GTR7_MOUSE
ID GTR7_MOUSE Reviewed; 513 AA.
AC P0C6A1;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Solute carrier family 2, facilitated glucose transporter member 7 {ECO:0000305};
DE AltName: Full=Glucose transporter type 7 {ECO:0000250|UniProtKB:Q6PXP3};
DE Short=GLUT-7 {ECO:0000250|UniProtKB:Q6PXP3};
GN Name=Slc2a7 {ECO:0000312|MGI:MGI:3650865};
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
CC -!- FUNCTION: Probable sugar transporter. Even if its physiological
CC substrate is subject to discussion, it is able to transport glucose and
CC fructose. Does not transport galactose, 2-deoxy-d-glucose and xylose.
CC {ECO:0000250|UniProtKB:Q6PXP3}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glucose(out) = D-glucose(in); Xref=Rhea:RHEA:60376,
CC ChEBI:CHEBI:4167; Evidence={ECO:0000250|UniProtKB:Q6PXP3};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-fructose(out) = D-fructose(in); Xref=Rhea:RHEA:60372,
CC ChEBI:CHEBI:37721; Evidence={ECO:0000250|UniProtKB:Q6PXP3};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q6PXP3};
CC Multi-pass membrane protein {ECO:0000255}. Apical cell membrane
CC {ECO:0000250|UniProtKB:Q6PXP3}; Multi-pass membrane protein
CC {ECO:0000255}.
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 (By similarity). However, another group coud not
CC confirm transporter activity for glucose or fructose (By similarity).
CC {ECO:0000250|UniProtKB:Q6PXP3}.
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DR EMBL; AL606971; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; P0C6A1; -.
DR SMR; P0C6A1; -.
DR STRING; 10090.ENSMUSP00000059106; -.
DR GlyGen; P0C6A1; 1 site.
DR PaxDb; P0C6A1; -.
DR PRIDE; P0C6A1; -.
DR ProteomicsDB; 271188; -.
DR MGI; MGI:3650865; Slc2a7.
DR eggNOG; KOG0569; Eukaryota.
DR InParanoid; P0C6A1; -.
DR Reactome; R-MMU-189200; Cellular hexose transport.
DR PRO; PR:P0C6A1; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P0C6A1; protein.
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; ISS:UniProtKB.
DR GO; GO:0055056; F:D-glucose transmembrane transporter activity; ISO:MGI.
DR GO; GO:0015149; F:hexose transmembrane transporter activity; IBA:GO_Central.
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 3: Inferred from homology;
KW Cell membrane; Glycoprotein; Membrane; Reference proteome; Sugar transport;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..513
FT /note="Solute carrier family 2, facilitated glucose
FT transporter member 7"
FT /id="PRO_0000317272"
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..282
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 283..303
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 304..322
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 323..343
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 344..351
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 352..372
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 373..380
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 381..401
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 402..416
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 417..437
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 438..446
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 447..467
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 468..513
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 494..513
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 295..296
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000250|UniProtKB:P11169"
FT BINDING 301
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000250|UniProtKB:P11169"
FT BINDING 332
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"
SQ SEQUENCE 513 AA; 55886 MW; C4FFBFE9EE8061B9 CRC64;
MEDKEIGTPL PLPHSEARLQ PTLVLTTLSA AFGSVFQYGY NIAVINTPHK VFKSFYNDTH
FERHGTFMDE STLLLLWSCT VSMFPLGGLL GSLVVGLMVN KWGRKGTLLI NNVFAITSAV
LMGVSKVARA FELIILSRVL VGICAGIAYS TLPMYLGELA PQNLRGALGT MTEVFVIIGV
LLAQIFSLQA ILGNATGWPI LLALTGVPAV IQLLSLPFFP ESPRYTLIEK GDEETARQAL
RRLRGQNYNV EAEMEEMRTE ERTEQAEGRL SVLNLFTFRP LRWQLISIVV LMAGQQLSGI
NAVNYYADVI YTSAGVDPTQ SQYVTLGSGV INLVMTLVSA VIIERLGRRI LLLSGYAICC
SACLVLTVAL LLQSTAPELS YLSIVCVFSY IVGHSIGPSP VPSVVRTEIV LQSSRTAAFT
VDGAVHWLTN FIVGLTFPSI QVAIGAYSFL VFAGVCILTA AYIYVVIPET KGRTFVEINC
AFAKRNGVEF PEEKEVATAK PHTPSLPTKE TAF
