Q7KWJ5 · HXT1_PLAF7
- ProteinHexose transporter 1
- GeneHT1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids504 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Sodium-independent facilitative hexose transporter (PubMed:10066789).
Can transport D-glucose and D-fructose (PubMed:10066789, PubMed:10954735, PubMed:12238947, PubMed:12792024, PubMed:31996846, PubMed:32860739).
Can transport D-mannose, D-galactose, D-xylose and D-glucosamine (PubMed:31996846).
Can transport D-glucose and D-fructose (PubMed:10066789, PubMed:10954735, PubMed:12238947, PubMed:12792024, PubMed:31996846, PubMed:32860739).
Can transport D-mannose, D-galactose, D-xylose and D-glucosamine (PubMed:31996846).
Miscellaneous
Experiments with hexose analogs indicate that hydroxyl groups at positions C-3 and C-4 of glucose are important for high affinity interactions with HT1.
Catalytic activity
- D-glucose(out) = D-glucose(in)This reaction proceeds in the forward direction.
- D-fructose(out) = D-fructose(in)This reaction proceeds in the forward direction.
- D-galactose(in) = D-galactose(out)This reaction proceeds in the backward direction.
- D-mannose(out) = D-mannose(in)This reaction proceeds in the forward direction.
- D-glucosamine(out) = D-glucosamine(in)This reaction proceeds in the forward direction.
- D-xylose(out) = D-xylose(in)This reaction proceeds in the forward direction.
Activity regulation
Inhibited by cytochalasin B (PubMed:10066789, PubMed:31996846).
Inhibited by compound 3361 (3-O-((undec-10-en)-1-yl)-D-glucose) (PubMed:12792024, PubMed:31996846, PubMed:32860739).
Inhibited by compound HTI-1 (PubMed:32860739).
Inhibited by compound 3361 (3-O-((undec-10-en)-1-yl)-D-glucose) (PubMed:12792024, PubMed:31996846, PubMed:32860739).
Inhibited by compound HTI-1 (PubMed:32860739).
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
0.48 mM | D-glucose | |||||
1 mM | D-glucose | |||||
11 mM | D-fructose | |||||
1.59 mM | D-glucose | |||||
0.8 mM | D-glucose | |||||
1.48 mM | D-mannose | |||||
9.54 mM | D-galactose | |||||
9.55 mM | D-fructose | |||||
14.69 mM | D-glucosamine |
Vmax | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|
2.5 μmol/min/mg | for D-glucose | ||||
21.11 μmol/min/mg | for D-glucose | ||||
13.04 μmol/min/mg | for D-mannose | ||||
50.29 μmol/min/mg | for D-galactose | ||||
33.11 μmol/min/mg | for D-fructose | ||||
8.72 μmol/min/mg | for D-glucosamine |
kcat is 19.35 sec-1 for D-glucose transport (PubMed:31996846).
kcat is 11.95 sec-1 for D-mannose transport (PubMed:31996846).
kcat is 46.10 sec-1 for D-galactose transport (PubMed:31996846).
kcat is 30.36 sec-1 for D-fructose transport (PubMed:31996846).
kcat is 8.01 sec-1 for D-glucosamine transport (PubMed:31996846).
kcat is 11.95 sec-1 for D-mannose transport (PubMed:31996846).
kcat is 46.10 sec-1 for D-galactose transport (PubMed:31996846).
kcat is 30.36 sec-1 for D-fructose transport (PubMed:31996846).
kcat is 8.01 sec-1 for D-glucosamine transport (PubMed:31996846).
Temperature Dependence
Active from 32 to 42 degrees Celsius (PubMed:12238947).
Retains 50% of its maximal activity at 20 degrees Celsius (PubMed:12238947).
Retains 50% of its maximal activity at 20 degrees Celsius (PubMed:12238947).
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 169 | alpha-D-glucose (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 169 | beta-D-glucose (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 305 | alpha-D-glucose (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 305 | beta-D-glucose (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 306 | alpha-D-glucose (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 311 | alpha-D-glucose (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 311 | beta-D-glucose (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 341 | beta-D-glucose (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 412 | alpha-D-glucose (UniProtKB | ChEBI) | ||||
Sequence: W |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | membrane | |
Cellular Component | plasma membrane | |
Molecular Function | fructose transmembrane transporter activity | |
Molecular Function | glucose transmembrane transporter activity | |
Molecular Function | hexose transmembrane transporter activity | |
Biological Process | hexose transmembrane transport | |
Biological Process | monosaccharide transmembrane transport |
Keywords
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameHexose transporter 1
- Short namesPfHT1
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Sar > Alveolata > Apicomplexa > Aconoidasida > Haemosporida > Plasmodiidae > Plasmodium > Plasmodium (Laverania)
Accessions
- Primary accessionQ7KWJ5
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Multi-pass membrane protein
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-29 | Cytoplasmic | ||||
Sequence: MTKSSKDICSENEGKKNGKSGFFSTSFKY | ||||||
Transmembrane | 30-50 | Helical | ||||
Sequence: VLSACIASFIFGYQVSVLNTI | ||||||
Topological domain | 51-78 | Extracellular | ||||
Sequence: KNFIVVEFEWCKGEKDRLNCSNNTIQSS | ||||||
Transmembrane | 79-99 | Helical | ||||
Sequence: FLLASVFIGAVLGCGFSGYLV | ||||||
Topological domain | 100-104 | Cytoplasmic | ||||
Sequence: QFGRR | ||||||
Transmembrane | 105-125 | Helical | ||||
Sequence: LSLLIIYNFFFLVSILTSITH | ||||||
Topological domain | 126-129 | Extracellular | ||||
Sequence: HFHT | ||||||
Transmembrane | 130-150 | Helical | ||||
Sequence: ILFARLLSGFGIGLVTVSVPM | ||||||
Topological domain | 151-165 | Cytoplasmic | ||||
Sequence: YISEMTHKDKKGAYG | ||||||
Transmembrane | 166-186 | Helical | ||||
Sequence: VMHQLFITFGIFVAVMLGLAM | ||||||
Topological domain | 187-207 | Extracellular | ||||
Sequence: GEGPKADSTEPLTSFAKLWWR | ||||||
Transmembrane | 208-228 | Helical | ||||
Sequence: LMFLFPSVISLIGILALVVFF | ||||||
Topological domain | 229-293 | Cytoplasmic | ||||
Sequence: KEETPYFLFEKGRIEESKNILKKIYETDNVDEPLNAIKEAVEQNESAKKNSLSLLSALKIPSYRY | ||||||
Transmembrane | 294-314 | Helical | ||||
Sequence: VIILGCLLSGLQQFTGINVLV | ||||||
Topological domain | 315-331 | Extracellular | ||||
Sequence: SNSNELYKEFLDSHLIT | ||||||
Transmembrane | 332-352 | Helical | ||||
Sequence: ILSVVMTAVNFLMTFPAIYIV | ||||||
Topological domain | 353-358 | Cytoplasmic | ||||
Sequence: EKLGRK | ||||||
Transmembrane | 359-379 | Helical | ||||
Sequence: TLLLWGCVGVLVAYLPTAIAN | ||||||
Topological domain | 380-392 | Extracellular | ||||
Sequence: EINRNSNFVKILS | ||||||
Transmembrane | 393-413 | Helical | ||||
Sequence: IVATFVMIISFAVSYGPVLWI | ||||||
Topological domain | 414-429 | Cytoplasmic | ||||
Sequence: YLHEMFPSEIKDSAAS | ||||||
Transmembrane | 430-450 | Helical | ||||
Sequence: LASLVNWVCAIIVVFPSDIII | ||||||
Topological domain | 451-455 | Extracellular | ||||
Sequence: KKSPS | ||||||
Transmembrane | 456-476 | Helical | ||||
Sequence: ILFIVFSVMSILTFFFIFFFI | ||||||
Topological domain | 477-504 | Cytoplasmic | ||||
Sequence: KETKGGEIGTSPYITMEERQKHMTKSVV |
Keywords
- Cellular component
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 48 | Reduces D-glucose and D-fructose transport activity. | ||||
Sequence: N → A | ||||||
Mutagenesis | 51 | Reduces D-glucose and D-fructose transport activity. Reduces susceptibility to inhibition by compound HTI-1. Reduces susceptibility to inhibition by compound HTI-1; when associated with A-447. | ||||
Sequence: K → A | ||||||
Mutagenesis | 51 | Reduces D-glucose and D-fructose transport activity. | ||||
Sequence: K → Q | ||||||
Mutagenesis | 168 | Reduces D-glucose and D-fructose transport activity. | ||||
Sequence: H → N | ||||||
Mutagenesis | 169 | Abolishes D-glucose and D-fructose transport activity. | ||||
Sequence: Q → A | ||||||
Mutagenesis | 169 | In one study, shown to abolish D-glucose and D-fructose transport activity. In another study, shown to abolish D-fructose transport with no significant effects on D-glucose uptake and affinity. Reduces susceptibility to inhibition by compound 3361. | ||||
Sequence: Q → N | ||||||
Mutagenesis | 302 | No significant effects on affinity for D-glucose and D-fructose. | ||||
Sequence: S → A | ||||||
Mutagenesis | 302-304 | No significant effects on affinity for D-glucose and D-fructose. | ||||
Sequence: SGL → AGT | ||||||
Mutagenesis | 304 | No significant effects on affinity for D-glucose and D-fructose. | ||||
Sequence: L → T | ||||||
Mutagenesis | 305 | Reduces D-glucose and D-fructose transport activity. | ||||
Sequence: Q → A | ||||||
Mutagenesis | 306 | Reduces D-glucose and D-fructose transport activity. | ||||
Sequence: Q → A | ||||||
Mutagenesis | 310 | Reduces D-glucose and D-fructose transport activity. | ||||
Sequence: I → A | ||||||
Mutagenesis | 311 | Reduces D-glucose and D-fructose transport activity. | ||||
Sequence: N → A | ||||||
Mutagenesis | 314 | Reduces D-glucose and D-fructose transport activity. | ||||
Sequence: V → F | ||||||
Mutagenesis | 315 | No significant effects on D-glucose and D-fructose transport activities. Reduces turnover number for D-glucose. | ||||
Sequence: S → A | ||||||
Mutagenesis | 315 | Reduces D-glucose and D-fructose transport activity. | ||||
Sequence: S → Y | ||||||
Mutagenesis | 316 | Reduces D-glucose and D-fructose transport activity. | ||||
Sequence: N → A or Y | ||||||
Mutagenesis | 317 | Reduces D-glucose and D-fructose transport activity. | ||||
Sequence: S → A | ||||||
Mutagenesis | 318 | Reduces D-glucose and D-fructose transport activity. | ||||
Sequence: N → A | ||||||
Mutagenesis | 319 | No significant effects on D-glucose and D-fructose transport activities. Reduces turnover number for D-glucose. | ||||
Sequence: E → A | ||||||
Mutagenesis | 341 | Abolishes D-glucose and D-fructose transport activity. | ||||
Sequence: N → A | ||||||
Mutagenesis | 403 | Reduces D-glucose and D-fructose transport activity. | ||||
Sequence: F → A | ||||||
Mutagenesis | 404 | Modestly reduces D-glucose and D-fructose transport activities and affinities for these substrates. | ||||
Sequence: A → E | ||||||
Mutagenesis | 412 | Reduces D-fructose transport with no significant effect on D-glucose uptake. | ||||
Sequence: W → A | ||||||
Mutagenesis | 435 | Reduces D-fructose transport with no significant effect on D-glucose uptake. | ||||
Sequence: N → A | ||||||
Mutagenesis | 436 | Reduces D-glucose and D-fructose transport activity. | ||||
Sequence: W → A | ||||||
Mutagenesis | 439 | Reduces D-glucose and D-fructose transport activity. | ||||
Sequence: A → N | ||||||
Mutagenesis | 447 | Reduces susceptibility to inhibition by compound HTI-1; when associated with A-51. | ||||
Sequence: D → A |
Chemistry
PTM/Processing
Features
Showing features for chain, modified residue (large scale data), disulfide bond.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000460194 | 1-504 | UniProt | Hexose transporter 1 | |||
Sequence: MTKSSKDICSENEGKKNGKSGFFSTSFKYVLSACIASFIFGYQVSVLNTIKNFIVVEFEWCKGEKDRLNCSNNTIQSSFLLASVFIGAVLGCGFSGYLVQFGRRLSLLIIYNFFFLVSILTSITHHFHTILFARLLSGFGIGLVTVSVPMYISEMTHKDKKGAYGVMHQLFITFGIFVAVMLGLAMGEGPKADSTEPLTSFAKLWWRLMFLFPSVISLIGILALVVFFKEETPYFLFEKGRIEESKNILKKIYETDNVDEPLNAIKEAVEQNESAKKNSLSLLSALKIPSYRYVIILGCLLSGLQQFTGINVLVSNSNELYKEFLDSHLITILSVVMTAVNFLMTFPAIYIVEKLGRKTLLLWGCVGVLVAYLPTAIANEINRNSNFVKILSIVATFVMIISFAVSYGPVLWIYLHEMFPSEIKDSAASLASLVNWVCAIIVVFPSDIIIKKSPSILFIVFSVMSILTFFFIFFFIKETKGGEIGTSPYITMEERQKHMTKSVV | |||||||
Modified residue (large scale data) | 4 | PTMeXchange | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 5 | PTMeXchange | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 10 | PTMeXchange | Phosphoserine | ||||
Sequence: S | |||||||
Disulfide bond | 61↔70 | UniProt | |||||
Sequence: CKGEKDRLNC | |||||||
Modified residue (large scale data) | 502 | PTMeXchange | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Structure
Sequence
- Sequence statusComplete
- Length504
- Mass (Da)56,417
- Last updated2004-07-05 v1
- Checksum79AE4CB7D514FA58
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
LN999943 EMBL· GenBank· DDBJ | CZT98059.1 EMBL· GenBank· DDBJ | Genomic DNA |