GTR5_RABIT
ID GTR5_RABIT Reviewed; 486 AA.
AC P46408;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 108.
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:7980458};
DE Short=GLUT-5 {ECO:0000303|PubMed:7980458};
GN Name=SLC2A5 {ECO:0000250|UniProtKB:P22732};
GN Synonyms=GLUT5 {ECO:0000303|PubMed:7980458};
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC STRAIN=New Zealand white; TISSUE=Small intestine;
RX PubMed=7980458; DOI=10.1042/bj3030877;
RA Miyamoto K., Tatsumi S., Morimoto A., Minami H., Yamamoto H., Sone K.,
RA Taketani Y., Nakabou Y., Oka T., Takeda E.;
RT "Characterization of the rabbit intestinal fructose transporter (GLUT5).";
RL Biochem. J. 303:877-883(1994).
CC -!- FUNCTION: Functions as a fructose transporter that has only low
CC activity with other monosaccharides (PubMed:7980458). Can mediate the
CC uptake of deoxyglucose, but with low efficiency (By similarity).
CC Essential for fructose uptake in the small intestine. Plays a role in
CC the regulation of salt uptake and blood pressure in response to dietary
CC fructose. Required for the development of high blood pressure in
CC response to high dietary fructose intake (By similarity).
CC {ECO:0000250|UniProtKB:P43427, ECO:0000250|UniProtKB:Q9WV38,
CC ECO:0000269|PubMed:7980458}.
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:0000269|PubMed:7980458}; 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 -!- TISSUE SPECIFICITY: Detected in jejunum. Detected at the intestinal
CC brush-border membrane (at protein level). Detected in duodenum, jejunum
CC and kidney. {ECO:0000269|PubMed:7980458}.
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; D26482; BAA05492.1; -; mRNA.
DR PIR; S53322; S53322.
DR RefSeq; NP_001075671.1; NM_001082202.1.
DR AlphaFoldDB; P46408; -.
DR SMR; P46408; -.
DR PRIDE; P46408; -.
DR KEGG; ocu:100008992; -.
DR InParanoid; P46408; -.
DR Proteomes; UP000001811; Unplaced.
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: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:0071332; P:cellular response to fructose stimulus; ISS:UniProtKB.
DR GO; GO:1990539; P:fructose import across plasma membrane; ISS:UniProtKB.
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; PS00217; SUGAR_TRANSPORT_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cell membrane; Glycoprotein; Membrane; Reference proteome;
KW Sugar transport; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..486
FT /note="Solute carrier family 2, facilitated glucose
FT transporter member 5"
FT /id="PRO_0000050371"
FT TOPO_DOM 1..19
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P43427"
FT TRANSMEM 20..40
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250|UniProtKB:P43427"
FT TOPO_DOM 41..69
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P43427"
FT TRANSMEM 70..92
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250|UniProtKB:P43427"
FT TOPO_DOM 93..99
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P43427"
FT TRANSMEM 100..120
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250|UniProtKB:P43427"
FT TOPO_DOM 121..127
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P43427"
FT TRANSMEM 128..150
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250|UniProtKB:P43427"
FT TOPO_DOM 151..162
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P43427"
FT TRANSMEM 163..183
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250|UniProtKB:P43427"
FT TOPO_DOM 184..192
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P43427"
FT TRANSMEM 193..211
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250|UniProtKB:P43427"
FT TOPO_DOM 212..274
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P43427"
FT TRANSMEM 275..294
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250|UniProtKB:P43427"
FT TOPO_DOM 295..306
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P43427"
FT TRANSMEM 307..327
FT /note="Helical; Name=8"
FT /evidence="ECO:0000250|UniProtKB:P43427"
FT TOPO_DOM 328..334
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P43427"
FT TRANSMEM 335..355
FT /note="Helical; Name=9"
FT /evidence="ECO:0000250|UniProtKB:P43427"
FT TOPO_DOM 356..363
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P43427"
FT TRANSMEM 364..385
FT /note="Helical; Name=10"
FT /evidence="ECO:0000250|UniProtKB:P43427"
FT TOPO_DOM 386..402
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P43427"
FT TRANSMEM 403..421
FT /note="Helical; Name=11"
FT /evidence="ECO:0000250|UniProtKB:P43427"
FT TOPO_DOM 422..426
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P43427"
FT TRANSMEM 427..447
FT /note="Helical; Name=12"
FT /evidence="ECO:0000250|UniProtKB:P43427"
FT TOPO_DOM 448..486
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P43427"
FT BINDING 33
FT /ligand="D-fructose"
FT /ligand_id="ChEBI:CHEBI:37721"
FT /evidence="ECO:0000250|UniProtKB:P43427"
FT BINDING 168
FT /ligand="D-fructose"
FT /ligand_id="ChEBI:CHEBI:37721"
FT /evidence="ECO:0000250|UniProtKB:P43427"
FT BINDING 284
FT /ligand="D-fructose"
FT /ligand_id="ChEBI:CHEBI:37721"
FT /evidence="ECO:0000250|UniProtKB:P43427"
FT BINDING 292..294
FT /ligand="D-fructose"
FT /ligand_id="ChEBI:CHEBI:37721"
FT /evidence="ECO:0000250|UniProtKB:P43427"
FT BINDING 379
FT /ligand="D-fructose"
FT /ligand_id="ChEBI:CHEBI:37721"
FT /evidence="ECO:0000250|UniProtKB:P43427"
FT BINDING 407..408
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 52
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 486 AA; 53854 MW; 61A141CB2ED5A6BC CRC64;
MEQEGQEKKK EGRLTLVLAL RTLIAAFGSS FQYAYNVSVC NSPSELMTEF YNDTYYDRTG
ELIDEFPLTL LWSVTVSMFP SGGFAGSLLV GPLVNKFGRK GALLFNNIFS IVPAILMGCS
KVARSFELII ISRLLVGICA GVSSNVVPMY LGELAPKNLR GALGVESQLF ITLGILVAQI
FGLRSIRQQK GWPILLGLTG GPAAAACPPF FPESPRYLLI GQEPRCRQKA LQSLRGWDSV
DRELEEIRRE DEAARAAGLV SVRALCAMRG LAWQLISVVP LMWQQLSGVN AIYYYDQIYL
SPLDTDTQYY TAATGAVNVL MTVCTVFVVE SWARLLLLLG FSPLAPTCCV LTAALALQDT
VSWMPYISIV CIIVYVIGHA IGPAIRSLYT EIFLQSGRPP TWWGQVHWLS NFTVGLVFPL
IQWAGLYSFI IFGVACLSTT VYTFLIVPET KGKSFIEIIR RFIRMNKVEV SPDREELKDF
PPDVSE
