GTR3_CANLF
ID GTR3_CANLF Reviewed; 495 AA.
AC P47842;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Solute carrier family 2, facilitated glucose transporter member 3 {ECO:0000305};
DE AltName: Full=Glucose transporter type 3, brain {ECO:0000303|PubMed:8654954};
DE Short=GLUT-3 {ECO:0000303|PubMed:8654954};
GN Name=SLC2A3 {ECO:0000250|UniProtKB:P11169};
GN Synonyms=GLUT3 {ECO:0000303|PubMed:8654954};
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain cortex;
RX PubMed=8654954; DOI=10.1016/0378-1119(95)00720-2;
RA Borson N.D., Salo W.L., Drewes L.R.;
RT "Canine brain glucose transporter 3: gene sequence, phylogenetic
RT comparisons and analysis of functional sites.";
RL Gene 168:251-256(1996).
CC -!- FUNCTION: Facilitative glucose transporter that can also mediate the
CC uptake of various other monosaccharides across the cell membrane.
CC Mediates the uptake of glucose, 2-deoxyglucose, galactose, mannose,
CC xylose and fucose, and probably also dehydroascorbate. Does not mediate
CC fructose transport. {ECO:0000250|UniProtKB:P11169}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glucose(out) = D-glucose(in); Xref=Rhea:RHEA:60376,
CC ChEBI:CHEBI:4167; Evidence={ECO:0000250|UniProtKB:P11169};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-galactose(in) = D-galactose(out); Xref=Rhea:RHEA:34915,
CC ChEBI:CHEBI:4139; Evidence={ECO:0000250|UniProtKB:P11169};
CC -!- ACTIVITY REGULATION: Deoxyglucose transport is inhibit by D-glucose, D-
CC galactose and maltose. Galactose transport is inhibited by D-glucose
CC and maltose. {ECO:0000250|UniProtKB:P11169}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P11169};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:P11169}. Perikaryon
CC {ECO:0000250|UniProtKB:Q07647}. Cell projection
CC {ECO:0000250|UniProtKB:Q07647}. Note=Localized to densely spaced
CC patches along neuronal processes. {ECO:0000250|UniProtKB:Q07647}.
CC -!- DOMAIN: Transport is mediated via a series of conformation changes,
CC switching between a conformation where the substrate-binding cavity is
CC accessible from the outside, and a another conformation where it is
CC accessible from the cytoplasm. {ECO:0000250|UniProtKB:P11169}.
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; L35267; AAA51454.1; -; mRNA.
DR RefSeq; NP_001003308.1; NM_001003308.1.
DR AlphaFoldDB; P47842; -.
DR SMR; P47842; -.
DR STRING; 9615.ENSCAFP00000052705; -.
DR PaxDb; P47842; -.
DR GeneID; 403997; -.
DR CTD; 6515; -.
DR eggNOG; KOG0569; Eukaryota.
DR InParanoid; P47842; -.
DR OrthoDB; 749998at2759; -.
DR Proteomes; UP000002254; Unplaced.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of 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:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0055056; F:D-glucose transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0005354; F:galactose transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0005536; F:glucose binding; ISS:UniProtKB.
DR GO; GO:0005355; F:glucose transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0015149; F:hexose transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0070837; P:dehydroascorbic acid transport; IBA:GO_Central.
DR GO; GO:0015757; P:galactose transmembrane transport; ISS:UniProtKB.
DR GO; GO:0046323; P:glucose import; IBA:GO_Central.
DR GO; GO:1904659; P:glucose transmembrane transport; ISS:UniProtKB.
DR GO; GO:0015749; P:monosaccharide transmembrane transport; IBA:GO_Central.
DR Gene3D; 1.20.1250.20; -; 1.
DR InterPro; IPR002945; Glc_transpt_3.
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; PR01192; GLUCTRSPORT3.
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; Cell projection; Glycoprotein; Membrane; Phosphoprotein;
KW Reference proteome; Sugar transport; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..495
FT /note="Solute carrier family 2, facilitated glucose
FT transporter member 3"
FT /id="PRO_0000050352"
FT TOPO_DOM 1..10
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P11169"
FT TRANSMEM 11..32
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250|UniProtKB:P11169, ECO:0000255"
FT TOPO_DOM 33..64
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P11169"
FT TRANSMEM 65..85
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250|UniProtKB:P11169, ECO:0000255"
FT TOPO_DOM 86..90
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P11169"
FT TRANSMEM 91..111
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250|UniProtKB:P11169, ECO:0000255"
FT TOPO_DOM 112..118
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P11169"
FT TRANSMEM 119..142
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250|UniProtKB:P11169, ECO:0000255"
FT TOPO_DOM 143..153
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P11169"
FT TRANSMEM 154..174
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250|UniProtKB:P11169, ECO:0000255"
FT TOPO_DOM 175..183
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P11169"
FT TRANSMEM 184..204
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250|UniProtKB:P11169, ECO:0000255"
FT TOPO_DOM 205..269
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P11169"
FT TRANSMEM 270..290
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250|UniProtKB:P11169, ECO:0000255"
FT TOPO_DOM 291..304
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P11169"
FT TRANSMEM 305..325
FT /note="Helical; Name=8"
FT /evidence="ECO:0000250|UniProtKB:P11169, ECO:0000255"
FT TOPO_DOM 326..331
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P11169"
FT TRANSMEM 332..352
FT /note="Helical; Name=9"
FT /evidence="ECO:0000250|UniProtKB:P11169, ECO:0000255"
FT TOPO_DOM 353..363
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P11169"
FT TRANSMEM 364..389
FT /note="Helical; Name=10"
FT /evidence="ECO:0000250|UniProtKB:P11169, ECO:0000255"
FT TOPO_DOM 390..399
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P11169"
FT TRANSMEM 400..420
FT /note="Helical; Name=11"
FT /evidence="ECO:0000250|UniProtKB:P11169, ECO:0000255"
FT TOPO_DOM 421..429
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 430..450
FT /note="Helical; Name=12"
FT /evidence="ECO:0000250|UniProtKB:P11169, ECO:0000255"
FT TOPO_DOM 451..495
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 277..279
FT /note="Important for selectivity against fructose"
FT /evidence="ECO:0000250|UniProtKB:P11169"
FT BINDING 159
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000250|UniProtKB:P11169"
FT BINDING 280..281
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000250|UniProtKB:P11169"
FT BINDING 286
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000250|UniProtKB:P11169"
FT BINDING 315
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000250|UniProtKB:P11169"
FT BINDING 378
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000250|UniProtKB:P11169"
FT BINDING 386
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000250|UniProtKB:P11169"
FT MOD_RES 232
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P32037"
FT MOD_RES 485
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q07647"
FT MOD_RES 492
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q07647"
FT CARBOHYD 43
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 495 AA; 54283 MW; 09063C013DAE39C3 CRC64;
MGTQKVTVSL IFALSIATIG SFQFGYNTGV INAPETIIKD FLNYTLEEKS ENLPTEVLLT
SLWSLSVAIF SVGGMIGSFS VGLFVNRFGR RNSMLMVNLL AVAGGCLMGF CKIAQSVEML
ILGRLIIGLF CGLCTGFVPM YIGEISPTAL RGAFGTLNQL GIVIGILVAQ IFGLKVIMGT
EELWPLLLGF TIIPAVLQSA ALPFCPESPR FLLINRKEEE NAKEILQRLW GTQDVSQDIQ
EMKDESARMA QEKQVTVLEL FRSRSYRQPI IISIMLQLSQ QLSGINAVFY YSTGIFKDAG
VEEPIYATIG AGVVNTIFTV VSLFLVERAG RRTLHMIGLG GMAVCSILMT ISLLLKDNYN
WMSFVCIGAI LVFVAFFEIG PGPIPWFIVA ELFSQGPRPA AMAVAGCSNW TSNFLVGLLF
PSAAFYLGAY VFIIFTGFLI VFLVFTFFKV PETRGRTFEE ITRAFEGQGQ DANRAEKGPI
VEMNSMQPVK ETATV
