FGT1_CAEEL
ID FGT1_CAEEL Reviewed; 510 AA.
AC O44827; H2L0B9;
DT 22-JAN-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 2.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Facilitated glucose transporter protein 1 {ECO:0000303|PubMed:24024580};
GN Name=fgt-1 {ECO:0000312|EMBL:CCD72384.1, ECO:0000312|WormBase:H17B01.1b};
GN ORFNames=H17B01.1;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B), FUNCTION, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=Bristol N2 {ECO:0000269|PubMed:24024580};
RX PubMed=24024580; DOI=10.1042/bj20131101;
RA Feng Y., Williams B.G., Koumanov F., Wolstenholme A.J., Holman G.D.;
RT "FGT-1 is the major glucose transporter in C. elegans and is central to
RT aging pathways.";
RL Biochem. J. 456:219-229(2013).
RN [2] {ECO:0000305, ECO:0000312|EMBL:CCD72384.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC STRAIN=Bristol N2 {ECO:0000312|EMBL:CCD72384.1};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3] {ECO:0000305}
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=23826391; DOI=10.1371/journal.pone.0068475;
RA Kitaoka S., Morielli A.D., Zhao F.Q.;
RT "FGT-1 is a mammalian GLUT2-like facilitative glucose transporter in
RT Caenorhabditis elegans whose malfunction induces fat accumulation in
RT intestinal cells.";
RL PLoS ONE 8:E68475-E68475(2013).
CC -!- FUNCTION: Facilitative glucose transporter that plays a role in glucose
CC metabolism and regulation of longevity. May also play a role in lipid
CC metabolism. Glucose transport activity of isoform a is competitively
CC inhibited by mannose, galactose and fructose, suggesting ability to
CC transport also other hexose sugars. {ECO:0000269|PubMed:23826391,
CC ECO:0000269|PubMed:24024580, ECO:0000303|PubMed:23826391}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.8 mM for 2-deoxy-D-glucose (isoform a at pH 7.6)
CC {ECO:0000269|PubMed:23826391};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23826391,
CC ECO:0000269|PubMed:24024580}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:23826391, ECO:0000269|PubMed:24024580}.
CC -!- SUBCELLULAR LOCATION: [Isoform a]: Basolateral cell membrane
CC {ECO:0000269|PubMed:23826391}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:23826391, ECO:0000269|PubMed:24024580}.
CC Note=Detected on the basolateral but not on the apicolateral membrane
CC of intestinal cells. {ECO:0000269|PubMed:23826391}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=b {ECO:0000269|PubMed:24024580}; Synonyms=FGT-1B
CC {ECO:0000303|PubMed:24024580};
CC IsoId=O44827-1; Sequence=Displayed;
CC Name=a {ECO:0000269|PubMed:24024580}; Synonyms=FGT-1A
CC {ECO:0000303|PubMed:24024580};
CC IsoId=O44827-2; Sequence=VSP_053583, VSP_053584;
CC -!- TISSUE SPECIFICITY: Isoform a is expressed in pharyngeal muscle and
CC intestinal cells in both embryos and adults (at protein level).
CC {ECO:0000269|PubMed:23826391}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown of the protein causes
CC reduced 2-deoxy-D-glucose uptake, glucose oxidation and glucose
CC conversion to triglyceride; simultaneous knockout of daf-2 or age-1
CC causes further reductions. The lifespan in low glucose environment is
CC extended by 20-25% after knockdown, with 7% extension in daf-2 mutant
CC background and no significant extension in age-1 mutant background. Fat
CC accumulation in intestinal cells is increased. Brood size and dauer
CC formation are not affected. {ECO:0000269|PubMed:23826391,
CC ECO:0000269|PubMed:24024580}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. Sugar
CC transporter (TC 2.A.1.1) family. Glucose transporter subfamily.
CC {ECO:0000255}.
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DR EMBL; FO081553; CCD72383.1; -; Genomic_DNA.
DR EMBL; FO081553; CCD72384.1; -; Genomic_DNA.
DR RefSeq; NP_493981.1; NM_061580.4. [O44827-2]
DR RefSeq; NP_493982.1; NM_061581.1. [O44827-1]
DR AlphaFoldDB; O44827; -.
DR SMR; O44827; -.
DR BioGRID; 38898; 2.
DR STRING; 6239.H17B01.1b; -.
DR EPD; O44827; -.
DR PaxDb; O44827; -.
DR PeptideAtlas; O44827; -.
DR EnsemblMetazoa; H17B01.1a.1; H17B01.1a.1; WBGene00019207. [O44827-2]
DR EnsemblMetazoa; H17B01.1b.1; H17B01.1b.1; WBGene00019207. [O44827-1]
DR GeneID; 173525; -.
DR KEGG; cel:CELE_H17B01.1; -.
DR UCSC; H17B01.1a; c. elegans. [O44827-1]
DR CTD; 173525; -.
DR WormBase; H17B01.1a; CE27184; WBGene00019207; fgt-1. [O44827-2]
DR WormBase; H17B01.1b; CE27185; WBGene00019207; fgt-1. [O44827-1]
DR eggNOG; KOG0569; Eukaryota.
DR GeneTree; ENSGT00940000166877; -.
DR InParanoid; O44827; -.
DR OMA; WVPPGYI; -.
DR OrthoDB; 749998at2759; -.
DR PhylomeDB; O44827; -.
DR Reactome; R-CEL-189200; Cellular hexose transport.
DR Reactome; R-CEL-196836; Vitamin C (ascorbate) metabolism.
DR Reactome; R-CEL-6798695; Neutrophil degranulation.
DR Reactome; R-CEL-8981373; Intestinal hexose absorption.
DR PRO; PR:O44827; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00019207; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR GO; GO:0016323; C:basolateral plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0015149; F:hexose transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:1904659; P:glucose transmembrane transport; IDA:WormBase.
DR GO; GO:0015749; P:monosaccharide transmembrane transport; IBA:GO_Central.
DR Gene3D; 1.20.1250.20; -; 1.
DR InterPro; IPR045263; GLUT.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR005828; MFS_sugar_transport-like.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR003663; Sugar/inositol_transpt.
DR InterPro; IPR005829; Sugar_transporter_CS.
DR PANTHER; PTHR23503; PTHR23503; 1.
DR Pfam; PF00083; Sugar_tr; 1.
DR PRINTS; PR00171; SUGRTRNSPORT.
DR SUPFAM; SSF103473; SSF103473; 1.
DR TIGRFAMs; TIGR00879; SP; 1.
DR PROSITE; PS50850; MFS; 1.
DR PROSITE; PS00217; SUGAR_TRANSPORT_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Membrane; Reference proteome;
KW Sugar transport; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..510
FT /note="Facilitated glucose transporter protein 1"
FT /id="PRO_0000425146"
FT TOPO_DOM 1..46
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 47..67
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 68..100
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 101..121
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 122..127
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 128..146
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 147..160
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 161..181
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 182..195
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 196..216
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 217..219
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 220..240
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 241..299
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 300..320
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 321..341
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 342..362
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 363..373
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 374..394
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 395..409
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 410..430
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TOPO_DOM 431..445
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 446..464
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255"
FT TOPO_DOM 465..470
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 471..491
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255"
FT TOPO_DOM 492..510
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 195
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000250|UniProtKB:P11169"
FT BINDING 315..316
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000250|UniProtKB:P11169"
FT BINDING 321
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000250|UniProtKB:P11169"
FT BINDING 352
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000250|UniProtKB:P11169"
FT BINDING 427
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000250|UniProtKB:P11169"
FT VAR_SEQ 1..18
FT /note="Missing (in isoform a)"
FT /evidence="ECO:0000303|PubMed:24024580"
FT /id="VSP_053583"
FT VAR_SEQ 19..39
FT /note="SKSPSSYSTPGTTTQKIIFPD -> MGVNDHDVSVPLQEVQSRTVE (in
FT isoform a)"
FT /evidence="ECO:0000303|PubMed:24024580"
FT /id="VSP_053584"
SQ SEQUENCE 510 AA; 55068 MW; A90D093A79C17111 CRC64;
MSEKSRSDTS ATASLSDSSK SPSSYSTPGT TTQKIIFPDG KLTKCLAFSA FVITLASFQF
GYHIGCVNAP GGLITEWIIG SHKDLFDKEL SRENADLAWS VAVSVFAVGG MIGGLSSGWL
ADKVGRRGAL FYNNLLALAA AALMGLAKSV GAYPMVILGR LIIGLNCGFS SALVPMFLTE
ISPNNLRGML GSLHQLLVTI AILVSQIFGL PHLLGTGDRW PLIFAFTVVP AVLQLALLML
CPESPKYTMA VRGQRNEAES ALKKLRDTED VSTEIEAMQE EATAAGVQEK PKMGDMFKGA
LLWPMSIAIM MMLAQQLSGI NVAMFYSTVI FRGAGLTGNE PFYATIGMGA VNVIMTLISV
WLVDHPKFGR RSLLLAGLTG MFVSTLLLVG ALTIQNSGGD KWASYSAIGF VLLFVISFAT
GPGAIPWFFV SEIFDSSARG NANSIAVMVN WAANLLVGLT FLPINNLMQQ YSFFIFSGFL
AFFIFYTWKF VPETKGKSIE QIQAEFEKRK
