ID GTR3_RABIT Reviewed; 494 AA.
AC Q9XSC2; G1TI27;
DT 16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 03-JUL-2019, sequence version 2.
DT 27-MAR-2024, entry version 111.
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:10095018};
DE Short=GLUT-3 {ECO:0000303|PubMed:10095018};
GN Name=SLC2A3 {ECO:0000250|UniProtKB:P11169};
GN Synonyms=GLUT3 {ECO:0000303|PubMed:10095018};
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=Thorbecke;
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 97-494, AND TISSUE SPECIFICITY.
RC STRAIN=New Zealand white;
RX PubMed=10095018; DOI=10.1016/s0006-8993(99)01143-9;
RA Devaskar S.U., Rajakumar P.A., Mink R.B., McKnight R.A., Thamotharan S.,
RA Hicks S.M.;
RT "Effect of development and hypoxic-ischemia upon rabbit brain glucose
RT transporter expression.";
RL Brain Res. 823:113-128(1999).
CC -!- FUNCTION: Facilitative glucose transporter. Can also mediate the uptake
CC of various other monosaccharides across the cell membrane. Mediates the
CC uptake of glucose, 2-deoxyglucose, galactose, mannose, xylose and
CC fucose, and probably also dehydroascorbate. Does not mediate fructose
CC transport. Required for mesendoderm differentiation (By similarity).
CC {ECO:0000250|UniProtKB:P11169, ECO:0000250|UniProtKB:P32037}.
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 -!- SUBUNIT: Interacts with SMIM43; the interaction may promote SLC2A3-
CC mediated glucose transport to meet the energy needs of mesendoderm
CC differentiation. {ECO:0000250|UniProtKB:P32037}.
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 stomach, placenta, lung and brain.
CC {ECO:0000269|PubMed:10095018}.
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; AAGW02051607; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAGW02051608; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AF117812; AAD26251.1; -; mRNA.
DR RefSeq; XP_002712807.1; XM_002712761.3.
DR AlphaFoldDB; Q9XSC2; -.
DR SMR; Q9XSC2; -.
DR STRING; 9986.ENSOCUP00000027226; -.
DR GlyCosmos; Q9XSC2; 1 site, No reported glycans.
DR PaxDb; 9986-ENSOCUP00000016591; -.
DR Ensembl; ENSOCUT00000024311.3; ENSOCUP00000016591.1; ENSOCUG00000008575.4.
DR GeneID; 100125981; -.
DR KEGG; ocu:100125981; -.
DR eggNOG; KOG0569; Eukaryota.
DR GeneTree; ENSGT00940000160313; -.
DR HOGENOM; CLU_001265_30_5_1; -.
DR InParanoid; Q9XSC2; -.
DR OMA; QIGCINA; -.
DR OrthoDB; 1899001at2759; -.
DR TreeFam; TF313762; -.
DR Proteomes; UP000001811; Chromosome 8.
DR Bgee; ENSOCUG00000008575; Expressed in upper lobe of left lung and 15 other cell types or tissues.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; ISS:UniProtKB.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
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:0015757; P:galactose transmembrane transport; ISS:UniProtKB.
DR GO; GO:1904659; P:glucose transmembrane transport; ISS:UniProtKB.
DR CDD; cd17431; MFS_GLUT_Class1; 1.
DR Gene3D; 1.20.1250.20; MFS general substrate transporter like domains; 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 NCBIfam; TIGR00879; SP; 1.
DR PANTHER; PTHR23503; SOLUTE CARRIER FAMILY 2; 1.
DR PANTHER; PTHR23503:SF99; SOLUTE CARRIER FAMILY 2, FACILITATED GLUCOSE TRANSPORTER MEMBER 3; 1.
DR Pfam; PF00083; Sugar_tr; 1.
DR PRINTS; PR01192; GLUCTRSPORT3.
DR PRINTS; PR00171; SUGRTRNSPORT.
DR SUPFAM; SSF103473; MFS general substrate transporter; 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_0000050357"
FT TOPO_DOM 1..10
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
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:0000305"
FT TRANSMEM 65..84
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250|UniProtKB:P11169, ECO:0000255"
FT TOPO_DOM 85..89
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 90..110
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250|UniProtKB:P11169, ECO:0000255"
FT TOPO_DOM 111..117
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 118..141
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250|UniProtKB:P11169, ECO:0000255"
FT TOPO_DOM 142..152
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 153..173
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250|UniProtKB:P11169, ECO:0000255"
FT TOPO_DOM 174..182
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 183..203
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250|UniProtKB:P11169, ECO:0000255"
FT TOPO_DOM 204..268
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 269..289
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250|UniProtKB:P11169, ECO:0000255"
FT TOPO_DOM 290..303
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 304..324
FT /note="Helical; Name=8"
FT /evidence="ECO:0000250|UniProtKB:P11169, ECO:0000255"
FT TOPO_DOM 325..330
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 331..351
FT /note="Helical; Name=9"
FT /evidence="ECO:0000250|UniProtKB:P11169, ECO:0000255"
FT TOPO_DOM 352..362
FT /note="Extracellular"
FT /evidence="ECO:0000305"
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:0000305"
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:0000305"
FT TRANSMEM 429..449
FT /note="Helical; Name=12"
FT /evidence="ECO:0000250|UniProtKB:P11169, ECO:0000255"
FT TOPO_DOM 450..494
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 276..278
FT /note="Important for selectivity against fructose"
FT /evidence="ECO:0000250|UniProtKB:P11169"
FT BINDING 158
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000250|UniProtKB:P11169"
FT BINDING 279..280
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000250|UniProtKB:P11169"
FT BINDING 285
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000250|UniProtKB:P11169"
FT BINDING 314
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 MOD_RES 231
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P32037"
FT MOD_RES 484
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q07647"
FT MOD_RES 491
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q07647"
FT CARBOHYD 43
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 110..113
FT /note="CKIS -> AKIA (in Ref. 2; AAD26251)"
FT /evidence="ECO:0000305"
FT CONFLICT 125..128
FT /note="VIGV -> LIGI (in Ref. 2; AAD26251)"
FT /evidence="ECO:0000305"
FT CONFLICT 144
FT /note="I -> V (in Ref. 2; AAD26251)"
FT /evidence="ECO:0000305"
FT CONFLICT 216..222
FT /note="KEEDEAK -> EEDEAKQIL (in Ref. 2; AAD26251)"
FT /evidence="ECO:0000305"
FT CONFLICT 249
FT /note="A -> R (in Ref. 2; AAD26251)"
FT /evidence="ECO:0000305"
FT CONFLICT 301
FT /note="K -> R (in Ref. 2; AAD26251)"
FT /evidence="ECO:0000305"
FT CONFLICT 373
FT /note="V -> A (in Ref. 2; AAD26251)"
FT /evidence="ECO:0000305"
FT CONFLICT 386..395
FT /note="FIVAELFSQG -> LIVTGLFSQD (in Ref. 2; AAD26251)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 494 AA; 53994 MW; 4742AE2A865D023C CRC64;
MGTTKVTPYL IFATSVAAIG SFQFGYNTGV INAPEMIIRD FLNYTLDEKL DEPPSRLLLT
NLWSLSVAIF SVGGMIGSFS VGLFNRFGRR NSMLIVNLLA VIGGCLMGFC KISESVEMLI
LGRLVIGVFC GLCTGFVPMY IGEISPTALR GAFGTLNQLG IVIGILVAQI FGLEIILGSE
VLWPVLLGFT IIPAILQSAA LPFCPESPRF LLINKKEEDE AKQILQRLWG TQDVAQDIQE
MKEESARMAQ EKQVTVLELF RAPSYRQPII ISIVLQLSQQ LSGINAVFYY STGIFKDAGV
KEPIYATIGA GVVNTIFTIV SVFLVERAGR RTLHLIGLGG MALCSVLMTV SLLLKDKYDT
MSLVCIAAIL IYVAFFEIGP GPIPWFIVAE LFSQGPRPAA MAVAGCSNWT SNFLVGLLFP
SAAYYLGAYV FVIFAVFLVA FFIFTFFKVP ETRGRTFEDI TRAFEGQAAE ANKLGKGPTM
EMNSIQPIET TTHV
//
