MOT1_BOVIN
ID MOT1_BOVIN Reviewed; 501 AA.
AC Q3MHW6;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 2.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Monocarboxylate transporter 1;
DE Short=MCT 1;
DE AltName: Full=Solute carrier family 16 member 1;
GN Name=SLC16A1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Ascending colon;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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 (By similarity). {ECO:0000250}.
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:0000250|UniProtKB:P53985};
CC Multi-pass membrane protein {ECO:0000255}.
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; BC104598; AAI04599.2; -; mRNA.
DR RefSeq; NP_001032396.1; NM_001037319.1.
DR RefSeq; XP_015319143.1; XM_015463657.1.
DR AlphaFoldDB; Q3MHW6; -.
DR SMR; Q3MHW6; -.
DR STRING; 9913.ENSBTAP00000020102; -.
DR PaxDb; Q3MHW6; -.
DR PeptideAtlas; Q3MHW6; -.
DR PRIDE; Q3MHW6; -.
DR Ensembl; ENSBTAT00000020102; ENSBTAP00000020102; ENSBTAG00000015107.
DR GeneID; 505775; -.
DR KEGG; bta:505775; -.
DR CTD; 6566; -.
DR VEuPathDB; HostDB:ENSBTAG00000015107; -.
DR VGNC; VGNC:34683; SLC16A1.
DR eggNOG; KOG2504; Eukaryota.
DR GeneTree; ENSGT00940000154955; -.
DR HOGENOM; CLU_001265_59_1_1; -.
DR InParanoid; Q3MHW6; -.
DR OMA; TYAGFCI; -.
DR OrthoDB; 916876at2759; -.
DR TreeFam; TF313792; -.
DR Proteomes; UP000009136; Chromosome 3.
DR Bgee; ENSBTAG00000015107; Expressed in rumen epithelium and 107 other tissues.
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; ISS:UniProtKB.
DR GO; GO:0015129; F:lactate transmembrane transporter activity; IEA:InterPro.
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 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 2: Evidence at transcript level;
KW Cell membrane; Membrane; Phosphoprotein; Reference proteome; Symport;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..501
FT /note="Monocarboxylate transporter 1"
FT /id="PRO_0000287190"
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..262
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 263..283
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 284..298
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 299..319
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 320..328
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 329..349
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 350..353
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 354..374
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 375..389
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 390..410
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 411..422
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 423..443
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 444..501
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 201..236
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 454..501
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 202..226
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 227
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P53986"
FT MOD_RES 231
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P53986"
FT MOD_RES 462
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P53985"
FT MOD_RES 467
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P53985"
FT MOD_RES 484
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P53985"
FT MOD_RES 499
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P53985"
SQ SEQUENCE 501 AA; 54297 MW; 140F7F091CCC3C32 CRC64;
MPPAVGGPVG YTPPDGGWGW AVVIGAFISI GFSYAFPKSI TVFFKEIEGI FNATTSEVSW
ISSIMLAVMY GGGPISSVLV NKYGSRPVMI VGGILSGSGL IAASFCNTVQ ELYFSVGVIG
GLGLAFNLNP ALTMIGKYFY KRRPLANGLA MAGSPVFLST LAPLNQAFFM IYGWRGSFLI
LGGLLLNCCV AGALMRPIGP KPTTAEKEKS KGSLQEAGKY ETKKGASDAN TDLIGGNPKE
EKKSIFQTLN TFLDLSLFKH RGFLLYLSGN VLMFFGLFTP LVFLSNYGKS KHYSSEKAAF
LLSILAFVDM VARPSMGLVA NTKWVRPRVQ YFFAASIIAN GLCHLAAPLS STYIELCIYA
GFFGFAFGWL SSVLFETLMD LVGPQRFSSA VGLVTIVECC PVLLGPPVLG RLNDIYGDYK
YTYWACGIIL IVAGIYLFIG MGINYRLLEK EQKAEKQQKK ESKDEETNVD VAEKPKEVID
AAESPEHKAT EEDPKEAESP V
