ID MOT4_MOUSE Reviewed; 470 AA. AC P57787; Q9ES80; Q9ESF8; DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot. DT 27-APR-2001, sequence version 1. DT 26-FEB-2020, entry version 145. DE RecName: Full=Monocarboxylate transporter 4; DE Short=MCT 4; DE AltName: Full=Solute carrier family 16 member 3; GN Name=Slc16a3; Synonyms=Mct4; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=C3H/HeJ; TISSUE=Skeletal muscle; RA Yoon H., Philp N.J.; RT "Cloning and expression of mouse MCT3 and MCT4."; RL Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=129; TISSUE=Mammary gland; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-430, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006; RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M., RA Thibault P.; RT "The phagosomal proteome in interferon-gamma-activated macrophages."; RL Immunity 30:143-154(2009). CC -!- FUNCTION: Proton-linked 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 (By similarity). {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane CC protein {ECO:0000250}. CC -!- SIMILARITY: Belongs to the major facilitator superfamily. CC Monocarboxylate porter (TC 2.A.1.13) family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF178954; AAG24271.1; -; mRNA. DR EMBL; AF204397; AAF67525.1; -; Genomic_DNA. DR EMBL; BC046525; AAH46525.1; -; mRNA. DR CCDS; CCDS25761.1; -. DR RefSeq; NP_001033742.1; NM_001038653.1. DR RefSeq; NP_001033743.1; NM_001038654.1. DR RefSeq; NP_109621.1; NM_030696.3. DR RefSeq; XP_011247623.1; XM_011249321.2. DR RefSeq; XP_011247624.1; XM_011249322.2. DR IntAct; P57787; 1. DR MINT; P57787; -. DR STRING; 10090.ENSMUSP00000068854; -. DR iPTMnet; P57787; -. DR PhosphoSitePlus; P57787; -. DR SwissPalm; P57787; -. DR EPD; P57787; -. DR jPOST; P57787; -. DR PaxDb; P57787; -. DR PeptideAtlas; P57787; -. DR PRIDE; P57787; -. DR Ensembl; ENSMUST00000070653; ENSMUSP00000068854; ENSMUSG00000025161. DR Ensembl; ENSMUST00000100130; ENSMUSP00000097706; ENSMUSG00000025161. DR Ensembl; ENSMUST00000168579; ENSMUSP00000125846; ENSMUSG00000025161. DR GeneID; 80879; -. DR KEGG; mmu:80879; -. DR UCSC; uc007muw.1; mouse. DR CTD; 9123; -. DR MGI; MGI:1933438; Slc16a3. DR eggNOG; ENOG410KCR7; Eukaryota. DR eggNOG; ENOG4111A50; LUCA. DR GeneTree; ENSGT00940000158181; -. DR HOGENOM; CLU_001265_59_1_1; -. DR InParanoid; P57787; -. DR KO; K08180; -. DR OMA; IFMMPIS; -. DR OrthoDB; 916876at2759; -. DR PhylomeDB; P57787; -. DR TreeFam; TF313792; -. DR Reactome; R-MMU-210991; Basigin interactions. DR Reactome; R-MMU-433692; Proton-coupled monocarboxylate transport. DR Reactome; R-MMU-70268; Pyruvate metabolism. DR PRO; PR:P57787; -. DR Proteomes; UP000000589; Chromosome 11. DR RNAct; P57787; protein. DR Bgee; ENSMUSG00000025161; Expressed in gastrocnemius and 160 other tissues. DR ExpressionAtlas; P57787; baseline and differential. DR Genevisible; P57787; MM. DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central. DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central. DR GO; GO:0099061; C:integral component of postsynaptic density membrane; ISO:MGI. DR GO; GO:0031965; C:nuclear membrane; ISO:MGI. DR GO; GO:0098688; C:parallel fiber to Purkinje cell synapse; ISO:MGI. DR GO; GO:0005886; C:plasma membrane; ISO:MGI. DR GO; GO:0015129; F:lactate transmembrane transporter activity; IEA:InterPro. DR GO; GO:0008028; F:monocarboxylic acid transmembrane transporter activity; IBA:GO_Central. DR GO; GO:0015293; F:symporter activity; IEA:UniProtKB-KW. DR GO; GO:0015718; P:monocarboxylic acid transport; IBA:GO_Central. DR GO; GO:0035879; P:plasma membrane lactate transport; ISO:MGI. DR InterPro; IPR004743; MCT. DR InterPro; IPR030756; MCT4. DR InterPro; IPR011701; MFS. DR InterPro; IPR020846; MFS_dom. DR InterPro; IPR036259; MFS_trans_sf. DR PANTHER; PTHR11360:SF27; PTHR11360:SF27; 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; Phosphoprotein; Reference proteome; Symport; KW Transmembrane; Transmembrane helix; Transport. FT CHAIN 1..470 FT /note="Monocarboxylate transporter 4" FT /id="PRO_0000211395" FT TOPO_DOM 1..17 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 18..38 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 39..61 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 62..82 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 83..84 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 85..105 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 106..109 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 110..130 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 131..149 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 150..170 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 171..179 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 180..200 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 201..231 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 232..252 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 253..267 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 268..288 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 289..298 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 299..319 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 320..321 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 322..342 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 343..355 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 356..376 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 377..391 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 392..412 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 413..470 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT MOD_RES 430 FT /note="Phosphoserine" FT /evidence="ECO:0000244|PubMed:19144319" FT MOD_RES 465 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:O15427" FT MOD_RES 469 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:O15427" SQ SEQUENCE 470 AA; 50373 MW; 34E872AC1C625DE7 CRC64; MGGAVVDEGP TGIKAPDGGW GWAVLFGCFI ITGFSYAFPK AVSVFFKELM HEFGIGYSDT AWISSILLAM LYGTGPLCSV CVNRFGCRPV MLVGGLFASL GMVAASFCRS IIQIYLTTGV ITGLGLALNF QPSLIMLNRY FNKRRPIANG LAAAGSPVFL CALSPLGQLL QDHYGWRGGF LILGGLLLNC CVCAALMRPL VAPQVGGGTE PRGPQRPPQR LLDLSVFRDR GFLIYAVAAS IMVLGLFVPP VFVVSYAKDM GVPDTKAAFL LTILGFIDIF ARPTAGFITG LKKVRPYSVY LFSFAMFFNG FTDLTGSTAT DYGGLVVFCI FFGISYGMVG ALQFEVLMAI VGTQKFSSAI GLVLLLEAVA VLIGPPSGGK LLDATKVYKY VFILAGAEVL TSSLVLLLGN FFCIGKRKRP EVTEPEEVAS EEKLHKPPVD VGVDSREVEH FLKAEPEKNG EVVHTPETSV //