GTR7_HUMAN
ID GTR7_HUMAN Reviewed; 512 AA.
AC Q6PXP3; A2A333;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Solute carrier family 2, facilitated glucose transporter member 7 {ECO:0000305};
DE AltName: Full=Glucose transporter type 7 {ECO:0000303|PubMed:15033637};
DE Short=GLUT-7 {ECO:0000303|PubMed:15033637};
DE Short=hGLUT7 {ECO:0000303|PubMed:16186102};
GN Name=SLC2A7 {ECO:0000303|PubMed:15033637, ECO:0000312|HGNC:HGNC:13445};
GN Synonyms=GLUT7 {ECO:0000303|PubMed:15033637};
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], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP TISSUE SPECIFICITY.
RX PubMed=15033637; DOI=10.1152/ajpgi.00396.2003;
RA Li Q., Manolescu A.R., Ritzel M., Yao S., Slugoski M., Young J.D.,
RA Chen X.-Z., Cheeseman C.I.;
RT "Cloning and functional characterization of the human GLUT7 isoform SLC2A7
RT from the small intestine.";
RL Am. J. Physiol. 287:G236-G242(2004).
RN [2]
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 [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 FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF ILE-302.
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 [5]
RP FUNCTION, AND SUBCELLULAR LOCATION.
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).
RN [6]
RP SUBCELLULAR LOCATION, FUNCTION, ACTIVITY REGULATION, AND INDUCTION BY
RP FRUCTOSE.
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).
CC -!- FUNCTION: Probable sugar transporter (PubMed:28083649). Even if its
CC physiological substrate is subject to discussion, it is able to
CC transport glucose and fructose (PubMed:29548810, PubMed:28083649,
CC PubMed:16186102). Does not transport galactose, 2-deoxy-d-glucose and
CC xylose (PubMed:15033637). {ECO:0000269|PubMed:15033637,
CC ECO:0000269|PubMed:16186102, ECO:0000269|PubMed:28083649,
CC ECO:0000269|PubMed:29548810}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glucose(out) = D-glucose(in); Xref=Rhea:RHEA:60376,
CC ChEBI:CHEBI:4167; Evidence={ECO:0000269|PubMed:16186102,
CC ECO:0000269|PubMed:29548810};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-fructose(out) = D-fructose(in); Xref=Rhea:RHEA:60372,
CC ChEBI:CHEBI:37721; Evidence={ECO:0000269|PubMed:16186102,
CC ECO:0000269|PubMed:29548810};
CC -!- ACTIVITY REGULATION: Glucose and fructose transport are inhibited by
CC the flavonoid apigenin. {ECO:0000269|PubMed:29548810}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=300 uM for glucose {ECO:0000269|PubMed:15033637};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16186102,
CC ECO:0000269|PubMed:28083649}; Multi-pass membrane protein
CC {ECO:0000255}. Apical cell membrane {ECO:0000269|PubMed:29548810};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in small intestine and colon
CC (PubMed:15033637). Weakly expressed in testis and prostate
CC (PubMed:15033637). {ECO:0000269|PubMed:15033637}.
CC -!- INDUCTION: Expression is increased in presence of fructose.
CC {ECO:0000269|PubMed:29548810}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. Sugar
CC transporter (TC 2.A.1.1) family. Glucose transporter subfamily.
CC {ECO:0000305}.
CC -!- CAUTION: According to some reports, mediates transmembrane transport of
CC glucose and fructose (PubMed:15033637, PubMed:16186102,
CC PubMed:29548810). However, another group could not confirm transporter
CC activity for glucose or fructose (PubMed:28083649).
CC {ECO:0000269|PubMed:15033637, ECO:0000269|PubMed:16186102,
CC ECO:0000269|PubMed:28083649, ECO:0000269|PubMed:29548810}.
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DR EMBL; AY571960; AAS78590.2; -; mRNA.
DR EMBL; AL158048; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471130; EAW71607.1; -; Genomic_DNA.
DR CCDS; CCDS98.2; -.
DR RefSeq; NP_997303.2; NM_207420.2.
DR AlphaFoldDB; Q6PXP3; -.
DR SMR; Q6PXP3; -.
DR BioGRID; 127578; 22.
DR IntAct; Q6PXP3; 1.
DR STRING; 9606.ENSP00000383698; -.
DR DrugBank; DB01914; D-glucose.
DR DrugBank; DB09341; Dextrose, unspecified form.
DR DrugBank; DB09502; Fludeoxyglucose (18F).
DR TCDB; 2.A.1.1.37; the major facilitator superfamily (mfs).
DR GlyGen; Q6PXP3; 1 site.
DR BioMuta; SLC2A7; -.
DR DMDM; 167008866; -.
DR jPOST; Q6PXP3; -.
DR MassIVE; Q6PXP3; -.
DR PaxDb; Q6PXP3; -.
DR PeptideAtlas; Q6PXP3; -.
DR PRIDE; Q6PXP3; -.
DR ProteomicsDB; 67261; -.
DR Antibodypedia; 49274; 21 antibodies from 10 providers.
DR DNASU; 155184; -.
DR Ensembl; ENST00000400906.2; ENSP00000383698.1; ENSG00000197241.4.
DR GeneID; 155184; -.
DR KEGG; hsa:155184; -.
DR MANE-Select; ENST00000400906.2; ENSP00000383698.1; NM_207420.3; NP_997303.2.
DR UCSC; uc009vmo.1; human.
DR CTD; 155184; -.
DR DisGeNET; 155184; -.
DR GeneCards; SLC2A7; -.
DR HGNC; HGNC:13445; SLC2A7.
DR HPA; ENSG00000197241; Tissue enriched (intestine).
DR MIM; 610371; gene.
DR neXtProt; NX_Q6PXP3; -.
DR PharmGKB; PA37770; -.
DR VEuPathDB; HostDB:ENSG00000197241; -.
DR eggNOG; KOG0569; Eukaryota.
DR GeneTree; ENSGT00940000162742; -.
DR HOGENOM; CLU_001265_30_11_1; -.
DR InParanoid; Q6PXP3; -.
DR OMA; WLFANAG; -.
DR OrthoDB; 749998at2759; -.
DR PhylomeDB; Q6PXP3; -.
DR TreeFam; TF313762; -.
DR PathwayCommons; Q6PXP3; -.
DR Reactome; R-HSA-189200; Cellular hexose transport.
DR BioGRID-ORCS; 155184; 8 hits in 1057 CRISPR screens.
DR ChiTaRS; SLC2A7; human.
DR GeneWiki; SLC2A7; -.
DR GenomeRNAi; 155184; -.
DR Pharos; Q6PXP3; Tdark.
DR PRO; PR:Q6PXP3; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q6PXP3; protein.
DR Bgee; ENSG00000197241; Expressed in duodenum and 3 other tissues.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0055056; F:D-glucose transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0005353; F:fructose transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0015149; F:hexose transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0051119; F:sugar transmembrane transporter activity; TAS:Reactome.
DR GO; GO:0015755; P:fructose transmembrane transport; IDA:UniProtKB.
DR GO; GO:1904659; P:glucose transmembrane transport; IDA:UniProtKB.
DR GO; GO:0008645; P:hexose transmembrane transport; TAS:Reactome.
DR GO; GO:0015749; P:monosaccharide transmembrane transport; IBA:GO_Central.
DR Gene3D; 1.20.1250.20; -; 1.
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; 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 Cell membrane; Glycoprotein; Membrane; Reference proteome; Sugar transport;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..512
FT /note="Solute carrier family 2, facilitated glucose
FT transporter member 7"
FT /id="PRO_0000317274"
FT TOPO_DOM 1..21
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 22..42
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 43..78
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 79..99
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 100..107
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 108..128
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 129..138
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 139..159
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 160..172
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 173..193
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 194..198
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 199..219
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 220..281
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 282..302
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 303..321
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 322..342
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 343..350
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 351..371
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 372..379
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 380..400
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 401..415
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 416..436
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 437..445
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 446..466
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 467..512
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 491..512
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 294..295
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000250|UniProtKB:P11169"
FT BINDING 300
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000250|UniProtKB:P11169"
FT BINDING 331
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000250|UniProtKB:P11169"
FT CARBOHYD 57
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VARIANT 135
FT /note="V -> I (in dbSNP:rs34545462)"
FT /id="VAR_052504"
FT VARIANT 261
FT /note="R -> Q (in dbSNP:rs12402973)"
FT /id="VAR_061879"
FT MUTAGEN 302
FT /note="I->S: Does not affect glucose or fructose
FT transport."
FT /evidence="ECO:0000269|PubMed:16186102"
FT MUTAGEN 302
FT /note="I->V: Abolished fructose transport."
FT /evidence="ECO:0000269|PubMed:16186102"
SQ SEQUENCE 512 AA; 55728 MW; DCA09E35AB720382 CRC64;
MENKEAGTPP PIPSREGRLQ PTLLLATLSA AFGSAFQYGY NLSVVNTPHK VFKSFYNETY
FERHATFMDG KLMLLLWSCT VSMFPLGGLL GSLLVGLLVD SCGRKGTLLI NNIFAIIPAI
LMGVSKVAKA FELIVFSRVV LGVCAGISYS ALPMYLGELA PKNLRGMVGT MTEVFVIVGV
FLAQIFSLQA ILGNPAGWPV LLALTGVPAL LQLLTLPFFP ESPRYSLIQK GDEATARQAL
RRLRGHTDME AELEDMRAEA RAERAEGHLS VLHLCALRSL RWQLLSIIVL MAGQQLSGIN
AINYYADTIY TSAGVEAAHS QYVTVGSGVV NIVMTITSAV LVERLGRRHL LLAGYGICGS
ACLVLTVVLL FQNRVPELSY LGIICVFAYI AGHSIGPSPV PSVVRTEIFL QSSRRAAFMV
DGAVHWLTNF IIGFLFPSIQ EAIGAYSFII FAGICLLTAI YIYVVIPETK GKTFVEINRI
FAKRNRVKLP EEKEETIDAG PPTASPAKET SF
