ID MOT11_HUMAN Reviewed; 447 AA. AC Q8NCK7; A0A590UJX4; I3L431; DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot. DT 28-JAN-2026, sequence version 2. DT 02-SEP-2026, entry version 153. DE RecName: Full=Monocarboxylate transporter 11; DE Short=MCT 11; DE AltName: Full=Solute carrier family 16 member 11; GN Name=SLC16A11; Synonyms=MCT11; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Mammary gland; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16625196; DOI=10.1038/nature04689; RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.; RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the RT human lineage."; RL Nature 440:1045-1049(2006). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Heart, and Lung; 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 [4] RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INVOLVEMENT IN T2D, AND RP VARIANTS ILE-89; GLY-103; SER-316 AND THR-419. RX PubMed=24390345; DOI=10.1038/nature12828; RG The SIGMA Type 2 Diabetes Consortium; RT "Sequence variants in SLC16A11 are a common risk factor for type 2 diabetes RT in Mexico."; RL Nature 506:97-101(2014). RN [5] RP FUNCTION, TRANSPORTER ACTIVITY, SUBCELLULAR LOCATION, INTERACTION WITH BSG, RP INVOLVEMENT IN T2D, AND CHARACTERIZATION OF VARIANTS ILE-89; GLY-103; RP SER-316 AND THR-419. RX PubMed=28666119; DOI=10.1016/j.cell.2017.06.011; RG MEDIA Consortium; RG SIGMA T2D Consortium; RA Rusu V., Hoch E., Mercader J.M., Tenen D.E., Gymrek M., Hartigan C.R., RA DeRan M., von Grotthuss M., Fontanillas P., Spooner A., Guzman G., RA Deik A.A., Pierce K.A., Dennis C., Clish C.B., Carr S.A., Wagner B.K., RA Schenone M., Ng M.C.Y., Chen B.H., Centeno-Cruz F., Zerrweck C., Orozco L., RA Altshuler D.M., Schreiber S.L., Florez J.C., Jacobs S.B.R., Lander E.S.; RT "Type 2 diabetes variants disrupt function of SLC16A11 through two distinct RT mechanisms."; RL Cell 170:199-212(2017). CC -!- FUNCTION: Proton-linked monocarboxylate transporter. It catalyzes the CC transport of pyruvate across the plasma membrane (PubMed:28666119). CC Probably involved in hepatic lipid metabolism: overexpression results CC in an increase of triacylglycerol(TAG) levels, small increases in CC intracellular diacylglycerols and decreases in lysophosphatidylcholine, CC cholesterol ester and sphingomyelin lipids (PubMed:24390345). CC {ECO:0000269|PubMed:24390345, ECO:0000269|PubMed:28666119}. CC -!- CATALYTIC ACTIVITY: CC Reaction=pyruvate(out) + H(+)(out) = pyruvate(in) + H(+)(in); CC Xref=Rhea:RHEA:64720, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378; CC Evidence={ECO:0000269|PubMed:28666119}; CC -!- SUBUNIT: Interacts with isoform 2 of BSG. CC {ECO:0000269|PubMed:28666119}. CC -!- INTERACTION: CC Q8NCK7; P35613: BSG; NbExp=5; IntAct=EBI-21840241, EBI-750709; CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane CC {ECO:0000269|PubMed:24390345}; Multi-pass membrane protein CC {ECO:0000255}. Cell membrane {ECO:0000269|PubMed:28666119}; Multi-pass CC membrane protein {ECO:0000255}. CC -!- TISSUE SPECIFICITY: Expressed in liver, salivary gland and thyroid. CC {ECO:0000269|PubMed:24390345}. CC -!- DISEASE: Type 2 diabetes mellitus (T2D) [MIM:125853]: A multifactorial CC disorder of glucose homeostasis caused by a lack of sensitivity to CC insulin. Affected individuals usually have an obese body habitus and CC manifestations of a metabolic syndrome characterized by diabetes, CC insulin resistance, hypertension and hypertriglyceridemia. The disease CC results in long-term complications that affect the eyes, kidneys, CC nerves, and blood vessels. {ECO:0000269|PubMed:24390345}. Note=Disease CC susceptibility is associated with variants affecting the gene CC represented in this entry. A risk haplotype spanning SLC16A11 is CC associated with a 20% increased risk for T2D. The haplotype includes 5 CC SLC16A11 variants in strong linkage disequilibrium: variants Ile-89, CC Gly-103, Ser-316, Thr-419 and a silent variant. This risk haplotype CC probably derives from H.sapiens neanderthalensis (Neanderthal) CC introgression and is present at 50% frequency in Native-American CC samples, 10% in east Asian, while it is rare in European and African CC samples populations. The risk haplotype contains a cis-eQTL that is CC responsible for reduced SLC16A11 expression in liver (PubMed:28666119). CC {ECO:0000269|PubMed:24390345, ECO:0000269|PubMed:28666119}. CC -!- SIMILARITY: Belongs to the major facilitator superfamily. CC Monocarboxylate porter (TC 2.A.1.13) family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAH93860.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC Sequence=AAH93886.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC Sequence=BAC11128.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={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; AK074674; BAC11128.1; ALT_INIT; mRNA. DR EMBL; AC040977; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC093860; AAH93860.1; ALT_INIT; mRNA. DR EMBL; BC093886; AAH93886.1; ALT_INIT; mRNA. DR CCDS; CCDS11086.2; -. DR RefSeq; NP_001357478.1; NM_001370549.1. DR RefSeq; NP_699188.2; NM_153357.3. DR AlphaFoldDB; Q8NCK7; -. DR SMR; Q8NCK7; -. DR BioGRID; 127822; 12. DR FunCoup; Q8NCK7; 328. DR IntAct; Q8NCK7; 559. DR STRING; 9606.ENSP00000310490; -. DR TCDB; 2.A.1.13.13; the major facilitator superfamily (mfs). DR GlyGen; Q8NCK7; 1 site. DR iPTMnet; Q8NCK7; -. DR PhosphoSitePlus; Q8NCK7; -. DR BioMuta; SLC16A11; -. DR DMDM; 74730153; -. DR MassIVE; Q8NCK7; -. DR PaxDb; 9606-ENSP00000310490; -. DR PeptideAtlas; Q8NCK7; -. DR Antibodypedia; 53202; 100 antibodies from 22 providers. DR DNASU; 162515; -. DR Ensembl; ENST00000574600.3; ENSP00000460927.2; ENSG00000174326.16. DR Ensembl; ENST00000662352.3; ENSP00000499634.1; ENSG00000174326.16. DR Ensembl; ENST00000892155.1; ENSP00000562214.1; ENSG00000174326.16. DR GeneID; 162515; -. DR MANE-Select; ENST00000574600.3; ENSP00000460927.2; NM_001370549.1; NP_001357478.1. DR UCSC; uc002gei.1; human. DR AGR; HGNC:23093; -. DR ClinPGx; PA134976903; -. DR CTD; 162515; -. DR DisGeNET; 162515; -. DR GeneCards; SLC16A11; -. DR HGNC; HGNC:23093; SLC16A11. DR MIM; 125853; phenotype. DR OpenTargets; ENSG00000174326; -. DR VEuPathDB; HostDB:ENSG00000174326; -. DR eggNOG; KOG2504; Eukaryota. DR GeneTree; ENSGT00940000162017; -. DR HOGENOM; CLU_152295_1_0_1; -. DR InParanoid; Q8NCK7; -. DR OrthoDB; 2213137at2759; -. DR PAN-GO; Q8NCK7; 2 GO annotations based on evolutionary models. DR PhylomeDB; Q8NCK7; -. DR PathwayCommons; Q8NCK7; -. DR SignaLink; Q8NCK7; -. DR BioGRID-ORCS; 162515; 25 hits in 1145 CRISPR screens. DR GenomeRNAi; 162515; -. DR Pharos; Q8NCK7; Tbio. DR PRO; PR:Q8NCK7; -. DR Proteomes; UP000005640; Chromosome 17. DR RNAct; Q8NCK7; protein. DR Bgee; ENSG00000174326; Expressed in right uterine tube and 92 other cell types or tissues. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0008028; F:monocarboxylic acid transmembrane transporter activity; IBA:GO_Central. DR GO; GO:0050833; F:pyruvate transmembrane transporter activity; IDA:UniProtKB. DR GO; GO:0006629; P:lipid metabolic process; IDA:UniProtKB. DR FunFam; 1.20.1250.20:FF:000187; Solute carrier family 16 member 11; 1. DR Gene3D; 1.20.1250.20; MFS general substrate transporter like domains; 1. DR InterPro; IPR011701; MFS. DR InterPro; IPR020846; MFS_dom. DR InterPro; IPR036259; MFS_trans_sf. DR InterPro; IPR050327; Proton-linked_MCT. DR PANTHER; PTHR11360; MONOCARBOXYLATE TRANSPORTER; 1. DR PANTHER; PTHR11360:SF80; MONOCARBOXYLATE TRANSPORTER 11; 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; Diabetes mellitus; Endoplasmic reticulum; Lipid metabolism; KW Membrane; Proteomics identification; Reference proteome; Symport; KW Transmembrane; Transmembrane helix; Transport. FT CHAIN 1..447 FT /note="Monocarboxylate transporter 11" FT /id="PRO_0000286673" FT TOPO_DOM 1..11 FT /note="Cytoplasmic" FT /evidence="ECO:0000305|PubMed:24390345" FT TRANSMEM 12..32 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 54..74 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 82..102 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 107..127 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 139..159 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 174..194 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 219..239 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 249..269 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 288..308 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 309..329 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 343..365 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 383..403 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 404..447 FT /note="Cytoplasmic" FT /evidence="ECO:0000305|PubMed:24390345" FT VARIANT 89 FT /note="V -> I (risk factor for T2D when associated with FT G-103, S-316 and T-419; reduced pyruvate transmembrane FT transporter activity, loss of interaction with BSG and FT decreased localization to plasma membrane when associated FT with G-103, S-316 and T-419; dbSNP:rs117767867)" FT /evidence="ECO:0000269|PubMed:24390345, FT ECO:0000269|PubMed:28666119" FT /id="VAR_070544" FT VARIANT 103 FT /note="D -> G (risk factor for T2D when associated with FT I-89, S-316 and T-419; reduced pyruvate transmembrane FT transporter activity, loss of interaction with BSG and FT decreased localization to plasma membrane when associated FT with I-89, S-316 and T-419; dbSNP:rs13342692)" FT /evidence="ECO:0000269|PubMed:24390345, FT ECO:0000269|PubMed:28666119" FT /id="VAR_032157" FT VARIANT 316 FT /note="G -> S (risk factor for T2D when associated with FT I-89, G-103 and T-419; reduced pyruvate transmembrane FT transporter activity, loss of interaction with BSG and FT decreased localization to plasma membrane when associated FT with I-89, G-103 and T-419; dbSNP:rs75418188)" FT /evidence="ECO:0000269|PubMed:24390345, FT ECO:0000269|PubMed:28666119" FT /id="VAR_070545" FT VARIANT 419 FT /note="P -> T (risk factor for T2D when associated with FT I-89, G-103 and S-316; reduced pyruvate transmembrane FT transporter activity, loss of interaction with BSG and FT decreased localization to plasma membrane when associated FT with I-89, G-103 and S-316; dbSNP:rs75493593)" FT /evidence="ECO:0000269|PubMed:24390345, FT ECO:0000269|PubMed:28666119" FT /id="VAR_070546" SQ SEQUENCE 447 AA; 45045 MW; 8C7AC1CEC5D4098D CRC64; MTPQPAGPPD GGWGWVVAAA AFAINGLSYG LLRSLGLAFP DLAEHFDRSA QDTAWISALA LAVQQAASPV GSALSTRWGA RPVVMVGGVL ASLGFVFSAF ASDLLHLYLG LGLLAGFGWA LVFAPALGTL SRYFSRRRVL AVGLALTGNG ASSLLLAPAL QLLLDTFGWR GALLLLGAIT LHLTPCGALL LPLVLPGDPP APPRSPLAAL GLSLFTRRAF SIFALGTALV GGGYFVPYVH LAPHALDRGL GGYGAALVVA VAAMGDAGAR LVCGWLADQG WVPLPRLLAV FGALTGLGLW VVGLVPVVGG EESWGGPLLA AAVAYGLSAG SYAPLVFGVL PGLVGVGGVV QATGLVMMLM SLGGLLGPPL SGFLRDETGD FTASFLLSGS LILSGSFIYI GLPRALPSCG PASPPATPPP ETGELLPAPQ AVLLSPGGPG STLDTTC //