G6PT3_HUMAN
ID G6PT3_HUMAN Reviewed; 501 AA.
AC Q8TED4; A8K2P9; Q6P599; Q7Z7P8; Q8TEM2;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 2.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Glucose-6-phosphate exchanger SLC37A2 {ECO:0000305|PubMed:21949678};
DE AltName: Full=Solute carrier family 37 member 2 {ECO:0000312|HGNC:HGNC:20644};
GN Name=SLC37A2 {ECO:0000312|HGNC:HGNC:20644};
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 [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Spleen;
RX PubMed=12693554; DOI=10.1093/dnares/10.1.49;
RA Jikuya H., Takano J., Kikuno R., Hirosawa M., Nagase T., Nomura N.,
RA Ohara O.;
RT "Characterization of long cDNA clones from human adult spleen. II. The
RT complete sequences of 81 cDNA clones.";
RL DNA Res. 10:49-57(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Adipose tissue, and Tongue;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 4).
RC TISSUE=Brain, and Pancreas;
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 [5]
RP FUNCTION, SUBCELLULAR LOCATION, ACTIVITY REGULATION, AND TISSUE
RP SPECIFICITY.
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).
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:0000269|PubMed:21949678}.
CC -!- ACTIVITY REGULATION: Inhibited by vanadate but not by chlorogenic acid.
CC {ECO:0000269|PubMed:21949678}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:21949678}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q8TED4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8TED4-2; Sequence=VSP_028963;
CC Name=3;
CC IsoId=Q8TED4-3; Sequence=VSP_028961, VSP_028962;
CC Name=4;
CC IsoId=Q8TED4-4; Sequence=VSP_028960;
CC -!- TISSUE SPECIFICITY: Detected in intestine and pancreas. Lower
CC expression is also detected in liver and kidney.
CC {ECO:0000269|PubMed:21949678}.
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=BAB84926.1; Type=Erroneous initiation; Note=Extended N-terminus.; 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; AK074100; BAB84926.1; ALT_INIT; mRNA.
DR EMBL; AK074207; BAB85016.1; -; mRNA.
DR EMBL; AK290314; BAF83003.1; -; mRNA.
DR EMBL; CH471065; EAW67622.1; -; Genomic_DNA.
DR EMBL; BC051314; AAH51314.1; -; mRNA.
DR EMBL; BC062990; AAH62990.1; -; mRNA.
DR CCDS; CCDS31714.1; -. [Q8TED4-2]
DR CCDS; CCDS44757.1; -. [Q8TED4-1]
DR RefSeq; NP_001138762.1; NM_001145290.1. [Q8TED4-1]
DR RefSeq; NP_938018.1; NM_198277.2. [Q8TED4-2]
DR AlphaFoldDB; Q8TED4; -.
DR SMR; Q8TED4; -.
DR BioGRID; 128584; 3.
DR STRING; 9606.ENSP00000311833; -.
DR TCDB; 2.A.1.4.8; the major facilitator superfamily (mfs).
DR GlyGen; Q8TED4; 3 sites.
DR iPTMnet; Q8TED4; -.
DR PhosphoSitePlus; Q8TED4; -.
DR BioMuta; SLC37A2; -.
DR DMDM; 160185473; -.
DR jPOST; Q8TED4; -.
DR MassIVE; Q8TED4; -.
DR PaxDb; Q8TED4; -.
DR PeptideAtlas; Q8TED4; -.
DR PRIDE; Q8TED4; -.
DR ProteomicsDB; 74448; -. [Q8TED4-1]
DR ProteomicsDB; 74449; -. [Q8TED4-2]
DR ProteomicsDB; 74450; -. [Q8TED4-3]
DR Antibodypedia; 19052; 119 antibodies from 28 providers.
DR DNASU; 219855; -.
DR Ensembl; ENST00000308074.4; ENSP00000311833.4; ENSG00000134955.12. [Q8TED4-2]
DR Ensembl; ENST00000403796.7; ENSP00000384407.3; ENSG00000134955.12. [Q8TED4-1]
DR GeneID; 219855; -.
DR KEGG; hsa:219855; -.
DR MANE-Select; ENST00000403796.7; ENSP00000384407.3; NM_001145290.2; NP_001138762.1.
DR UCSC; uc001qbn.4; human. [Q8TED4-1]
DR CTD; 219855; -.
DR DisGeNET; 219855; -.
DR GeneCards; SLC37A2; -.
DR HGNC; HGNC:20644; SLC37A2.
DR HPA; ENSG00000134955; Tissue enhanced (salivary).
DR MIM; 619136; gene.
DR neXtProt; NX_Q8TED4; -.
DR OpenTargets; ENSG00000134955; -.
DR PharmGKB; PA134917577; -.
DR VEuPathDB; HostDB:ENSG00000134955; -.
DR eggNOG; KOG2533; Eukaryota.
DR GeneTree; ENSGT00940000158657; -.
DR HOGENOM; CLU_001265_31_6_1; -.
DR InParanoid; Q8TED4; -.
DR OMA; AMPYLID; -.
DR OrthoDB; 964162at2759; -.
DR PhylomeDB; Q8TED4; -.
DR TreeFam; TF314991; -.
DR PathwayCommons; Q8TED4; -.
DR Reactome; R-HSA-70263; Gluconeogenesis. [Q8TED4-2]
DR BioGRID-ORCS; 219855; 15 hits in 1077 CRISPR screens.
DR ChiTaRS; SLC37A2; human.
DR GenomeRNAi; 219855; -.
DR Pharos; Q8TED4; Tbio.
DR PRO; PR:Q8TED4; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q8TED4; protein.
DR Bgee; ENSG00000134955; Expressed in right adrenal gland and 156 other tissues.
DR ExpressionAtlas; Q8TED4; baseline and differential.
DR Genevisible; Q8TED4; HS.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0061513; F:glucose 6-phosphate:inorganic phosphate antiporter activity; IDA:UniProtKB.
DR GO; GO:0008643; P:carbohydrate transport; IEA:UniProtKB-KW.
DR GO; GO:0015760; P:glucose-6-phosphate transport; IDA:UniProtKB.
DR GO; GO:0035435; P:phosphate ion transmembrane transport; IDA: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 2: Evidence at transcript 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_0000308322"
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..138
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 145..165
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 189..209
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 210..230
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 302..322
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..262
FT /note="Disordered"
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 1..375
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_028960"
FT VAR_SEQ 347..385
FT /note="GGIVAGLVSDYTNGRATTCCVMLILAAPMMFLYNYIGQD -> DVPVQLHWP
FT GRDCQLHSDADHLWGPGQWPIRAHHHCCLC (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:12693554"
FT /id="VSP_028961"
FT VAR_SEQ 386..501
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:12693554"
FT /id="VSP_028962"
FT VAR_SEQ 498..501
FT /note="YKEI -> SSMVLTHQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_028963"
FT VARIANT 96
FT /note="I -> V (in dbSNP:rs55752830)"
FT /id="VAR_061803"
FT VARIANT 268
FT /note="G -> S (in dbSNP:rs34485243)"
FT /id="VAR_036794"
FT CONFLICT 207
FT /note="W -> R (in Ref. 2; BAB85016)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 501 AA; 54436 MW; 5B19560992231164 CRC64;
MRSSLAPGVW FFRAFSRDSW FRGLILLLTF LIYACYHMSR KPISIVKSRL HQNCSEQIKP
INDTHSLNDT MWCSWAPFDK DNYKELLGGV DNAFLIAYAI GMFISGVFGE RLPLRYYLSA
GMLLSGLFTS LFGLGYFWNI HELWYFVVIQ VCNGLVQTTG WPSVVTCVGN WFGKGKRGFI
MGIWNSHTSV GNILGSLIAG IWVNGQWGLS FIVPGIITAV MGVITFLFLI EHPEDVDCAP
PQHHGEPAEN QDNPEDPGNS PCSIRESGLE TVAKCSKGPC EEPAAISFFG ALRIPGVVEF
SLCLLFAKLV SYTFLYWLPL YIANVAHFSA KEAGDLSTLF DVGGIIGGIV AGLVSDYTNG
RATTCCVMLI LAAPMMFLYN YIGQDGIASS IVMLIICGGL VNGPYALITT AVSADLGTHK
SLKGNAKALS TVTAIIDGTG SIGAALGPLL AGLISPTGWN NVFYMLISAD VLACLLLCRL
VYKEILAWKV SLSRGSGYKE I
