SLC37A4
entrez
2542
canonical
uniprot
O43826
canonical
ensembl
ENSG00000137700
resolver
ensembl
ENSG00000281500
resolver
ensp
ENSP00000475991
resolver
ensp
ENSP00000476176
resolver
ensp
ENSP00000518341
resolver
enst
ENST00000710552
resolver
genesymbol
SLC37A4
resolver
genesymbol_syn
G6PT
resolver
genesymbol_syn
G6PT1
resolver
hgnc
HGNC:4061
resolver
uniprot
A0AB56JF70
resolver
uniprot
A8K0S7
resolver
uniprot
B4DUH2
resolver
uniprot
O96016
resolver
uniprot
Q5J7V4
resolver
uniprot
Q9UI19
resolver
uniprot
Q9UNS4
resolver
uniprot_entry
A0AB56JF70_HUMAN
resolver
uniprot_entry
A8K0S7_HUMAN
resolver
uniprot_entry
B4DUH2_HUMAN
resolver
uniprot_entry
G6PT1_HUMAN
resolver
uniprot_sec
O96016
resolver
uniprot_sec
Q5J7V4
resolver
uniprot_sec
Q9UI19
resolver
uniprot_sec
Q9UNS4
resolver
activity_regulation
ACTIVITY REGULATION: Inhibited by vanadate and chlorogenic acid (PubMed:21949678, PubMed:41136424). Chlorogenic acid inhibits by blocking a [the?] binding pocket for glucose-6-phosphate (PubMed:41136424). {ECO:0000269|PubMed:21949678, ECO:0000269|PubMed:41136424}.
uniprot
proteins
amino_acid_sequence
MAAQGYGYYRTVIFSAMFGGYSLYYFNRKTFSFVMPSLVEEIPLDKDDLGFITSSQSAAYAISKFVSGVLSDQMSARWLFSSGLLLVGLVNIFFAWSSTVPVFAALWFLNGLAQGLGWPPCGKVLRKWFEPSQFGTWWAILSTSMNLAGGLGPILATILAQSYSWRSTLALSGALCVVVSFLCLLLIHNEPADVGLRNLDPMPSEGKKGSLKEESTLQELLLSPYLWVLSTGYLVVFGVKTCCTDWGQFFLIQEKGQSALVGSSYMSALEVGGLVGSIAAGYLSDRAMAKAGLSNYGNPRHGLLLFMMAGMTVSMYLFRVTVTSDSPKLWILVLGAVFGFSSYGPIALFGVIANESAPPNLCGTSHAIVGLMANVGGFLAGLPFSTIAKHYSWSTAFWVAEVICAASTAAFFLLRNIRTKMGRVSKKAE
uniprot
proteins
disease_involvement
DISEASE: Glycogen storage disease 1B (GSD1B) [MIM:232220]: A metabolic disorder characterized by impairment of terminal steps of glycogenolysis and gluconeogenesis. Patients manifest a wide range of clinical symptoms and biochemical abnormalities, including hypoglycemia, severe hepatomegaly due to excessive accumulation of glycogen, kidney enlargement, growth retardation, lactic acidemia, hyperlipidemia, and hyperuricemia. Glycogen storage disease type 1B patients also present a tendency towards infections associated with neutropenia, relapsing aphthous gingivostomatitis, and inflammatory bowel disease. {ECO:0000269|PubMed:10026167, ECO:0000269|PubMed:10482875, ECO:0000269|PubMed:10482962, ECO:0000269|PubMed:10518030, ECO:0000269|PubMed:10874322, ECO:0000269|PubMed:10923042, ECO:0000269|PubMed:10931421, ECO:0000269|PubMed:11071391, ECO:0000269|PubMed:11949931, ECO:0000269|PubMed:12409273, ECO:0000269|PubMed:15059622, ECO:0000269|PubMed:15669677, ECO:0000269|PubMed:15953877, ECO:0000269|PubMed:19579760, ECO:0000269|PubMed:21629566, ECO:0000269|PubMed:35304602, ECO:0000269|PubMed:9428641, ECO:0000269|PubMed:9675154, ECO:0000269|PubMed:9758626, ECO:0000269|PubMed:9781688, ECO:0000269|PubMed:9856496, ECO:0000269|Ref.22}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Glycogen storage disease 1C (GSD1C) [MIM:232240]: A metabolic disorder characterized by impairment of terminal steps of glycogenolysis and gluconeogenesis. Patients manifest a wide range of clinical symptoms and biochemical abnormalities, including hypoglycemia, severe hepatomegaly due to excessive accumulation of glycogen, kidney enlargement, growth retardation, lactic acidemia, hyperlipidemia, and hyperuricemia. {ECO:0000269|PubMed:9758626}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Glycogen storage disease 1D (GSD1D) [MIM:232240]: A metabolic disorder characterized by impairment of terminal steps of glycogenolysis and gluconeogenesis. Patients manifest a wide range of clinical symptoms and biochemical abnormalities, including hypoglycemia, severe hepatomegaly due to excessive accumulation of glycogen, kidney enlargement, growth retardation, lactic acidemia, hyperlipidemia, and hyperuricemia. {ECO:0000269|PubMed:9758626}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Congenital disorder of glycosylation 2W (CDG2W) [MIM:619525]: A form of congenital disorder of glycosylation, a genetically heterogeneous group of multisystem disorders caused by a defect in glycoprotein biosynthesis and characterized by under-glycosylated serum glycoproteins. Congenital disorders of glycosylation result in a wide variety of clinical features, such as defects in the nervous system development, psychomotor retardation, dysmorphic features, hypotonia, coagulation disorders, and immunodeficiency. The broad spectrum of features reflects the critical role of N-glycoproteins during embryonic development, differentiation, and maintenance of cell functions. CDG2W is an autosomal dominant disorder characterized by liver dysfunction and coagulation deficiencies. {ECO:0000269|PubMed:32884905, ECO:0000269|PubMed:33728255, ECO:0000269|PubMed:33964207}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
function
FUNCTION: Inorganic phosphate and glucose-6-phosphate antiporter of the endoplasmic reticulum (PubMed:10026167, PubMed:21949678). Transports cytoplasmic glucose-6-phosphate into the lumen of the endoplasmic reticulum and translocates inorganic phosphate into the opposite direction (PubMed:41136424, PubMed:41225049, PubMed:33964207). Responsible for glucose production through glycogenolysis and gluconeogenesis and plays a central role in homeostatic regulation of blood glucose levels (PubMed:10026167, PubMed:21949678, PubMed:33964207). {ECO:0000269|PubMed:10026167, ECO:0000269|PubMed:21949678, ECO:0000269|PubMed:33964207, ECO:0000269|PubMed:41136424, ECO:0000269|PubMed:41225049}.
uniprot
proteins
mass_dalton
46360
uniprot
proteins
mutagenesis
MUTAGEN 21; /note="Y->A: Impairs glucose-6-phosphate uptake."; /evidence="ECO:0000269|PubMed:41225049"; MUTAGEN 25; /note="Y->A: Impairs glucose-6-phosphate uptake."; /evidence="ECO:0000269|PubMed:41225049"; MUTAGEN 28; /note="R->A: Impairs glucose-6-phosphate uptake."; /evidence="ECO:0000269|PubMed:41136424, ECO:0000269|PubMed:41225049"; MUTAGEN 60; /note="Y->A: Impairs glucose-6-phosphate uptake."; /evidence="ECO:0000269|PubMed:41225049"; MUTAGEN 72; /note="D->A: Impairs glucose-6-phosphate uptake."; /evidence="ECO:0000269|PubMed:41136424"; MUTAGEN 118; /note="W->A: Impairs glucose-6-phosphate uptake."; /evidence="ECO:0000269|PubMed:41225049"; MUTAGEN 166; /note="R->L: Impairs glucose-6-phosphate uptake."; /evidence="ECO:0000269|PubMed:41136424"; MUTAGEN 240; /note="K->A,C: Impairs glucose-6-phosphate uptake."; /evidence="ECO:0000269|PubMed:41136424"; MUTAGEN 285; /note="D->A: Impairs glucose-6-phosphate uptake."; /evidence="ECO:0000269|PubMed:41136424
uniprot
proteins
protein_family
Major facilitator superfamily
uniprot
proteins
protein_family
Organophosphate:Pi antiporter (OPA) (TC 2.A.1.4) family
uniprot
proteins
pubmed
10023055
uniprot
proteins
pubmed
10026167
uniprot
proteins
pubmed
10323254
uniprot
proteins
pubmed
10482875
uniprot
proteins
pubmed
10482962
uniprot
proteins
pubmed
10518030
uniprot
proteins
pubmed
10874322
uniprot
proteins
pubmed
10923042
uniprot
proteins
pubmed
10931421
uniprot
proteins
pubmed
11071391
uniprot
proteins
pubmed
11949931
uniprot
proteins
pubmed
12409273
uniprot
proteins
pubmed
15059622
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15669677
uniprot
proteins
pubmed
15953877
uniprot
proteins
pubmed
19579760
uniprot
proteins
pubmed
21629566
uniprot
proteins
pubmed
21949678
uniprot
proteins
pubmed
32884905
uniprot
proteins
pubmed
33728255
uniprot
proteins
pubmed
33964207
uniprot
proteins
pubmed
35304602
uniprot
proteins
pubmed
41136424
uniprot
proteins
pubmed
41225049
uniprot
proteins
pubmed
9428641
uniprot
proteins
pubmed
9675154
uniprot
proteins
pubmed
9758626
uniprot
proteins
pubmed
9781688
uniprot
proteins
pubmed
9856496
uniprot
proteins
sequence_length
429
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:21949678, ECO:0000269|PubMed:32884905, ECO:0000269|PubMed:33964207}; Multi-pass membrane protein {ECO:0000255}.
uniprot
proteins
transmembrane_region
TRANSMEM 12..33; /note="Helical; Name=1"; /evidence="ECO:0000269|PubMed:41136424, ECO:0000269|PubMed:41225049, ECO:0007744|PDB:9KUY, ECO:0007744|PDB:9KV0, ECO:0007744|PDB:9KVV, ECO:0007744|PDB:9W1N, ECO:0007744|PDB:9W1O, ECO:0007744|PDB:9W1P, ECO:0007744|PDB:9W1Q, ECO:0007744|PDB:9W1R"; TRANSMEM 50..70; /note="Helical; Name=2"; /evidence="ECO:0000269|PubMed:41136424, ECO:0000269|PubMed:41225049, ECO:0007744|PDB:9KUY, ECO:0007744|PDB:9KV0, ECO:0007744|PDB:9KVV, ECO:0007744|PDB:9W1N, ECO:0007744|PDB:9W1O, ECO:0007744|PDB:9W1P, ECO:0007744|PDB:9W1Q, ECO:0007744|PDB:9W1R"; TRANSMEM 78..96; /note="Helical; Name=3"; /evidence="ECO:0000269|PubMed:41136424, ECO:0000269|PubMed:41225049, ECO:0007744|PDB:9KUY, ECO:0007744|PDB:9KV0, ECO:0007744|PDB:9KVV, ECO:0007744|PDB:9W1N, ECO:0007744|PDB:9W1O, ECO:0007744|PDB:9W1P, ECO:0007744|PDB:9W1Q, ECO:0007744|PDB:9W1R"; TRANSMEM 102..118; /note="Helical; Name=4"; /evidence="ECO:0000269|PubMed:41136424, ECO:0000269|PubMed:41225049, ECO:0007744|PDB:9KUY, ECO:0007744|PDB:9KV0, ECO:0007744|PDB:9KVV, ECO:0007744|PDB:9W1N, ECO:0007744|PDB:9W1O, ECO:0007744|PDB:9W1P, ECO:0007744|PDB:9W1Q, ECO:0007744|PDB:9W1R"; TRANSMEM 139..159; /note="Helical; Name=5"; /evidence="ECO:0000269|PubMed:41136424, ECO:0000269|PubMed:41225049, ECO:0007744|PDB:9KUY, ECO:0007744|PDB:9KV0, ECO:0007744|PDB:9KVV, ECO:0007744|PDB:9W1N, ECO:0007744|PDB:9W1O, ECO:0007744|PDB:9W1P, ECO:0007744|PDB:9W1Q, ECO:0007744|PDB:9W1R"; TRANSMEM 169..187; /note="Helical; Name=6"; /evidence="ECO:0000269|PubMed:41136424, ECO:0000269|PubMed:41225049, ECO:0007744|PDB:9KUY, ECO:0007744|PDB:9KV0, ECO:0007744|PDB:9KVV, ECO:0007744|PDB:9W1N, ECO:0007744|PDB:9W1O, ECO:0007744|PDB:9W1P, ECO:0007744|PDB:9W1Q, ECO:0007744|PDB:9W1R"; TRANSMEM 226..247; /note="Helical; Name=7"; /evidence="ECO:0000269|PubMed:41136424, ECO:0000269|PubMed:41225049, ECO:0007744|PDB:9KUY, ECO:0007744|PDB:9KV0, ECO:0007744|PDB:9KVV, ECO:0007744|PDB:9W1N, ECO:0007744|PDB:9W1O, ECO:0007744|PDB:9W1P, ECO:0007744|PDB:9W1Q, ECO:0007744|PDB:9W1R"; TRANSMEM 266..283; /note="Helical; Name=8"; /evidence="ECO:0000269|PubMed:41136424, ECO:0000269|PubMed:41225049, ECO:0007744|PDB:9KUY, ECO:0007744|PDB:9KV0, ECO:0007744|PDB:9KVV, ECO:0007744|PDB:9W1N, ECO:0007744|PDB:9W1O, ECO:0007744|PDB:9W1P, ECO:0007744|PDB:9W1Q, ECO:0007744|PDB:9W1R"; TRANSMEM 302..320; /note="Helical; Name=9"; /evidence="ECO:0000269|PubMed:41136424, ECO:0000269|PubMed:41225049, ECO:0007744|PDB:9KUY, ECO:0007744|PDB:9KV0, ECO:0007744|PDB:9KVV, ECO:0007744|PDB:9W1N, ECO:0007744|PDB:9W1O, ECO:0007744|PDB:9W1P, ECO:0007744|PDB:9W1Q, ECO:0007744|PDB:9W1R"; TRANSMEM 329..349; /note="Helical; Name=10"; /evidence="ECO:0000269|PubMed:41136424, ECO:0000269|PubMed:41225049, ECO:0007744|PDB:9KUY, ECO:0007744|PDB:9KV0, ECO:0007744|PDB:9KVV, ECO:0007744|PDB:9W1N, ECO:0007744|PDB:9W1O, ECO:0007744|PDB:9W1P, ECO:0007744|PDB:9W1Q, ECO:0007744|PDB:9W1R"; TRANSMEM 367..384; /note="Helical; Name=11"; /evidence="ECO:0000269|PubMed:41136424, ECO:0000269|PubMed:41225049, ECO:0007744|PDB:9KUY, ECO:0007744|PDB:9KV0, ECO:0007744|PDB:9KVV, ECO:0007744|PDB:9W1N, ECO:0007744|PDB:9W1O, ECO:0007744|PDB:9W1P, ECO:0007744|PDB:9W1Q, ECO:0007744|PDB:9W1R"; TRANSMEM 395..414; /note="Helical; Name=12"; /evidence="ECO:0000269|PubMed:41136424, ECO:0000269|PubMed:41225049, ECO:0007744|PDB:9KUY, ECO:0007744|PDB:9KV0, ECO:0007744|PDB:9KVV, ECO:0007744|PDB:9W1N, ECO:0007744|PDB:9W1O, ECO:0007744|PDB:9W1P, ECO:0007744|PDB:9W1Q, ECO:0007744|PDB:9W1R
uniprot
proteins