ID GTR5_HUMAN Reviewed; 501 AA. AC P22732; Q14770; Q5T977; Q8IVB3; DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1991, sequence version 1. DT 02-SEP-2026, entry version 228. DE RecName: Full=Solute carrier family 2, facilitated glucose transporter member 5 {ECO:0000305}; DE AltName: Full=Fructose transporter {ECO:0000305}; DE AltName: Full=Glucose transporter type 5, small intestine {ECO:0000303|PubMed:1695905}; DE Short=GLUT-5 {ECO:0000303|PubMed:1695905}; GN Name=SLC2A5 {ECO:0000312|HGNC:HGNC:11010}; GN Synonyms=GLUT5 {ECO:0000303|PubMed:1695905}; 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), FUNCTION, SUBCELLULAR LOCATION, RP TISSUE SPECIFICITY, AND ACTIVITY REGULATION. RC TISSUE=Jejunum; RX PubMed=1695905; DOI=10.1016/s0021-9258(19)38295-x; RA Kayano T., Burant C.F., Fukumoto H., Gould G.W., Fan Y.-S., Eddy R.L., RA Byers M.G., Shows T.B., Seino S., Bell G.I.; RT "Human facilitative glucose transporters. Isolation, functional RT characterization, and gene localization of cDNAs encoding an isoform RT (GLUT5) expressed in small intestine, kidney, muscle, and adipose tissue RT and an unusual glucose transporter pseudogene-like sequence (GLUT6)."; RL J. Biol. Chem. 265:13276-13282(1990). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION. RC TISSUE=Fetal liver; RX PubMed=8037665; DOI=10.1042/bj3010169; RA Mahraoui L., Takeda J., Mesonero J., Chantret I., Dussaulx E., Bell G.I., RA Brot-Laroche E.; RT "Regulation of expression of the human fructose transporter (GLUT5) by RT cyclic AMP."; RL Biochem. J. 301:169-175(1994). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Brain, and Umbilical cord blood; 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [5] 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 [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Lymph, and Prostate; 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 [7] RP FUNCTION, TRANSPORTER ACTIVITY, AND SUBCELLULAR LOCATION. RX PubMed=8333543; DOI=10.1152/ajpgi.1993.264.6.g1169; RA Rand E.B., Depaoli A.M., Davidson N.O., Bell G.I., Burant C.F.; RT "Sequence, tissue distribution, and functional characterization of the rat RT fructose transporter GLUT5."; RL Am. J. Physiol. 264:G1169-G1176(1993). RN [8] RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RX PubMed=7619085; DOI=10.1042/bj3090007; RA Blakemore S.J., Aledo J.C., James J., Campbell F.C., Lucocq J.M., RA Hundal H.S.; RT "The GLUT5 hexose transporter is also localized to the basolateral membrane RT of the human jejunum."; RL Biochem. J. 309:7-12(1995). RN [9] RP MASS SPECTROMETRY. RC TISSUE=Mammary cancer; RX PubMed=11840567; RX DOI=10.1002/1615-9861(200202)2:2<212::aid-prot212>3.0.co;2-h; RA Harris R.A., Yang A., Stein R.C., Lucy K., Brusten L., Herath A., RA Parekh R., Waterfield M.D., O'Hare M.J., Neville M.A., Page M.J., RA Zvelebil M.J.; RT "Cluster analysis of an extensive human breast cancer cell line protein RT expression map database."; RL Proteomics 2:212-223(2002). RN [10] RP FUNCTION. RX PubMed=16186102; DOI=10.1074/jbc.m508678200; RA Manolescu A., Salas-Burgos A.M., Fischbarg J., Cheeseman C.I.; RT "Identification of a hydrophobic residue as a key determinant of fructose RT transport by the facilitative hexose transporter SLC2A7 (GLUT7)."; RL J. Biol. Chem. 280:42978-42983(2005). RN [11] RP FUNCTION, TRANSPORTER ACTIVITY, AND ACTIVITY REGULATION. RX PubMed=29548810; DOI=10.1016/j.bcp.2018.03.011; RA Gauer J.S., Tumova S., Lippiat J.D., Kerimi A., Williamson G.; RT "Differential patterns of inhibition of the sugar transporters GLUT2, GLUT5 RT and GLUT7 by flavonoids."; RL Biochem. Pharmacol. 152:11-20(2018). RN [12] RP BIOPHYSICOCHEMICAL PROPERTIES, AND CHARACTERIZATION OF VARIANT VAL-296. RX PubMed=17710649; DOI=10.1080/09687680701298143; RA Manolescu A.R., Augustin R., Moley K., Cheeseman C.; RT "A highly conserved hydrophobic motif in the exofacial vestibule of RT fructose transporting SLC2A proteins acts as a critical determinant of RT their substrate selectivity."; RL Mol. Membr. Biol. 24:455-463(2007). RN [13] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [14] RP FUNCTION, TRANSPORTER ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR RP LOCATION, VARIANT VAL-296, AND CHARACTERIZATION OF VARIANT VAL-296. RX PubMed=28083649; DOI=10.1007/s00232-016-9945-7; RA Ebert K., Ludwig M., Geillinger K.E., Schoberth G.C., Essenwanger J., RA Stolz J., Daniel H., Witt H.; RT "Reassessment of GLUT7 and GLUT9 as putative fructose and glucose RT transporters."; RL J. Membr. Biol. 250:171-182(2017). CC -!- FUNCTION: Functions as a fructose transporter that has only low CC activity with other monosaccharides (PubMed:16186102, PubMed:17710649, CC PubMed:28083649, PubMed:29548810, PubMed:8333543). Can mediate the CC uptake of 2-deoxyglucose, but with low efficiency (PubMed:1695905). CC Essential for fructose uptake in the small intestine (By similarity). CC Plays a role in the regulation of salt uptake and blood pressure in CC response to dietary fructose (By similarity). Required for the CC development of high blood pressure in response to high dietary fructose CC intake (By similarity). {ECO:0000250|UniProtKB:Q9WV38, CC ECO:0000269|PubMed:16186102, ECO:0000269|PubMed:1695905, CC ECO:0000269|PubMed:17710649, ECO:0000269|PubMed:28083649, CC ECO:0000269|PubMed:29548810, ECO:0000269|PubMed:8333543}. CC -!- CATALYTIC ACTIVITY: CC Reaction=D-fructose(out) = D-fructose(in); Xref=Rhea:RHEA:60372, CC ChEBI:CHEBI:37721; Evidence={ECO:0000269|PubMed:17710649, CC ECO:0000269|PubMed:28083649, ECO:0000269|PubMed:29548810, CC ECO:0000269|PubMed:8333543}; CC -!- ACTIVITY REGULATION: The uptake of 2-deoxyglucose is inhibited by CC cytochalasin B. Fructose transport is inhibited by the flavonoids CC epigallocatechin gallate and apigenin but not quercetin CC (PubMed:29548810). {ECO:0000269|PubMed:1695905, CC ECO:0000269|PubMed:29548810}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=0.63 mM for D-glucose {ECO:0000269|PubMed:17710649}; CC KM=30.1 mM for D-fructose {ECO:0000269|PubMed:28083649}; CC -!- INTERACTION: CC P22732; Q3SXY8: ARL13B; NbExp=4; IntAct=EBI-2825135, EBI-11343438; CC P22732; Q99437: ATP6V0B; NbExp=3; IntAct=EBI-2825135, EBI-3904417; CC P22732; P21964: COMT; NbExp=3; IntAct=EBI-2825135, EBI-372265; CC P22732; P34910-2: EVI2B; NbExp=3; IntAct=EBI-2825135, EBI-17640610; CC P22732; Q96P31-6: FCRL3; NbExp=3; IntAct=EBI-2825135, EBI-17443171; CC P22732; O14880: MGST3; NbExp=3; IntAct=EBI-2825135, EBI-724754; CC P22732; Q96E29: MTERF3; NbExp=3; IntAct=EBI-2825135, EBI-7825321; CC P22732; O75459: PAGE1; NbExp=3; IntAct=EBI-2825135, EBI-2559100; CC P22732; Q9NY72: SCN3B; NbExp=3; IntAct=EBI-2825135, EBI-17247926; CC P22732; Q8N3G9: TMEM130; NbExp=3; IntAct=EBI-2825135, EBI-19763514; CC P22732; Q96Q45-2: TMEM237; NbExp=3; IntAct=EBI-2825135, EBI-10982110; CC -!- SUBCELLULAR LOCATION: Apical cell membrane CC {ECO:0000250|UniProtKB:Q9WV38}; Multi-pass membrane protein CC {ECO:0000250|UniProtKB:Q9WV38}. Cell membrane CC {ECO:0000269|PubMed:1695905, ECO:0000269|PubMed:28083649, CC ECO:0000269|PubMed:7619085, ECO:0000269|PubMed:8333543}; Multi-pass CC membrane protein {ECO:0000250|UniProtKB:Q9WV38}. Cell membrane, CC sarcolemma {ECO:0000250|UniProtKB:P43427}. Note=Localized on the apical CC membrane of jejunum villi, but also on lateral plasma membranes of the CC villi. Transport to the cell membrane is dependent on RAB11A. CC {ECO:0000250|UniProtKB:Q9WV38}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P22732-1; Sequence=Displayed; CC Name=2; CC IsoId=P22732-2; Sequence=VSP_042031; CC -!- TISSUE SPECIFICITY: Detected in skeletal muscle, and in jejunum brush CC border membrane and basolateral membrane (at protein level) CC (PubMed:7619085). Expressed in small intestine, and at much lower CC levels in kidney, skeletal muscle, and adipose tissue. CC {ECO:0000269|PubMed:1695905, ECO:0000269|PubMed:7619085}. CC -!- INDUCTION: By forskolin in Caco-2 cells. {ECO:0000269|PubMed:8037665}. CC -!- MASS SPECTROMETRY: Mass=54973.98; Method=MALDI; CC Evidence={ECO:0000269|PubMed:11840567}; CC -!- SIMILARITY: Belongs to the major facilitator superfamily. Sugar CC transporter (TC 2.A.1.1) family. Glucose transporter subfamily. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAB60641.1; Type=Erroneous gene model prediction; 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; M55531; AAA52570.1; -; mRNA. DR EMBL; U11843; AAB60641.1; ALT_SEQ; Genomic_DNA. DR EMBL; U05344; AAB60641.1; JOINED; Genomic_DNA. DR EMBL; U11839; AAB60641.1; JOINED; Genomic_DNA. DR EMBL; U11840; AAB60641.1; JOINED; Genomic_DNA. DR EMBL; U11841; AAB60641.1; JOINED; Genomic_DNA. DR EMBL; U11842; AAB60641.1; JOINED; Genomic_DNA. DR EMBL; AK289849; BAF82538.1; -; mRNA. DR EMBL; AK290398; BAF83087.1; -; mRNA. DR EMBL; AL158048; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471130; EAW71610.1; -; Genomic_DNA. DR EMBL; BC001692; AAH01692.1; -; mRNA. DR EMBL; BC001820; AAH01820.1; -; mRNA. DR EMBL; BC035878; AAH35878.1; -; mRNA. DR CCDS; CCDS44054.1; -. [P22732-2] DR CCDS; CCDS99.1; -. [P22732-1] DR PIR; A36629; A36629. DR PIR; G02864; G02864. DR RefSeq; NP_001129057.1; NM_001135585.2. [P22732-2] DR RefSeq; NP_001315548.1; NM_001328619.2. [P22732-1] DR RefSeq; NP_003030.1; NM_003039.3. [P22732-1] DR RefSeq; XP_047284544.1; XM_047428588.1. [P22732-1] DR RefSeq; XP_047284547.1; XM_047428591.1. [P22732-1] DR RefSeq; XP_047284550.1; XM_047428594.1. [P22732-1] DR RefSeq; XP_047284554.1; XM_047428598.1. [P22732-1] DR RefSeq; XP_047284558.1; XM_047428602.1. [P22732-1] DR RefSeq; XP_047284562.1; XM_047428606.1. [P22732-1] DR RefSeq; XP_047284568.1; XM_047428612.1. [P22732-1] DR RefSeq; XP_047284570.1; XM_047428614.1. [P22732-1] DR RefSeq; XP_047284571.1; XM_047428615.1. [P22732-1] DR RefSeq; XP_054194374.1; XM_054338399.1. [P22732-1] DR RefSeq; XP_054194375.1; XM_054338400.1. [P22732-1] DR RefSeq; XP_054194376.1; XM_054338401.1. [P22732-1] DR RefSeq; XP_054194377.1; XM_054338402.1. [P22732-1] DR RefSeq; XP_054194378.1; XM_054338403.1. [P22732-1] DR RefSeq; XP_054194379.1; XM_054338404.1. [P22732-1] DR RefSeq; XP_054194380.1; XM_054338405.1. [P22732-1] DR AlphaFoldDB; P22732; -. DR SMR; P22732; -. DR BioGRID; 112409; 148. DR FunCoup; P22732; 282. DR IntAct; P22732; 134. DR NDEx; IQUERY-CP-SLC2A5; 5 NDEx IQuery Curated Pathways. DR STRING; 9606.ENSP00000366641; -. DR BindingDB; P22732; -. DR ChEMBL; CHEMBL5875; -. DR DrugBank; DB01914; D-glucose. DR DrugBank; DB09502; Fludeoxyglucose (18F). DR DrugBank; DB09344; Invert sugar. DR TCDB; 2.A.1.1.13; the major facilitator superfamily (mfs). DR GlyCosmos; P22732; 1 site, No reported glycans. DR GlyGen; P22732; 2 sites. DR iPTMnet; P22732; -. DR PhosphoSitePlus; P22732; -. DR BioMuta; SLC2A5; -. DR DMDM; 121764; -. DR jPOST; P22732; -. DR MassIVE; P22732; -. DR PaxDb; 9606-ENSP00000366641; -. DR PeptideAtlas; P22732; -. DR ProteomicsDB; 54029; -. [P22732-1] DR ProteomicsDB; 54030; -. [P22732-2] DR Antibodypedia; 1404; 476 antibodies from 35 providers. DR DNASU; 6518; -. DR Ensembl; ENST00000377414.7; ENSP00000366631.3; ENSG00000142583.19. [P22732-2] DR Ensembl; ENST00000377424.9; ENSP00000366641.4; ENSG00000142583.19. [P22732-1] DR Ensembl; ENST00000941832.1; ENSP00000611891.1; ENSG00000142583.19. [P22732-1] DR Ensembl; ENST00000941833.1; ENSP00000611892.1; ENSG00000142583.19. [P22732-1] DR GeneID; 6518; -. DR KEGG; hsa:6518; -. DR MANE-Select; ENST00000377424.9; ENSP00000366641.4; NM_003039.3; NP_003030.1. DR UCSC; uc001apo.4; human. [P22732-1] DR AGR; HGNC:11010; -. DR ClinPGx; PA35880; -. DR CTD; 6518; -. DR DisGeNET; 6518; -. DR GeneCards; SLC2A5; -. DR HGNC; HGNC:11010; SLC2A5. DR HPA; ENSG00000142583; Tissue enhanced (bone marrow, intestine, skeletal muscle, testis). DR MalaCards; SLC2A5; -. DR MIM; 138230; gene. DR OpenTargets; ENSG00000142583; -. DR VEuPathDB; HostDB:ENSG00000142583; -. DR eggNOG; KOG0569; Eukaryota. DR GeneTree; ENSGT00940000156846; -. DR HOGENOM; CLU_001265_30_5_1; -. DR InParanoid; P22732; -. DR OMA; QTTVSWM; -. DR OrthoDB; 4540492at2759; -. DR PAN-GO; P22732; 6 GO annotations based on evolutionary models. DR PhylomeDB; P22732; -. DR BioCyc; MetaCyc:ENSG00000142583-MONOMER; -. DR PathwayCommons; P22732; -. DR Reactome; R-HSA-6798695; Neutrophil degranulation. DR Reactome; R-HSA-8981373; Intestinal hexose absorption. DR SignaLink; P22732; -. DR SIGNOR; P22732; -. DR Agora; ENSG00000142583; Agora Nominated Target for Alzheimer's Disease. DR BioGRID-ORCS; 6518; 11 hits in 1142 CRISPR screens. DR ChiTaRS; SLC2A5; human. DR GenomeRNAi; 6518; -. DR Pharos; P22732; Tbio. DR PRO; PR:P22732; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; P22732; protein. DR Bgee; ENSG00000142583; Expressed in jejunal mucosa and 154 other cell types or tissues. DR ExpressionAtlas; P22732; baseline and differential. DR GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0042383; C:sarcolemma; ISS:UniProtKB. DR GO; GO:0035579; C:specific granule membrane; TAS:Reactome. DR GO; GO:0055056; F:D-glucose transmembrane transporter activity; IBA:GO_Central. DR GO; GO:0070061; F:fructose binding; ISS:UniProtKB. DR GO; GO:0005353; F:fructose transmembrane transporter activity; IDA:UniProtKB. DR GO; GO:0005975; P:carbohydrate metabolic process; TAS:ProtInc. DR GO; GO:0071332; P:cellular response to fructose stimulus; ISS:UniProtKB. DR GO; GO:1904659; P:D-glucose transmembrane transport; TAS:ProtInc. DR GO; GO:0070837; P:dehydroascorbic acid transport; IBA:GO_Central. DR GO; GO:1990539; P:fructose import across plasma membrane; IDA:UniProtKB. DR GO; GO:0015755; P:fructose transmembrane transport; IDA:UniProtKB. DR GO; GO:0106001; P:intestinal hexose absorption; TAS:Reactome. DR GO; GO:0003044; P:regulation of systemic arterial blood pressure mediated by a chemical signal; ISS:UniProtKB. DR GO; GO:0009750; P:response to fructose; ISS:UniProtKB. DR CDD; cd17432; MFS_GLUT_Class2; 1. DR FunFam; 1.20.1250.20:FF:001511; Solute carrier family 2, facilitated glucose transporter member 5; 1. DR Gene3D; 1.20.1250.20; MFS general substrate transporter like domains; 1. DR InterPro; IPR002442; Fru_transpt_5. DR InterPro; IPR045263; GLUT. DR InterPro; IPR020846; MFS_dom. DR InterPro; IPR005828; MFS_sugar_transport-like. DR InterPro; IPR036259; MFS_trans_sf. DR InterPro; IPR003663; Sugar/inositol_transpt. DR InterPro; IPR005829; Sugar_transporter_CS. DR NCBIfam; TIGR00879; SP; 1. DR PANTHER; PTHR23503; SOLUTE CARRIER FAMILY 2; 1. DR PANTHER; PTHR23503:SF32; SOLUTE CARRIER FAMILY 2, FACILITATED GLUCOSE TRANSPORTER MEMBER 5; 1. DR Pfam; PF00083; Sugar_tr; 1. DR PRINTS; PR01194; GLUCTRSPORT5. DR PRINTS; PR00171; SUGRTRNSPORT. DR SUPFAM; SSF103473; MFS general substrate transporter; 1. DR PROSITE; PS50850; MFS; 1. DR PROSITE; PS00216; SUGAR_TRANSPORT_1; 1. DR PROSITE; PS00217; SUGAR_TRANSPORT_2; 1. PE 1: Evidence at protein level; KW Acetylation; Alternative splicing; Cell membrane; Glycoprotein; Membrane; KW Proteomics identification; Reference proteome; Sugar transport; KW Transmembrane; Transmembrane helix; Transport. FT CHAIN 1..501 FT /note="Solute carrier family 2, facilitated glucose FT transporter member 5" FT /id="PRO_0000050369" FT TOPO_DOM 1..18 FT /note="Cytoplasmic" FT /evidence="ECO:0000250|UniProtKB:P43427" FT TRANSMEM 19..39 FT /note="Helical; Name=1" FT /evidence="ECO:0000250|UniProtKB:P43427" FT TOPO_DOM 40..68 FT /note="Extracellular" FT /evidence="ECO:0000250|UniProtKB:P43427" FT TRANSMEM 69..91 FT /note="Helical; Name=2" FT /evidence="ECO:0000250|UniProtKB:P43427" FT TOPO_DOM 92..98 FT /note="Cytoplasmic" FT /evidence="ECO:0000250|UniProtKB:P43427" FT TRANSMEM 99..119 FT /note="Helical; Name=3" FT /evidence="ECO:0000250|UniProtKB:P43427" FT TOPO_DOM 120..126 FT /note="Extracellular" FT /evidence="ECO:0000250|UniProtKB:P43427" FT TRANSMEM 127..149 FT /note="Helical; Name=4" FT /evidence="ECO:0000250|UniProtKB:P43427" FT TOPO_DOM 150..161 FT /note="Cytoplasmic" FT /evidence="ECO:0000250|UniProtKB:P43427" FT TRANSMEM 162..182 FT /note="Helical; Name=5" FT /evidence="ECO:0000250|UniProtKB:P43427" FT TOPO_DOM 183..192 FT /note="Extracellular" FT /evidence="ECO:0000250|UniProtKB:P43427" FT TRANSMEM 193..213 FT /note="Helical; Name=6" FT /evidence="ECO:0000250|UniProtKB:P43427" FT TOPO_DOM 214..277 FT /note="Cytoplasmic" FT /evidence="ECO:0000250|UniProtKB:P43427" FT TRANSMEM 278..298 FT /note="Helical; Name=7" FT /evidence="ECO:0000250|UniProtKB:P43427" FT TOPO_DOM 299..313 FT /note="Extracellular" FT /evidence="ECO:0000250|UniProtKB:P43427" FT TRANSMEM 314..334 FT /note="Helical; Name=8" FT /evidence="ECO:0000250|UniProtKB:P43427" FT TOPO_DOM 335..342 FT /note="Cytoplasmic" FT /evidence="ECO:0000250|UniProtKB:P43427" FT TRANSMEM 343..363 FT /note="Helical; Name=9" FT /evidence="ECO:0000250|UniProtKB:P43427" FT TOPO_DOM 364..371 FT /note="Extracellular" FT /evidence="ECO:0000250|UniProtKB:P43427" FT TRANSMEM 372..394 FT /note="Helical; Name=10" FT /evidence="ECO:0000250|UniProtKB:P43427" FT TOPO_DOM 395..412 FT /note="Cytoplasmic" FT /evidence="ECO:0000250|UniProtKB:P43427" FT TRANSMEM 413..433 FT /note="Helical; Name=11" FT /evidence="ECO:0000250|UniProtKB:P43427" FT TOPO_DOM 434..439 FT /note="Extracellular" FT /evidence="ECO:0000250|UniProtKB:P43427" FT TRANSMEM 440..460 FT /note="Helical; Name=12" FT /evidence="ECO:0000250|UniProtKB:P43427" FT TOPO_DOM 461..501 FT /note="Cytoplasmic" FT /evidence="ECO:0000250|UniProtKB:P43427" FT BINDING 32 FT /ligand="D-fructose" FT /ligand_id="ChEBI:CHEBI:37721" FT /evidence="ECO:0000250|UniProtKB:P43427" FT BINDING 167 FT /ligand="D-fructose" FT /ligand_id="ChEBI:CHEBI:37721" FT /evidence="ECO:0000250|UniProtKB:P43427" FT BINDING 288 FT /ligand="D-fructose" FT /ligand_id="ChEBI:CHEBI:37721" FT /evidence="ECO:0000250|UniProtKB:P43427" FT BINDING 296..298 FT /ligand="D-fructose" FT /ligand_id="ChEBI:CHEBI:37721" FT /evidence="ECO:0000250|UniProtKB:P43427" FT BINDING 387 FT /ligand="D-fructose" FT /ligand_id="ChEBI:CHEBI:37721" FT /evidence="ECO:0000250|UniProtKB:P43427" FT BINDING 419..420 FT /ligand="D-fructose" FT /ligand_id="ChEBI:CHEBI:37721" FT /evidence="ECO:0000250|UniProtKB:P43427" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0007744|PubMed:22814378" FT CARBOHYD 51 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT VAR_SEQ 192..501 FT /note="WPILLGLTGVPAALQLLLLPFFPESPRYLLIQKKDEAAAKKALQTLRGWDSV FT DREVAEIRQEDEAEKAAGFISVLKLFRMRSLRWQLLSIIVLMGGQQLSGVNAIYYYADQ FT IYLSAGVPEEHVQYVTAGTGAVNVVMTFCAVFVVELLGRRLLLLLGFSICLIACCVLTA FT ALALQDTVSWMPYISIVCVISYVIGHALGPSPIPALLITEIFLQSSRPSAFMVGGSVHW FT LSNFTVGLIFPFIQEGLGPYSFIVFAVICLLTTIYIFLIVPETKAKTFIEINQIFTKMN FT KVSEVYPEKEELKELPPVTSEQ -> EFRTSREHPHPFTTTLGPLLVFQSHHHRTGLSA FT DWSLLTGWMSLGGPSCPEPT (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:15489334" FT /id="VSP_042031" FT VARIANT 296 FT /note="I -> V (does not affect D-fructose or D-glucose FT transport; dbSNP:rs1451503051)" FT /evidence="ECO:0000269|PubMed:17710649, FT ECO:0000269|PubMed:28083649" FT /id="VAR_081827" FT CONFLICT 202 FT /note="P -> G (in Ref. 2; AAB60641)" FT /evidence="ECO:0000305" SQ SEQUENCE 501 AA; 54974 MW; 090B12F529C7B857 CRC64; MEQQDQSMKE GRLTLVLALA TLIAAFGSSF QYGYNVAAVN SPALLMQQFY NETYYGRTGE FMEDFPLTLL WSVTVSMFPF GGFIGSLLVG PLVNKFGRKG ALLFNNIFSI VPAILMGCSR VATSFELIII SRLLVGICAG VSSNVVPMYL GELAPKNLRG ALGVVPQLFI TVGILVAQIF GLRNLLANVD GWPILLGLTG VPAALQLLLL PFFPESPRYL LIQKKDEAAA KKALQTLRGW DSVDREVAEI RQEDEAEKAA GFISVLKLFR MRSLRWQLLS IIVLMGGQQL SGVNAIYYYA DQIYLSAGVP EEHVQYVTAG TGAVNVVMTF CAVFVVELLG RRLLLLLGFS ICLIACCVLT AALALQDTVS WMPYISIVCV ISYVIGHALG PSPIPALLIT EIFLQSSRPS AFMVGGSVHW LSNFTVGLIF PFIQEGLGPY SFIVFAVICL LTTIYIFLIV PETKAKTFIE INQIFTKMNK VSEVYPEKEE LKELPPVTSE Q //