ID G6PT1_HUMAN Reviewed; 429 AA. AC O43826; O96016; Q5J7V4; Q9UI19; Q9UNS4; DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1998, sequence version 1. DT 27-MAR-2024, entry version 208. DE RecName: Full=Glucose-6-phosphate exchanger SLC37A4 {ECO:0000305|PubMed:10026167, ECO:0000305|PubMed:21949678}; DE AltName: Full=Glucose-5-phosphate transporter; DE AltName: Full=Glucose-6-phosphate translocase {ECO:0000303|PubMed:9428641}; DE AltName: Full=Solute carrier family 37 member 4 {ECO:0000312|HGNC:HGNC:4061}; DE AltName: Full=Transformation-related gene 19 protein {ECO:0000312|EMBL:AAS00495.1}; DE Short=TRG-19 {ECO:0000312|EMBL:AAS00495.1}; GN Name=SLC37A4 {ECO:0000312|HGNC:HGNC:4061}; Synonyms=G6PT, G6PT1; GN ORFNames=PRO0685, TRG19 {ECO:0000312|EMBL:AAS00495.1}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT GSD1B CYS-339. RC TISSUE=Urinary bladder; RX PubMed=9428641; DOI=10.1016/s0014-5793(97)01463-4; RA Gerin I., Veiga-Da-Cunha M., Achouri Y., Collet J.-F., van Schaftingen E.; RT "Sequence of a putative glucose 6-phosphate translocase, mutated in RT glycogen storage disease type Ib."; RL FEBS Lett. 419:235-238(1997). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), AND VARIANT GSD1B ARG-118. RX PubMed=9856496; DOI=10.1007/s004390050856; RA Ihara K., Kuromaru R., Hara T.; RT "Genomic structure of the human glucose 6-phosphate translocase gene and RT novel mutations in the gene of a Japanese patient with glycogen storage RT disease type Ib."; RL Hum. Genet. 103:493-496(1998). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, TRANSPORTER ACTIVITY, VARIANTS RP GSD1B HIS-28; GLU-149 AND ARG-183, AND CHARACTERIZATION OF VARIANTS GSD1B RP HIS-28; GLU-149 AND ARG-183. RC TISSUE=Liver; RX PubMed=10026167; DOI=10.1074/jbc.274.9.5532; RA Hiraiwa H., Pan C.-J., Lin B., Moses S.W., Chou J.Y.; RT "Inactivation of the glucose 6-phosphate transporter causes glycogen RT storage disease type 1b."; RL J. Biol. Chem. 274:5532-5536(1999). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Fetal liver; RA Zhang C., Yu Y., Zhang S., Ouyang S., Luo L., Wei H., Zhou G., Zhang Y., RA Liu M., He F.; RT "Functional prediction of the coding sequences of 9 new genes deduced by RT analysis of cDNA clones from human fetal liver."; RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2). RA Li Y., van de Werve G.; RT "Four different transcripts of putative glucose-6-phosphate translocase in RT human leukocytes."; RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING. RX PubMed=10023055; DOI=10.1016/s0378-1119(98)00614-3; RA Gerin I., Veiga-Da-Cunha M., Noel G., Van Schaftingen E.; RT "Structure of the gene mutated in glycogen storage disease type Ib."; RL Gene 227:189-195(1999). RN [7] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=10323254; DOI=10.1007/s004390050948; RA Janecke A.R., Bosshard N.U., Mayatepek E., Schulze A., Gitzelmann R., RA Burchell A., Bartram C.R., Janssen B.; RT "Molecular diagnosis of type 1c glycogen storage disease."; RL Hum. Genet. 104:275-277(1999). RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RA Kim J.W.; RT "Identification of a human transformation gene."; RL Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases. RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [10] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Colon, Eye, and Lung; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [11] RP FUNCTION, SUBCELLULAR LOCATION, ACTIVITY REGULATION, AND TRANSPORTER RP ACTIVITY. RX PubMed=21949678; DOI=10.1371/journal.pone.0023157; RA Pan C.J., Chen S.Y., Jun H.S., Lin S.R., Mansfield B.C., Chou J.Y.; RT "SLC37A1 and SLC37A2 are phosphate-linked, glucose-6-phosphate RT antiporters."; RL PLoS ONE 6:E23157-E23157(2011). RN [12] RP REVIEW ON GSD1B VARIANTS, AND VARIANTS GSD1B HIS-28; PRO-85; ASN-278; RP ASP-339 AND ASP-373. RX PubMed=11949931; DOI=10.2174/1566524024605798; RA Chou J.Y., Matern D., Mansfield B.C., Chen Y.-T.; RT "Type I glycogen storage diseases: disorders of the glucose-6-phosphatase RT complex."; RL Curr. Mol. Med. 2:121-143(2002). RN [13] RP VARIANTS GSD1B ASP-20; CYS-28; ARG-55; ARG-68; ASP-88 AND ARG-150, VARIANT RP ILE-198, AND INVOLVEMENT IN GSD1C AND GSD1D. RX PubMed=9758626; DOI=10.1086/302068; RA Veiga-da-Cunha M., Gerin I., Chen Y.-T., de Barsy T., de Lonlay P., RA Dionisi-Vici C., Fenske C.D., Lee P.J., Leonard J.V., Maire I., RA McConkie-Rosell A., Schweitzer S., Vikkula M., Van Schaftingen E.; RT "A gene on chromosome 11q23 coding for a putative glucose-6-phosphate RT translocase is mutated in glycogen-storage disease types Ib and Ic."; RL Am. J. Hum. Genet. 63:976-983(1998). RN [14] RP VARIANT GSD1B HIS-300. RX PubMed=9781688; DOI=10.1016/s0014-5793(98)01129-6; RA Marcolongo P., Barone V., Priori G., Pirola B., Giglio S., Biasucci G., RA Zammarchi E., Parenti G., Burchell A., Benedetti A., Sorrentino V.; RT "Structure and mutation analysis of the glycogen storage disease type 1b RT gene."; RL FEBS Lett. 436:247-250(1998). RN [15] RP ERRATUM OF PUBMED:9781688. RA Marcolongo P., Barone V., Priori G., Giglio S., Benedetti A., RA Sorrentino V.; RL FEBS Lett. 445:451-451(1999). RN [16] RP VARIANTS GSD1B ARG-50; ARG-176; ARG-183 AND CYS-300, AND VARIANTS GSD1C RP PRO-133 AND SER-376. RX PubMed=10482962; DOI=10.1038/sj.ejhg.5200366; RA Veiga-da-Cunha M., Gerin I., Chen Y.-T., Lee P.J., Leonard J.V., Maire I., RA Wendel U., Vikkula M., Van Schaftingen E.; RT "The putative glucose 6-phosphate translocase gene is mutated in RT essentially all cases of glycogen storage disease type I non-a."; RL Eur. J. Hum. Genet. 7:717-723(1999). RN [17] RP VARIANT GSD1B THR-367. RX PubMed=10518030; DOI=10.1016/s0014-5793(99)01248-x; RA Galli L., Orrico A., Marcolongo P., Fulceri R., Burchell A., Melis D., RA Parini R., Gatti R., Lam C.-W., Benedetti A., Sorrentino V.; RT "Mutations in the glucose-6-phosphate transporter (G6PT) gene in patients RT with glycogen storage diseases type 1b and 1c."; RL FEBS Lett. 459:255-258(1999). RN [18] RP VARIANT GSD1B ARG-118. RX PubMed=9675154; DOI=10.1006/bbrc.1998.8985; RA Kure S., Suzuki Y., Matsubara Y., Sakamoto O., Shintaku H., Isshiki G., RA Hoshida C., Izumi I., Sakura N., Narisawa K.; RT "Molecular analysis of glycogen storage disease type Ib: identification of RT a prevalent mutation among Japanese patients and assignment of a putative RT glucose-6-phosphate translocase gene to chromosome 11."; RL Biochem. Biophys. Res. Commun. 248:426-431(1998). RN [19] RP VARIANTS GSD1B ARG-118 AND VAL-235 DEL. RX PubMed=10482875; RX DOI=10.1002/(sici)1096-8628(19990917)86:3<253::aid-ajmg11>3.0.co;2-7; RA Hou D.-C., Kure S., Suzuki Y., Hasegawa Y., Hara Y., Inoue T., Kida Y., RA Matsubara Y., Narisawa K.; RT "Glycogen storage disease type Ib: structural and mutational analysis of RT the microsomal glucose-6-phosphate transporter gene."; RL Am. J. Med. Genet. 86:253-257(1999). RN [20] RP VARIANT GSD1B GLU-149. RA Lam C.-W., Tong S.-F., Lam Y.-Y., Chan B.-Y., Ma C.-H., Lim P.-L.; RT "Identification of a novel missense mutation (G149E) in the glucose-6- RT phosphate translocase gene in a Chinese family with glycogen storage RT disease 1b."; RL Hum. Mutat. 13:507-507(1999). RN [21] RP VARIANT GSD1B ARG-54. RX PubMed=11071391; DOI=10.1007/s004390000371; RA Janecke A.R., Lindner M., Erdel M., Mayatepek E., Moeslinger D., RA Podskarbi T., Fresser F., Stoeckler-Ipsiroglu S., Hoffmann G.F., RA Utermann G.; RT "Mutation analysis in glycogen storage disease type 1 non-a."; RL Hum. Genet. 107:285-289(2000). RN [22] RP VARIANT GSD1B LEU-191. RX PubMed=10874322; RX DOI=10.1002/1098-1004(200007)16:1<94::aid-humu26>3.0.co;2-q; RA Lam C.-W., Chan K.-Y., Tong S.-F., Chan B.Y., Chan Y.-T., Chan Y.-W.; RT "A novel missense mutation (P191L) in the glucose-6-phosphate translocase RT gene identified in a Chinese family with glycogen storage disease 1b."; RL Hum. Mutat. 16:94-94(2000). RN [23] RP VARIANTS GSD1B LYS-27; LEU-153 AND PRO-301. RX PubMed=10923042; RX DOI=10.1002/1098-1004(200008)16:2<177::aid-humu13>3.0.co;2-8; RA Santer R., Rischewski J., Block G., Kinner M., Wendel U., Schaub J., RA Schneppenheim R.; RT "Molecular analysis in glycogen storage disease 1 non-A: DHPLC detection of RT the highly prevalent exon 8 mutations of the G6PT1 gene in German RT patients."; RL Hum. Mutat. 16:177-177(2000). RN [24] RP VARIANT GSD1B ASP-339. RX PubMed=10931421; DOI=10.1067/mpd.2000.107472; RA Kure S., Hou D.-C., Suzuki Y., Yamagishi A., Hiratsuka M., Fukuda T., RA Sugie H., Kondo N., Matsubara Y., Narisawa K.; RT "Glycogen storage disease type Ib without neutropenia."; RL J. Pediatr. 137:253-256(2000). RN [25] RP VARIANT GSD1B HIS-24. RX PubMed=12409273; DOI=10.1016/s1096-7192(02)00110-5; RA Yuen Y.-P., Cheng W.-F., Tong S.-F., Chan Y.-T., Chan Y.-W., Lam C.-W.; RT "Novel missense mutation (Y24H) in the G6PT1 gene causing glycogen storage RT disease type 1b."; RL Mol. Genet. Metab. 77:249-251(2002). RN [26] RP VARIANT GSD1B PRO-229. RX PubMed=15669677; DOI=10.1023/b:boli.0000042987.43395.c6; RA Trioche P., Petit F., Francoual J., Gajdos V., Capel L., Poues C., RA Labrune P.; RT "Allelic heterogeneity of glycogen storage disease type Ib in French RT patients: a study of 11 cases."; RL J. Inherit. Metab. Dis. 27:621-623(2004). RN [27] RP VARIANT GSD1B ARG-118. RX PubMed=15059622; DOI=10.1016/j.ymgme.2003.12.004; RA Kojima K., Kure S., Kamada F., Hao K., Ichinohe A., Sato K., Aoki Y., RA Yoichi S., Kubota M., Horikawa R., Utsumi A., Miura M., Ogawa S., RA Kanazawa M., Kohno Y., Inokuchi M., Hasegawa T., Narisawa K., Matsubara Y.; RT "Genetic testing of glycogen storage disease type Ib in Japan: five novel RT G6PT1 mutations and a rapid detection method for a prevalent mutation RT W118R."; RL Mol. Genet. Metab. 81:343-346(2004). RN [28] RP VARIANT GSD1B VAL-148. RX PubMed=15953877; DOI=10.3346/jkms.2005.20.3.499; RA Han S.H., Ki C.S., Lee J.E., Hong Y.J., Son B.K., Lee K.H., Choe Y.H., RA Lee S.Y., Kim J.W.; RT "A novel mutation (A148V) in the glucose 6-phosphate translocase (SLC37A4) RT gene in a Korean patient with glycogen storage disease type 1b."; RL J. Korean Med. Sci. 20:499-501(2005). RN [29] RP VARIANT GSD1B ARG-246. RX PubMed=19579760; DOI=10.1016/s1875-9572(09)60048-6; RA Hsiao H.J., Chang H.H., Hwu W.L., Lam C.W., Lee N.C., Chien Y.H.; RT "Glycogen storage disease type Ib: the first case in Taiwan."; RL Pediatr. Neonatol. 50:125-128(2009). RN [30] RP VARIANT GSD1B GLU-50. RX PubMed=21629566; DOI=10.4172/1747-0862.1000046; RA Dissanayake V.H., Jayasinghe J.D., Thilakaratne V., Jayasekara R.W.; RT "A novel mutation in SLC37A4 gene in a Sri Lankan boy with glycogen storage RT disease type Ib associated with very early onset neutropenia."; RL J. Mol. Genet. Med. 5:262-263(2011). RN [31] RP INVOLVEMENT IN CDG2W, VARIANT CDG2W 423-ARG--GLU-429 DEL, CHARACTERIZATION RP OF VARIANT CDG2W 423-ARG--GLU-429 DEL, AND SUBCELLULAR LOCATION. RX PubMed=32884905; DOI=10.1016/j.ymgmr.2020.100636; RA Marquardt T., Bzduch V., Hogrebe M., Rust S., Reunert J., Grueneberg M., RA Park J., Callewaert N., Lachmann R., Wada Y., Engel T.; RT "SLC37A4-CDG: Mislocalization of the glucose-6-phosphate transporter to the RT Golgi causes a new congenital disorder of glycosylation."; RL Mol. Genet. Metab. Rep. 25:100636-100636(2020). RN [32] RP INVOLVEMENT IN CDG2W, CHARACTERIZATION OF VARIANT CDG2W 423-ARG--GLU-429 RP DEL, SUBCELLULAR LOCATION, FUNCTION, AND TRANSPORTER ACTIVITY. RX PubMed=33964207; DOI=10.1016/j.ajhg.2021.04.013; RG University of Washington Center for Mendelian Genomics (UW-CMG); RA Ng B.G., Sosicka P., Fenaille F., Harroche A., Vuillaumier-Barrot S., RA Porterfield M., Xia Z.J., Wagner S., Bamshad M.J., Vergnes-Boiteux M.C., RA Cholet S., Dalton S., Dell A., Dupre T., Fiore M., Haslam S.M., RA Huguenin Y., Kumagai T., Kulik M., McGoogan K., Michot C., Nickerson D.A., RA Pascreau T., Borgel D., Raymond K., Warad D., Flanagan-Steet H., Steet R., RA Tiemeyer M., Seta N., Bruneel A., Freeze H.H.; RT "A mutation in SLC37A4 causes a dominantly inherited congenital disorder of RT glycosylation characterized by liver dysfunction."; RL Am. J. Hum. Genet. 108:1040-1052(2021). RN [33] RP INVOLVEMENT IN CDG2W, AND VARIANT CDG2W 423-ARG--GLU-429 DEL. RX PubMed=33728255; DOI=10.1002/jmd2.12195; RA Wilson M.P., Quelhas D., Leao-Teles E., Sturiale L., Rymen D., RA Keldermans L., Race V., Souche E., Rodrigues E., Campos T., RA Van Schaftingen E., Foulquier F., Garozzo D., Matthijs G., Jaeken J.; RT "SLC37A4-CDG: Second patient."; RL JIMD Rep. 58:122-128(2021). CC -!- FUNCTION: Inorganic phosphate and glucose-6-phosphate antiporter of the CC endoplasmic reticulum. Transports cytoplasmic glucose-6-phosphate into CC the lumen of the endoplasmic reticulum and translocates inorganic CC phosphate into the opposite direction (PubMed:33964207). Forms with CC glucose-6-phosphatase the complex responsible for glucose production CC through glycogenolysis and gluconeogenesis. Hence, it plays a central CC role in homeostatic regulation of blood glucose levels. CC {ECO:0000269|PubMed:10026167, ECO:0000269|PubMed:21949678, CC ECO:0000269|PubMed:33964207}. CC -!- CATALYTIC ACTIVITY: CC Reaction=D-glucose 6-phosphate(in) + phosphate(out) = D-glucose 6- CC phosphate(out) + phosphate(in); Xref=Rhea:RHEA:71535, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:61548; CC Evidence={ECO:0000269|PubMed:10026167, ECO:0000269|PubMed:21949678, CC ECO:0000269|PubMed:33964207}; CC -!- ACTIVITY REGULATION: Inhibited by vanadate and chlorogenic acid. CC {ECO:0000269|PubMed:21949678}. CC -!- INTERACTION: CC O43826; Q13323: BIK; NbExp=3; IntAct=EBI-6269684, EBI-700794; CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane CC {ECO:0000269|PubMed:21949678, ECO:0000269|PubMed:32884905, CC ECO:0000269|PubMed:33964207}; Multi-pass membrane protein CC {ECO:0000255}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=O43826-1; Sequence=Displayed; CC Name=2; CC IsoId=O43826-2; Sequence=VSP_006171; CC -!- TISSUE SPECIFICITY: Mostly expressed in liver and kidney. CC -!- DISEASE: Glycogen storage disease 1B (GSD1B) [MIM:232220]: A metabolic CC disorder characterized by impairment of terminal steps of CC glycogenolysis and gluconeogenesis. Patients manifest a wide range of CC clinical symptoms and biochemical abnormalities, including CC hypoglycemia, severe hepatomegaly due to excessive accumulation of CC glycogen, kidney enlargement, growth retardation, lactic acidemia, CC hyperlipidemia, and hyperuricemia. Glycogen storage disease type 1B CC patients also present a tendency towards infections associated with CC neutropenia, relapsing aphthous gingivostomatitis, and inflammatory CC bowel disease. {ECO:0000269|PubMed:10026167, CC ECO:0000269|PubMed:10482875, ECO:0000269|PubMed:10482962, CC ECO:0000269|PubMed:10518030, ECO:0000269|PubMed:10874322, CC ECO:0000269|PubMed:10923042, ECO:0000269|PubMed:10931421, CC ECO:0000269|PubMed:11071391, ECO:0000269|PubMed:11949931, CC ECO:0000269|PubMed:12409273, ECO:0000269|PubMed:15059622, CC ECO:0000269|PubMed:15669677, ECO:0000269|PubMed:15953877, CC ECO:0000269|PubMed:19579760, ECO:0000269|PubMed:21629566, CC ECO:0000269|PubMed:9428641, ECO:0000269|PubMed:9675154, CC ECO:0000269|PubMed:9758626, ECO:0000269|PubMed:9781688, CC ECO:0000269|PubMed:9856496, ECO:0000269|Ref.20}. Note=The disease is CC caused by variants affecting the gene represented in this entry. CC -!- DISEASE: Glycogen storage disease 1C (GSD1C) [MIM:232240]: A metabolic CC disorder characterized by impairment of terminal steps of CC glycogenolysis and gluconeogenesis. Patients manifest a wide range of CC clinical symptoms and biochemical abnormalities, including CC hypoglycemia, severe hepatomegaly due to excessive accumulation of CC glycogen, kidney enlargement, growth retardation, lactic acidemia, CC hyperlipidemia, and hyperuricemia. {ECO:0000269|PubMed:9758626}. CC Note=The disease is caused by variants affecting the gene represented CC in this entry. CC -!- DISEASE: Glycogen storage disease 1D (GSD1D) [MIM:232240]: A metabolic CC disorder characterized by impairment of terminal steps of CC glycogenolysis and gluconeogenesis. Patients manifest a wide range of CC clinical symptoms and biochemical abnormalities, including CC hypoglycemia, severe hepatomegaly due to excessive accumulation of CC glycogen, kidney enlargement, growth retardation, lactic acidemia, CC hyperlipidemia, and hyperuricemia. {ECO:0000269|PubMed:9758626}. CC Note=The disease is caused by variants affecting the gene represented CC in this entry. CC -!- DISEASE: Congenital disorder of glycosylation 2W (CDG2W) [MIM:619525]: CC A form of congenital disorder of glycosylation, a genetically CC heterogeneous group of multisystem disorders caused by a defect in CC glycoprotein biosynthesis and characterized by under-glycosylated serum CC glycoproteins. Congenital disorders of glycosylation result in a wide CC variety of clinical features, such as defects in the nervous system CC development, psychomotor retardation, dysmorphic features, hypotonia, CC coagulation disorders, and immunodeficiency. The broad spectrum of CC features reflects the critical role of N-glycoproteins during embryonic CC development, differentiation, and maintenance of cell functions. CDG2W CC is an autosomal dominant disorder characterized by liver dysfunction CC and coagulation deficiencies. {ECO:0000269|PubMed:32884905, CC ECO:0000269|PubMed:33728255, ECO:0000269|PubMed:33964207}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- SIMILARITY: Belongs to the major facilitator superfamily. CC Organophosphate:Pi antiporter (OPA) (TC 2.A.1.4) family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAF16691.1; Type=Frameshift; Evidence={ECO:0000305}; CC -!- WEB RESOURCE: Name=Mendelian genes solute carrier family 37 CC (glucose-6-phosphate transporter), member 4 (SLC37A4); Note=Leiden Open CC Variation Database (LOVD); CC URL="https://databases.lovd.nl/shared/genes/SLC37A4"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; Y15409; CAA75608.1; -; mRNA. DR EMBL; AF078163; AAC72916.1; -; Genomic_DNA. DR EMBL; AF097831; AAD19898.1; -; Genomic_DNA. DR EMBL; AF111852; AAF16691.1; ALT_FRAME; mRNA. DR EMBL; AF110819; AAF37735.1; -; mRNA. DR EMBL; AF110820; AAF37736.1; -; mRNA. DR EMBL; Y17864; CAA76898.1; -; Genomic_DNA. DR EMBL; AF116864; AAD13111.1; -; Genomic_DNA. DR EMBL; AF116862; AAD13111.1; JOINED; Genomic_DNA. DR EMBL; AF116863; AAD13111.1; JOINED; Genomic_DNA. DR EMBL; AY423732; AAS00495.1; -; mRNA. DR EMBL; CH471065; EAW67432.1; -; Genomic_DNA. DR EMBL; BC002400; AAH02400.1; -; mRNA. DR EMBL; BC003589; AAH03589.1; -; mRNA. DR EMBL; BC014663; AAH14663.1; -; mRNA. DR EMBL; BC015650; AAH15650.1; -; mRNA. DR EMBL; BC064563; AAH64563.1; -; mRNA. DR RefSeq; NP_001157749.1; NM_001164277.1. [O43826-1] DR RefSeq; NP_001157750.1; NM_001164278.1. [O43826-2] DR RefSeq; NP_001157751.1; NM_001164279.1. DR RefSeq; NP_001157752.1; NM_001164280.1. [O43826-1] DR RefSeq; NP_001458.1; NM_001467.5. [O43826-1] DR AlphaFoldDB; O43826; -. DR SMR; O43826; -. DR BioGRID; 108817; 51. DR IntAct; O43826; 5. DR MINT; O43826; -. DR STRING; 9606.ENSP00000476176; -. DR BindingDB; O43826; -. DR ChEMBL; CHEMBL3217398; -. DR TCDB; 2.A.1.4.5; the major facilitator superfamily (mfs). DR iPTMnet; O43826; -. DR PhosphoSitePlus; O43826; -. DR SwissPalm; O43826; -. DR BioMuta; SLC37A4; -. DR EPD; O43826; -. DR jPOST; O43826; -. DR MassIVE; O43826; -. DR MaxQB; O43826; -. DR PaxDb; 9606-ENSP00000476176; -. DR PeptideAtlas; O43826; -. DR ProteomicsDB; 49192; -. [O43826-1] DR ProteomicsDB; 49193; -. [O43826-2] DR Pumba; O43826; -. DR DNASU; 2542; -. DR Ensembl; ENST00000642844.2; ENSP00000493469.1; ENSG00000281500.4. [O43826-1] DR Ensembl; ENST00000710540.1; ENSP00000518334.1; ENSG00000281500.4. [O43826-2] DR Ensembl; ENST00000710542.1; ENSP00000518335.1; ENSG00000281500.4. [O43826-1] DR Ensembl; ENST00000710545.1; ENSP00000518336.1; ENSG00000281500.4. [O43826-2] DR Ensembl; ENST00000710550.1; ENSP00000518339.1; ENSG00000281500.4. [O43826-1] DR GeneID; 2542; -. DR KEGG; hsa:2542; -. DR MANE-Select; ENST00000642844.3; ENSP00000493469.1; NM_001164277.2; NP_001157749.1. DR AGR; HGNC:4061; -. DR CTD; 2542; -. DR DisGeNET; 2542; -. DR GeneCards; SLC37A4; -. DR GeneReviews; SLC37A4; -. DR HGNC; HGNC:4061; SLC37A4. DR MalaCards; SLC37A4; -. DR MIM; 232220; phenotype. DR MIM; 232240; phenotype. DR MIM; 602671; gene. DR MIM; 619525; phenotype. DR neXtProt; NX_O43826; -. DR Orphanet; 79259; Glycogen storage disease due to glucose-6-phosphatase deficiency type Ib. DR PharmGKB; PA28472; -. DR eggNOG; KOG2533; Eukaryota. DR InParanoid; O43826; -. DR OrthoDB; 130766at2759; -. DR PhylomeDB; O43826; -. DR PathwayCommons; O43826; -. DR Reactome; R-HSA-3229133; Glycogen storage disease type Ib (SLC37A4). DR Reactome; R-HSA-70263; Gluconeogenesis. DR SignaLink; O43826; -. DR BioGRID-ORCS; 2542; 11 hits in 295 CRISPR screens. DR ChiTaRS; SLC37A4; human. DR GeneWiki; SLC37A4; -. DR GenomeRNAi; 2542; -. DR Pharos; O43826; Tchem. DR PRO; PR:O43826; -. DR Proteomes; UP000005640; Unplaced. DR RNAct; O43826; Protein. DR GO; GO:0005783; C:endoplasmic reticulum; NAS:UniProtKB. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0061513; F:glucose 6-phosphate:inorganic phosphate antiporter activity; IDA:UniProtKB. DR GO; GO:0015152; F:glucose-6-phosphate transmembrane transporter activity; IDA:UniProtKB. DR GO; GO:0008643; P:carbohydrate transport; IEA:UniProtKB-KW. DR GO; GO:0006094; P:gluconeogenesis; TAS:Reactome. DR GO; GO:0042593; P:glucose homeostasis; IDA:UniProtKB. DR GO; GO:0006006; P:glucose metabolic process; NAS:UniProtKB. DR GO; GO:0015760; P:glucose-6-phosphate transport; IDA:UniProtKB. DR GO; GO:0035435; P:phosphate ion transmembrane transport; IDA:UniProtKB. DR CDD; cd17343; MFS_SLC37A4; 1. DR Gene3D; 1.20.1250.20; MFS general substrate transporter like domains; 2. DR InterPro; IPR011701; MFS. DR InterPro; IPR020846; MFS_dom. DR InterPro; IPR036259; MFS_trans_sf. DR InterPro; IPR021159; Sugar-P_transporter_CS. DR InterPro; IPR000849; Sugar_P_transporter. DR NCBIfam; TIGR00881; 2A0104; 1. DR PANTHER; PTHR43826; GLUCOSE-6-PHOSPHATE EXCHANGER SLC37A4; 1. DR PANTHER; PTHR43826:SF3; GLUCOSE-6-PHOSPHATE EXCHANGER SLC37A4; 1. DR Pfam; PF07690; MFS_1; 1. DR PIRSF; PIRSF002808; Hexose_phosphate_transp; 1. DR SUPFAM; SSF103473; MFS general substrate transporter; 1. DR PROSITE; PS00942; GLPT; 1. DR PROSITE; PS50850; MFS; 1. PE 1: Evidence at protein level; KW Alternative splicing; Antiport; Congenital disorder of glycosylation; KW Disease variant; Endoplasmic reticulum; Glycogen storage disease; Membrane; KW Reference proteome; Sugar transport; Transmembrane; Transmembrane helix; KW Transport. FT CHAIN 1..429 FT /note="Glucose-6-phosphate exchanger SLC37A4" FT /id="PRO_0000199891" FT TRANSMEM 84..104 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 105..125 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 139..159 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 167..187 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 219..239 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 260..280 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 302..322 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 329..349 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 368..388 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 394..414 FT /note="Helical" FT /evidence="ECO:0000255" FT VAR_SEQ 328 FT /note="K -> KDVAFWTLALHPLAELTGFTEHE (in isoform 2)" FT /evidence="ECO:0000303|Ref.5" FT /id="VSP_006171" FT VARIANT 20 FT /note="G -> D (in GSD1B; dbSNP:rs193302881)" FT /evidence="ECO:0000269|PubMed:9758626" FT /id="VAR_025581" FT VARIANT 24 FT /note="Y -> H (in GSD1B; dbSNP:rs193302887)" FT /evidence="ECO:0000269|PubMed:12409273" FT /id="VAR_025582" FT VARIANT 27 FT /note="N -> K (in GSD1B; dbSNP:rs193302889)" FT /evidence="ECO:0000269|PubMed:10923042" FT /id="VAR_025583" FT VARIANT 28 FT /note="R -> C (in GSD1B; dbSNP:rs193302882)" FT /evidence="ECO:0000269|PubMed:9758626" FT /id="VAR_025584" FT VARIANT 28 FT /note="R -> H (in GSD1B; inactive glucose-6-phosphate FT transport; dbSNP:rs121908978)" FT /evidence="ECO:0000269|PubMed:10026167, FT ECO:0000269|PubMed:11949931" FT /id="VAR_016840" FT VARIANT 50 FT /note="G -> E (in GSD1B; dbSNP:rs193302877)" FT /evidence="ECO:0000269|PubMed:21629566" FT /id="VAR_066394" FT VARIANT 50 FT /note="G -> R (in GSD1B; dbSNP:rs193302894)" FT /evidence="ECO:0000269|PubMed:10482962" FT /id="VAR_025585" FT VARIANT 54 FT /note="S -> R (in GSD1B; dbSNP:rs193302898)" FT /evidence="ECO:0000269|PubMed:11071391" FT /id="VAR_025586" FT VARIANT 55 FT /note="S -> R (in GSD1B; dbSNP:rs193302884)" FT /evidence="ECO:0000269|PubMed:9758626" FT /id="VAR_025587" FT VARIANT 68 FT /note="G -> R (in GSD1B; dbSNP:rs193302885)" FT /evidence="ECO:0000269|PubMed:9758626" FT /id="VAR_025588" FT VARIANT 85 FT /note="L -> P (in GSD1B; dbSNP:rs193302899)" FT /evidence="ECO:0000269|PubMed:11949931" FT /id="VAR_025589" FT VARIANT 88 FT /note="G -> D (in GSD1B; dbSNP:rs193302886)" FT /evidence="ECO:0000269|PubMed:9758626" FT /id="VAR_025590" FT VARIANT 118 FT /note="W -> R (in GSD1B; dbSNP:rs80356489)" FT /evidence="ECO:0000269|PubMed:10482875, FT ECO:0000269|PubMed:15059622, ECO:0000269|PubMed:9675154, FT ECO:0000269|PubMed:9856496" FT /id="VAR_007850" FT VARIANT 133 FT /note="Q -> P (in GSD1C; dbSNP:rs193302896)" FT /evidence="ECO:0000269|PubMed:10482962" FT /id="VAR_025591" FT VARIANT 148 FT /note="A -> V (in GSD1B; dbSNP:rs193302879)" FT /evidence="ECO:0000269|PubMed:15953877" FT /id="VAR_066395" FT VARIANT 149 FT /note="G -> E (in GSD1B; inactive glucose-6-phosphate FT transport; dbSNP:rs193302892)" FT /evidence="ECO:0000269|PubMed:10026167, ECO:0000269|Ref.20" FT /id="VAR_003184" FT VARIANT 150 FT /note="G -> R (in GSD1B; dbSNP:rs193302883)" FT /evidence="ECO:0000269|PubMed:9758626" FT /id="VAR_025592" FT VARIANT 153 FT /note="P -> L (in GSD1B; dbSNP:rs193302890)" FT /evidence="ECO:0000269|PubMed:10923042" FT /id="VAR_025593" FT VARIANT 176 FT /note="C -> R (in GSD1B; dbSNP:rs193302895)" FT /evidence="ECO:0000269|PubMed:10482962" FT /id="VAR_025594" FT VARIANT 183 FT /note="C -> R (in GSD1B; inactive glucose-6-phosphate FT transport; dbSNP:rs193302893)" FT /evidence="ECO:0000269|PubMed:10026167, FT ECO:0000269|PubMed:10482962" FT /id="VAR_025595" FT VARIANT 191 FT /note="P -> L (in GSD1B; dbSNP:rs193302888)" FT /evidence="ECO:0000269|PubMed:10874322" FT /id="VAR_032113" FT VARIANT 198 FT /note="N -> I (in dbSNP:rs34203644)" FT /evidence="ECO:0000269|PubMed:9758626" FT /id="VAR_025596" FT VARIANT 229 FT /note="L -> P (in GSD1B; dbSNP:rs193302902)" FT /evidence="ECO:0000269|PubMed:15669677" FT /id="VAR_025597" FT VARIANT 235 FT /note="Missing (in GSD1B)" FT /evidence="ECO:0000269|PubMed:10482875" FT /id="VAR_012356" FT VARIANT 246 FT /note="W -> R (in GSD1B; dbSNP:rs193302878)" FT /evidence="ECO:0000269|PubMed:19579760" FT /id="VAR_066396" FT VARIANT 278 FT /note="I -> N (in GSD1B; dbSNP:rs193302900)" FT /evidence="ECO:0000269|PubMed:11949931" FT /id="VAR_025598" FT VARIANT 300 FT /note="R -> C (in GSD1B; dbSNP:rs193302880)" FT /evidence="ECO:0000269|PubMed:10482962" FT /id="VAR_066397" FT VARIANT 300 FT /note="R -> H (in GSD1B; dbSNP:rs193302903)" FT /evidence="ECO:0000269|PubMed:9781688" FT /id="VAR_025599" FT VARIANT 301 FT /note="H -> P (in GSD1B; dbSNP:rs193302891)" FT /evidence="ECO:0000269|PubMed:10923042" FT /id="VAR_025600" FT VARIANT 339 FT /note="G -> C (in GSD1B; dbSNP:rs80356490)" FT /evidence="ECO:0000269|PubMed:9428641" FT /id="VAR_003185" FT VARIANT 339 FT /note="G -> D (in GSD1B; dbSNP:rs121908980)" FT /evidence="ECO:0000269|PubMed:10931421, FT ECO:0000269|PubMed:11949931" FT /id="VAR_025601" FT VARIANT 367 FT /note="A -> T (in GSD1B; dbSNP:rs80356492)" FT /evidence="ECO:0000269|PubMed:10518030" FT /id="VAR_025602" FT VARIANT 373 FT /note="A -> D (in GSD1B; dbSNP:rs193302901)" FT /evidence="ECO:0000269|PubMed:11949931" FT /id="VAR_025603" FT VARIANT 376 FT /note="G -> S (in GSD1C; dbSNP:rs193302897)" FT /evidence="ECO:0000269|PubMed:10482962" FT /id="VAR_025604" FT VARIANT 423..429 FT /note="Missing (in CDG2W; affects the endoplasmic reticulum FT subcellular location, relocalizing the protein either to FT the Golgi apparatus, or to a distinct, non-Golgi FT compartment, possibly endoplasmic reticulum exit sites; FT when transfected into HepG2 cells, significantly changes FT the protein glycosylation pattern, such as that of FT transferrin; does not affect glucose-6-phosphate transport FT activity)" FT /evidence="ECO:0000269|PubMed:32884905, FT ECO:0000269|PubMed:33728255, ECO:0000269|PubMed:33964207" FT /id="VAR_086301" FT CONFLICT 109 FT /note="L -> F (in Ref. 3; AAD19898)" FT /evidence="ECO:0000305" SQ SEQUENCE 429 AA; 46360 MW; C0399332FE72694B CRC64; MAAQGYGYYR TVIFSAMFGG YSLYYFNRKT FSFVMPSLVE EIPLDKDDLG FITSSQSAAY AISKFVSGVL SDQMSARWLF SSGLLLVGLV NIFFAWSSTV PVFAALWFLN GLAQGLGWPP CGKVLRKWFE PSQFGTWWAI LSTSMNLAGG LGPILATILA QSYSWRSTLA LSGALCVVVS FLCLLLIHNE PADVGLRNLD PMPSEGKKGS LKEESTLQEL LLSPYLWVLS TGYLVVFGVK TCCTDWGQFF LIQEKGQSAL VGSSYMSALE VGGLVGSIAA GYLSDRAMAK AGLSNYGNPR HGLLLFMMAG MTVSMYLFRV TVTSDSPKLW ILVLGAVFGF SSYGPIALFG VIANESAPPN LCGTSHAIVG LMANVGGFLA GLPFSTIAKH YSWSTAFWVA EVICAASTAA FFLLRNIRTK MGRVSKKAE //