MOT1_CRILO
ID MOT1_CRILO Reviewed; 494 AA.
AC Q03064;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 25-MAY-2022, entry version 99.
DE RecName: Full=Monocarboxylate transporter 1;
DE Short=MCT 1;
DE AltName: Full=Solute carrier family 16 member 1;
GN Name=SLC16A1; Synonyms=MCT1;
OS Cricetulus longicaudatus (Long-tailed dwarf hamster) (Chinese hamster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Cricetulus.
OX NCBI_TaxID=10030;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Ovary;
RX PubMed=8124722; DOI=10.1016/0092-8674(94)90361-1;
RA Garcia C.K., Goldstein J.L., Pathak R.K., Anderson R.G.W., Brown M.S.;
RT "Molecular characterization of a membrane transporter for lactate,
RT pyruvate, and other monocarboxylates: implications for the Cori cycle.";
RL Cell 76:865-873(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], MUTAGENESIS OF PHE-360, FUNCTION, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Ovary;
RX PubMed=1429658; DOI=10.1016/s0021-9258(18)50064-8;
RA Kim C.M., Goldstein J.L., Brown M.S.;
RT "cDNA cloning of MEV, a mutant protein that facilitates cellular uptake of
RT mevalonate, and identification of the point mutation responsible for its
RT gain of function.";
RL J. Biol. Chem. 267:23113-23121(1992).
RN [3]
RP LACK OF GLYCOSYLATION AT ASN-52.
RX PubMed=8603082; DOI=10.1016/0005-2736(95)00254-5;
RA Carpenter L., Poole R.C., Halestrap A.P.;
RT "Cloning and sequencing of the monocarboxylate transporter from mouse
RT Ehrlich Lettre tumour cell confirms its identity as MCT1 and demonstrates
RT that glycosylation is not required for MCT1 function.";
RL Biochim. Biophys. Acta 1279:157-163(1996).
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. Depending on the tissue and on
CC cicumstances, mediates the import or export of lactic acid and ketone
CC bodies. Required for normal nutrient assimilation, increase of white
CC adipose tissue and body weight gain when on a high-fat diet. Plays a
CC role in cellular responses to a high-fat diet by modulating the
CC cellular levels of lactate and pyruvate, small molecules that
CC contribute to the regulation of central metabolic pathways and insulin
CC secretion, with concomitant effects on plasma insulin levels and blood
CC glucose homeostasis. {ECO:0000269|PubMed:1429658,
CC ECO:0000269|PubMed:8124722}.
CC -!- SUBUNIT: Interacts with BSG; interaction mediates SLC16A1 targeting to
CC the plasma membrane (By similarity). Interacts with EMB; interaction
CC mediates SLC16A1 targeting to the plasma membrane (By similarity).
CC {ECO:0000250|UniProtKB:P53985, ECO:0000250|UniProtKB:P53987}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:1429658,
CC ECO:0000269|PubMed:8124722}; Multi-pass membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed at abundant levels in erythrocytes,
CC cardiac muscle, basolateral intestinal epithelium, skeletal muscle
CC myocytes, testis and at low levels in liver. In the stomach and in the
CC proximal tubules of the kidney, present on the basolateral surfaces of
CC epithelial cells. Expressed on sperm heads in the testis and proximal
CC epididymis. In the distal epididymis, it disappeared from sperm and
CC appeared on the microvillar surface of the lining epithelium. Also
CC expressed in lung, cecum and eye. {ECO:0000269|PubMed:1429658,
CC ECO:0000269|PubMed:8124722}.
CC -!- PTM: Not glycosylated.
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; M97382; AAB59630.1; -; mRNA.
DR EMBL; L25842; AAB59731.1; -; mRNA.
DR PIR; A44458; A44458.
DR AlphaFoldDB; Q03064; -.
DR SMR; Q03064; -.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0015129; F:lactate transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0015293; F:symporter activity; IEA:UniProtKB-KW.
DR GO; GO:0035879; P:plasma membrane lactate transport; ISS:UniProtKB.
DR Gene3D; 1.20.1250.20; -; 1.
DR InterPro; IPR004743; MCT.
DR InterPro; IPR030757; MCT1.
DR InterPro; IPR011701; MFS.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR036259; MFS_trans_sf.
DR PANTHER; PTHR11360:SF24; PTHR11360:SF24; 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; Phosphoprotein; Symport; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..494
FT /note="Monocarboxylate transporter 1"
FT /id="PRO_0000211380"
FT TOPO_DOM 1..15
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 16..36
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 37..59
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 60..80
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 81..86
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 87..107
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 108..111
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 112..132
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 133..143
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 144..164
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 165..166
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 167..187
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 188..255
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 256..276
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 277..291
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 292..312
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 313..321
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 322..342
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 343..346
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 347..367
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 368..382
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 383..403
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 404..415
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 416..436
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 437..494
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 447..494
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 447..474
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 475..494
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 52
FT /note="Not glycosylated"
FT /evidence="ECO:0000269|PubMed:8603082"
FT MOD_RES 210
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P53986"
FT MOD_RES 213
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P53985"
FT MOD_RES 220
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P53986"
FT MOD_RES 224
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P53986"
FT MOD_RES 230
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P53986"
FT MOD_RES 461
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P53985"
FT MOD_RES 462
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P53985"
FT MOD_RES 463
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P53986"
FT MOD_RES 478
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P53985"
FT MOD_RES 483
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P53986"
FT MOD_RES 484
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P53986"
FT MOD_RES 492
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P53985"
FT MUTAGEN 360
FT /note="F->C: Gain of function as mevalonate transporter."
FT /evidence="ECO:0000269|PubMed:1429658"
SQ SEQUENCE 494 AA; 53173 MW; D77C4A4023684318 CRC64;
MPPAIGGPVG YTPPDGGWGW AVVVGAFISI GFSYAFPKSI TVFFKEIEGI FNATTSEVSW
ISSIMLAVMY AGGPISSVLV NKYGSRPVMI AGGCLSGCGL IAASFCNTVQ ELYLCIGVIG
GLGLAFNLNP ALTMIGKYFY KKRPLANGLA MAGSPVFLST LAPLNQAFFG IFGWRGSFLI
LGGLLLNCCV AGSLMRPIGP KPGKIEKLKS KESLQEAGKS EANTDLMGGS PKGEKRSVLQ
TINKFLDLSL FAHRGFLLYL SGNVVMFFGL FTPLVFLSNY GKSQHYSSEK SAFLLSILAF
VDMVARPSMG LAANTKWIRP RIQYFFAASV VANGVCHLLA PLSTSYIGFC IYAGVFGFAF
GWLSSVLFET LMDLVGPQRF SSAVGLVTIV ECCPVLLGPP LLGRLNDMYG DYKYTYWACG
VILIIAGIYL FIGMGINYRL VAKEQKAEEK QKQEEGKEDD TSTDVDEKPK ELTKATESPQ
QNSSGDPAEE ESPV
