GTR7_RAT
ID GTR7_RAT Reviewed; 512 AA.
AC A4ZYQ5;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Solute carrier family 2, facilitated glucose transporter member 7 {ECO:0000305};
DE AltName: Full=Glucose transporter type 7 {ECO:0000303|Ref.1};
DE Short=GLUT-7 {ECO:0000303|Ref.1};
GN Name=Slc2a7 {ECO:0000312|RGD:1583902}; Synonyms=GLUT7 {ECO:0000303|Ref.1};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley;
RA Kinnaird A.S., Manolescu A., O'Neill D.D., Witkowska K., Cheeseman C.I.;
RT "Rattus norvegicus GLUT7 hexose transporter.";
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
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; EF501821; ABP68403.1; -; mRNA.
DR RefSeq; NP_001094490.1; NM_001101020.1.
DR AlphaFoldDB; A4ZYQ5; -.
DR SMR; A4ZYQ5; -.
DR GlyGen; A4ZYQ5; 1 site.
DR PRIDE; A4ZYQ5; -.
DR GeneID; 100362644; -.
DR CTD; 155184; -.
DR RGD; 1583902; Slc2a7.
DR InParanoid; A4ZYQ5; -.
DR OrthoDB; 749998at2759; -.
DR PhylomeDB; A4ZYQ5; -.
DR Reactome; R-RNO-189200; Cellular hexose transport.
DR PRO; PR:A4ZYQ5; -.
DR Proteomes; UP000002494; Unplaced.
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:0015149; F:hexose transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015749; P:monosaccharide transmembrane transport; IBA:GO_Central.
DR GO; GO:1901700; P:response to oxygen-containing compound; IEA:UniProt.
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 2: Evidence at transcript 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_0000317273"
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"
SQ SEQUENCE 512 AA; 55691 MW; E40861624BFB18E8 CRC64;
MENKEAGTPP PIPSREGRLQ PTLLLATLSA AFGSAFQYGY NLSVVNTPHK VFKSFYNETY
FERHATFMDG KLMLLLWSCT VSMFPLGGLL GSLLVGLLVD SCGRKGTLLI NNIFAIIPAI
LMGVSKVAKA FELIVFSRVV LGVCAGISYS ALPMYLGELA PKNLRGMVGT VTEVFVIVGV
FLAQIFSLQA ILGNPAGWPV LLALTGVPAL LQLLTLPFFP ESPRYSLIQK GDEATARQAL
RRLRGHTDME AELEDMRAEA RAERAEGHLS VLHLCALRSL RWQLLSIIVL MAGQQLSGIN
AVNYYADTIY TSAGVEAAHS QYVTVGSGVV NIVMTITSAV LVERLGRRHL LLAGYGICGS
ACLVLTVVLL FQNRVPELSY LGIICVFAYI AGHSIGPSPV PPVVRTEIFL QSSRRAAFMV
DGAVHWLTNF IIGFLFPSIQ EAIGAYSFII FAGICLLTAI YIYVVIPETK GKTFVEINRI
FAKRNRVKLP EEKEETIDAG PPTASPAKET SF
