ID   Q8BLF7_MOUSE            Unreviewed;       493 AA.
AC   Q8BLF7;
DT   01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2003, sequence version 1.
DT   24-JAN-2024, entry version 131.
DE   RecName: Full=Solute carrier family 2, facilitated glucose transporter member 3 {ECO:0000256|ARBA:ARBA00039287, ECO:0000256|RuleBase:RU368110};
DE            Short=GLUT-3 {ECO:0000256|RuleBase:RU368110};
DE   AltName: Full=Glucose transporter type 3 {ECO:0000256|RuleBase:RU368110};
GN   Name=Slc2a3 {ECO:0000313|MGI:MGI:95757};
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090 {ECO:0000313|EMBL:BAC32311.1};
RN   [1] {ECO:0000313|EMBL:BAC32311.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAC32311.1};
RC   TISSUE=Parthenogenote {ECO:0000313|EMBL:BAC32311.1};
RX   PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2] {ECO:0000313|EMBL:BAC32311.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAC32311.1};
RC   TISSUE=Parthenogenote {ECO:0000313|EMBL:BAC32311.1};
RX   PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to prepare
RT   full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [3] {ECO:0000313|EMBL:BAC32311.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAC32311.1};
RC   TISSUE=Parthenogenote {ECO:0000313|EMBL:BAC32311.1};
RX   PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M., Sumi N.,
RA   Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A., Yamamoto R.,
RA   Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K., Fujiwake S.,
RA   Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M., Yoneda Y.,
RA   Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J., Okazaki Y.,
RA   Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format sequencing
RT   pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [4] {ECO:0000313|EMBL:BAC32311.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAC32311.1};
RC   TISSUE=Parthenogenote {ECO:0000313|EMBL:BAC32311.1};
RX   PubMed=11217851; DOI=10.1038/35055500;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [5] {ECO:0000313|EMBL:BAC32311.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAC32311.1};
RC   TISSUE=Parthenogenote {ECO:0000313|EMBL:BAC32311.1};
RA   Adachi J., Aizawa K., Akimura T., Arakawa T., Bono H., Carninci P.,
RA   Fukuda S., Furuno M., Hanagaki T., Hara A., Hashizume W., Hayashida K.,
RA   Hayatsu N., Hiramoto K., Hiraoka T., Hirozane T., Hori F., Imotani K.,
RA   Ishii Y., Itoh M., Kagawa I., Kasukawa T., Katoh H., Kawai J., Kojima Y.,
RA   Kondo S., Konno H., Kouda M., Koya S., Kurihara C., Matsuyama T.,
RA   Miyazaki A., Murata M., Nakamura M., Nishi K., Nomura K., Numazaki R.,
RA   Ohno M., Ohsato N., Okazaki Y., Saito R., Saitoh H., Sakai C., Sakai K.,
RA   Sakazume N., Sano H., Sasaki D., Shibata K., Shinagawa A., Shiraki T.,
RA   Sogabe Y., Tagami M., Tagawa A., Takahashi F., Takaku-Akahira S.,
RA   Takeda Y., Tanaka T., Tomaru A., Toya T., Yasunishi A., Muramatsu M.,
RA   Hayashizaki Y.;
RL   Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN   [6] {ECO:0000313|EMBL:BAC32311.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAC32311.1};
RC   TISSUE=Parthenogenote {ECO:0000313|EMBL:BAC32311.1};
RX   PubMed=12466851; DOI=10.1038/nature01266;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [7] {ECO:0000313|EMBL:BAC32311.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAC32311.1};
RC   TISSUE=Parthenogenote {ECO:0000313|EMBL:BAC32311.1};
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [8] {ECO:0000313|EMBL:BAC32311.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAC32311.1};
RC   TISSUE=Parthenogenote {ECO:0000313|EMBL:BAC32311.1};
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
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:0000256|RuleBase:RU368110}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-galactose(in) = D-galactose(out); Xref=Rhea:RHEA:34915,
CC         ChEBI:CHEBI:4139; Evidence={ECO:0000256|ARBA:ARBA00034046};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-glucose(out) = D-glucose(in); Xref=Rhea:RHEA:60376,
CC         ChEBI:CHEBI:4167; Evidence={ECO:0000256|ARBA:ARBA00000618,
CC         ECO:0000256|RuleBase:RU368110};
CC   -!- SUBUNIT: Interacts with SMIM43; the interaction may promote SLC2A3-
CC       mediated glucose transport to meet the energy needs of mesendoderm
CC       differentiation. {ECO:0000256|ARBA:ARBA00038786}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|RuleBase:RU368110};
CC       Multi-pass membrane protein {ECO:0000256|RuleBase:RU368110}. Cell
CC       projection {ECO:0000256|ARBA:ARBA00004316,
CC       ECO:0000256|RuleBase:RU368110}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}. Perikaryon
CC       {ECO:0000256|ARBA:ARBA00004484, ECO:0000256|RuleBase:RU368110}.
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:0000256|RuleBase:RU368110}.
CC   -!- SIMILARITY: Belongs to the major facilitator superfamily. Sugar
CC       transporter (TC 2.A.1.1) family. Glucose transporter subfamily.
CC       {ECO:0000256|RuleBase:RU368110}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|RuleBase:RU368110}.
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DR   EMBL; AK045328; BAC32311.1; -; mRNA.
DR   RefSeq; NP_035531.3; NM_011401.4.
DR   AlphaFoldDB; Q8BLF7; -.
DR   EPD; Q8BLF7; -.
DR   DNASU; 20527; -.
DR   GeneID; 20527; -.
DR   KEGG; mmu:20527; -.
DR   AGR; MGI:95757; -.
DR   CTD; 6515; -.
DR   MGI; MGI:95757; Slc2a3.
DR   OrthoDB; 1899001at2759; -.
DR   BioGRID-ORCS; 20527; 2 hits in 75 CRISPR screens.
DR   ChiTaRS; Slc2a3; mouse.
DR   GO; GO:0042995; C:cell projection; IEA:UniProtKB-SubCell.
DR   GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005536; F:glucose binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0005355; F:glucose transmembrane transporter activity; IEA:UniProtKB-UniRule.
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.
DR   Genevisible; Q8BLF7; MM.
PE   2: Evidence at transcript level;
KW   Cell membrane {ECO:0000256|RuleBase:RU368110};
KW   Cell projection {ECO:0000256|ARBA:ARBA00023273};
KW   Glycoprotein {ECO:0000256|RuleBase:RU368110};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU368110};
KW   Sugar transport {ECO:0000256|RuleBase:RU368110};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU368110};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|RuleBase:RU368110}; Transport {ECO:0000256|RuleBase:RU003346}.
FT   TRANSMEM        61..83
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU368110"
FT   TRANSMEM        95..114
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU368110"
FT   TRANSMEM        120..142
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU368110"
FT   TRANSMEM        154..177
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU368110"
FT   TRANSMEM        305..326
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU368110"
FT   TRANSMEM        333..355
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU368110"
FT   TRANSMEM        361..379
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU368110"
FT   TRANSMEM        400..420
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU368110"
FT   TRANSMEM        426..448
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU368110"
FT   DOMAIN          13..454
FT                   /note="Major facilitator superfamily (MFS) profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50850"
FT   REGION          469..493
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   493 AA;  53452 MW;  855F52F977923082 CRC64;
     MGTTKVTPSL VFAVTVATIG SFQFGYNTGV INAPETILKD FLNYTLEERL EDLPSEGLLT
     ALWSLCVAIF SVGGMIGSFS VGLFVNRFGR RNSMLLVNLL AIIAGCLMGF AKIAESVEML
     ILGRLLIGIF CGLCTGFVPM YIGEVSPTAL RGAFGTLNQL GIVVGILVAQ IFGLDFILGS
     EELWPGLLGL TIIPAILQSA ALPFCPESPR FLLINKKEED QATEILQRLW GTSDVVQEIQ
     EMKDESVRMS QEKQVTVLEL FRSPNYVQPL LISIVLQLSQ QLSGINAVFY YSTGIFKDAG
     VQEPIYATIG AGVVNTIFTV VSLFLVERAG RRTLHMIGLG GMAVCSVFMT ISLLLKDDYE
     AMSFVCIVAI LIYVAFFEIG PGPIPWFIVA ELFSQGPRPA AIAVAGCCNW TSSFLVGMLF
     PSAAAYLGAY VFIIFAAFLI FFLIFTFFKV PETKGRTFED IARAFEGQAH SGKGPAGVEL
     NSMQPVKETP GNA
//