SLC5A1
entrez
6523
canonical
uniprot
P13866
canonical
ensembl
ENSG00000100170
resolver
ensp
ENSP00000266088
resolver
ensp
ENSP00000444898
resolver
genesymbol
SLC5A1
resolver
genesymbol_syn
NAGT
resolver
genesymbol_syn
SGLT1
resolver
hgnc
HGNC:11036
resolver
uniprot
B2R7E2
resolver
uniprot
B7Z4Q9
resolver
uniprot
B7ZA69
resolver
uniprot_entry
SC5A1_HUMAN
resolver
uniprot_sec
B2R7E2
resolver
uniprot_sec
B7Z4Q9
resolver
uniprot_sec
B7ZA69
resolver
activity_regulation
ACTIVITY REGULATION: Enhanced by the interaction with PDZK1IP1/MAP17; but unlike SLC5A2/SGLT2, PDZK1IP1 is not essential for SLC5A1 transporter activity (PubMed:37217492). Inhibited by phlorizin (PubMed:20980548, PubMed:34880492). Possibly modulated by cholesterol binding (PubMed:34880492). {ECO:0000269|PubMed:20980548, ECO:0000269|PubMed:34880492, ECO:0000269|PubMed:37217492}.
uniprot
proteins
amino_acid_sequence
MDSSTWSPKTTAVTRPVETHELIRNAADISIIVIYFVVVMAVGLWAMFSTNRGTVGGFFLAGRSMVWWPIGASLFASNIGSGHFVGLAGTGAASGIAIGGFEWNALVLVVVLGWLFVPIYIKAGVVTMPEYLRKRFGGQRIQVYLSLLSLLLYIFTKISADIFSGAIFINLALGLNLYLAIFLLLAITALYTITGGLAAVIYTDTLQTVIMLVGSLILTGFAFHEVGGYDAFMEKYMKAIPTIVSDGNTTFQEKCYTPRADSFHIFRDPLTGDLPWPGFIFGMSILTLWYWCTDQVIVQRCLSAKNMSHVKGGCILCGYLKLMPMFIMVMPGMISRILYTEKIACVVPSECEKYCGTKVGCTNIAYPTLVVELMPNGLRGLMLSVMLASLMSSLTSIFNSASTLFTMDIYAKVRKRASEKELMIAGRLFILVLIGISIAWVPIVQSAQSGQLFDYIQSITSYLGPPIAAVFLLAIFWKRVNEPGAFWGLILGLLIGISRMITEFAYGTGSCMEPSNCPTIICGVHYLYFAIILFAISFITIVVISLLTKPIPDVHLYRLCWSLRNSKEERIDLDAEEENIQEGPKETIEIETQVPEKKKGIFRRAYDLFCGLEQHGAPKMTEEEEKAMKMKMTDTSEKPLWRTVLNVNGIILVTVAVFCHAYFA
uniprot
proteins
disease_involvement
DISEASE: Glucose/galactose malabsorption (GGM) [MIM:606824]: An autosomal recessive disorder characterized by neonatal onset of severe diarrhea and dehydration which are usually fatal unless glucose and galactose are eliminated from the diet. {ECO:0000269|PubMed:10036327, ECO:0000269|PubMed:11406349, ECO:0000269|PubMed:2008213, ECO:0000269|PubMed:8195156, ECO:0000269|PubMed:8563765}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
function
FUNCTION: Electrogenic Na(+)-coupled sugar symporter that actively transports D-glucose or D-galactose at the plasma membrane, with a Na(+) to sugar coupling ratio of 2:1. Transporter activity is driven by a transmembrane Na(+) electrochemical gradient set by the Na(+)/K(+) pump (PubMed:20980548, PubMed:34880492, PubMed:35077764, PubMed:8563765, PubMed:37217492). Has a primary role in the transport of dietary monosaccharides from enterocytes to blood. Responsible for the absorption of D-glucose or D-galactose across the apical brush-border membrane of enterocytes, whereas basolateral exit is provided by GLUT2. Additionally, functions as a D-glucose sensor in enteroendocrine cells, triggering the secretion of the incretins GCG and GIP that control food intake and energy homeostasis (By similarity) (PubMed:8563765). Together with SGLT2, functions in reabsorption of D-glucose from glomerular filtrate, playing a nonredundant role in the S3 segment of the proximal tubules (By similarity). Transports D-glucose into endometrial epithelial cells, controlling glycogen synthesis and nutritional support for the embryo as well as the decidual transformation of endometrium prior to conception (PubMed:28974690). Acts as a water channel enabling passive water transport across the plasma membrane in response to the osmotic gradient created upon sugar and Na(+) uptake. Has high water conductivity, comparable to aquaporins, and therefore is expected to play an important role in transepithelial water permeability, especially in the small intestine. {ECO:0000250|UniProtKB:Q8C3K6, ECO:0000269|PubMed:14695256, ECO:0000269|PubMed:20980548, ECO:0000269|PubMed:26945065, ECO:0000269|PubMed:28974690, ECO:0000269|PubMed:34880492, ECO:0000269|PubMed:35077764, ECO:0000269|PubMed:37217492, ECO:0000269|PubMed:8563765}.
uniprot
proteins
mass_dalton
73498
uniprot
proteins
mutagenesis
MUTAGEN 67; /note="W->A: Strong reduction in D-glucose transporter activity."; /evidence="ECO:0000269|PubMed:34880492"; MUTAGEN 77; /note="S->A: Loss of activity."; /evidence="ECO:0000269|PubMed:34880492"; MUTAGEN 83; /note="H->L: Acquires D-mannose, D-fructose and L-sorbose transporter activity; when associated with A-287 and C-290."; /evidence="ECO:0000269|PubMed:35077764"; MUTAGEN 83; /note="H->Q: Loss of D-glucose transporter activity."; /evidence="ECO:0000269|PubMed:34880492"; MUTAGEN 204; /note="D->A: Loss of activity."; /evidence="ECO:0000269|PubMed:34880492"; MUTAGEN 248; /note="N->Q: Loss of N-glycosylation."; /evidence="ECO:0000269|PubMed:8567640"; MUTAGEN 287; /note="T->A: Acquires D-mannose, D-fructose and L-sorbose transporter activity; when associated with L-83 and C-290."; /evidence="ECO:0000269|PubMed:35077764"; MUTAGEN 287; /note="T->N: Loss of D-glucose transporter activity. Has strict selectivity for D-galactose."; /evidence="ECO:0000269|PubMed:34880492, ECO:0000269|PubMed:35077764"; MUTAGEN 287; /note="T->S,A: Has normal D-glucose and D-galactose transporter activity."; /evidence="ECO:0000269|PubMed:34880492, ECO:0000269|PubMed:35077764"; MUTAGEN 290; /note="Y->C: Loss of D-galactose transporter activity. Has strict selectivity for D-glucose. Acquires D-mannose, D-fructose and L-sorbose transporter activity; when associated with A-287 and L-83."; /evidence="ECO:0000269|PubMed:35077764"; MUTAGEN 291; /note="W->A: Loss of D-glucose transporter activity."; /evidence="ECO:0000269|PubMed:34880492"; MUTAGEN 292; /note="C->A: Has no effect on water permeability."; /evidence="ECO:0000269|PubMed:26945065"; MUTAGEN 321; /note="K->Q: Acquires D-mannose and D-allose transporter activity comparable to glucose and galactose."; /evidence="ECO:0000269|PubMed:35077764"; MUTAGEN 363; /note="N->A: Loss of water permeation."; /evidence="ECO:0000269|PubMed:34880492"; MUTAGEN 396; /note="S->A: Loss of activity."; /evidence="ECO:0000269|PubMed:34880492"; MUTAGEN 451; /note="Q->A: Strong reduction in water permeation."; /evidence="ECO:0000269|PubMed:34880492"; MUTAGEN 452; /note="L->A: Loss of water permeation."; /evidence="ECO:0000269|PubMed:34880492"; MUTAGEN 454; /note="D->A: Has no effect on water permeation."; /evidence="ECO:0000269|PubMed:34880492"; MUTAGEN 457; /note="Q->A: Loss of D-glucose transporter activity."; /evidence="ECO:0000269|PubMed:34880492"; MUTAGEN 457; /note="Q->C: Strong reduction in D-glucose transporter activity."; /evidence="ECO:0000269|PubMed:34880492"; MUTAGEN 460; /note="T->A: Loss of D-glucose transporter activity."; /evidence="ECO:0000269|PubMed:34880492"; MUTAGEN 641; /note="W->A: Slightly reduced D-glucose transporter activity."; /evidence="ECO:0000269|PubMed:34880492"; MUTAGEN 660..661; /note="HA->WG: Loss of D-glucose transporter activity."; /evidence="ECO:0000269|PubMed:34880492
uniprot
proteins
post_translational_modification
PTM: N-glycosylation is not necessary for the cotransporter function. {ECO:0000269|PubMed:8567640}.
uniprot
proteins
protein_family
Sodium:solute symporter (SSF) (TC 2.A.21) family
uniprot
proteins
pubmed
10036327
uniprot
proteins
pubmed
10591208
uniprot
proteins
pubmed
11406349
uniprot
proteins
pubmed
14695256
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15461802
uniprot
proteins
pubmed
2008213
uniprot
proteins
pubmed
20980548
uniprot
proteins
pubmed
2490366
uniprot
proteins
pubmed
26945065
uniprot
proteins
pubmed
28974690
uniprot
proteins
pubmed
34880492
uniprot
proteins
pubmed
35077764
uniprot
proteins
pubmed
37217492
uniprot
proteins
pubmed
8195156
uniprot
proteins
pubmed
8563765
uniprot
proteins
pubmed
8567640
uniprot
proteins
sequence_length
664
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000269|PubMed:26945065}; Multi-pass membrane protein {ECO:0000269|PubMed:34880492, ECO:0000269|PubMed:37217492}.
uniprot
proteins
transmembrane_region
TRANSMEM 25..47; /note="Helical; Name=TM0"; /evidence="ECO:0000269|PubMed:34880492, ECO:0000269|PubMed:37217492, ECO:0007744|PDB:7SL8, ECO:0007744|PDB:7SLA, ECO:0007744|PDB:7YNI"; TRANSMEM 67..90; /note="Helical; Name=TM1"; /evidence="ECO:0000269|PubMed:34880492, ECO:0000269|PubMed:37217492, ECO:0007744|PDB:7SL8, ECO:0007744|PDB:7SLA, ECO:0007744|PDB:7YNI"; TRANSMEM 96..117; /note="Helical; Name=TM2"; /evidence="ECO:0000269|PubMed:34880492, ECO:0000269|PubMed:37217492, ECO:0007744|PDB:7SL8, ECO:0007744|PDB:7SLA, ECO:0007744|PDB:7YNI"; TRANSMEM 140..169; /note="Helical; Name=TM3"; /evidence="ECO:0000269|PubMed:34880492, ECO:0000269|PubMed:37217492, ECO:0007744|PDB:7SL8, ECO:0007744|PDB:7SLA, ECO:0007744|PDB:7YNI"; TRANSMEM 177..193; /note="Helical; Name=TM4"; /evidence="ECO:0000269|PubMed:34880492, ECO:0000269|PubMed:37217492, ECO:0007744|PDB:7SL8, ECO:0007744|PDB:7SLA, ECO:0007744|PDB:7YNI"; TRANSMEM 203..221; /note="Helical; Name=TM5"; /evidence="ECO:0000269|PubMed:34880492, ECO:0000269|PubMed:37217492, ECO:0007744|PDB:7SL8, ECO:0007744|PDB:7SLA, ECO:0007744|PDB:7YNI"; TRANSMEM 276..295; /note="Helical; Name=TM6"; /evidence="ECO:0000269|PubMed:34880492, ECO:0000269|PubMed:37217492, ECO:0007744|PDB:7SL8, ECO:0007744|PDB:7SLA, ECO:0007744|PDB:7YNI"; TRANSMEM 310..331; /note="Helical; Name=TM7"; /evidence="ECO:0000269|PubMed:34880492, ECO:0000269|PubMed:37217492, ECO:0007744|PDB:7SL8, ECO:0007744|PDB:7SLA, ECO:0007744|PDB:7YNI"; TRANSMEM 376..406; /note="Helical; Name=TM8"; /evidence="ECO:0000269|PubMed:34880492, ECO:0000269|PubMed:37217492, ECO:0007744|PDB:7SL8, ECO:0007744|PDB:7SLA, ECO:0007744|PDB:7YNI"; TRANSMEM 423..444; /note="Helical; Name=TM9"; /evidence="ECO:0000269|PubMed:34880492, ECO:0000269|PubMed:37217492, ECO:0007744|PDB:7SL8, ECO:0007744|PDB:7SLA, ECO:0007744|PDB:7YNI"; TRANSMEM 452..477; /note="Helical; Name=TM10"; /evidence="ECO:0000269|PubMed:34880492, ECO:0000269|PubMed:37217492, ECO:0007744|PDB:7SL8, ECO:0007744|PDB:7SLA, ECO:0007744|PDB:7YNI"; TRANSMEM 482..504; /note="Helical; Name=TM11"; /evidence="ECO:0000269|PubMed:34880492, ECO:0000269|PubMed:37217492, ECO:0007744|PDB:7SL8, ECO:0007744|PDB:7SLA, ECO:0007744|PDB:7YNI"; TRANSMEM 526..547; /note="Helical; Name=TM12"; /evidence="ECO:0000269|PubMed:34880492, ECO:0000269|PubMed:37217492, ECO:0007744|PDB:7SL8, ECO:0007744|PDB:7SLA, ECO:0007744|PDB:7YNI"; TRANSMEM 645..662; /note="Helical; Name=TM13"; /evidence="ECO:0000269|PubMed:34880492, ECO:0000269|PubMed:37217492, ECO:0007744|PDB:7SL8, ECO:0007744|PDB:7SLA, ECO:0007744|PDB:7YNI
uniprot
proteins