FGTH1_CAEEL
ID FGTH1_CAEEL Reviewed; 516 AA.
AC O44616;
DT 22-JAN-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 2.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Facilitated glucose transporter homolog {ECO:0000303|PubMed:23826391};
GN ORFNames=R09B5.11;
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:0000312|EMBL:CCD68888.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|EMBL:CCD68888.1};
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 [2] {ECO:0000305}
RP FUNCTION, ABSENCE OF GLUCOSE TRANSPORTER ACTIVITY, SUBCELLULAR LOCATION,
RP AND TISSUE SPECIFICITY.
RC STRAIN=Bristol N2 {ECO:0000269|PubMed:23826391};
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: Appears to have no transport activity for glucose.
CC {ECO:0000269|PubMed:23826391}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23826391};
CC Multi-pass membrane protein {ECO:0000255, ECO:0000269|PubMed:23826391}.
CC -!- TISSUE SPECIFICITY: Expressed in seam cells from the early embryonic
CC stage through the L2 stage (at protein level).
CC {ECO:0000269|PubMed:23826391}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. Sugar
CC transporter (TC 2.A.1.1) family. {ECO:0000255}.
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DR EMBL; FO081061; CCD68888.1; -; Genomic_DNA.
DR PIR; C88950; C88950.
DR RefSeq; NP_503413.2; NM_071012.5.
DR AlphaFoldDB; O44616; -.
DR SMR; O44616; -.
DR STRING; 6239.R09B5.11; -.
DR EPD; O44616; -.
DR PaxDb; O44616; -.
DR PRIDE; O44616; -.
DR EnsemblMetazoa; R09B5.11.1; R09B5.11.1; WBGene00019979.
DR GeneID; 178634; -.
DR KEGG; cel:CELE_R09B5.11; -.
DR UCSC; R09B5.11; c. elegans.
DR CTD; 178634; -.
DR WormBase; R09B5.11; CE30296; WBGene00019979; -.
DR eggNOG; KOG0569; Eukaryota.
DR HOGENOM; CLU_001265_30_5_1; -.
DR InParanoid; O44616; -.
DR OMA; LNATWTV; -.
DR OrthoDB; 749998at2759; -.
DR PhylomeDB; O44616; -.
DR Reactome; R-CEL-189200; Cellular hexose transport.
DR Reactome; R-CEL-6798695; Neutrophil degranulation.
DR Reactome; R-CEL-8981373; Intestinal hexose absorption.
DR PRO; PR:O44616; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00019979; Expressed in adult organism and 2 other tissues.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015149; F:hexose transmembrane transporter activity; IBA:GO_Central.
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 Cell membrane; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..516
FT /note="Facilitated glucose transporter homolog"
FT /id="PRO_0000425147"
FT TOPO_DOM 1..47
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 48..68
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 69..101
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 102..122
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 123..138
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 139..159
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 160..161
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 162..182
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 183..200
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 201..221
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 222
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 223..243
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 244..306
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 307..327
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 328..344
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 345..365
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 366..376
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 377..397
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 398..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..444
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 445..465
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255"
FT TOPO_DOM 466..471
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 472..492
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255"
FT TOPO_DOM 493..516
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..23
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 516 AA; 57609 MW; 4152B72150088C9F CRC64;
MNAVVASQNK NDRSFSNMES ESSSNVEKSE KENHHQSLPD ENWTPFLFFC ISSIALASFQ
DGFQIGCINA PGPLIIDWIK KCHFELFGEV LSQYQADFIW SVAVSMFSVG GMFGSFCSGF
LADKFGRKST LLYNNILALL AAVCLSTSKL FNFYPMIVFG RFLVGLNCGI TSGLVPMFLT
ELAPANLRGK CGSFHQLNIS VAIVLSQALG LPQIFGTQVG WPYIFACVAI PTFLQLATIP
FCVESPKYLI SKLNDREEAR RILEKLRGHT KVDEELEHMV QETMVTVEPL HQPGYVSLFK
GDNQWPMIVS ILMMFSQQFS GISAVTFYST LIFKRNGLSG NEPMYATVGF GCIKLIATFG
CLFLIDHPKF GRKRLHIAGL SGMCISSILI VITLTLSNAG YHWASYMNVL FILSFVVTFA
FGPGPIPWFF TSELFDSATR GRAAAVSATS NWVANWMVGL TFLPINNIIH QYAFLMFTFF
TFTFAIFTWK FVPETKGKSP SAIRKELAFM RKRICS
