G6PT3_MOUSE
ID G6PT3_MOUSE Reviewed; 501 AA.
AC Q9WU81; Q571N8; Q6P4P0; Q8BV90; Q8C144; Q8R1Y0;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Glucose-6-phosphate exchanger SLC37A2 {ECO:0000305};
DE AltName: Full=Solute carrier family 37 member 2 {ECO:0000312|MGI:MGI:1929693};
DE AltName: Full=cAMP-inducible protein 2 {ECO:0000303|PubMed:11004510};
GN Name=Slc37a2 {ECO:0000312|MGI:MGI:1929693};
GN Synonyms=Ci2 {ECO:0000303|PubMed:11004510};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=11004510; DOI=10.1016/s0167-4781(00)00133-0;
RA Takahashi Y., Miyata M., Zheng P., Imazato T., Horwitz A., Smith J.D.;
RT "Identification of cAMP analogue inducible genes in RAW264 macrophages.";
RL Biochim. Biophys. Acta 1492:385-394(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Bone, Skin, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=FVB/N; TISSUE=Heart, Lung, and Salivary gland;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 60-501 (ISOFORM 2).
RC TISSUE=Embryonic intestine;
RA Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene. The
RT complete nucleotide sequences of mouse KIAA-homologous cDNAs identified by
RT screening of terminal sequences of cDNA clones randomly sampled from size-
RT fractionated libraries.";
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Inorganic phosphate and glucose-6-phosphate antiporter. May
CC transport cytoplasmic glucose-6-phosphate into the lumen of the
CC endoplasmic reticulum and translocate inorganic phosphate into the
CC opposite direction. Independent of a lumenal glucose-6-phosphatase. May
CC not play a role in homeostatic regulation of blood glucose levels.
CC {ECO:0000250|UniProtKB:Q8TED4}.
CC -!- ACTIVITY REGULATION: Inhibited by vanadate but not by chlorogenic acid.
CC {ECO:0000250|UniProtKB:Q8TED4}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q8TED4}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9WU81-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9WU81-2; Sequence=VSP_028964;
CC -!- TISSUE SPECIFICITY: Highly expressed in bone marrow derived
CC macrophages, and weakly in spleen. {ECO:0000269|PubMed:11004510}.
CC -!- INDUCTION: Up-regulated by cAMP in macrophages.
CC {ECO:0000269|PubMed:11004510}.
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=BAD90337.1; Type=Frameshift; Evidence={ECO:0000305};
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; AF121081; AAD24571.1; -; mRNA.
DR EMBL; AK028984; BAC26224.1; -; mRNA.
DR EMBL; AK031045; BAC27227.1; -; mRNA.
DR EMBL; AK079414; BAC37639.1; -; mRNA.
DR EMBL; AK079823; BAC37758.1; -; mRNA.
DR EMBL; BC022752; AAH22752.1; -; mRNA.
DR EMBL; BC063326; AAH63326.1; -; mRNA.
DR EMBL; AK220151; BAD90337.1; ALT_FRAME; mRNA.
DR CCDS; CCDS40582.1; -. [Q9WU81-1]
DR CCDS; CCDS52769.1; -. [Q9WU81-2]
DR RefSeq; NP_001139432.1; NM_001145960.1. [Q9WU81-2]
DR RefSeq; NP_064654.3; NM_020258.4. [Q9WU81-1]
DR AlphaFoldDB; Q9WU81; -.
DR SMR; Q9WU81; -.
DR STRING; 10090.ENSMUSP00000124569; -.
DR GlyGen; Q9WU81; 3 sites.
DR iPTMnet; Q9WU81; -.
DR PhosphoSitePlus; Q9WU81; -.
DR SwissPalm; Q9WU81; -.
DR EPD; Q9WU81; -.
DR jPOST; Q9WU81; -.
DR MaxQB; Q9WU81; -.
DR PaxDb; Q9WU81; -.
DR PeptideAtlas; Q9WU81; -.
DR PRIDE; Q9WU81; -.
DR ProteomicsDB; 272929; -. [Q9WU81-1]
DR ProteomicsDB; 272930; -. [Q9WU81-2]
DR Antibodypedia; 19052; 119 antibodies from 28 providers.
DR DNASU; 56857; -.
DR Ensembl; ENSMUST00000115068; ENSMUSP00000110720; ENSMUSG00000032122. [Q9WU81-1]
DR Ensembl; ENSMUST00000161114; ENSMUSP00000124569; ENSMUSG00000032122. [Q9WU81-2]
DR GeneID; 56857; -.
DR KEGG; mmu:56857; -.
DR UCSC; uc009ouk.2; mouse. [Q9WU81-1]
DR UCSC; uc009oul.2; mouse. [Q9WU81-2]
DR CTD; 219855; -.
DR MGI; MGI:1929693; Slc37a2.
DR VEuPathDB; HostDB:ENSMUSG00000032122; -.
DR eggNOG; KOG2533; Eukaryota.
DR GeneTree; ENSGT00940000158657; -.
DR HOGENOM; CLU_001265_31_6_1; -.
DR InParanoid; Q9WU81; -.
DR OMA; AMPYLID; -.
DR OrthoDB; 964162at2759; -.
DR PhylomeDB; Q9WU81; -.
DR TreeFam; TF314991; -.
DR Reactome; R-MMU-70263; Gluconeogenesis.
DR BioGRID-ORCS; 56857; 5 hits in 75 CRISPR screens.
DR ChiTaRS; Slc37a2; mouse.
DR PRO; PR:Q9WU81; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q9WU81; protein.
DR Bgee; ENSMUSG00000032122; Expressed in parotid gland and 110 other tissues.
DR Genevisible; Q9WU81; MM.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0061513; F:glucose 6-phosphate:inorganic phosphate antiporter activity; ISS:UniProtKB.
DR GO; GO:0015169; F:glycerol-3-phosphate transmembrane transporter activity; ISA:MGI.
DR GO; GO:0008643; P:carbohydrate transport; IEA:UniProtKB-KW.
DR GO; GO:0015760; P:glucose-6-phosphate transport; ISS:UniProtKB.
DR GO; GO:0006072; P:glycerol-3-phosphate metabolic process; ISA:MGI.
DR GO; GO:0015794; P:glycerol-3-phosphate transmembrane transport; ISA:MGI.
DR GO; GO:0006127; P:glycerophosphate shuttle; ISA:MGI.
DR GO; GO:0035435; P:phosphate ion transmembrane transport; ISS:UniProtKB.
DR CDD; cd17344; MFS_SLC37A1_2; 1.
DR Gene3D; 1.20.1250.20; -; 2.
DR InterPro; IPR011701; MFS.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR044740; SLC37A1_2.
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; PS50850; MFS; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Antiport; Endoplasmic reticulum; Glycoprotein;
KW Membrane; Reference proteome; Sugar transport; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..501
FT /note="Glucose-6-phosphate exchanger SLC37A2"
FT /id="PRO_0000308323"
FT TRANSMEM 19..39
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 88..108
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 118..140
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 142..164
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 179..199
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 210..230
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 303..323
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 334..354
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 362..382
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 391..411
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 434..454
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 462..482
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 240..266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 240..255
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 53
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 62
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 68
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 498..501
FT /note="YKQI -> SSLALTHPR (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072, ECO:0000303|Ref.4"
FT /id="VSP_028964"
FT CONFLICT 339
FT /note="L -> V (in Ref. 2; BAC37639)"
FT /evidence="ECO:0000305"
FT CONFLICT 423
FT /note="K -> E (in Ref. 3; AAH63326)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 501 AA; 55073 MW; 3E053502DF907FBC CRC64;
MRSSLAPGVW FLRAFSRDSW FRGFILLLTF LIYACYHMSR KPISIVKSRL HQNCSEMVRP
VNDTHDLNDT TWCSWSPFDK DDYKELLGAV DNAFLVAYAI GMFISGIFGE RLPLRYYLSA
GMVLSGLFTS LFGLGYFWNI HMLWYFVLIQ ICNGLVQTTG WPSVVTCVGN WFGKGKRGFI
MGIWNSHTSV GNILGSLIAG VWVNQHWGLS FIVPGIITAI MGVITFLFLI EYPEDVDCTP
PRHHDDPEKE QDNPEDPVNS PYSSRESNVD IAASSSKEQG PEPEAISFLG ALRIPGVIEF
SLCLLFAKLV SYTFLYWLPL YIFNVAHFSA KEAGDLSTLF DVGGIIGGIM AGLISDYTNS
RATTCCIMLI LAAPMMFLYN YIGQNGITSS IVMLIICGVL VNGPYALITT AVSADLGTHE
SLKGNAKALS TVTAIIDGTG SIGAALGPLL AGLISPTGWN NVFYMLISAD VLACLLLCRL
VYKEILAWKT ACGRSSGYKQ I
