G6PT1_HUMAN
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 03-AUG-2022, entry version 201.
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, VARIANT GSD1B HIS-28, AND
RP CHARACTERIZATION OF VARIANT HIS-28.
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, AND ACTIVITY REGULATION.
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, AND FUNCTION.
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 -!- 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:10482962,
CC ECO:0000269|PubMed:9758626}. Note=The disease is caused by variants
CC affecting the gene represented 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 (glucose-6-
CC phosphate transporter), member 4 (SLC37A4); Note=Leiden Open Variation
CC Database (LOVD);
CC URL="https://databases.lovd.nl/shared/genes/SLC37A4";
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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; 47.
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 BioMuta; SLC37A4; -.
DR EPD; O43826; -.
DR jPOST; O43826; -.
DR MassIVE; O43826; -.
DR MaxQB; O43826; -.
DR PeptideAtlas; O43826; -.
DR PRIDE; O43826; -.
DR ProteomicsDB; 49192; -. [O43826-1]
DR ProteomicsDB; 49193; -. [O43826-2]
DR DNASU; 2542; -.
DR Ensembl; ENST00000642844.2; ENSP00000493469.1; ENSG00000281500.3. [O43826-1]
DR Ensembl; ENST00000645735.2; ENSP00000495653.1; ENSG00000281500.3. [O43826-1]
DR GeneID; 2542; -.
DR KEGG; hsa:2542; -.
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 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; 10 hits in 240 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; TAS:Reactome.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; NAS: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 Gene3D; 1.20.1250.20; -; 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 Pfam; PF07690; MFS_1; 1.
DR PIRSF; PIRSF002808; Hexose_phosphate_transp; 1.
DR SUPFAM; SSF103473; SSF103473; 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; dbSNP:rs193302892)"
FT /evidence="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; dbSNP:rs193302893)"
FT /evidence="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
