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 24-JAN-2024, entry version 99.
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, TRANSPORTER ACTIVITY, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
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 symporter (PubMed:7829520).
CC Catalyzes the rapid transport across the plasma membrane of
CC monocarboxylates such as L-lactate, pyruvate and ketone bodies,
CC acetoacetate, beta-hydroxybutyrate and acetate. Dimerization is
CC functionally required and both subunits work cooperatively in
CC transporting substrate (By similarity). {ECO:0000250|UniProtKB:O60669,
CC ECO:0000269|PubMed:7829520}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+)(out) + pyruvate(out) = H(+)(in) + pyruvate(in);
CC Xref=Rhea:RHEA:64720, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378;
CC Evidence={ECO:0000269|PubMed:7829520};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64721;
CC Evidence={ECO:0000250|UniProtKB:O60669};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:64722;
CC Evidence={ECO:0000250|UniProtKB:O60669};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-methyl-2-oxobutanoate(out) + H(+)(out) = 3-methyl-2-
CC oxobutanoate(in) + H(+)(in); Xref=Rhea:RHEA:71783, ChEBI:CHEBI:11851,
CC ChEBI:CHEBI:15378; Evidence={ECO:0000250|UniProtKB:Q63344};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-lactate(in) + H(+)(in) = (S)-lactate(out) + H(+)(out);
CC Xref=Rhea:RHEA:29415, ChEBI:CHEBI:15378, ChEBI:CHEBI:16651;
CC Evidence={ECO:0000250|UniProtKB:Q63344};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetoacetate(out) + H(+)(out) = acetoacetate(in) + H(+)(in);
CC Xref=Rhea:RHEA:71775, ChEBI:CHEBI:13705, ChEBI:CHEBI:15378;
CC Evidence={ECO:0000250|UniProtKB:Q63344};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-3-hydroxybutanoate(out) + H(+)(out) = (R)-3-
CC hydroxybutanoate(in) + H(+)(in); Xref=Rhea:RHEA:71795,
CC ChEBI:CHEBI:10983, ChEBI:CHEBI:15378;
CC Evidence={ECO:0000250|UniProtKB:Q63344};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-methyl-2-oxopentanoate(out) + H(+)(out) = 4-methyl-2-
CC oxopentanoate(in) + H(+)(in); Xref=Rhea:RHEA:71779,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17865;
CC Evidence={ECO:0000250|UniProtKB:Q63344};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-3-hydroxybutanoate(out) + H(+)(out) = (S)-3-
CC hydroxybutanoate(in) + H(+)(in); Xref=Rhea:RHEA:71871,
CC ChEBI:CHEBI:11047, ChEBI:CHEBI:15378;
CC Evidence={ECO:0000250|UniProtKB:Q63344};
CC -!- ACTIVITY REGULATION: Transport activity exhibits steep dependence on
CC substrate concentration. Substrate concentration sensitivity of SLC16A7
CC arises from the strong inter-subunit cooperativity of the SLC16A7 dimer
CC during transport. Inhibited by AR-C155858.
CC {ECO:0000250|UniProtKB:O60669}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.8 mM for pyruvate {ECO:0000269|PubMed:7829520};
CC -!- SUBUNIT: Homodimer (By similarity). Interacts with GRID2IP (By
CC similarity). Interacts with EMB; interaction mediates SLC16A7 targeting
CC to the plasma membrane (By similarity). Interacts with isoform 2 of BSG
CC (By similarity). {ECO:0000250|UniProtKB:O60669,
CC ECO:0000250|UniProtKB:O70451, ECO:0000250|UniProtKB:Q63344}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:7829520};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:O60669}. Basolateral
CC cell membrane {ECO:0000269|PubMed:7829520}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:O60669}. Cytoplasm
CC {ECO:0000250|UniProtKB:O70451}. Note=Requires the ancillary protein,
CC EMB for plasma membrane localization (By similarity). Colocalizes with
CC BSG in spermatozoa. Detected in the cytoplasm of Sertoli cells (By
CC similarity). {ECO:0000250|UniProtKB:O70451,
CC ECO:0000250|UniProtKB:Q63344}.
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.ENSMAUP00000014089; -.
DR GeneID; 101835011; -.
DR KEGG; maua:101835011; -.
DR CTD; 9194; -.
DR eggNOG; KOG2504; Eukaryota.
DR OrthoDB; 2917104at2759; -.
DR Proteomes; UP000189706; Unplaced.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR GO; GO:0015129; F:lactate transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0050833; F:pyruvate transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0015293; F:symporter activity; IDA:UniProtKB.
DR GO; GO:0035873; P:lactate transmembrane transport; ISS:UniProtKB.
DR GO; GO:1901475; P:pyruvate transmembrane transport; IDA:UniProtKB.
DR Gene3D; 1.20.1250.20; MFS general substrate transporter like domains; 1.
DR InterPro; IPR004743; MCT.
DR InterPro; IPR011701; MFS.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR036259; MFS_trans_sf.
DR NCBIfam; TIGR00892; 2A0113; 1.
DR PANTHER; PTHR11360; MONOCARBOXYLATE TRANSPORTER; 1.
DR PANTHER; PTHR11360:SF25; MONOCARBOXYLATE TRANSPORTER 2; 1.
DR Pfam; PF07690; MFS_1; 1.
DR SUPFAM; SSF103473; MFS general substrate transporter; 1.
DR PROSITE; PS50850; MFS; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cytoplasm; Membrane; Reference proteome; Symport;
KW Transmembrane; 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:0000305"
FT TRANSMEM 17..37
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 38..60
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 61..81
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 82..87
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 88..108
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 109..116
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 117..137
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 138..144
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 145..165
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 166..174
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 175..195
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 196..245
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 246..266
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 267..282
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 283..303
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 304..311
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 312..332
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 333..337
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 338..358
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TOPO_DOM 359..372
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 373..393
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255"
FT TOPO_DOM 394..405
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 406..426
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255"
FT TOPO_DOM 427..484
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
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"
FT SITE 292
FT /note="May be protonated during monocarboxylate transport"
FT /evidence="ECO:0000250|UniProtKB:O60669"
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
//
