MOT2_MOUSE
ID MOT2_MOUSE Reviewed; 484 AA.
AC O70451;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Monocarboxylate transporter 2;
DE Short=MCT 2;
DE AltName: Full=Solute carrier family 16 member 7;
GN Name=Slc16a7; Synonyms=Mct2;
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 [MRNA].
RC STRAIN=129; TISSUE=Kidney;
RX PubMed=9725820; DOI=10.1152/ajpendo.1998.275.3.e516;
RA Koehler-Stec E.M., Simpson I.A., Vannucci S.J., Landschulz K.T.,
RA Landschulz W.H.;
RT "Monocarboxylate transporter expression in mouse brain.";
RL Am. J. Physiol. 275:E516-E524(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Testis;
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 [3]
RP INTERACTION WITH GRID2IP.
RX PubMed=17496809; DOI=10.1097/wnr.0b013e3280586821;
RA Watanabe-Kaneko K., Sonoda T., Miyagi Y., Yamashita T., Okuda K.,
RA Kawamoto S.;
RT "The synaptic scaffolding protein Delphilin interacts with monocarboxylate
RT transporter 2.";
RL NeuroReport 18:489-493(2007).
RN [4]
RP INTERACTION WITH BSG, TISSUE SPECIFICITY, AND FUNCTION.
RX PubMed=21792931; DOI=10.1002/jcp.22949;
RA Mannowetz N., Wandernoth P., Wennemuth G.;
RT "Basigin interacts with both MCT1 and MCT2 in murine spermatozoa.";
RL J. Cell. Physiol. 227:2154-2162(2012).
CC -!- FUNCTION: Proton-coupled 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. Functions as high-affinity pyruvate
CC transporter. {ECO:0000269|PubMed:21792931}.
CC -!- SUBUNIT: Interacts with GRID2IP (PubMed:17496809). Interacts with
CC isoform 2 of BSG (PubMed:21792931). Interacts with EMB (By similarity).
CC {ECO:0000250|UniProtKB:Q63344, ECO:0000269|PubMed:17496809,
CC ECO:0000269|PubMed:21792931}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Detected in testis and in spermatozoa (at protein
CC level). {ECO:0000269|PubMed:21792931}.
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; AF058054; AAC13719.1; -; mRNA.
DR EMBL; AK076612; BAC36415.1; -; mRNA.
DR CCDS; CCDS24218.1; -.
DR RefSeq; NP_035521.1; NM_011391.1.
DR RefSeq; XP_006513469.1; XM_006513406.3.
DR RefSeq; XP_006513471.1; XM_006513408.3.
DR RefSeq; XP_006513472.1; XM_006513409.3.
DR RefSeq; XP_006513473.1; XM_006513410.3.
DR RefSeq; XP_006513474.1; XM_006513411.1.
DR RefSeq; XP_006513475.1; XM_006513412.3.
DR RefSeq; XP_006513476.1; XM_006513413.3.
DR RefSeq; XP_017169350.1; XM_017313861.1.
DR AlphaFoldDB; O70451; -.
DR SMR; O70451; -.
DR STRING; 10090.ENSMUSP00000065433; -.
DR iPTMnet; O70451; -.
DR PhosphoSitePlus; O70451; -.
DR jPOST; O70451; -.
DR PaxDb; O70451; -.
DR PRIDE; O70451; -.
DR ProteomicsDB; 252596; -.
DR Antibodypedia; 1576; 256 antibodies from 36 providers.
DR DNASU; 20503; -.
DR Ensembl; ENSMUST00000063318; ENSMUSP00000065433; ENSMUSG00000020102.
DR Ensembl; ENSMUST00000105257; ENSMUSP00000100892; ENSMUSG00000020102.
DR Ensembl; ENSMUST00000210780; ENSMUSP00000147560; ENSMUSG00000020102.
DR Ensembl; ENSMUST00000211781; ENSMUSP00000147968; ENSMUSG00000020102.
DR GeneID; 20503; -.
DR KEGG; mmu:20503; -.
DR UCSC; uc007hgx.1; mouse.
DR CTD; 9194; -.
DR MGI; MGI:1330284; Slc16a7.
DR VEuPathDB; HostDB:ENSMUSG00000020102; -.
DR eggNOG; KOG2504; Eukaryota.
DR GeneTree; ENSGT00940000157309; -.
DR HOGENOM; CLU_001265_59_1_1; -.
DR InParanoid; O70451; -.
DR OMA; ALNWPVR; -.
DR OrthoDB; 916876at2759; -.
DR PhylomeDB; O70451; -.
DR TreeFam; TF313792; -.
DR Reactome; R-MMU-433692; Proton-coupled monocarboxylate transport.
DR BioGRID-ORCS; 20503; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Slc16a7; mouse.
DR PRO; PR:O70451; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; O70451; protein.
DR Bgee; ENSMUSG00000020102; Expressed in spermatid and 233 other tissues.
DR ExpressionAtlas; O70451; baseline and differential.
DR Genevisible; O70451; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
DR GO; GO:0098686; C:hippocampal mossy fiber to CA3 synapse; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0099061; C:integral component of postsynaptic density membrane; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0098688; C:parallel fiber to Purkinje cell synapse; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; ISO:MGI.
DR GO; GO:0015129; F:lactate transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0008028; F:monocarboxylic acid transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0050833; F:pyruvate transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0015293; F:symporter activity; IEA:UniProtKB-KW.
DR GO; GO:0035873; P:lactate transmembrane transport; ISS:UniProtKB.
DR GO; GO:0015718; P:monocarboxylic acid transport; IBA:GO_Central.
DR GO; GO:0035879; P:plasma membrane lactate transport; ISO:MGI.
DR GO; GO:1901475; P:pyruvate transmembrane transport; ISS:UniProtKB.
DR Gene3D; 1.20.1250.20; -; 1.
DR InterPro; IPR004743; MCT.
DR InterPro; IPR027178; MCT2.
DR InterPro; IPR011701; MFS.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR036259; MFS_trans_sf.
DR PANTHER; PTHR11360:SF25; PTHR11360:SF25; 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 Cell membrane; Membrane; Reference proteome; Symport; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..484
FT /note="Monocarboxylate transporter 2"
FT /id="PRO_0000211388"
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..60
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 61..81
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 82..90
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 91..111
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 112..116
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 117..137
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 138..149
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 150..170
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 171..174
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 175..195
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 196..245
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 246..266
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 267..281
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 282..302
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 303..311
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 312..332
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 333..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..405
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 406..426
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 427..484
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 438..484
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 445..461
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 484 AA; 52604 MW; A23B62BCA4C5DF5E CRC64;
MPSEPSAPLP QPLPPDGGWG WVVVCASFIS IGFSYAFPKA VTVFFKDIQE IFNTTSSQIA
WISSIMLAVM YAGGPISSVL VNNYGSRPVV IVGGLLCCIG MILASYSNSV IELYLTVGFI
GGLGLAFNLQ PALTIIGKYF YRRRPLANGC AMAGSPVFLS TLAPFNQYLF NNYGWKGSFL
ILGGIFLHSC VAGCLMRPVG PSPNTKKSKS KVGSRHDSTL KKASKVSTAQ KVNRFLDFSL
FMHRGFLIYL SGNVILFLGI FAPIIFLAQY AKHIGVDDYN SAFLLSVMAF IDMFARPSVG
LIANTSLIRP RIQYLFSSAI IFTGICHLLC PLATTYSALV VYVVFFGLGF GSISSLLFEC
LMDIVGATRF SSAVGLTTIV ECCPVLFGPP LAGKLLDITG EYKYLYIASG TVVLVSGTYL
LIGNAINYRL LDKERKREKA KKKKSASHAS REMEALNRSK QDEVTVKASN AHNPPSDRDK
ESNI
