GTR5_HUMAN
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 03-AUG-2022, entry version 209.
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:8333543, PubMed:16186102,
CC PubMed:28083649, PubMed:17710649, PubMed:29548810). 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=3; 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};
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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_001135585.1. [P22732-2]
DR RefSeq; NP_001315548.1; NM_001328619.1. [P22732-1]
DR RefSeq; NP_003030.1; NM_003039.2. [P22732-1]
DR RefSeq; XP_005263548.1; XM_005263491.3.
DR RefSeq; XP_016857622.1; XM_017002133.1.
DR RefSeq; XP_016857623.1; XM_017002134.1.
DR RefSeq; XP_016857624.1; XM_017002135.1.
DR RefSeq; XP_016857625.1; XM_017002136.1.
DR RefSeq; XP_016857626.1; XM_017002137.1.
DR RefSeq; XP_016857627.1; XM_017002138.1.
DR RefSeq; XP_016857629.1; XM_017002140.1.
DR RefSeq; XP_016857630.1; XM_017002141.1.
DR AlphaFoldDB; P22732; -.
DR SMR; P22732; -.
DR BioGRID; 112409; 43.
DR IntAct; P22732; 23.
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 GlyGen; P22732; 1 site.
DR iPTMnet; P22732; -.
DR PhosphoSitePlus; P22732; -.
DR BioMuta; SLC2A5; -.
DR DMDM; 121764; -.
DR jPOST; P22732; -.
DR MassIVE; P22732; -.
DR PaxDb; P22732; -.
DR PeptideAtlas; P22732; -.
DR PRIDE; P22732; -.
DR ProteomicsDB; 54029; -. [P22732-1]
DR ProteomicsDB; 54030; -. [P22732-2]
DR Antibodypedia; 1404; 446 antibodies from 33 providers.
DR DNASU; 6518; -.
DR Ensembl; ENST00000377414.7; ENSP00000366631.3; ENSG00000142583.18. [P22732-2]
DR Ensembl; ENST00000377424.9; ENSP00000366641.4; ENSG00000142583.18. [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 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 MIM; 138230; gene.
DR neXtProt; NX_P22732; -.
DR OpenTargets; ENSG00000142583; -.
DR PharmGKB; PA35880; -.
DR VEuPathDB; HostDB:ENSG00000142583; -.
DR eggNOG; KOG0569; Eukaryota.
DR GeneTree; ENSGT00940000156846; -.
DR HOGENOM; CLU_001265_30_5_1; -.
DR InParanoid; P22732; -.
DR OMA; VAQFLCM; -.
DR OrthoDB; 326501at2759; -.
DR PhylomeDB; P22732; -.
DR TreeFam; TF313762; -.
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 BioGRID-ORCS; 6518; 9 hits in 1060 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 152 other tissues.
DR ExpressionAtlas; P22732; baseline and differential.
DR Genevisible; P22732; HS.
DR GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
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:0070061; F:fructose binding; ISS:UniProtKB.
DR GO; GO:0005353; F:fructose transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0005355; F:glucose transmembrane transporter activity; TAS:ProtInc.
DR GO; GO:0015149; F:hexose transmembrane transporter activity; IBA:GO_Central.
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:1990539; P:fructose import across plasma membrane; IDA:UniProtKB.
DR GO; GO:0015755; P:fructose transmembrane transport; IDA:UniProtKB.
DR GO; GO:1904659; P:glucose transmembrane transport; TAS:ProtInc.
DR GO; GO:0106001; P:intestinal hexose absorption; TAS:Reactome.
DR GO; GO:0015749; P:monosaccharide transmembrane transport; IBA:GO_Central.
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 Gene3D; 1.20.1250.20; -; 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 PANTHER; PTHR23503; PTHR23503; 1.
DR Pfam; PF00083; Sugar_tr; 1.
DR PRINTS; PR01194; GLUCTRSPORT5.
DR PRINTS; PR00171; SUGRTRNSPORT.
DR SUPFAM; SSF103473; SSF103473; 1.
DR TIGRFAMs; TIGR00879; SP; 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 Reference proteome; Sugar transport; Transmembrane; Transmembrane helix;
KW 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
