MOT8_RAT
ID MOT8_RAT Reviewed; 545 AA.
AC Q8K1P8;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 25-MAY-2022, entry version 109.
DE RecName: Full=Monocarboxylate transporter 8;
DE Short=MCT 8;
DE AltName: Full=Solute carrier family 16 member 2;
GN Name=SLC16A2; Synonyms=Mct8;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=12871948; DOI=10.1074/jbc.m300909200;
RA Friesema E.C.H., Ganguly S., Abdalla A., Manning Fox J.E., Halestrap A.P.,
RA Visser T.J.;
RT "Identification of monocarboxylate transporter 8 as a specific thyroid
RT hormone transporter.";
RL J. Biol. Chem. 278:40128-40135(2003).
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:0000269|PubMed:12871948}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=4.0 uM for T3 (at 25 degrees Celsius)
CC {ECO:0000269|PubMed:12871948};
CC KM=2.2 uM for rT3 (at 25 degrees Celsius)
CC {ECO:0000269|PubMed:12871948};
CC KM=4.7 uM for T4 (at 25 degrees Celsius)
CC {ECO:0000269|PubMed:12871948};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P36021}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12871948};
CC Multi-pass membrane protein {ECO:0000269|PubMed:12871948}.
CC -!- TISSUE SPECIFICITY: Expressed at highest levels in liver, lower levels
CC in brain, kidney and heart (at protein level).
CC {ECO:0000269|PubMed:12871948}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily.
CC Monocarboxylate porter (TC 2.A.1.13) family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJ496570; CAD43059.1; -; mRNA.
DR RefSeq; NP_671749.1; NM_147216.1.
DR AlphaFoldDB; Q8K1P8; -.
DR SMR; Q8K1P8; -.
DR STRING; 10116.ENSRNOP00000042040; -.
DR ChEMBL; CHEMBL2073720; -.
DR PhosphoSitePlus; Q8K1P8; -.
DR PaxDb; Q8K1P8; -.
DR GeneID; 259248; -.
DR KEGG; rno:259248; -.
DR UCSC; RGD:628608; rat.
DR CTD; 6567; -.
DR RGD; 628608; Slc16a2.
DR eggNOG; KOG2504; Eukaryota.
DR InParanoid; Q8K1P8; -.
DR OrthoDB; 916876at2759; -.
DR PhylomeDB; Q8K1P8; -.
DR Reactome; R-RNO-879518; Transport of organic anions.
DR SABIO-RK; Q8K1P8; -.
DR PRO; PR:Q8K1P8; -.
DR Proteomes; UP000002494; Unplaced.
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; IDA:ARUK-UCL.
DR GO; GO:0015171; F:amino acid transmembrane transporter activity; ISO:RGD.
DR GO; GO:0015293; F:symporter activity; IEA:UniProtKB-KW.
DR GO; GO:0015349; F:thyroid hormone transmembrane transporter activity; IMP:RGD.
DR GO; GO:0089718; P:amino acid import across plasma membrane; ISO:RGD.
DR GO; GO:0006520; P:cellular amino acid metabolic process; ISO:RGD.
DR GO; GO:0009914; P:hormone transport; IMP:RGD.
DR GO; GO:2000178; P:negative regulation of neural precursor cell proliferation; ISO:RGD.
DR GO; GO:0006590; P:thyroid hormone generation; ISO:RGD.
DR GO; GO:0042403; P:thyroid hormone metabolic process; ISO:RGD.
DR GO; GO:0070327; P:thyroid hormone transport; ISS:UniProtKB.
DR GO; GO:0070460; P:thyroid-stimulating hormone secretion; ISO:RGD.
DR GO; GO:0150104; P:transport across blood-brain barrier; ISO:RGD.
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_0000247988"
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..181
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 182..202
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 203..204
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 205..225
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 226..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:0000250|UniProtKB:O70324"
SQ SEQUENCE 545 AA; 60118 MW; 74EF7A3DCB9F0DE3 CRC64;
MALPSPASEE AEGPCQEANQ EYQEPVCSPV PEPEPEPEPE PEPEPEPVPV PPPEPQPEPE
PQPLPDPAPL PVLGFEAEPV QEPEPTPTVE TRGTARGFQP PEGGFGWIVV FAATWCNGSI
FGIHNSVGIL YSMLLEEEKE KNRQVEFQAA WVGALAMGMI FFCSPIVSIF TDRLGCRITA
TTGAAVAFIG LHTSSFTSPL SLRYFTYGIL FGCGCSFAFQ PSLVILDHYF QRRLGLANGV
VSAGSSIFSM SFPFLIKMLG DRIKLAQTFQ VLSTFMFVLT LLSLTYRPLL PSSQDTPSKR
GAHTLRQRFL VQFRKYFNMR VFRQRTYRIW AFGIAAAALG YFVPYVHLMK YVEDKFKEIK
ETWVLLVCIG ATSGLGRLVS GHISDSIPGL KKIYLQVLSF LLLGLMSMMI PLCRDFGGLI
VVCLFLGLCD GFFITIMAPI AFELVGPMQA SQAIGYLLGM MALPMIAGPP IAGLLRNCFG
NYHVAFYFAG VPPIIGAVIL FFVPLMHQRM FKKEQRESSK DKMLSHDPDP NGELLPGSPT
PEEPI
