GTR3_SHEEP
ID GTR3_SHEEP Reviewed; 494 AA.
AC P47843;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 121.
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:9250701};
DE Short=GLUT-3 {ECO:0000303|PubMed:9250701};
GN Name=SLC2A3 {ECO:0000250|UniProtKB:P11169};
GN Synonyms=GLUT3 {ECO:0000303|PubMed:9250701};
OS Ovis aries (Sheep).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Ovis.
OX NCBI_TaxID=9940;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Coopworth;
RX PubMed=8653093;
RA Bennett B.L., Prosser C.G., Grigor M.R.;
RT "Isolation of cDNAs and tissue specific expression of ovine glucose
RT transporters.";
RL Biochem. Mol. Biol. Int. 37:9-16(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 88-248, AND TISSUE SPECIFICITY.
RC TISSUE=Placenta;
RX PubMed=9250701; DOI=10.1016/s0143-4004(97)80039-2;
RA Currie M.J., Bassett N.S., Gluckman P.D.;
RT "Ovine glucose transporter-1 and -3: cDNA partial sequences and
RT developmental gene expression in the placenta.";
RL Placenta 18:393-401(1997).
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 -!- TISSUE SPECIFICITY: Detected in placenta. {ECO:0000269|PubMed:9250701}.
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; L39214; AAC41629.1; -; mRNA.
DR EMBL; U89030; AAB49313.1; -; mRNA.
DR RefSeq; NP_001009770.1; NM_001009770.1.
DR AlphaFoldDB; P47843; -.
DR SMR; P47843; -.
DR STRING; 9940.ENSOARP00000002361; -.
DR Ensembl; ENSOART00000002412; ENSOARP00000002361; ENSOARG00000002234.
DR Ensembl; ENSOART00020017209; ENSOARP00020014215; ENSOARG00020011245.
DR GeneID; 443308; -.
DR KEGG; oas:443308; -.
DR CTD; 6515; -.
DR eggNOG; KOG0569; Eukaryota.
DR HOGENOM; CLU_001265_30_5_1; -.
DR OMA; WIDFALF; -.
DR OrthoDB; 749998at2759; -.
DR Proteomes; UP000002356; Chromosome 3.
DR Bgee; ENSOARG00000002234; Expressed in gastric lymph node and 56 other tissues.
DR GO; GO:0002080; C:acrosomal membrane; IEA:Ensembl.
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:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0055056; F:D-glucose transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0033300; F:dehydroascorbic acid transmembrane transporter activity; IEA:Ensembl.
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:0015757; P:galactose transmembrane transport; ISS:UniProtKB.
DR GO; GO:1904659; P:glucose transmembrane transport; ISS:UniProtKB.
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..494
FT /note="Solute carrier family 2, facilitated glucose
FT transporter member 3"
FT /id="PRO_0000050359"
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:0000250|UniProtKB:P11169"
FT TRANSMEM 430..450
FT /note="Helical; Name=12"
FT /evidence="ECO:0000250|UniProtKB:P11169, ECO:0000255"
FT TOPO_DOM 451..494
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P11169"
FT REGION 277..279
FT /note="Important for selectivity against fructose"
FT /evidence="ECO:0000250|UniProtKB:P11169"
FT REGION 473..494
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 494 AA; 54195 MW; A89204D3EA74BFBA CRC64;
MGTTKVTTPL IFAISIATIG SFQFGYNTGV INAPEAIIKD FLNYTLEERS ETPPSSVLLT
SLWSLSVAIF SVGGMIGSFS VGLFVNRFGR RNSMLIVNLL AIAGGCLMGF CKIAESVEML
ILGRLIIGLF CGLCTGFVPM YIGEISPTAL RGAFGTLNQL GIVIGILVAQ IFGLKVILGT
EDLWPLLLGF TILPAIIQCA ALPFCPESPR FLLINRKEEE KAKEILQRLW GTEDVAQDIQ
EMKDESMRMS QEKQVTVLEL FRAPNYRQPI IISIMLQLSQ QLSGINAVFY YSTGIFKDAG
VQEPVYATIG AGVVNTIFTV VSVFLVERAG RRTLHLIGLG GMAFCSILMT ISLLLKDNYS
WMSFICIGAI LVFVAFFEIG PGPIPWFIVA ELFGQGPRPA AMAVAGCSNW TSNFLVGLLF
PSATFYLGAY VFIVFTVFLV IFWVFTFFKV PETRGRTFEE ITRAFEGQVQ TGTRGEKGPI
MEMNSIQPTK DTNA
