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Database: UniProt
Entry: M7BIQ1_CHEMY
LinkDB: M7BIQ1_CHEMY
Original site: M7BIQ1_CHEMY 
ID   M7BIQ1_CHEMY            Unreviewed;       449 AA.
AC   M7BIQ1;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   RecName: Full=Monocarboxylate transporter 2 {ECO:0000256|ARBA:ARBA00015820};
DE   AltName: Full=Solute carrier family 16 member 7 {ECO:0000256|ARBA:ARBA00029783};
DE   Flags: Fragment;
GN   ORFNames=UY3_10961 {ECO:0000313|EMBL:EMP31923.1};
OS   Chelonia mydas (Green sea-turtle) (Chelonia agassizi).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC   Americhelydia; Chelonioidea; Cheloniidae; Chelonia.
OX   NCBI_TaxID=8469 {ECO:0000313|EMBL:EMP31923.1, ECO:0000313|Proteomes:UP000031443};
RN   [1] {ECO:0000313|Proteomes:UP000031443}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23624526; DOI=10.1038/ng.2615;
RA   Wang Z., Pascual-Anaya J., Zadissa A., Li W., Niimura Y., Huang Z., Li C.,
RA   White S., Xiong Z., Fang D., Wang B., Ming Y., Chen Y., Zheng Y.,
RA   Kuraku S., Pignatelli M., Herrero J., Beal K., Nozawa M., Li Q., Wang J.,
RA   Zhang H., Yu L., Shigenobu S., Wang J., Liu J., Flicek P., Searle S.,
RA   Wang J., Kuratani S., Yin Y., Aken B., Zhang G., Irie N.;
RT   "The draft genomes of soft-shell turtle and green sea turtle yield insights
RT   into the development and evolution of the turtle-specific body plan.";
RL   Nat. Genet. 45:701-706(2013).
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:0000256|ARBA:ARBA00034273};
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:0000256|ARBA:ARBA00034262};
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:0000256|ARBA:ARBA00034245};
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:0000256|ARBA:ARBA00034218};
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:0000256|ARBA:ARBA00034216};
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:0000256|ARBA:ARBA00034229};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64721;
CC         Evidence={ECO:0000256|ARBA:ARBA00034229};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:64722;
CC         Evidence={ECO:0000256|ARBA:ARBA00034229};
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:0000256|ARBA:ARBA00034277};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC       Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Cytoplasm
CC       {ECO:0000256|ARBA:ARBA00004496}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
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DR   EMBL; KB543130; EMP31923.1; -; Genomic_DNA.
DR   AlphaFoldDB; M7BIQ1; -.
DR   STRING; 8469.M7BIQ1; -.
DR   eggNOG; KOG2504; Eukaryota.
DR   Proteomes; UP000031443; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008028; F:monocarboxylic acid transmembrane transporter activity; IEA:InterPro.
DR   CDD; cd17427; MFS_MCT2; 1.
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   4: Predicted;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000031443};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   TRANSMEM        16..36
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        57..79
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        99..123
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        144..163
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        175..194
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        245..266
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        278..301
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        313..332
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        338..357
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        369..391
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        403..425
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          18..434
FT                   /note="Major facilitator superfamily (MFS) profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50850"
FT   NON_TER         449
FT                   /evidence="ECO:0000313|EMBL:EMP31923.1"
SQ   SEQUENCE   449 AA;  48928 MW;  B0CDD4478137F3B5 CRC64;
     MPPATTAPQY APPDGGWGWV VVFGAFISIG FSYAFPKAIT VFFKEIQEIF HTSYSEIAWI
     SSIMLAVMYA GGPISSVLVN KYGCRPVMMA GGVLCSFGMI ASSFCNSVLE LYVCVGIVGG
     LGLAFNLQPA LTMIGKYFYK KRPIANGLAM AGSPVFLSTL APLNQFLFNA FGWKGSFLIL
     GGLLLNCCVA GSLMRPVGPK PVPPVKKDVE KGSGDSALHM NNKKSSFWQT VNKYLDLSLF
     KHRGFLVYLS GNVIMFVGFF APIVFLAPYA KHKGIDEYSA AFLLSILAFV DMFARPSMGL
     VANSKYIRPK IQYFFSFAVL YNGICHIMCP LAEDYTGLVV YAVLFGFAFG MVSSILFESL
     MDLVGAARFS SAVGLVTIVE CCPVLLGPPL GGWLVDITGD YKYMYIVCGS IVIVASIWLF
     IGNAINYRLL AKEKNLEDKK QKALKKEAE
//
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