MOT7_MOUSE
ID MOT7_MOUSE Reviewed; 607 AA.
AC B1AT66; D3Z3P6; E9Q5J8; Q3TCY8; Q8C086; Q91W47;
DT 21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 101.
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=Mct7;
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 [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Medulla oblongata;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Eye;
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-319; SER-322 AND SER-325, AND
RP IDENTIFICATION BY 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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=B1AT66-1; Sequence=Displayed;
CC Name=2;
CC IsoId=B1AT66-2; Sequence=VSP_042512;
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; AK032026; BAC27657.1; -; mRNA.
DR EMBL; AK170472; BAE41817.1; -; mRNA.
DR EMBL; AL645791; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466558; EDL34359.1; -; Genomic_DNA.
DR EMBL; CH466558; EDL34361.1; -; Genomic_DNA.
DR EMBL; BC017129; AAH17129.1; -; mRNA.
DR CCDS; CCDS25580.1; -. [B1AT66-1]
DR CCDS; CCDS36360.1; -. [B1AT66-2]
DR RefSeq; NP_001025013.1; NM_001029842.1. [B1AT66-1]
DR RefSeq; NP_598799.1; NM_134038.2. [B1AT66-2]
DR RefSeq; XP_006532010.1; XM_006531947.2.
DR AlphaFoldDB; B1AT66; -.
DR SMR; B1AT66; -.
DR STRING; 10090.ENSMUSP00000065628; -.
DR iPTMnet; B1AT66; -.
DR PhosphoSitePlus; B1AT66; -.
DR SwissPalm; B1AT66; -.
DR EPD; B1AT66; -.
DR MaxQB; B1AT66; -.
DR PaxDb; B1AT66; -.
DR PeptideAtlas; B1AT66; -.
DR PRIDE; B1AT66; -.
DR ProteomicsDB; 290281; -. [B1AT66-1]
DR ProteomicsDB; 290282; -. [B1AT66-2]
DR Antibodypedia; 31766; 44 antibodies from 19 providers.
DR DNASU; 104681; -.
DR Ensembl; ENSMUST00000070152; ENSMUSP00000065628; ENSMUSG00000041920. [B1AT66-1]
DR Ensembl; ENSMUST00000070872; ENSMUSP00000067423; ENSMUSG00000041920. [B1AT66-2]
DR GeneID; 104681; -.
DR KEGG; mmu:104681; -.
DR UCSC; uc007mcl.1; mouse. [B1AT66-1]
DR CTD; 9120; -.
DR MGI; MGI:2144585; Slc16a6.
DR VEuPathDB; HostDB:ENSMUSG00000041920; -.
DR eggNOG; KOG2504; Eukaryota.
DR GeneTree; ENSGT00940000155575; -.
DR HOGENOM; CLU_001265_59_1_1; -.
DR InParanoid; B1AT66; -.
DR OMA; SNCFGHR; -.
DR OrthoDB; 916876at2759; -.
DR PhylomeDB; B1AT66; -.
DR TreeFam; TF313792; -.
DR BioGRID-ORCS; 104681; 0 hits in 75 CRISPR screens.
DR ChiTaRS; Slc16a6; mouse.
DR PRO; PR:B1AT66; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; B1AT66; protein.
DR Bgee; ENSMUSG00000041920; Expressed in retinal neural layer and 226 other tissues.
DR ExpressionAtlas; B1AT66; baseline and differential.
DR Genevisible; B1AT66; 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: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 Alternative splicing; Cell membrane; Membrane; Phosphoprotein;
KW Reference proteome; Symport; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..607
FT /note="Monocarboxylate transporter 7"
FT /id="PRO_0000416126"
FT TOPO_DOM 1..105
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 106..126
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 127..146
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 147..167
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 168..175
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 176..196
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 197..202
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 203..223
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 224..233
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 234..254
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 255..268
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 269..289
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 290..383
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 384..404
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 405..414
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 415..435
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 436..442
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 443..463
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 464..465
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 466..486
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 487..507
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 508..528
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 529..536
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 537..557
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 558..607
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 319
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 322
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 325
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 332
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15403"
FT VAR_SEQ 1..84
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_042512"
FT CONFLICT 37
FT /note="A -> T (in Ref. 1; BAC27657)"
FT /evidence="ECO:0000305"
FT CONFLICT 243
FT /note="E -> D (in Ref. 1; BAC27657)"
FT /evidence="ECO:0000305"
FT CONFLICT 302
FT /note="E -> K (in Ref. 1; BAE41817)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 607 AA; 66236 MW; ED0E45D224D7587B CRC64;
MRASGQGPQR RRRGWATRDD SAVTFRDPQP RQPAGGARAL RGPDPRGPAR AHQAGPLLAG
ARRSQHMVGG APPRPAETGC SRSRMTQKNS KLCARANVYT QVPDGGWGWA VAVSFFFVEV
FTYGIIKSFG VFFNDLMDSF DESNSKISWI ISICVFVLTF TAPLSTVLSN RFGHRLVVMA
GGLLISLGMI TASFSQRVYH MYISIGVISG LGYCFSFLPT VTILSQYFDK RRSVVTAVAS
TGECFAVFAF APAITALKEH IGWRYSLLFV GLLQLNIMVC GALLRPIIIQ GPGQSPKAVT
LEPRREVQYM LENEKTRTSI DSIDSGVELT TSPKNVPSEA KMEQETRAEQ QQTLVTAPKH
SQMKAPLLDF SVLKEKSFIC YALFGLFATL GFFAPSLYII PLGISLGIDP DRAAFLLSTM
AIAEVFGRIG AGFVLNREPI RKIYIELICV ILLTASLFAF TFATEFWGLM LCSVFFGSMV
GTIGGTHIPM LAEDDVVGIE KMSSAAGVYV FIQSISGLAG PPLAGLLVDQ SKIYSRAFYS
CAAGMCLAAV CLALVRPCKK GLCQNSHSGE NQTDRQRGKA LQDIPEDFLE MDLGKCEHRA
HMKMDPV
