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Solute carrier family 2, facilitated glucose transporter member 1 (Glucose transporter type 1, erythrocyte/brain) (GLUT-1)

 GTR1_RAT                Reviewed;         492 AA.
P11167;
01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
01-JUL-1989, sequence version 1.
22-NOV-2017, entry version 155.
RecName: Full=Solute carrier family 2, facilitated glucose transporter member 1;
AltName: Full=Glucose transporter type 1, erythrocyte/brain;
Short=GLUT-1;
Name=Slc2a1; Synonyms=Glut-1, Glut1;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
TISSUE=Brain;
PubMed=3016720; DOI=10.1073/pnas.83.16.5784;
Birnbaum M.J., Haspel H.C., Rosen O.M.;
"Cloning and characterization of a cDNA encoding the rat brain
glucose-transporter protein.";
Proc. Natl. Acad. Sci. U.S.A. 83:5784-5788(1986).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
TISSUE=Brain;
PubMed=3198639;
Williams S.A., Birnbaum M.J.;
"The rat facilitated glucose transporter gene. Transformation and
serum-stimulated transcription initiate from identical sites.";
J. Biol. Chem. 263:19513-19518(1988).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Prostate;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
INTERACTION WITH GIPC, AND TISSUE SPECIFICITY.
STRAIN=Fischer 344; TISSUE=Brain;
PubMed=10198040; DOI=10.1091/mbc.10.4.819;
Bunn R.C., Jensen M.A., Reed B.C.;
"Protein interactions with the glucose transporter binding protein
GLUT1CBP that provide a link between GLUT1 and the cytoskeleton.";
Mol. Biol. Cell 10:819-832(1999).
[5]
INTERACTION WITH SGTA.
PubMed=15708368; DOI=10.1016/j.abb.2004.12.020;
Liou S.T., Wang C.;
"Small glutamine-rich tetratricopeptide repeat-containing protein is
composed of three structural units with distinct functions.";
Arch. Biochem. Biophys. 435:253-263(2005).
[6]
TISSUE SPECIFICITY.
PubMed=21076856; DOI=10.1007/s11010-010-0634-z;
Zoidis E., Ghirlanda-Keller C., Schmid C.;
"Stimulation of glucose transport in osteoblastic cells by parathyroid
hormone and insulin-like growth factor I.";
Mol. Cell. Biochem. 348:33-42(2011).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-478, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- FUNCTION: Facilitative glucose transporter. This isoform may be
responsible for constitutive or basal glucose uptake. Has a very
broad substrate specificity; can transport a wide range of aldoses
including both pentoses and hexoses (By similarity).
{ECO:0000250}.
-!- SUBUNIT: Found in a complex with ADD2, DMTN and SLC2A1. Interacts
(via C-terminus cytoplasmic region) with DMTN. Interacts with
SNX27; the interaction is required when endocytosed to prevent
degradation in lysosomes and promote recycling to the plasma
membrane. Interacts with STOM (By similarity). Interacts with GIPC
(via PDZ domain) (PubMed:10198040). Interacts with SGTA (via Gln-
rich region) (PubMed:15708368). {ECO:0000250|UniProtKB:P11166,
ECO:0000269|PubMed:10198040, ECO:0000269|PubMed:15708368}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass
membrane protein {ECO:0000250}. Melanosome {ECO:0000250}.
Note=Localizes primarily at the cell surface. {ECO:0000250}.
-!- TISSUE SPECIFICITY: Detected in osteoblastic cells (at protein
level). Detected in brain, and at lower levels in kidney, heart
and lung. {ECO:0000269|PubMed:10198040,
ECO:0000269|PubMed:21076856, ECO:0000269|PubMed:3016720,
ECO:0000269|PubMed:3198639}.
-!- SIMILARITY: Belongs to the major facilitator superfamily. Sugar
transporter (TC 2.A.1.1) family. Glucose transporter subfamily.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; M13979; AAA41248.1; -; mRNA.
EMBL; M22063; AAA41297.1; -; Genomic_DNA.
EMBL; M22061; AAA41297.1; JOINED; Genomic_DNA.
EMBL; M22062; AAA41297.1; JOINED; Genomic_DNA.
EMBL; BC061873; AAH61873.1; -; mRNA.
PIR; A25949; A25949.
RefSeq; NP_620182.1; NM_138827.1.
UniGene; Rn.3205; -.
ProteinModelPortal; P11167; -.
BioGrid; 246902; 1.
STRING; 10116.ENSRNOP00000061340; -.
BindingDB; P11167; -.
ChEMBL; CHEMBL5214; -.
iPTMnet; P11167; -.
PhosphoSitePlus; P11167; -.
SwissPalm; P11167; -.
PaxDb; P11167; -.
PRIDE; P11167; -.
Ensembl; ENSRNOT00000064452; ENSRNOP00000061340; ENSRNOG00000007284.
GeneID; 24778; -.
KEGG; rno:24778; -.
CTD; 6513; -.
RGD; 3704; Slc2a1.
eggNOG; KOG0569; Eukaryota.
eggNOG; COG0477; LUCA.
GeneTree; ENSGT00760000119022; -.
HOGENOM; HOG000202871; -.
HOVERGEN; HBG014816; -.
InParanoid; P11167; -.
KO; K07299; -.
OMA; LQCIVLP; -.
OrthoDB; EOG091G0A9K; -.
PhylomeDB; P11167; -.
TreeFam; TF313762; -.
Reactome; R-RNO-189200; Cellular hexose transport.
Reactome; R-RNO-196836; Vitamin C (ascorbate) metabolism.
Reactome; R-RNO-422356; Regulation of insulin secretion.
Reactome; R-RNO-5653890; Lactose synthesis.
SABIO-RK; P11167; -.
PRO; PR:P11167; -.
Proteomes; UP000002494; Chromosome 5.
Bgee; ENSRNOG00000007284; -.
ExpressionAtlas; P11167; baseline and differential.
Genevisible; P11167; RN.
GO; GO:0016324; C:apical plasma membrane; ISO:RGD.
GO; GO:0016323; C:basolateral plasma membrane; ISO:RGD.
GO; GO:0072562; C:blood microparticle; ISO:RGD.
GO; GO:0005901; C:caveola; IDA:RGD.
GO; GO:0005911; C:cell-cell junction; IDA:RGD.
GO; GO:0030864; C:cortical actin cytoskeleton; ISS:UniProtKB.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; ISO:RGD.
GO; GO:0070062; C:extracellular exosome; ISO:RGD.
GO; GO:0001939; C:female pronucleus; ISO:RGD.
GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
GO; GO:0014704; C:intercalated disc; IDA:RGD.
GO; GO:0005622; C:intracellular; ISO:RGD.
GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
GO; GO:0016020; C:membrane; ISO:RGD.
GO; GO:0045121; C:membrane raft; ISO:RGD.
GO; GO:0030496; C:midbody; ISO:RGD.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0042383; C:sarcolemma; IDA:RGD.
GO; GO:0031982; C:vesicle; ISO:RGD.
GO; GO:0030018; C:Z disc; IDA:RGD.
GO; GO:0055056; F:D-glucose transmembrane transporter activity; IDA:UniProtKB.
GO; GO:0033300; F:dehydroascorbic acid transporter activity; IDA:UniProtKB.
GO; GO:0005355; F:glucose transmembrane transporter activity; IDA:RGD.
GO; GO:0042802; F:identical protein binding; ISO:RGD.
GO; GO:0019900; F:kinase binding; IPI:RGD.
GO; GO:0043621; F:protein self-association; ISS:UniProtKB.
GO; GO:0042910; F:xenobiotic transporter activity; IDA:RGD.
GO; GO:0071474; P:cellular hyperosmotic response; IEP:RGD.
GO; GO:0042149; P:cellular response to glucose starvation; ISO:RGD.
GO; GO:0071260; P:cellular response to mechanical stimulus; IEP:RGD.
GO; GO:0021987; P:cerebral cortex development; IEP:RGD.
GO; GO:0070837; P:dehydroascorbic acid transport; IDA:UniProtKB.
GO; GO:0007565; P:female pregnancy; IEP:RGD.
GO; GO:1904659; P:glucose transmembrane transport; ISO:RGD.
GO; GO:0015758; P:glucose transport; IDA:UniProtKB.
GO; GO:0006461; P:protein complex assembly; ISS:UniProtKB.
GO; GO:0032868; P:response to insulin; IEP:RGD.
GO; GO:0006970; P:response to osmotic stress; IEP:RGD.
GO; GO:1904016; P:response to Thyroglobulin triiodothyronine; IEP:RGD.
GO; GO:0042908; P:xenobiotic transport; IDA:RGD.
CDD; cd06174; MFS; 1.
InterPro; IPR002439; Glu_transpt_1.
InterPro; IPR020846; MFS_dom.
InterPro; IPR005828; MFS_sugar_transport-like.
InterPro; IPR036259; MFS_trans_sf.
InterPro; IPR003663; Sugar/inositol_transpt.
InterPro; IPR005829; Sugar_transporter_CS.
Pfam; PF00083; Sugar_tr; 1.
PRINTS; PR01190; GLUCTRSPORT1.
PRINTS; PR00171; SUGRTRNSPORT.
SUPFAM; SSF103473; SSF103473; 2.
TIGRFAMs; TIGR00879; SP; 1.
PROSITE; PS50850; MFS; 1.
PROSITE; PS00216; SUGAR_TRANSPORT_1; 1.
PROSITE; PS00217; SUGAR_TRANSPORT_2; 1.
1: Evidence at protein level;
Acetylation; Cell membrane; Complete proteome; Glycoprotein; Membrane;
Phosphoprotein; Reference proteome; Sugar transport; Transmembrane;
Transmembrane helix; Transport.
CHAIN 1 492 Solute carrier family 2, facilitated
glucose transporter member 1.
/FTId=PRO_0000050342.
TOPO_DOM 1 11 Cytoplasmic. {ECO:0000250}.
TRANSMEM 12 33 Helical; Name=1. {ECO:0000250}.
TOPO_DOM 34 66 Extracellular. {ECO:0000250}.
TRANSMEM 67 87 Helical; Name=2. {ECO:0000250}.
TOPO_DOM 88 90 Cytoplasmic. {ECO:0000250}.
TRANSMEM 91 112 Helical; Name=3. {ECO:0000250}.
TOPO_DOM 113 120 Extracellular. {ECO:0000250}.
TRANSMEM 121 144 Helical; Name=4. {ECO:0000250}.
TOPO_DOM 145 155 Cytoplasmic. {ECO:0000250}.
TRANSMEM 156 176 Helical; Name=5. {ECO:0000250}.
TOPO_DOM 177 185 Extracellular. {ECO:0000250}.
TRANSMEM 186 206 Helical; Name=6. {ECO:0000250}.
TOPO_DOM 207 271 Cytoplasmic. {ECO:0000250}.
TRANSMEM 272 293 Helical; Name=7. {ECO:0000250}.
TOPO_DOM 294 306 Extracellular. {ECO:0000250}.
TRANSMEM 307 328 Helical; Name=8. {ECO:0000250}.
TOPO_DOM 329 334 Cytoplasmic. {ECO:0000250}.
TRANSMEM 335 355 Helical; Name=9. {ECO:0000250}.
TOPO_DOM 356 365 Extracellular. {ECO:0000250}.
TRANSMEM 366 388 Helical; Name=10. {ECO:0000250}.
TOPO_DOM 389 401 Cytoplasmic. {ECO:0000250}.
TRANSMEM 402 422 Helical; Name=11. {ECO:0000250}.
TOPO_DOM 423 429 Extracellular. {ECO:0000250}.
TRANSMEM 430 450 Helical; Name=12. {ECO:0000250}.
TOPO_DOM 451 492 Cytoplasmic. {ECO:0000250}.
REGION 282 288 Monosaccharide binding. {ECO:0000250}.
BINDING 317 317 Monosaccharide. {ECO:0000250}.
BINDING 388 388 Monosaccharide. {ECO:0000250}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000250|UniProtKB:P11166}.
MOD_RES 465 465 Phosphoserine.
{ECO:0000250|UniProtKB:P11166}.
MOD_RES 478 478 Phosphothreonine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 490 490 Phosphoserine.
{ECO:0000250|UniProtKB:P11166}.
CARBOHYD 45 45 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
SEQUENCE 492 AA; 53963 MW; 05719AB061D0F67C CRC64;
MEPSSKKVTG RLMLAVGGAV LGSLQFGYNT GVINAPQKVI EEFYNQTWNH RYGESIPSTT
LTTLWSLSVA IFSVGGMIGS FSVGLFVNRF GRRNSMLMMN LLAFVSAVLM GFSKLGKSFE
MLILGRFIIG VYCGLTTGFV PMYVGEVSPT ALRGALGTLH QLGIVVGILI AQVFGLDSIM
GNADLWPLLL SVIFIPALLQ CILLPFCPES PRFLLINRNE ENRAKSVLKK LRGTADVTRD
LQEMKEEGRQ MMREKKVTIL ELFRSPAYRQ PILIAVVLQL SQQLSGINAV FYYSTSIFEK
AGVQQPVYAT IGSGIVNTAF TVVSLFVVER AGRRTLHLIG LAGMAGCAVL MTIALALLEQ
LPWMSYLSIV AIFGFVAFFE VGPGPIPWFI VAELFSQGPR PAAVAVAGFS NWTSNFIVGM
CFQYVEQLCG PYVFIIFTVL LVLFFIFTYF KVPETKGRTF DEIASGFRQG GASQSDKTPE
ELFHPLGADS QV


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