SLC5A2
entrez
6524
canonical
uniprot
P31639
canonical
ensembl
ENSG00000140675
resolver
ensp
ENSP00000327943
resolver
ensp
ENSP00000410601
resolver
genesymbol
SLC5A2
resolver
genesymbol_syn
SGLT2
resolver
hgnc
HGNC:11037
resolver
uniprot
A2RRD2
resolver
uniprot_entry
SC5A2_HUMAN
resolver
uniprot_sec
A2RRD2
resolver
activity_regulation
ACTIVITY REGULATION: Enhanced by the interaction with PDZK1IP1/MAP17 (PubMed:37217492). Inhibited by natural product phlorizin and diabetic drugs, including empagliflozin and dapagliflozin, canagliflozin, and sotagliflozin (PubMed:20980548, PubMed:28592437, PubMed:38057552). Empagliflozin is selective for SLC5A2/SGLT2 over SLC5A1/SGLT1 and it inhibits by occupying the sugar-binding site in SLC5A2 (PubMed:34880493). {ECO:0000269|PubMed:20980548, ECO:0000269|PubMed:28592437, ECO:0000269|PubMed:34880493, ECO:0000269|PubMed:37217492, ECO:0000269|PubMed:38057552}.
uniprot
proteins
amino_acid_sequence
MEEHTEAGSAPEMGAQKALIDNPADILVIAAYFLLVIGVGLWSMCRTNRGTVGGYFLAGRSMVWWPVGASLFASNIGSGHFVGLAGTGAASGLAVAGFEWNALFVVLLLGWLFAPVYLTAGVITMPQYLRKRFGGRRIRLYLSVLSLFLYIFTKISVDMFSGAVFIQQALGWNIYASVIALLGITMIYTVTGGLAALMYTDTVQTFVILGGACILMGYAFHEVGGYSGLFDKYLGAATSLTVSEDPAVGNISSFCYRPRPDSYHLLRHPVTGDLPWPALLLGLTIVSGWYWCSDQVIVQRCLAGKSLTHIKAGCILCGYLKLTPMFLMVMPGMISRILYPDEVACVVPEVCRRVCGTEVGCSNIAYPRLVVKLMPNGLRGLMLAVMLAALMSSLASIFNSSSTLFTMDIYTRLRPRAGDRELLLVGRLWVVFIVVVSVAWLPVVQAAQGGQLFDYIQAVSSYLAPPVSAVFVLALFVPRVNEQGAFWGLIGGLLMGLARLIPEFSFGSGSCVQPSACPAFLCGVHYLYFAIVLFFCSGLLTLTVSLCTAPIPRKHLHRLVFSLRHSKEEREDLDADEQQGSSLPVQNGCPESAMEMNEPQAPAPSLFRQCLLWFCGMSRGGVGSPPPLTQEEAAAAARRLEDISEDPSWARVVNLNALLMMAVAVFLWGFYA
uniprot
proteins
disease_involvement
DISEASE: Renal glucosuria (GLYS) [MIM:233100]: A disorder characterized by persistent isolated glucosuria, normal fasting serum glucose concentration, decreased renal tubular resorption of glucose from the urine, and absence of any other signs of tubular dysfunction. {ECO:0000269|PubMed:14614622}. 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 at the plasma membrane, with a Na(+) to sugar coupling ratio of 1:1 (PubMed:20980548, PubMed:28592437, PubMed:34880493, PubMed:37217492, PubMed:38057552). Transporter activity is driven by a transmembrane Na(+) electrochemical gradient set by the Na(+)/K(+) pump (PubMed:20980548, PubMed:28592437, PubMed:34880493). Unlike SLC5A1/SGLT1, requires the auxiliary protein PDZK1IP1/MAP17 for full transporter activity (PubMed:37217492). Has a primary role in D-glucose reabsorption from glomerular filtrate across the brush border of the early proximal tubules of the kidney (By similarity). {ECO:0000250|UniProtKB:Q923I7, ECO:0000269|PubMed:20980548, ECO:0000269|PubMed:28592437, ECO:0000269|PubMed:34880493, ECO:0000269|PubMed:37217492, ECO:0000269|PubMed:38057552}.
uniprot
proteins
mass_dalton
72897
uniprot
proteins
mutagenesis
MUTAGEN 74; /note="S->A: Impairs phlorizin binding and its inhibition on glucose uptake."; /evidence="ECO:0000269|PubMed:38057552"; MUTAGEN 95; /note="V->I: Strong reduction in D-glucose transporter activity. Impairs inhibition by empagliflozin on glucose uptake."; /evidence="ECO:0000269|PubMed:34880493"; MUTAGEN 98; /note="F->A: Slightly decreases D-glucose transporter activity. Abolishes empagliflozin binding and its inhibition on glucose uptake. Impairs phlorizin binding and its inhibition on glucose uptake."; /evidence="ECO:0000269|PubMed:34880493, ECO:0000269|PubMed:38057552"; MUTAGEN 157; /note="V->A: Decreases D-glucose transporter activity. Impairs inhibition by empagliflozin on glucose uptake."; /evidence="ECO:0000269|PubMed:34880493"; MUTAGEN 201; /note="D->A: Impairs phlorizin binding and its inhibition on glucose uptake."; /evidence="ECO:0000269|PubMed:38057552"; MUTAGEN 283; /note="L->M: Strong reduction in D-glucose transporter activity. Impairs inhibition by empagliflozin on glucose uptake."; /evidence="ECO:0000269|PubMed:34880493"; MUTAGEN 453; /note="F->A: Slightly decreases D-glucose transporter activity. Impairs empagliflozin binding and its inhibition on glucose uptake. Impairs phlorizin binding and its inhibition on glucose uptake."; /evidence="ECO:0000269|PubMed:34880493, ECO:0000269|PubMed:38057552
uniprot
proteins
protein_family
Sodium:solute symporter (SSF) (TC 2.A.21) family
uniprot
proteins
pubmed
1415574
uniprot
proteins
pubmed
14614622
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15616553
uniprot
proteins
pubmed
20980548
uniprot
proteins
pubmed
28592437
uniprot
proteins
pubmed
34880493
uniprot
proteins
pubmed
37217492
uniprot
proteins
pubmed
38057552
uniprot
proteins
sequence_length
672
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000305|PubMed:34880493, ECO:0000305|PubMed:37217492, ECO:0000305|PubMed:38057552}; Multi-pass membrane protein {ECO:0000269|PubMed:34880493, ECO:0000269|PubMed:37217492, ECO:0000269|PubMed:38057552}.
uniprot
proteins
transmembrane_region
TRANSMEM 23..44; /note="Helical; Name=TM0"; /evidence="ECO:0000269|PubMed:34880493, ECO:0000269|PubMed:37217492, ECO:0000269|PubMed:38057552, ECO:0007744|PDB:7VSI, ECO:0007744|PDB:7YNJ, ECO:0007744|PDB:7YNK, ECO:0007744|PDB:8HB0, ECO:0007744|PDB:8HDH, ECO:0007744|PDB:8HEZ, ECO:0007744|PDB:8HG7, ECO:0007744|PDB:8HIN"; TRANSMEM 64..85; /note="Helical; Name=TM1"; /evidence="ECO:0000269|PubMed:34880493, ECO:0000269|PubMed:37217492, ECO:0000269|PubMed:38057552, ECO:0007744|PDB:7VSI, ECO:0007744|PDB:7YNJ, ECO:0007744|PDB:7YNK, ECO:0007744|PDB:8HB0, ECO:0007744|PDB:8HDH, ECO:0007744|PDB:8HEZ, ECO:0007744|PDB:8HG7, ECO:0007744|PDB:8HIN"; TRANSMEM 94..114; /note="Helical; Name=TM2"; /evidence="ECO:0000269|PubMed:34880493, ECO:0000269|PubMed:37217492, ECO:0000269|PubMed:38057552, ECO:0007744|PDB:7VSI, ECO:0007744|PDB:7YNJ, ECO:0007744|PDB:7YNK, ECO:0007744|PDB:8HB0, ECO:0007744|PDB:8HDH, ECO:0007744|PDB:8HEZ, ECO:0007744|PDB:8HG7, ECO:0007744|PDB:8HIN"; TRANSMEM 137..166; /note="Helical; Name=TM3"; /evidence="ECO:0000269|PubMed:34880493, ECO:0000269|PubMed:37217492, ECO:0000269|PubMed:38057552, ECO:0007744|PDB:7VSI, ECO:0007744|PDB:7YNJ, ECO:0007744|PDB:7YNK, ECO:0007744|PDB:8HB0, ECO:0007744|PDB:8HDH, ECO:0007744|PDB:8HEZ, ECO:0007744|PDB:8HG7, ECO:0007744|PDB:8HIN"; TRANSMEM 174..195; /note="Helical; Name=TM4"; /evidence="ECO:0000269|PubMed:34880493, ECO:0000269|PubMed:37217492, ECO:0000269|PubMed:38057552, ECO:0007744|PDB:7VSI, ECO:0007744|PDB:7YNJ, ECO:0007744|PDB:7YNK, ECO:0007744|PDB:8HB0, ECO:0007744|PDB:8HDH, ECO:0007744|PDB:8HEZ, ECO:0007744|PDB:8HG7, ECO:0007744|PDB:8HIN"; TRANSMEM 196..217; /note="Helical; Name=TM5"; /evidence="ECO:0000269|PubMed:34880493, ECO:0000269|PubMed:37217492, ECO:0000269|PubMed:38057552, ECO:0007744|PDB:7VSI, ECO:0007744|PDB:7YNJ, ECO:0007744|PDB:7YNK, ECO:0007744|PDB:8HB0, ECO:0007744|PDB:8HDH, ECO:0007744|PDB:8HEZ, ECO:0007744|PDB:8HG7, ECO:0007744|PDB:8HIN"; TRANSMEM 276..295; /note="Helical; Name=TM6"; /evidence="ECO:0000269|PubMed:34880493, ECO:0000269|PubMed:37217492, ECO:0000269|PubMed:38057552, ECO:0007744|PDB:7VSI, ECO:0007744|PDB:7YNJ, ECO:0007744|PDB:7YNK, ECO:0007744|PDB:8HB0, ECO:0007744|PDB:8HDH, ECO:0007744|PDB:8HEZ, ECO:0007744|PDB:8HG7, ECO:0007744|PDB:8HIN"; TRANSMEM 310..331; /note="Helical; Name=TM7"; /evidence="ECO:0000269|PubMed:34880493, ECO:0000269|PubMed:37217492, ECO:0000269|PubMed:38057552, ECO:0007744|PDB:7VSI, ECO:0007744|PDB:7YNJ, ECO:0007744|PDB:7YNK, ECO:0007744|PDB:8HB0, ECO:0007744|PDB:8HDH, ECO:0007744|PDB:8HEZ, ECO:0007744|PDB:8HG7, ECO:0007744|PDB:8HIN"; TRANSMEM 376..406; /note="Helical; Name=TM8"; /evidence="ECO:0000269|PubMed:34880493, ECO:0000269|PubMed:37217492, ECO:0000269|PubMed:38057552, ECO:0007744|PDB:7VSI, ECO:0007744|PDB:7YNJ, ECO:0007744|PDB:7YNK, ECO:0007744|PDB:8HB0, ECO:0007744|PDB:8HDH, ECO:0007744|PDB:8HEZ, ECO:0007744|PDB:8HG7, ECO:0007744|PDB:8HIN"; TRANSMEM 425..446; /note="Helical; Name=TM9"; /evidence="ECO:0000269|PubMed:34880493, ECO:0000269|PubMed:37217492, ECO:0000269|PubMed:38057552, ECO:0007744|PDB:7VSI, ECO:0007744|PDB:7YNJ, ECO:0007744|PDB:7YNK, ECO:0007744|PDB:8HB0, ECO:0007744|PDB:8HDH, ECO:0007744|PDB:8HEZ, ECO:0007744|PDB:8HG7, ECO:0007744|PDB:8HIN"; TRANSMEM 452..477; /note="Helical; Name=TM10"; /evidence="ECO:0000269|PubMed:34880493, ECO:0000269|PubMed:37217492, ECO:0000269|PubMed:38057552, ECO:0007744|PDB:7VSI, ECO:0007744|PDB:7YNJ, ECO:0007744|PDB:7YNK, ECO:0007744|PDB:8HB0, ECO:0007744|PDB:8HDH, ECO:0007744|PDB:8HEZ, ECO:0007744|PDB:8HG7, ECO:0007744|PDB:8HIN"; TRANSMEM 483..505; /note="Helical; Name=TM11"; /evidence="ECO:0000269|PubMed:34880493, ECO:0000269|PubMed:37217492, ECO:0000269|PubMed:38057552, ECO:0007744|PDB:7VSI, ECO:0007744|PDB:7YNJ, ECO:0007744|PDB:7YNK, ECO:0007744|PDB:8HB0, ECO:0007744|PDB:8HDH, ECO:0007744|PDB:8HEZ, ECO:0007744|PDB:8HG7, ECO:0007744|PDB:8HIN"; TRANSMEM 524..547; /note="Helical; Name=TM12"; /evidence="ECO:0000269|PubMed:34880493, ECO:0000269|PubMed:37217492, ECO:0000269|PubMed:38057552, ECO:0007744|PDB:7VSI, ECO:0007744|PDB:7YNJ, ECO:0007744|PDB:7YNK, ECO:0007744|PDB:8HB0, ECO:0007744|PDB:8HDH, ECO:0007744|PDB:8HEZ, ECO:0007744|PDB:8HG7, ECO:0007744|PDB:8HIN"; TRANSMEM 652..670; /note="Helical; Name=TM13"; /evidence="ECO:0000269|PubMed:34880493, ECO:0000269|PubMed:37217492, ECO:0000269|PubMed:38057552, ECO:0007744|PDB:7VSI, ECO:0007744|PDB:7YNJ, ECO:0007744|PDB:7YNK, ECO:0007744|PDB:8HB0, ECO:0007744|PDB:8HDH, ECO:0007744|PDB:8HEZ, ECO:0007744|PDB:8HG7, ECO:0007744|PDB:8HIN
uniprot
proteins