GTR3_CHICK
ID GTR3_CHICK Reviewed; 496 AA.
AC P28568;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Solute carrier family 2, facilitated glucose transporter member 3 {ECO:0000305};
DE AltName: Full=CEF-GT3 {ECO:0000303|PubMed:1875932};
DE AltName: Full=Glucose transporter type 3 {ECO:0000303|PubMed:1875932};
DE Short=GLUT-3 {ECO:0000303|PubMed:1875932};
GN Name=SLC2A3 {ECO:0000250|UniProtKB:P11169};
GN Synonyms=GLUT3 {ECO:0000303|PubMed:1875932};
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1875932; DOI=10.1128/mcb.11.9.4448-4454.1991;
RA White M.K., Rall T.B., Weber M.J.;
RT "Differential regulation of glucose transporter isoforms by the src
RT oncogene in chicken embryo fibroblasts.";
RL Mol. Cell. Biol. 11:4448-4454(1991).
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; M37785; AAA48662.1; -; mRNA.
DR PIR; A41264; A41264.
DR RefSeq; NP_990842.1; NM_205511.1.
DR AlphaFoldDB; P28568; -.
DR SMR; P28568; -.
DR STRING; 9031.ENSGALP00000036432; -.
DR PaxDb; P28568; -.
DR GeneID; 396517; -.
DR KEGG; gga:396517; -.
DR CTD; 144195; -.
DR VEuPathDB; HostDB:geneid_396517; -.
DR eggNOG; KOG0569; Eukaryota.
DR InParanoid; P28568; -.
DR OrthoDB; 749998at2759; -.
DR PhylomeDB; P28568; -.
DR Reactome; R-GGA-352832; Glucose transport.
DR PRO; PR:P28568; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-SubCell.
DR GO; GO:0005615; C:extracellular space; IDA:AgBase.
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:0005886; C:plasma membrane; TAS:Reactome.
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; Reference proteome;
KW Sugar transport; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..496
FT /note="Solute carrier family 2, facilitated glucose
FT transporter member 3"
FT /id="PRO_0000050360"
FT TOPO_DOM 1..11
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P11169"
FT TRANSMEM 12..33
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250|UniProtKB:P11169, ECO:0000255"
FT TOPO_DOM 34..65
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P11169"
FT TRANSMEM 66..86
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250|UniProtKB:P11169, ECO:0000255"
FT TOPO_DOM 87..91
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P11169"
FT TRANSMEM 92..112
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250|UniProtKB:P11169"
FT TOPO_DOM 113..119
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P11169"
FT TRANSMEM 120..143
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250|UniProtKB:P11169, ECO:0000255"
FT TOPO_DOM 144..154
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P11169"
FT TRANSMEM 155..175
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250|UniProtKB:P11169, ECO:0000255"
FT TOPO_DOM 176..184
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P11169"
FT TRANSMEM 185..205
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250|UniProtKB:P11169, ECO:0000255"
FT TOPO_DOM 206..270
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P11169"
FT TRANSMEM 271..291
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250|UniProtKB:P11169, ECO:0000255"
FT TOPO_DOM 292..305
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P11169"
FT TRANSMEM 306..326
FT /note="Helical; Name=8"
FT /evidence="ECO:0000250|UniProtKB:P11169, ECO:0000255"
FT TOPO_DOM 327..332
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P11169"
FT TRANSMEM 333..353
FT /note="Helical; Name=9"
FT /evidence="ECO:0000250|UniProtKB:P11169, ECO:0000255"
FT TOPO_DOM 354..362
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P11169"
FT TRANSMEM 363..388
FT /note="Helical; Name=10"
FT /evidence="ECO:0000250|UniProtKB:P11169, ECO:0000255"
FT TOPO_DOM 389..398
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P11169"
FT TRANSMEM 399..419
FT /note="Helical; Name=11"
FT /evidence="ECO:0000250|UniProtKB:P11169, ECO:0000255"
FT TOPO_DOM 420..428
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P11169"
FT TRANSMEM 429..449
FT /note="Helical; Name=12"
FT /evidence="ECO:0000250|UniProtKB:P11169, ECO:0000255"
FT TOPO_DOM 450..496
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P11169"
FT REGION 278..280
FT /note="Important for selectivity against fructose"
FT /evidence="ECO:0000250|UniProtKB:P11169"
FT REGION 464..496
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 160
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000250|UniProtKB:P11169"
FT BINDING 281..282
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000250|UniProtKB:P11169"
FT BINDING 287
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000250|UniProtKB:P11169"
FT BINDING 316
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000250|UniProtKB:P11169"
FT BINDING 377
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000250|UniProtKB:P11169"
FT BINDING 385
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000250|UniProtKB:P11169"
FT CARBOHYD 44
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 496 AA; 54175 MW; 75B3C0F61A7A92A5 CRC64;
MADKKKITAS LIYAVSVAAI GSLQFGYNTG VINAPEKIIQ AFYNRTLSQR SGETISPELL
TSLWSLSVAI FSVGGMIGSF SVSLFFNRFG RRNSMLLVNV LAFAGGALMA LSKIAKAVEM
LIIGRFIIGL FCGLCTGFVP MYISEVSPTS LRGAFGTLNQ LGIVVGILVA QIFGLEGIMG
TEALWPLLLG FTIVPAVLQC VALLFCPESP RFLLINKMEE EKAQTVLQKL RGTQDVSQDI
SEMKEESAKM SQEKKATVLE LFRSPNYRQP IIISITLQLS QQLSGINAVF YYSTGIFERA
GITQPVYATI GAGVVNTVFT VVSLFLVERA GRRTLHLVGL GGMAVCAAVM TIALALKEKW
IRYISIVATF GFVALFEIGP GPIPWFIVAE LFSQGPRPAA MAVAGCSNWT SNFLVGMLFP
YAEKLCGPYV FLIFLVFLLI FFIFTYFKVP ETKGRTFEDI SRGFEEQVET SSPSSPPIEK
NPMVEMNSIE PDKEVA
