ID   MOT5_HUMAN              Reviewed;         487 AA.
AC   O15374; A8K3V5; B2R9C9; B4DJ67; B4DPX7; E7EPY8; G3V175; Q5T612; Q8WU09;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   24-JAN-2024, entry version 170.
DE   RecName: Full=Monocarboxylate transporter 5;
DE            Short=MCT 5;
DE   AltName: Full=Monocarboxylate transporter 4;
DE            Short=MCT 4;
DE   AltName: Full=Solute carrier family 16 member 4;
GN   Name=SLC16A4; Synonyms=MCT4, MCT5;
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] (ISOFORMS 1; 2; 4 AND 5), AND
RP   VARIANT HIS-264.
RC   TISSUE=Lung, Mesangial cell, Placenta, and Substantia nigra;
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=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA   Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA   Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA   Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA   Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA   Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA   Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA   Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA   Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA   Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA   Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA   Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA   Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA   Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA   McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA   Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA   Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA   Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA   Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA   Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA   White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA   Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA   Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA   Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   TISSUE=Brain;
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       O15374-3; Q9BRK0: REEP2; NbExp=3; IntAct=EBI-12889748, EBI-11337973;
CC       O15374-3; Q96Q45-2: TMEM237; NbExp=3; IntAct=EBI-12889748, EBI-10982110;
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=5;
CC       Name=1;
CC         IsoId=O15374-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=O15374-2; Sequence=VSP_046242, VSP_046243;
CC       Name=3;
CC         IsoId=O15374-3; Sequence=VSP_046244;
CC       Name=4;
CC         IsoId=O15374-4; Sequence=VSP_046456, VSP_046458;
CC       Name=5;
CC         IsoId=O15374-5; Sequence=VSP_046457;
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; U59185; AAB72035.1; -; mRNA.
DR   EMBL; AK290720; BAF83409.1; -; mRNA.
DR   EMBL; AK295946; BAG58729.1; -; mRNA.
DR   EMBL; AK298539; BAG60739.1; -; mRNA.
DR   EMBL; AK313735; BAG36476.1; -; mRNA.
DR   EMBL; AL355488; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471122; EAW56443.1; -; Genomic_DNA.
DR   EMBL; CH471122; EAW56445.1; -; Genomic_DNA.
DR   EMBL; CH471122; EAW56446.1; -; Genomic_DNA.
DR   EMBL; BC021664; AAH21664.1; -; mRNA.
DR   CCDS; CCDS55621.1; -. [O15374-4]
DR   CCDS; CCDS55622.1; -. [O15374-2]
DR   CCDS; CCDS55623.1; -. [O15374-5]
DR   CCDS; CCDS55624.1; -. [O15374-3]
DR   CCDS; CCDS823.1; -. [O15374-1]
DR   RefSeq; NP_001188475.1; NM_001201546.1. [O15374-5]
DR   RefSeq; NP_001188476.1; NM_001201547.1. [O15374-2]
DR   RefSeq; NP_001188477.1; NM_001201548.1. [O15374-4]
DR   RefSeq; NP_001188478.1; NM_001201549.1. [O15374-3]
DR   RefSeq; NP_004687.1; NM_004696.2. [O15374-1]
DR   RefSeq; XP_005271374.1; XM_005271317.4. [O15374-1]
DR   AlphaFoldDB; O15374; -.
DR   SMR; O15374; -.
DR   BioGRID; 114570; 12.
DR   IntAct; O15374; 4.
DR   MINT; O15374; -.
DR   STRING; 9606.ENSP00000358794; -.
DR   DrugBank; DB00119; Pyruvic acid.
DR   TCDB; 2.A.1.13.7; the major facilitator superfamily (mfs).
DR   iPTMnet; O15374; -.
DR   PhosphoSitePlus; O15374; -.
DR   BioMuta; SLC16A4; -.
DR   jPOST; O15374; -.
DR   MassIVE; O15374; -.
DR   MaxQB; O15374; -.
DR   PaxDb; 9606-ENSP00000358794; -.
DR   PeptideAtlas; O15374; -.
DR   ProteomicsDB; 17467; -.
DR   ProteomicsDB; 32280; -.
DR   ProteomicsDB; 4352; -.
DR   ProteomicsDB; 48616; -. [O15374-1]
DR   ProteomicsDB; 74621; -.
DR   Antibodypedia; 20096; 157 antibodies from 24 providers.
DR   DNASU; 9122; -.
DR   Ensembl; ENST00000369779.9; ENSP00000358794.4; ENSG00000168679.18. [O15374-1]
DR   Ensembl; ENST00000369781.8; ENSP00000358796.4; ENSG00000168679.18. [O15374-3]
DR   Ensembl; ENST00000437429.6; ENSP00000394790.2; ENSG00000168679.18. [O15374-4]
DR   Ensembl; ENST00000472422.6; ENSP00000432495.1; ENSG00000168679.18. [O15374-5]
DR   Ensembl; ENST00000541986.5; ENSP00000446087.1; ENSG00000168679.18. [O15374-2]
DR   GeneID; 9122; -.
DR   KEGG; hsa:9122; -.
DR   MANE-Select; ENST00000369779.9; ENSP00000358794.4; NM_004696.3; NP_004687.1.
DR   UCSC; uc001dzo.3; human. [O15374-1]
DR   AGR; HGNC:10925; -.
DR   CTD; 9122; -.
DR   DisGeNET; 9122; -.
DR   GeneCards; SLC16A4; -.
DR   HGNC; HGNC:10925; SLC16A4.
DR   HPA; ENSG00000168679; Tissue enriched (kidney).
DR   MIM; 603878; gene.
DR   neXtProt; NX_O15374; -.
DR   OpenTargets; ENSG00000168679; -.
DR   PharmGKB; PA35816; -.
DR   VEuPathDB; HostDB:ENSG00000168679; -.
DR   eggNOG; KOG2504; Eukaryota.
DR   GeneTree; ENSGT00940000158411; -.
DR   HOGENOM; CLU_001265_59_2_1; -.
DR   InParanoid; O15374; -.
DR   OMA; CKTNGCF; -.
DR   OrthoDB; 1937075at2759; -.
DR   PhylomeDB; O15374; -.
DR   TreeFam; TF313792; -.
DR   PathwayCommons; O15374; -.
DR   SignaLink; O15374; -.
DR   SIGNOR; O15374; -.
DR   BioGRID-ORCS; 9122; 6 hits in 1156 CRISPR screens.
DR   ChiTaRS; SLC16A4; human.
DR   GeneWiki; SLC16A4; -.
DR   GenomeRNAi; 9122; -.
DR   Pharos; O15374; Tbio.
DR   PRO; PR:O15374; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   RNAct; O15374; Protein.
DR   Bgee; ENSG00000168679; Expressed in palpebral conjunctiva and 146 other cell types or tissues.
DR   ExpressionAtlas; O15374; baseline and differential.
DR   GO; GO:0016020; C:membrane; TAS:ProtInc.
DR   GO; GO:0005886; C:plasma 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   CDD; cd17421; MFS_MCT5; 1.
DR   Gene3D; 1.20.1250.20; MFS general substrate transporter like domains; 2.
DR   InterPro; IPR011701; MFS.
DR   InterPro; IPR020846; MFS_dom.
DR   InterPro; IPR036259; MFS_trans_sf.
DR   PANTHER; PTHR11360; MONOCARBOXYLATE TRANSPORTER; 1.
DR   PANTHER; PTHR11360:SF14; MONOCARBOXYLATE TRANSPORTER 5; 1.
DR   Pfam; PF07690; MFS_1; 1.
DR   SUPFAM; SSF103473; MFS general substrate transporter; 1.
DR   PROSITE; PS50850; MFS; 1.
DR   Genevisible; O15374; HS.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell membrane; Membrane; Reference proteome; Symport;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..487
FT                   /note="Monocarboxylate transporter 5"
FT                   /id="PRO_0000211398"
FT   TOPO_DOM        1..16
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        17..37
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        38..59
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        60..80
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        81..87
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        88..108
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        109
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        110..129
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        130..143
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        144..164
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        165..174
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        175..195
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        196..299
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        300..320
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        321..337
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        338..358
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        359..372
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        373..393
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        394
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        395..415
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        416..425
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        426..446
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        447..458
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        459..479
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        480..487
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          206..250
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        223..238
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         1..120
FT                   /note="MLKREGKVQPYTKTLDGGWGWMIVIHFFLVNVFVMGMTKTFAIFFVVFQEEF
FT                   EGTSEQIGWIGSIMSSLRFCAGPLVAIICDILGEKTTSILGAFVVTGGYLISSWATSIP
FT                   FLCVTMGLL -> MGMDDCDSFF (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_046456"
FT   VAR_SEQ         1..34
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_046242"
FT   VAR_SEQ         38..73
FT                   /note="TKTFAIFFVVFQEEFEGTSEQIGWIGSIMSSLRFCA -> DDCDSFFP (in
FT                   isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_046243"
FT   VAR_SEQ         74..121
FT                   /note="Missing (in isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_046457"
FT   VAR_SEQ         176..343
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_046244"
FT   VAR_SEQ         446..487
FT                   /note="GWLYDYTQTYNGSFYFSGICYLLSSVSFFFVPLAERWKNSLT -> EIIPSF
FT                   QAGYMIIPRHTMALSTSLAYAISSLQFPFFLYHWPKDGKTV (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_046458"
FT   VARIANT         185
FT                   /note="A -> T (in dbSNP:rs35157487)"
FT                   /id="VAR_053655"
FT   VARIANT         264
FT                   /note="N -> H (in dbSNP:rs2271885)"
FT                   /evidence="ECO:0000269|PubMed:14702039"
FT                   /id="VAR_020309"
FT   CONFLICT        25
FT                   /note="I -> V (in Ref. 2; BAF83409)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   487 AA;  54022 MW;  3CF236C69CC29631 CRC64;
     MLKREGKVQP YTKTLDGGWG WMIVIHFFLV NVFVMGMTKT FAIFFVVFQE EFEGTSEQIG
     WIGSIMSSLR FCAGPLVAII CDILGEKTTS ILGAFVVTGG YLISSWATSI PFLCVTMGLL
     PGLGSAFLYQ VAAVVTTKYF KKRLALSTAI ARSGMGLTFL LAPFTKFLID LYDWTGALIL
     FGAIALNLVP SSMLLRPIHI KSENNSGIKD KGSSLSAHGP EAHATETHCH ETEESTIKDS
     TTQKAGLPSK NLTVSQNQSE EFYNGPNRNR LLLKSDEESD KVISWSCKQL FDISLFRNPF
     FYIFTWSFLL SQLAYFIPTF HLVARAKTLG IDIMDASYLV SVAGILETVS QIISGWVADQ
     NWIKKYHYHK SYLILCGITN LLAPLATTFP LLMTYTICFA IFAGGYLALI LPVLVDLCRN
     STVNRFLGLA SFFAGMAVLS GPPIAGWLYD YTQTYNGSFY FSGICYLLSS VSFFFVPLAE
     RWKNSLT
//