GTR5_BOVIN
ID GTR5_BOVIN Reviewed; 501 AA.
AC P58353; A7MBF2;
DT 16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 131.
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:0000250|UniProtKB:P22732};
DE Short=GLUT-5 {ECO:0000250|UniProtKB:P22732};
GN Name=SLC2A5 {ECO:0000250|UniProtKB:P22732};
GN Synonyms=GLUT5 {ECO:0000250|UniProtKB:P22732};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Kidney;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 253-456.
RC TISSUE=Small intestine;
RX PubMed=11599048; DOI=10.1002/mrd.1099;
RA Augustin R., Pocar P., Navarrete-Santos A., Wrenzycki C., Gandolfi F.,
RA Niemann H., Fischer B.;
RT "Glucose transporter expression is developmentally regulated in in vitro
RT derived bovine preimplantation embryos.";
RL Mol. Reprod. Dev. 60:370-376(2001).
RN [3] {ECO:0007744|PDB:4YB9}
RP X-RAY CRYSTALLOGRAPHY (3.20 ANGSTROMS) OF 1-473, SUBCELLULAR LOCATION, AND
RP TOPOLOGY.
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. 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 {ECO:0000305}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:26416735}. Cell membrane,
CC sarcolemma {ECO:0000250|UniProtKB:P43427}. Note=Localized on the apical
CC membrane of jejunum villi, but also on lateral plasma membranes of the
CC villi. 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; BC151530; AAI51531.1; -; mRNA.
DR EMBL; AF308830; AAK63203.1; -; mRNA.
DR RefSeq; NP_001094512.1; NM_001101042.2.
DR PDB; 4YB9; X-ray; 3.20 A; D=1-473.
DR PDBsum; 4YB9; -.
DR AlphaFoldDB; P58353; -.
DR SMR; P58353; -.
DR STRING; 9913.ENSBTAP00000045621; -.
DR PaxDb; P58353; -.
DR PRIDE; P58353; -.
DR ABCD; P58353; 1 sequenced antibody.
DR Ensembl; ENSBTAT00000009606; ENSBTAP00000009606; ENSBTAG00000007302.
DR Ensembl; ENSBTAT00000048616; ENSBTAP00000045621; ENSBTAG00000034323.
DR GeneID; 282868; -.
DR KEGG; bta:282868; -.
DR CTD; 6518; -.
DR VEuPathDB; HostDB:ENSBTAG00000007302; -.
DR VEuPathDB; HostDB:ENSBTAG00000034323; -.
DR eggNOG; KOG0569; Eukaryota.
DR GeneTree; ENSGT00940000156846; -.
DR HOGENOM; CLU_001265_30_11_1; -.
DR InParanoid; P58353; -.
DR OMA; VAQFLCM; -.
DR OrthoDB; 326501at2759; -.
DR Proteomes; UP000009136; Chromosome 14.
DR Proteomes; UP000009136; Chromosome 16.
DR Bgee; ENSBTAG00000034323; Expressed in placenta and 49 other tissues.
DR ExpressionAtlas; P58353; baseline.
DR GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0042383; C:sarcolemma; ISS:UniProtKB.
DR GO; GO:0070061; F:fructose binding; ISS:UniProtKB.
DR GO; GO:0005353; F:fructose transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0015149; F:hexose transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0071332; P:cellular response to fructose stimulus; ISS:UniProtKB.
DR GO; GO:1990539; P:fructose import across plasma membrane; ISS:UniProtKB.
DR GO; GO:0015755; P:fructose transmembrane transport; IBA:GO_Central.
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; 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 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..501
FT /note="Solute carrier family 2, facilitated glucose
FT transporter member 5"
FT /id="PRO_0000050367"
FT TOPO_DOM 1..18
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:26416735"
FT TRANSMEM 19..39
FT /note="Helical; Name=1"
FT /evidence="ECO:0000269|PubMed:26416735"
FT TOPO_DOM 40..68
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:26416735"
FT TRANSMEM 69..91
FT /note="Helical; Name=2"
FT /evidence="ECO:0000269|PubMed:26416735"
FT TOPO_DOM 92..98
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:26416735"
FT TRANSMEM 99..119
FT /note="Helical; Name=3"
FT /evidence="ECO:0000269|PubMed:26416735"
FT TOPO_DOM 120..126
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:26416735"
FT TRANSMEM 127..149
FT /note="Helical; Name=4"
FT /evidence="ECO:0000269|PubMed:26416735"
FT TOPO_DOM 150..161
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:26416735"
FT TRANSMEM 162..182
FT /note="Helical; Name=5"
FT /evidence="ECO:0000269|PubMed:26416735"
FT TOPO_DOM 183..192
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:26416735"
FT TRANSMEM 193..213
FT /note="Helical; Name=6"
FT /evidence="ECO:0000269|PubMed:26416735"
FT TOPO_DOM 214..277
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:26416735"
FT TRANSMEM 278..298
FT /note="Helical; Name=7"
FT /evidence="ECO:0000269|PubMed:26416735"
FT TOPO_DOM 299..313
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:26416735"
FT TRANSMEM 314..334
FT /note="Helical; Name=8"
FT /evidence="ECO:0000269|PubMed:26416735"
FT TOPO_DOM 335..342
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:26416735"
FT TRANSMEM 343..363
FT /note="Helical; Name=9"
FT /evidence="ECO:0000269|PubMed:26416735"
FT TOPO_DOM 364..371
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:26416735"
FT TRANSMEM 372..394
FT /note="Helical; Name=10"
FT /evidence="ECO:0000269|PubMed:26416735"
FT TOPO_DOM 395..412
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:26416735"
FT TRANSMEM 413..433
FT /note="Helical; Name=11"
FT /evidence="ECO:0000269|PubMed:26416735"
FT TOPO_DOM 434..439
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:26416735"
FT TRANSMEM 440..460
FT /note="Helical; Name=12"
FT /evidence="ECO:0000269|PubMed:26416735"
FT TOPO_DOM 461..501
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:26416735"
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"
FT CONFLICT 255
FT /note="R -> E (in Ref. 2; AAK63203)"
FT /evidence="ECO:0000305"
FT CONFLICT 353
FT /note="F -> L (in Ref. 2; AAK63203)"
FT /evidence="ECO:0000305"
FT CONFLICT 454
FT /note="V -> I (in Ref. 2; AAK63203)"
FT /evidence="ECO:0000305"
FT HELIX 20..23
FT /evidence="ECO:0007829|PDB:4YB9"
FT HELIX 28..37
FT /evidence="ECO:0007829|PDB:4YB9"
FT TURN 38..40
FT /evidence="ECO:0007829|PDB:4YB9"
FT HELIX 43..55
FT /evidence="ECO:0007829|PDB:4YB9"
FT HELIX 64..87
FT /evidence="ECO:0007829|PDB:4YB9"
FT HELIX 89..93
FT /evidence="ECO:0007829|PDB:4YB9"
FT HELIX 98..108
FT /evidence="ECO:0007829|PDB:4YB9"
FT HELIX 110..117
FT /evidence="ECO:0007829|PDB:4YB9"
FT TURN 119..121
FT /evidence="ECO:0007829|PDB:4YB9"
FT HELIX 124..127
FT /evidence="ECO:0007829|PDB:4YB9"
FT HELIX 129..153
FT /evidence="ECO:0007829|PDB:4YB9"
FT STRAND 156..158
FT /evidence="ECO:0007829|PDB:4YB9"
FT HELIX 160..162
FT /evidence="ECO:0007829|PDB:4YB9"
FT HELIX 165..179
FT /evidence="ECO:0007829|PDB:4YB9"
FT TURN 183..186
FT /evidence="ECO:0007829|PDB:4YB9"
FT TURN 189..191
FT /evidence="ECO:0007829|PDB:4YB9"
FT HELIX 192..197
FT /evidence="ECO:0007829|PDB:4YB9"
FT HELIX 198..200
FT /evidence="ECO:0007829|PDB:4YB9"
FT HELIX 201..209
FT /evidence="ECO:0007829|PDB:4YB9"
FT HELIX 210..212
FT /evidence="ECO:0007829|PDB:4YB9"
FT HELIX 217..222
FT /evidence="ECO:0007829|PDB:4YB9"
FT HELIX 227..234
FT /evidence="ECO:0007829|PDB:4YB9"
FT HELIX 246..250
FT /evidence="ECO:0007829|PDB:4YB9"
FT HELIX 253..260
FT /evidence="ECO:0007829|PDB:4YB9"
FT HELIX 266..270
FT /evidence="ECO:0007829|PDB:4YB9"
FT STRAND 272..274
FT /evidence="ECO:0007829|PDB:4YB9"
FT HELIX 275..289
FT /evidence="ECO:0007829|PDB:4YB9"
FT HELIX 294..305
FT /evidence="ECO:0007829|PDB:4YB9"
FT TURN 306..308
FT /evidence="ECO:0007829|PDB:4YB9"
FT HELIX 313..338
FT /evidence="ECO:0007829|PDB:4YB9"
FT HELIX 341..362
FT /evidence="ECO:0007829|PDB:4YB9"
FT TURN 367..370
FT /evidence="ECO:0007829|PDB:4YB9"
FT HELIX 371..387
FT /evidence="ECO:0007829|PDB:4YB9"
FT TURN 388..393
FT /evidence="ECO:0007829|PDB:4YB9"
FT HELIX 394..402
FT /evidence="ECO:0007829|PDB:4YB9"
FT TURN 405..407
FT /evidence="ECO:0007829|PDB:4YB9"
FT HELIX 408..436
FT /evidence="ECO:0007829|PDB:4YB9"
FT HELIX 438..440
FT /evidence="ECO:0007829|PDB:4YB9"
FT HELIX 443..458
FT /evidence="ECO:0007829|PDB:4YB9"
SQ SEQUENCE 501 AA; 55393 MW; 6752DA90FFFDC3F3 CRC64;
MEPQDPVKRE GRLTPVIVLA TLIAAFGSSF QYGYNVAAIN SPSEFMKDFY NYTYYDRVGE
YMNEFYLTLL WSVTVSMFPF GGFLGSLMVG PLVNNLGRKG TLLFNNIFSI VPALLMGFSE
LAKSFEMIIV ARVLVGICAG LSSNVVPMYL GELAPKNWRG ALGVVPQLFI TIGILVAQIF
GLRSLLANEE GWPILLGLTG IPAVLQLLFL PFFPESPRYL LIQKKDEAAA KSALRRLRGW
HDVDAEIEEI LEEDRAEKAV GFISVLKLFK MRSLRWQVIS IIVLMAGQQL SGVNAIYYYA
DQIYLSAGVN EDDVQYVTAG TGAVNVLITV CAIFVVELMG RRFLLLLGFS VCFTACCVLT
GALALQDVIS WMPYVSIACV ISYVIGHALG PSPIPALLVT EIFLQSSRPA AYMVAGTVHW
LSNFTVGLVF PFIQVGLGAY SFVIFAVICL LTTVYIFLII PETKSKTFIE INRIFIKMNK
VPGVHPEKEE LKEFPPSTAR Q
