GTR5_SHEEP
ID GTR5_SHEEP Reviewed; 501 AA.
AC Q8WMN1;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 91.
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|Ref.1};
DE Short=GLUT-5 {ECO:0000303|Ref.1};
GN Name=SLC2A5 {ECO:0000250|UniProtKB:P22732};
GN Synonyms=GLUT5 {ECO:0000303|Ref.1};
OS Ovis aries (Sheep).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Ovis.
OX NCBI_TaxID=9940;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Small intestine;
RA Wood I.S., Castano-Merediz E.F., Dyer J., Shirazi-Beechey S.P.;
RT "Nutrient regulation of Glut5 in sheep intestine.";
RL Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Functions as a fructose transporter that has only low
CC activity with other monosaccharides. Can mediate the uptake of
CC deoxyglucose, but with low efficiency. Essential for fructose uptake in
CC the small intestine. Plays a role in the regulation of salt uptake and
CC blood pressure in response to dietary fructose. Required for the
CC development of high blood pressure in response to high dietary fructose
CC intake. {ECO:0000250|UniProtKB:P43427, ECO:0000250|UniProtKB:Q9WV38}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-fructose(out) = D-fructose(in); Xref=Rhea:RHEA:60372,
CC ChEBI:CHEBI:37721; Evidence={ECO:0000250|UniProtKB:P22732};
CC -!- SUBCELLULAR LOCATION: Apical cell membrane
CC {ECO:0000250|UniProtKB:Q9WV38}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q9WV38}. Cell membrane
CC {ECO:0000250|UniProtKB:Q9WV38}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q9WV38}. Cell membrane, sarcolemma
CC {ECO:0000250|UniProtKB:P43427}. Note=Localized on the apical membrane
CC of jejunum villi, but also on lateral plasma membranes of the villi.
CC Transport to the cell membrane is dependent on RAB11A.
CC {ECO:0000250|UniProtKB:Q9WV38}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. Sugar
CC transporter (TC 2.A.1.1) family. Glucose transporter subfamily.
CC {ECO:0000305}.
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DR EMBL; AJ315928; CAC86964.1; -; mRNA.
DR RefSeq; NP_001009451.1; NM_001009451.1.
DR AlphaFoldDB; Q8WMN1; -.
DR SMR; Q8WMN1; -.
DR STRING; 9940.ENSOARP00000009608; -.
DR Ensembl; ENSOART00020029058; ENSOARP00020024057; ENSOARG00020018688.
DR Ensembl; ENSOART00020029119; ENSOARP00020024113; ENSOARG00020018688.
DR GeneID; 443507; -.
DR KEGG; oas:443507; -.
DR CTD; 6518; -.
DR eggNOG; KOG0569; Eukaryota.
DR OrthoDB; 326501at2759; -.
DR Proteomes; UP000002356; Unplaced.
DR GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0042383; C:sarcolemma; IEA:UniProtKB-SubCell.
DR GO; GO:0005353; F:fructose transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0071332; P:cellular response to fructose stimulus; 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 2: Evidence at transcript level;
KW Acetylation; Cell membrane; Glycoprotein; Membrane; Reference proteome;
KW Sugar transport; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..501
FT /note="Solute carrier family 2, facilitated glucose
FT transporter member 5"
FT /id="PRO_0000317271"
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:0000250|UniProtKB:P22732"
FT CARBOHYD 51
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 501 AA; 55547 MW; 23F0B43E944C9AD5 CRC64;
MEPQDPVKRE GRLTPVIVLA TLIAAFGSSF QYGYNVATIN SPSEFMKDFY NYTYYDRVGE
YMNEFYLTLL WSVTVSMFPF GGFLGSLMVG PLVNNLGRKG TLLFNNIFSI VPALLMGFSD
LAKSFEMIIV ARVLVGICAG LSSNVVPMYL GELAPKNWRG ALGVVPQLFI TIGILVAQIF
GLRSLLANEE GWPILLGLTG IPAVLQLLFL PFFPESPRYL LIQKKDEEAA KRALRRLRGW
HDVDAEIEEI LEEDRAEKAA GFISVLKLFK MRSLRWQVIS IIVLMAGQQL SGVNAIYYYA
DQIYLSAGVK EDDVQYVTAG TGAVNVLITV CAIFVVELMG RRFLLLLGFS VCFTACCVLT
GALAMQDVIS WMPYVSIACV ISYVIGHALG PSPIPALLVT EIFLQSSRPA AYMVAGTVHW
LSNFTVGLVF PFIQVGLGAY SFVIFAVICF LTTVYIFLII PETKSKTFIE INQIFIKMNK
VPGVHPEKEE LKEFPPSTAR Q
