MOT7_HUMAN
ID MOT7_HUMAN Reviewed; 523 AA.
AC O15403; Q6P1X3;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 2.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Monocarboxylate transporter 7;
DE Short=MCT 7;
DE AltName: Full=Monocarboxylate transporter 6;
DE Short=MCT 6;
DE AltName: Full=Solute carrier family 16 member 6;
GN Name=SLC16A6; Synonyms=MCT6, MCT7;
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], AND VARIANT ILE-204.
RC TISSUE=Blood;
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 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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-237 AND SER-240, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-237; SER-240 AND SER-247, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
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 O15403; O76024: WFS1; NbExp=3; IntAct=EBI-11041701, EBI-720609;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily.
CC Monocarboxylate porter (TC 2.A.1.13) family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC52014.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U79745; AAC52014.1; ALT_FRAME; mRNA.
DR EMBL; CH471099; EAW89052.1; -; Genomic_DNA.
DR EMBL; BC064832; AAH64832.1; -; mRNA.
DR CCDS; CCDS11675.1; -.
DR RefSeq; NP_001167637.1; NM_001174166.1.
DR RefSeq; NP_004685.2; NM_004694.4.
DR RefSeq; XP_011523763.1; XM_011525461.2.
DR RefSeq; XP_016880780.1; XM_017025291.1.
DR RefSeq; XP_016880781.1; XM_017025292.1.
DR AlphaFoldDB; O15403; -.
DR SMR; O15403; -.
DR BioGRID; 114568; 10.
DR IntAct; O15403; 11.
DR STRING; 9606.ENSP00000319991; -.
DR DrugBank; DB00119; Pyruvic acid.
DR TCDB; 2.A.1.13.15; the major facilitator superfamily (mfs).
DR iPTMnet; O15403; -.
DR PhosphoSitePlus; O15403; -.
DR BioMuta; SLC16A6; -.
DR jPOST; O15403; -.
DR MassIVE; O15403; -.
DR MaxQB; O15403; -.
DR PaxDb; O15403; -.
DR PeptideAtlas; O15403; -.
DR PRIDE; O15403; -.
DR ProteomicsDB; 48641; -.
DR Antibodypedia; 31766; 44 antibodies from 19 providers.
DR DNASU; 9120; -.
DR Ensembl; ENST00000327268.8; ENSP00000319991.4; ENSG00000108932.13.
DR Ensembl; ENST00000580666.6; ENSP00000462985.1; ENSG00000108932.13.
DR GeneID; 9120; -.
DR KEGG; hsa:9120; -.
DR MANE-Select; ENST00000580666.6; ENSP00000462985.1; NM_004694.5; NP_004685.2.
DR UCSC; uc002jgz.3; human.
DR CTD; 9120; -.
DR DisGeNET; 9120; -.
DR GeneCards; SLC16A6; -.
DR HGNC; HGNC:10927; SLC16A6.
DR HPA; ENSG00000108932; Tissue enhanced (choroid plexus, epididymis, retina).
DR MIM; 603880; gene.
DR neXtProt; NX_O15403; -.
DR OpenTargets; ENSG00000108932; -.
DR PharmGKB; PA35818; -.
DR VEuPathDB; HostDB:ENSG00000108932; -.
DR eggNOG; KOG2504; Eukaryota.
DR GeneTree; ENSGT00940000155575; -.
DR HOGENOM; CLU_001265_59_1_1; -.
DR InParanoid; O15403; -.
DR OMA; SNCFGHR; -.
DR OrthoDB; 515367at2759; -.
DR PhylomeDB; O15403; -.
DR TreeFam; TF313792; -.
DR PathwayCommons; O15403; -.
DR SignaLink; O15403; -.
DR BioGRID-ORCS; 9120; 11 hits in 1073 CRISPR screens.
DR ChiTaRS; SLC16A6; human.
DR GenomeRNAi; 9120; -.
DR Pharos; O15403; Tdark.
DR PRO; PR:O15403; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; O15403; protein.
DR Bgee; ENSG00000108932; Expressed in corpus epididymis and 164 other tissues.
DR ExpressionAtlas; O15403; baseline and differential.
DR Genevisible; O15403; 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; -; 1.
DR InterPro; IPR030766; MCT7.
DR InterPro; IPR011701; MFS.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR036259; MFS_trans_sf.
DR PANTHER; PTHR11360:SF20; PTHR11360:SF20; 1.
DR Pfam; PF07690; MFS_1; 1.
DR SUPFAM; SSF103473; SSF103473; 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..523
FT /note="Monocarboxylate transporter 7"
FT /id="PRO_0000211400"
FT TOPO_DOM 1..21
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 22..42
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 43..62
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 63..83
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 84..91
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 92..112
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 113..118
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 119..139
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 140..149
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 150..170
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 171..184
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 185..205
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 206..299
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 300..320
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 321..330
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 331..351
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 352..358
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 359..379
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 380..381
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 382..402
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 403..423
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 424..444
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 445..452
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 453..473
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 474..523
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOD_RES 234
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:B1AT66"
FT MOD_RES 237
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648"
FT MOD_RES 240
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648"
FT MOD_RES 247
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT VARIANT 121
FT /note="I -> T (in dbSNP:rs35397826)"
FT /id="VAR_053656"
FT VARIANT 204
FT /note="F -> I (in dbSNP:rs7222013)"
FT /evidence="ECO:0000269|PubMed:9425115"
FT /id="VAR_053657"
FT VARIANT 217
FT /note="E -> D (in dbSNP:rs3744307)"
FT /id="VAR_053658"
FT VARIANT 221
FT /note="E -> V (in dbSNP:rs4410141)"
FT /id="VAR_053659"
FT CONFLICT 481
FT /note="H -> R (in Ref. 1; AAC52014)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 523 AA; 57393 MW; 994FB5DCB9404340 CRC64;
MTQNKLKLCS KANVYTEVPD GGWGWAVAVS FFFVEVFTYG IIKTFGVFFN DLMDSFNESN
SRISWIISIC VFVLTFSAPL ATVLSNRFGH RLVVMLGGLL VSTGMVAASF SQEVSHMYVA
IGIISGLGYC FSFLPTVTIL SQYFGKRRSI VTAVASTGEC FAVFAFAPAI MALKERIGWR
YSLLFVGLLQ LNIVIFGALL RPIFIRGPAS PKIVIQENRK EAQYMLENEK TRTSIDSIDS
GVELTTSPKN VPTHTNLELE PKADMQQVLV KTSPRPSEKK APLLDFSILK EKSFICYALF
GLFATLGFFA PSLYIIPLGI SLGIDQDRAA FLLSTMAIAE VFGRIGAGFV LNREPIRKIY
IELICVILLT VSLFAFTFAT EFWGLMSCSI FFGFMVGTIG GTHIPLLAED DVVGIEKMSS
AAGVYIFIQS IAGLAGPPLA GLLVDQSKIY SRAFYSCAAG MALAAVCLAL VRPCKMGLCQ
HHHSGETKVV SHRGKTLQDI PEDFLEMDLA KNEHRVHVQM EPV
