GTR5_RAT
ID GTR5_RAT Reviewed; 502 AA.
AC P43427;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 155.
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:8333543};
DE Short=GLUT-5 {ECO:0000303|PubMed:8333543};
GN Name=Slc2a5 {ECO:0000312|RGD:68328};
GN Synonyms=Glut5 {ECO:0000303|PubMed:8333543};
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], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, DEVELOPMENTAL STAGE, AND ACTIVITY REGULATION.
RC STRAIN=Sprague-Dawley; TISSUE=Jejunum;
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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND INDUCTION BY FRUCTOSE.
RC STRAIN=Sprague-Dawley; TISSUE=Jejunum;
RX PubMed=8404647; DOI=10.1210/endo.133.5.8404647;
RA Inukai K., Asano T., Katagiri H., Ishihara H., Anai M., Fukushima Y.,
RA Tsukuda K., Kikuchi M., Yazaki Y., Oka Y.;
RT "Cloning and increased expression with fructose feeding of rat jejunal
RT GLUT5.";
RL Endocrinology 133:2009-2014(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Intestine;
RA Kasahara T., Kasahara M.;
RL Submitted (FEB-1994) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
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 [5]
RP FUNCTION, SUBCELLULAR LOCATION, ACTIVITY REGULATION, TISSUE SPECIFICITY,
RP AND INDUCTION BY FRUCTOSE.
RX PubMed=9820812; DOI=10.1042/bj3360361;
RA Darakhshan F., Hajduch E., Kristiansen S., Richter E.A., Hundal H.S.;
RT "Biochemical and functional characterization of the GLUT5 fructose
RT transporter in rat skeletal muscle.";
RL Biochem. J. 336:361-366(1998).
RN [6] {ECO:0007744|PDB:4YBQ}
RP X-RAY CRYSTALLOGRAPHY (3.27 ANGSTROMS), FUNCTION, TRANSPORTER ACTIVITY,
RP SUBCELLULAR LOCATION, TOPOLOGY, ACTIVITY REGULATION, AND MUTAGENESIS OF
RP GLN-166.
RX PubMed=26416735; DOI=10.1038/nature14909;
RA Nomura N., Verdon G., Kang H.J., Shimamura T., Nomura Y., Sonoda Y.,
RA Hussien S.A., Qureshi A.A., Coincon M., Sato Y., Abe H., Nakada-Nakura Y.,
RA Hino T., Arakawa T., Kusano-Arai O., Iwanari H., Murata T., Kobayashi T.,
RA Hamakubo T., Kasahara M., Iwata S., Drew D.;
RT "Structure and mechanism of the mammalian fructose transporter GLUT5.";
RL Nature 526:397-401(2015).
CC -!- FUNCTION: Functions as a fructose transporter that has only low
CC activity with other monosaccharides (PubMed:26416735, PubMed:8333543,
CC PubMed:9820812). Can mediate the uptake of deoxyglucose, but with low
CC efficiency (PubMed:8333543). Essential for fructose uptake in the small
CC intestine (By similarity). Plays a role in the regulation of salt
CC uptake and blood pressure in response to dietary fructose (By
CC similarity). Required for the development of high blood pressure in
CC response to high dietary fructose intake (By similarity).
CC {ECO:0000250|UniProtKB:Q9WV38, ECO:0000269|PubMed:26416735,
CC ECO:0000269|PubMed:8333543, ECO:0000269|PubMed:9820812}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-fructose(out) = D-fructose(in); Xref=Rhea:RHEA:60372,
CC ChEBI:CHEBI:37721; Evidence={ECO:0000269|PubMed:26416735};
CC -!- ACTIVITY REGULATION: Fructose uptake is inhibited by mercury ions
CC (PubMed:26416735). Fructose uptake is only slightly inhibited by
CC cytochalasin B (PubMed:8333543, PubMed:9820812).
CC {ECO:0000269|PubMed:26416735, ECO:0000269|PubMed:8333543,
CC ECO:0000269|PubMed:9820812}.
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:26416735, ECO:0000269|PubMed:8333543,
CC ECO:0000269|PubMed:9820812}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:26416735}. Cell membrane, sarcolemma
CC {ECO:0000269|PubMed:9820812}. Note=Localized on the apical membrane of
CC 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 -!- TISSUE SPECIFICITY: Detected in jejunum (PubMed:8404647,
CC PubMed:9820812). Detected in kidney, skeletal muscle, brain and adipose
CC tissue (at protein level) (PubMed:9820812). Detected in small intestine
CC and in kidney, and at much lower levels in brain. Detected in
CC enterocytes in duodenum, jejunum, and ileum (PubMed:8333543).
CC {ECO:0000269|PubMed:8333543, ECO:0000269|PubMed:8404647,
CC ECO:0000269|PubMed:9820812}.
CC -!- DEVELOPMENTAL STAGE: Detected in small intestine during embryogenesis,
CC but expression is much higher in adult. {ECO:0000269|PubMed:8333543}.
CC -!- INDUCTION: Up-regulated in jejunum by a diet with a high fructose
CC content (at protein level) (PubMed:8404647, PubMed:9820812). Up-
CC regulated in kidney by a diet with a high fructose content (at protein
CC level) (PubMed:9820812). Up-regulated in jejunum by a diet with a high
CC fructose content (PubMed:8404647). {ECO:0000269|PubMed:8404647,
CC ECO:0000269|PubMed:9820812}.
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; L05195; AAA02627.1; -; mRNA.
DR EMBL; D13871; BAA02983.1; -; mRNA.
DR EMBL; D28562; BAA05912.1; -; mRNA.
DR EMBL; BC076378; AAH76378.1; -; mRNA.
DR PIR; I53268; I53268.
DR RefSeq; NP_113929.1; NM_031741.1.
DR PDB; 4YBQ; X-ray; 3.27 A; A/B=1-502.
DR PDBsum; 4YBQ; -.
DR AlphaFoldDB; P43427; -.
DR SMR; P43427; -.
DR STRING; 10116.ENSRNOP00000024054; -.
DR GlyGen; P43427; 1 site.
DR PaxDb; P43427; -.
DR ABCD; P43427; 1 sequenced antibody.
DR Ensembl; ENSRNOT00000024054; ENSRNOP00000024054; ENSRNOG00000017693.
DR GeneID; 65197; -.
DR KEGG; rno:65197; -.
DR UCSC; RGD:68328; rat.
DR CTD; 6518; -.
DR RGD; 68328; Slc2a5.
DR eggNOG; KOG0569; Eukaryota.
DR GeneTree; ENSGT00940000156846; -.
DR HOGENOM; CLU_001265_30_5_1; -.
DR InParanoid; P43427; -.
DR OrthoDB; 326501at2759; -.
DR Reactome; R-RNO-6798695; Neutrophil degranulation.
DR Reactome; R-RNO-8981373; Intestinal hexose absorption.
DR PRO; PR:P43427; -.
DR Proteomes; UP000002494; Chromosome 5.
DR Bgee; ENSRNOG00000017693; Expressed in jejunum and 17 other tissues.
DR ExpressionAtlas; P43427; baseline and differential.
DR Genevisible; P43427; RN.
DR GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0042383; C:sarcolemma; IDA:UniProtKB.
DR GO; GO:0070061; F:fructose binding; IDA:UniProtKB.
DR GO; GO:0005353; F:fructose transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0005355; F:glucose transmembrane transporter activity; IDA:RGD.
DR GO; GO:0015149; F:hexose transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0071332; P:cellular response to fructose stimulus; IDA:UniProtKB.
DR GO; GO:1990539; P:fructose import across plasma membrane; IDA:UniProtKB.
DR GO; GO:0015755; P:fructose transmembrane transport; IDA:RGD.
DR GO; GO:1904659; P:glucose transmembrane transport; IDA:RGD.
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; ISO:RGD.
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 3D-structure; Acetylation; Cell membrane; Glycoprotein; Membrane;
KW Reference proteome; Sugar transport; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..502
FT /note="Solute carrier family 2, facilitated glucose
FT transporter member 5"
FT /id="PRO_0000050372"
FT TOPO_DOM 1..17
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:26416735"
FT TRANSMEM 18..38
FT /note="Helical; Name=1"
FT /evidence="ECO:0000269|PubMed:26416735"
FT TOPO_DOM 39..67
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:26416735"
FT TRANSMEM 68..90
FT /note="Helical; Name=2"
FT /evidence="ECO:0000269|PubMed:26416735"
FT TOPO_DOM 91..97
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:26416735"
FT TRANSMEM 98..118
FT /note="Helical; Name=3"
FT /evidence="ECO:0000269|PubMed:26416735"
FT TOPO_DOM 119..125
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:26416735"
FT TRANSMEM 126..148
FT /note="Helical; Name=4"
FT /evidence="ECO:0000269|PubMed:26416735"
FT TOPO_DOM 149..160
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:26416735"
FT TRANSMEM 161..181
FT /note="Helical; Name=5"
FT /evidence="ECO:0000269|PubMed:26416735"
FT TOPO_DOM 182..191
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:26416735"
FT TRANSMEM 192..212
FT /note="Helical; Name=6"
FT /evidence="ECO:0000269|PubMed:26416735"
FT TOPO_DOM 213..276
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:26416735"
FT TRANSMEM 277..297
FT /note="Helical; Name=7"
FT /evidence="ECO:0000269|PubMed:26416735"
FT TOPO_DOM 298..312
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:26416735"
FT TRANSMEM 313..333
FT /note="Helical; Name=8"
FT /evidence="ECO:0000269|PubMed:26416735"
FT TOPO_DOM 334..341
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:26416735"
FT TRANSMEM 342..362
FT /note="Helical; Name=9"
FT /evidence="ECO:0000269|PubMed:26416735"
FT TOPO_DOM 363..370
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:26416735"
FT TRANSMEM 371..393
FT /note="Helical; Name=10"
FT /evidence="ECO:0000269|PubMed:26416735"
FT TOPO_DOM 394..411
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:26416735"
FT TRANSMEM 412..432
FT /note="Helical; Name=11"
FT /evidence="ECO:0000269|PubMed:26416735"
FT TOPO_DOM 433..438
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:26416735"
FT TRANSMEM 439..459
FT /note="Helical; Name=12"
FT /evidence="ECO:0000269|PubMed:26416735"
FT TOPO_DOM 460..502
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:26416735"
FT BINDING 31
FT /ligand="D-fructose"
FT /ligand_id="ChEBI:CHEBI:37721"
FT /evidence="ECO:0000269|PubMed:26416735"
FT BINDING 166
FT /ligand="D-fructose"
FT /ligand_id="ChEBI:CHEBI:37721"
FT /evidence="ECO:0000269|PubMed:26416735"
FT BINDING 287
FT /ligand="D-fructose"
FT /ligand_id="ChEBI:CHEBI:37721"
FT /evidence="ECO:0000269|PubMed:26416735"
FT BINDING 295..297
FT /ligand="D-fructose"
FT /ligand_id="ChEBI:CHEBI:37721"
FT /evidence="ECO:0000269|PubMed:26416735"
FT BINDING 386
FT /ligand="D-fructose"
FT /ligand_id="ChEBI:CHEBI:37721"
FT /evidence="ECO:0000269|PubMed:26416735"
FT BINDING 418..419
FT /ligand="D-fructose"
FT /ligand_id="ChEBI:CHEBI:37721"
FT /evidence="ECO:0000269|PubMed:26416735"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P22732"
FT CARBOHYD 50
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 166
FT /note="Q->E: Impairs D-fructose binding."
FT /evidence="ECO:0000269|PubMed:26416735"
FT CONFLICT 164
FT /note="V -> A (in Ref. 1; AAA02627)"
FT /evidence="ECO:0000305"
FT CONFLICT 285
FT /note="A -> T (in Ref. 2; BAA02983)"
FT /evidence="ECO:0000305"
FT CONFLICT 452
FT /note="T -> S (in Ref. 2; BAA02983)"
FT /evidence="ECO:0000305"
FT CONFLICT 479
FT /note="K -> N (in Ref. 1; AAA02627)"
FT /evidence="ECO:0000305"
FT HELIX 14..37
FT /evidence="ECO:0007829|PDB:4YBQ"
FT TURN 41..43
FT /evidence="ECO:0007829|PDB:4YBQ"
FT HELIX 62..86
FT /evidence="ECO:0007829|PDB:4YBQ"
FT HELIX 88..120
FT /evidence="ECO:0007829|PDB:4YBQ"
FT HELIX 124..152
FT /evidence="ECO:0007829|PDB:4YBQ"
FT HELIX 155..186
FT /evidence="ECO:0007829|PDB:4YBQ"
FT HELIX 191..208
FT /evidence="ECO:0007829|PDB:4YBQ"
FT HELIX 209..211
FT /evidence="ECO:0007829|PDB:4YBQ"
FT HELIX 216..220
FT /evidence="ECO:0007829|PDB:4YBQ"
FT HELIX 226..237
FT /evidence="ECO:0007829|PDB:4YBQ"
FT STRAND 238..240
FT /evidence="ECO:0007829|PDB:4YBQ"
FT HELIX 243..257
FT /evidence="ECO:0007829|PDB:4YBQ"
FT HELIX 264..269
FT /evidence="ECO:0007829|PDB:4YBQ"
FT HELIX 274..288
FT /evidence="ECO:0007829|PDB:4YBQ"
FT HELIX 292..306
FT /evidence="ECO:0007829|PDB:4YBQ"
FT HELIX 310..338
FT /evidence="ECO:0007829|PDB:4YBQ"
FT HELIX 340..367
FT /evidence="ECO:0007829|PDB:4YBQ"
FT HELIX 371..388
FT /evidence="ECO:0007829|PDB:4YBQ"
FT TURN 389..392
FT /evidence="ECO:0007829|PDB:4YBQ"
FT HELIX 393..401
FT /evidence="ECO:0007829|PDB:4YBQ"
FT TURN 404..406
FT /evidence="ECO:0007829|PDB:4YBQ"
FT HELIX 407..436
FT /evidence="ECO:0007829|PDB:4YBQ"
FT HELIX 437..439
FT /evidence="ECO:0007829|PDB:4YBQ"
FT HELIX 440..457
FT /evidence="ECO:0007829|PDB:4YBQ"
FT HELIX 467..479
FT /evidence="ECO:0007829|PDB:4YBQ"
SQ SEQUENCE 502 AA; 55543 MW; 871FEDEFA1E7884D CRC64;
MEKEDQEKTG KLTLVLALAT FLAAFGSSFQ YGYNVAAVNS PSEFMQQFYN DTYYDRNKEN
IESFTLTLLW SLTVSMFPFG GFIGSLMVGF LVNNLGRKGA LLFNNIFSIL PAILMGCSKI
AKSFEIIIAS RLLVGICAGI SSNVVPMYLG ELAPKNLRGA LGVVPQLFIT VGILVAQLFG
LRSVLASEEG WPILLGLTGV PAGLQLLLLP FFPESPRYLL IQKKNESAAE KALQTLRGWK
DVDMEMEEIR KEDEAEKAAG FISVWKLFRM QSLRWQLIST IVLMAGQQLS GVNAIYYYAD
QIYLSAGVKS NDVQYVTAGT GAVNVFMTMV TVFVVELWGR RNLLLIGFST CLTACIVLTV
ALALQNTISW MPYVSIVCVI VYVIGHAVGP SPIPALFITE IFLQSSRPSA YMIGGSVHWL
SNFIVGLIFP FIQVGLGPYS FIIFAIICLL TTIYIFMVVP ETKGRTFVEI NQIFAKKNKV
SDVYPEKEEK ELNDLPPATR EQ
