MOT8_MOUSE
ID MOT8_MOUSE Reviewed; 545 AA.
AC O70324; Q8K3S9;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 2.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Monocarboxylate transporter 8;
DE Short=MCT 8;
DE AltName: Full=Solute carrier family 16 member 2;
DE AltName: Full=X-linked PEST-containing transporter;
GN Name=Slc16a2; Synonyms=Mct8, Xpct;
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=BALB/cJ; TISSUE=Liver;
RX PubMed=9545634; DOI=10.1006/geno.1997.5173;
RA Debrand E., Heard E., Avner P.;
RT "Cloning and localization of the murine Xpct gene: evidence for complex
RT rearrangements during the evolution of the region around the Xist gene.";
RL Genomics 48:296-303(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/Sv;
RX PubMed=12045143; DOI=10.1101/gr.152902;
RA Chureau C., Prissette M., Bourdet A., Barbe V., Cattolico L., Jones L.,
RA Eggen A., Avner P., Duret L.;
RT "Comparative sequence analysis of the X-inactivation center region in
RT mouse, human and bovine.";
RL Genome Res. 12:894-908(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Olfactory epithelium;
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 THR-540, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, and Kidney;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Very active and specific thyroid hormone transporter.
CC Stimulates cellular uptake of thyroxine (T4), triiodothyronine (T3),
CC reverse triiodothyronine (rT3) and diidothyronine. Does not transport
CC Leu, Phe, Trp or Tyr. {ECO:0000250|UniProtKB:Q8K1P8}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P36021}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q8K1P8};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:Q8K1P8}.
CC -!- TISSUE SPECIFICITY: Highly expressed in liver and 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; AF045692; AAC40078.1; -; mRNA.
DR EMBL; AJ421478; CAD33931.1; -; Genomic_DNA.
DR EMBL; BC080678; AAH80678.1; -; mRNA.
DR CCDS; CCDS30330.1; -.
DR RefSeq; NP_033223.2; NM_009197.2.
DR AlphaFoldDB; O70324; -.
DR SMR; O70324; -.
DR STRING; 10090.ENSMUSP00000037629; -.
DR TCDB; 2.A.1.13.3; the major facilitator superfamily (mfs).
DR iPTMnet; O70324; -.
DR PhosphoSitePlus; O70324; -.
DR jPOST; O70324; -.
DR PaxDb; O70324; -.
DR PeptideAtlas; O70324; -.
DR PRIDE; O70324; -.
DR ProteomicsDB; 291388; -.
DR Antibodypedia; 522; 185 antibodies from 30 providers.
DR DNASU; 20502; -.
DR Ensembl; ENSMUST00000042664; ENSMUSP00000037629; ENSMUSG00000033965.
DR GeneID; 20502; -.
DR KEGG; mmu:20502; -.
DR UCSC; uc009tzy.1; mouse.
DR CTD; 6567; -.
DR MGI; MGI:1203732; Slc16a2.
DR VEuPathDB; HostDB:ENSMUSG00000033965; -.
DR eggNOG; KOG2504; Eukaryota.
DR GeneTree; ENSGT00940000159450; -.
DR HOGENOM; CLU_001265_59_5_1; -.
DR InParanoid; O70324; -.
DR OMA; EFKTAWV; -.
DR OrthoDB; 916876at2759; -.
DR PhylomeDB; O70324; -.
DR TreeFam; TF313792; -.
DR Reactome; R-MMU-879518; Transport of organic anions.
DR BioGRID-ORCS; 20502; 5 hits in 73 CRISPR screens.
DR ChiTaRS; Slc16a2; mouse.
DR PRO; PR:O70324; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; O70324; protein.
DR Bgee; ENSMUSG00000033965; Expressed in choroid plexus of fourth ventricle and 222 other tissues.
DR ExpressionAtlas; O70324; baseline and differential.
DR Genevisible; O70324; MM.
DR GO; GO:0016324; C:apical plasma membrane; IDA:ARUK-UCL.
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:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0015171; F:amino acid transmembrane transporter activity; ISO:MGI.
DR GO; GO:0015293; F:symporter activity; IEA:UniProtKB-KW.
DR GO; GO:0015349; F:thyroid hormone transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0089718; P:amino acid import across plasma membrane; ISO:MGI.
DR GO; GO:0006520; P:cellular amino acid metabolic process; ISO:MGI.
DR GO; GO:0009914; P:hormone transport; ISO:MGI.
DR GO; GO:2000178; P:negative regulation of neural precursor cell proliferation; ISO:MGI.
DR GO; GO:0006590; P:thyroid hormone generation; IMP:MGI.
DR GO; GO:0042403; P:thyroid hormone metabolic process; ISO:MGI.
DR GO; GO:0070327; P:thyroid hormone transport; IMP:MGI.
DR GO; GO:0070460; P:thyroid-stimulating hormone secretion; IMP:MGI.
DR GO; GO:0150104; P:transport across blood-brain barrier; ISO:MGI.
DR Gene3D; 1.20.1250.20; -; 2.
DR InterPro; IPR030761; MCT8.
DR InterPro; IPR011701; MFS.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR036259; MFS_trans_sf.
DR PANTHER; PTHR11360:SF123; PTHR11360:SF123; 1.
DR Pfam; PF07690; MFS_1; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
DR PROSITE; PS50850; MFS; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cell membrane; Membrane; Phosphoprotein; Reference proteome;
KW Repeat; Symport; Transmembrane; Transmembrane helix; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P36021"
FT CHAIN 2..545
FT /note="Monocarboxylate transporter 8"
FT /id="PRO_0000211402"
FT TOPO_DOM 2..102
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 103..123
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 124..149
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 150..170
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 171..177
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 178..198
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 199..206
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 207..227
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 228..235
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 236..256
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 257..264
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 265..285
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 286..328
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 329..349
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 350..362
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 363..383
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 384..392
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 393..413
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 414..415
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 416..436
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 437..453
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 454..474
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 475..483
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 484..504
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 505..545
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 29..50
FT /note="1"
FT REPEAT 51..72
FT /note="2"
FT REGION 1..98
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 29..72
FT /note="2 X 22 AA approximate tandem repeats"
FT REGION 514..545
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 44..72
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 514..528
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P36021"
FT MOD_RES 540
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 62
FT /note="Q -> QPLPDPAPLPELGFEAEPEPQ (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 227
FT /note="G -> D (in Ref. 1; AAC40078)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 545 AA; 60025 MW; ACCC7EC6B902A6DE CRC64;
MALPSPASEE AEGPCQEANQ EYQEPVCSPV PEPEPEPEPE PEPDPEPVPV PPPEPQPEPE
PQPLPDPAPL PELGFEAEPV QEPEPTPTVE TRGTARGFQP PEGGFGWIVV FAATWCNGSI
FGIHNSVGIL YSMLLEEEKE KNRQVEFQAA WVGALAMGMI FFCSPIVSIF TDRLGCRITA
TTGAAVAFIG LHTSSFTSSL SLRYFTYGIL FGCGCSFAFQ PSLVILGHYF QRRLGLANGV
VSAGSSIFSM SFPFLIKMLG DKIKLAQTFQ VLSTFMFVLT LLSLTYRPLL PSSQDTPSKR
GAHTLRQRFL VQFRKYFNMR VFRQRTYRIW AFGIAAAALG YFVPYVHLMK YVEDKFKEIK
ETWVLLVCIG ATSGLGRLVS GHISDSIPGL KKIYLQVLSF LLLGLMSMMI PLCRDFGGLI
VVCLFLGLCD GFFITIMAPI AFELVGPMQA SQAIGYLLGM MALPMIAGPP IAGLLRNCFG
DYHVAFYFAG VPPIIGAVIL FFVPLMHQRM FKKEQRDSSK DKMLSHDPDP NGELLPGSPT
PEEPI
