MOT6_HUMAN
ID MOT6_HUMAN Reviewed; 505 AA.
AC O15375; B4E288;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Monocarboxylate transporter 6;
DE Short=MCT 6;
DE AltName: Full=Monocarboxylate transporter 5;
DE Short=MCT 5;
DE AltName: Full=Solute carrier family 16 member 5;
GN Name=SLC16A5; Synonyms=MCT5, MCT6;
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 [MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
RX PubMed=9425115; DOI=10.1042/bj3290321;
RA Price N.T., Jackson V.N., Halestrap A.P.;
RT "Cloning and sequencing of four new mammalian monocarboxylate transporter
RT (MCT) homologues confirms the existence of a transporter family with an
RT ancient past.";
RL Biochem. J. 329:321-328(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Trachea;
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Blood, and Pancreas;
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).
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 -!- INTERACTION:
CC O15375; O95967: EFEMP2; NbExp=3; IntAct=EBI-12874738, EBI-743414;
CC O15375; Q9UJY1: HSPB8; NbExp=3; IntAct=EBI-12874738, EBI-739074;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O15375-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O15375-2; Sequence=VSP_056660, VSP_056661;
CC -!- TISSUE SPECIFICITY: Highly expressed in kidney.
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; U59299; AAC52013.1; -; mRNA.
DR EMBL; AK304163; BAG65050.1; -; mRNA.
DR EMBL; AC111186; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC009684; AAH09684.1; -; mRNA.
DR EMBL; BC033611; AAH33611.1; -; mRNA.
DR CCDS; CCDS11713.1; -. [O15375-1]
DR RefSeq; NP_001258694.1; NM_001271765.1. [O15375-1]
DR RefSeq; NP_004686.1; NM_004695.3. [O15375-1]
DR AlphaFoldDB; O15375; -.
DR SMR; O15375; -.
DR BioGRID; 114569; 7.
DR IntAct; O15375; 4.
DR STRING; 9606.ENSP00000390564; -.
DR DrugBank; DB00119; Pyruvic acid.
DR TCDB; 2.A.1.13.11; the major facilitator superfamily (mfs).
DR iPTMnet; O15375; -.
DR PhosphoSitePlus; O15375; -.
DR BioMuta; SLC16A5; -.
DR MassIVE; O15375; -.
DR MaxQB; O15375; -.
DR PaxDb; O15375; -.
DR PeptideAtlas; O15375; -.
DR PRIDE; O15375; -.
DR ProteomicsDB; 48617; -. [O15375-1]
DR ProteomicsDB; 5804; -.
DR Antibodypedia; 46001; 33 antibodies from 12 providers.
DR DNASU; 9121; -.
DR Ensembl; ENST00000329783.9; ENSP00000330141.4; ENSG00000170190.16. [O15375-1]
DR Ensembl; ENST00000450736.6; ENSP00000390564.2; ENSG00000170190.16. [O15375-1]
DR Ensembl; ENST00000538213.6; ENSP00000440212.2; ENSG00000170190.16. [O15375-2]
DR Ensembl; ENST00000580123.5; ENSP00000463434.1; ENSG00000170190.16. [O15375-1]
DR GeneID; 9121; -.
DR KEGG; hsa:9121; -.
DR MANE-Select; ENST00000329783.9; ENSP00000330141.4; NM_004695.4; NP_004686.1.
DR UCSC; uc002jmr.5; human. [O15375-1]
DR CTD; 9121; -.
DR DisGeNET; 9121; -.
DR GeneCards; SLC16A5; -.
DR HGNC; HGNC:10926; SLC16A5.
DR HPA; ENSG00000170190; Tissue enhanced (kidney).
DR MIM; 603879; gene.
DR neXtProt; NX_O15375; -.
DR OpenTargets; ENSG00000170190; -.
DR PharmGKB; PA35817; -.
DR VEuPathDB; HostDB:ENSG00000170190; -.
DR eggNOG; KOG2504; Eukaryota.
DR GeneTree; ENSGT00940000159666; -.
DR InParanoid; O15375; -.
DR OMA; SMPQVHI; -.
DR OrthoDB; 916876at2759; -.
DR PhylomeDB; O15375; -.
DR TreeFam; TF313792; -.
DR PathwayCommons; O15375; -.
DR SignaLink; O15375; -.
DR BioGRID-ORCS; 9121; 77 hits in 1078 CRISPR screens.
DR ChiTaRS; SLC16A5; human.
DR GenomeRNAi; 9121; -.
DR Pharos; O15375; Tdark.
DR PRO; PR:O15375; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; O15375; protein.
DR Bgee; ENSG00000170190; Expressed in metanephros cortex and 143 other tissues.
DR ExpressionAtlas; O15375; baseline and differential.
DR Genevisible; O15375; HS.
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:0016020; C:membrane; TAS:ProtInc.
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 Gene3D; 1.20.1250.20; -; 2.
DR InterPro; IPR004743; MCT.
DR InterPro; IPR030760; MCT6.
DR InterPro; IPR011701; MFS.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR036259; MFS_trans_sf.
DR PANTHER; PTHR11360:SF21; PTHR11360:SF21; 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 Alternative splicing; Cell membrane; Membrane; Reference proteome; Symport;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..505
FT /note="Monocarboxylate transporter 6"
FT /id="PRO_0000211399"
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..53
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 54..74
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 75..80
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 81..101
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 102..110
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 111..131
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 132..137
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 138..158
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 159..171
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 172..192
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 193..239
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 240..260
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 261..274
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 275..295
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 296..305
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 306..326
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 327..329
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 330..350
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 351..367
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 368..388
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 389..396
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 397..417
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 418..505
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 443..464
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1
FT /note="M -> MPRPTRGPLATSQGWCPSVTPGTWAAATLAVRPWQRRQQRM (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056660"
FT VAR_SEQ 456..505
FT /note="CQSSRQPRPAGVNKHLWGCPASSRTSHEWLLWPKAVLQAKQTALGWNSPT
FT -> YVTSV (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056661"
SQ SEQUENCE 505 AA; 54994 MW; E0F7B4BD607D2364 CRC64;
MPQALERADG SWAWVVLLAT MVTQGLTLGF PTCIGIFFTE LQWEFQASNS ETSWFPSILT
AVLHMAGPLC SILVGRFGCR VTVMLGGVLA SLGMVASSFS HNLSQLYFTA GFITGLGMCF
SFQSSITVLG FYFVRRRVLA NALASMGVSL GITLWPLLSR YLLENLGWRG TFLVFGGIFL
HCCICGAIIR PVATSVAPET KECPPPPPET PALGCLAACG RTIQRHLAFD ILRHNTGYCV
YILGVMWSVL GFPLPQVFLV PYAMWHSVDE QQAALLISII GFSNIFLRPL AGLMAGRPAF
ASHRKYLFSL ALLLNGLTNL VCAASGDFWV LVGYCLAYSV SMSGIGALIF QVLMDIVPMD
QFPRALGLFT VLDGLAFLIS PPLAGLLLDA TNNFSYVFYM SSFFLISAAL FMGGSFYALQ
KKEQGKQAVA ADALERDLFL EAKDGPGKQR SPEIMCQSSR QPRPAGVNKH LWGCPASSRT
SHEWLLWPKA VLQAKQTALG WNSPT
