC       similarity). Interacts with BSG (By similarity).
CC       {ECO:0000250|UniProtKB:O70451, ECO:0000250|UniProtKB:Q63344}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:7829520};
CC       Multi-pass membrane protein {ECO:0000269|PubMed:7829520}.
CC   -!- TISSUE SPECIFICITY: Abundant on the surface of hepatocytes. Present on
CC       parietal cells of the oxyntic gland of the stomach, on the basolateral
CC       surface of epithelial cells in the collecting ducts of the kidney, on
CC       sperm tails throughout the epididymis. Expressed in mitochondria-rich
CC       skeletal muscle fibers and cardiac myocytes (at protein level).
CC       {ECO:0000269|PubMed:7829520}.
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; L31957; AAC42046.1; -; mRNA.
DR   PIR; A55626; A55626.
DR   RefSeq; NP_001268256.1; NM_001281327.1.
DR   AlphaFoldDB; P53988; -.
DR   SMR; P53988; -.
DR   STRING; 10036.XP_005079894.1; -.
DR   GeneID; 101835011; -.
DR   CTD; 9194; -.
DR   eggNOG; KOG2504; Eukaryota.
DR   OrthoDB; 916876at2759; -.
DR   Proteomes; UP000189706; Unplaced.
DR   GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR   GO; GO:0015129; F:lactate transmembrane transporter activity; ISS:UniProtKB.
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: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..484
FT                   /note="Monocarboxylate transporter 2"
FT                   /id="PRO_0000211386"
FT   TOPO_DOM        1..16
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        17..37
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        38..60
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        61..81
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        82..87
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        88..108
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        109..116
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        117..137
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        138..144
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        145..165
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        166..174
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        175..195
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        196..245
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        246..266
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        267..282
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        283..303
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        304..311
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        312..332
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        333..337
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        338..358
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        359..372
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        373..393
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        394..405
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        406..426
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        427..484
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          201..224
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          437..484
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        445..461
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   484 AA;  52832 MW;  8D36EE7B585EF5FD CRC64;
     MPSETAVPPP HPIPPDGGWG WVVVGAAFIS IGFSYAFPKA VTVFFKDIQQ IFQASYSEIA
     WISSIMLAVM YAGGPISSVL VNNYGSRPVV IIGGLLCCTG MILASFSNSV LELYLTIGFI
     GGLGLAFNLQ PALTIIGKYF YRRRPMANGL AMAGSPVFLS SLAPFNQYLF NSYGWKGSFL
     ILGGIFLHSC VAGCLMRPVQ TSPRKSKSKS KVGSRQDGSM KKASKVSTAE KINRFLDFSL
     FKHRGFLIYL SGNVIMFLGF FAPIIFLAPY AKDKGVDEYN AALLLSVMAF VDMFARPTGG
     LIANSKLIRP RIQYFFSFAI VFTGICHLLC PLADTYPALV VYSIFFGYGF GSVSSVLFET
     LMDLVGPARF SSAVGLATIV ECCPVLLGPP LAGKLVDKTK DYKYMYIASG TIVVISGIYL
     FIGNAINYRL LAKERKREKA RKKKSATHPS RESEALSRSK QDDVSVKVSN PHNSPSDRER
     ESNI