GTR1_RABIT
ID GTR1_RABIT Reviewed; 492 AA.
AC P13355;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Solute carrier family 2, facilitated glucose transporter member 1 {ECO:0000305};
DE AltName: Full=Glucose transporter type 1, erythrocyte/brain {ECO:0000250|UniProtKB:P11166};
DE Short=GLUT-1 {ECO:0000250|UniProtKB:P11166};
GN Name=SLC2A1 {ECO:0000250|UniProtKB:P11166};
GN Synonyms=GLUT1 {ECO:0000250|UniProtKB:P11166};
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 [MRNA].
RC TISSUE=Brain;
RX PubMed=3408493; DOI=10.1016/0006-291x(88)90268-9;
RA Asano T., Shibasaki Y., Kasuga M., Kanazawa Y., Takaku F., Akanuma Y.,
RA Oka Y.;
RT "Cloning of a rabbit brain glucose transporter cDNA and alteration of
RT glucose transporter mRNA during tissue development.";
RL Biochem. Biophys. Res. Commun. 154:1204-1211(1988).
CC -!- FUNCTION: Facilitative glucose transporter, which is responsible for
CC constitutive or basal glucose uptake. Has a very broad substrate
CC specificity; can transport a wide range of aldoses including both
CC pentoses and hexoses. Most important energy carrier of the brain:
CC present at the blood-brain barrier and assures the energy-independent,
CC facilitative transport of glucose into the brain (By similarity). In
CC association with BSG and NXNL1, promotes retinal cone survival by
CC increasing glucose uptake into photoreceptors (By similarity).
CC {ECO:0000250|UniProtKB:P11166, ECO:0000250|UniProtKB:P46896}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glucose(out) = D-glucose(in); Xref=Rhea:RHEA:60376,
CC ChEBI:CHEBI:4167; Evidence={ECO:0000250|UniProtKB:P11166};
CC -!- ACTIVITY REGULATION: The uptake of glucose is inhibited by cytochalasin
CC B. Glucose uptake is increased in response to phorbol ester 12-O-
CC tetradecanoylphorbol-13-acetate (TPA) treatment: TPA-induced glucose
CC uptake requires phosphorylation at Ser-226.
CC {ECO:0000250|UniProtKB:P11166}.
CC -!- SUBUNIT: Found in a complex with ADD2, DMTN and SLC2A1. Interacts (via
CC C-terminus cytoplasmic region) with DMTN. Interacts with SNX27; the
CC interaction is required when endocytosed to prevent degradation in
CC lysosomes and promote recycling to the plasma membrane. Interacts with
CC GIPC (via PDZ domain). Interacts with STOM. Interacts with SGTA (via
CC Gln-rich region) (By similarity). Interacts with BSG (By similarity).
CC {ECO:0000250|UniProtKB:P11166, ECO:0000250|UniProtKB:P11167}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P11166};
CC Multi-pass membrane protein {ECO:0000255}. Photoreceptor inner segment
CC {ECO:0000250|UniProtKB:P17809}.
CC -!- PTM: Phosphorylation at Ser-226 by PKC promotes glucose uptake by
CC increasing cell membrane localization. {ECO:0000250|UniProtKB:P11166}.
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; M21747; AAA31444.1; -; mRNA.
DR PIR; A30797; A30797.
DR RefSeq; NP_001099157.1; NM_001105687.1.
DR AlphaFoldDB; P13355; -.
DR SMR; P13355; -.
DR STRING; 9986.ENSOCUP00000005131; -.
DR PRIDE; P13355; -.
DR GeneID; 100125988; -.
DR KEGG; ocu:100125988; -.
DR CTD; 6513; -.
DR eggNOG; KOG0569; Eukaryota.
DR InParanoid; P13355; -.
DR OrthoDB; 749998at2759; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0030864; C:cortical actin cytoskeleton; ISS:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0001917; C:photoreceptor inner segment; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0005355; F:glucose transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0043621; F:protein self-association; ISS:UniProtKB.
DR GO; GO:1904659; P:glucose transmembrane transport; ISS:UniProtKB.
DR GO; GO:0045494; P:photoreceptor cell maintenance; ISS:UniProtKB.
DR GO; GO:0065003; P:protein-containing complex assembly; ISS:UniProtKB.
DR Gene3D; 1.20.1250.20; -; 1.
DR InterPro; IPR002439; Glu_transpt_1.
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; PR01190; GLUCTRSPORT1.
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 Acetylation; Cell membrane; Glycoprotein; Membrane; Phosphoprotein;
KW Reference proteome; Sugar transport; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..492
FT /note="Solute carrier family 2, facilitated glucose
FT transporter member 1"
FT /id="PRO_0000050341"
FT TOPO_DOM 1..11
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P11166"
FT TRANSMEM 12..33
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250|UniProtKB:P11166"
FT TOPO_DOM 34..66
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P11166"
FT TRANSMEM 67..87
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250|UniProtKB:P11166"
FT TOPO_DOM 88..90
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P11166"
FT TRANSMEM 91..112
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250|UniProtKB:P11166"
FT TOPO_DOM 113..120
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P11166"
FT TRANSMEM 121..144
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250|UniProtKB:P11166"
FT TOPO_DOM 145..155
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P11166"
FT TRANSMEM 156..176
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250|UniProtKB:P11166"
FT TOPO_DOM 177..185
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P11166"
FT TRANSMEM 186..206
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250|UniProtKB:P11166"
FT TOPO_DOM 207..271
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P11166"
FT TRANSMEM 272..293
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250|UniProtKB:P11166"
FT TOPO_DOM 294..306
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P11166"
FT TRANSMEM 307..328
FT /note="Helical; Name=8"
FT /evidence="ECO:0000250|UniProtKB:P11166"
FT TOPO_DOM 329..334
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P11166"
FT TRANSMEM 335..355
FT /note="Helical; Name=9"
FT /evidence="ECO:0000250|UniProtKB:P11166"
FT TOPO_DOM 356..365
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P11166"
FT TRANSMEM 366..388
FT /note="Helical; Name=10"
FT /evidence="ECO:0000250|UniProtKB:P11166"
FT TOPO_DOM 389..401
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P11166"
FT TRANSMEM 402..422
FT /note="Helical; Name=11"
FT /evidence="ECO:0000250|UniProtKB:P11166"
FT TOPO_DOM 423..429
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P11166"
FT TRANSMEM 430..450
FT /note="Helical; Name=12"
FT /evidence="ECO:0000250|UniProtKB:P11166"
FT TOPO_DOM 451..492
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P11166"
FT REGION 468..492
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 161
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000250|UniProtKB:P11169"
FT BINDING 282..283
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000250|UniProtKB:P11169"
FT BINDING 288
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000250|UniProtKB:P11169"
FT BINDING 317
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000250|UniProtKB:P11169"
FT BINDING 380
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000250|UniProtKB:P11169"
FT BINDING 388
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000250|UniProtKB:P11169"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P11166"
FT MOD_RES 226
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11166"
FT MOD_RES 465
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11166"
FT MOD_RES 478
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P11166"
FT MOD_RES 490
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11166"
FT CARBOHYD 45
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 492 AA; 54098 MW; 575F8FC947F2B869 CRC64;
MEPSSKKVTG RLMLAVGGAV LGSLQFGYNT GVINAPQKVI EEFYNQTWIH RYGERILPTT
LTTLWSLSVA IFSVGGMIGS FSVGLFVNRF GRRNSMLMMN LLAFVSAVLM GFSKLAKSFE
MLILGRFIIG VYCGLTTGFV PMYVGEVSPT ALRGALGTLH QLGIVVGILI AQVFGLDSIM
GNEDLWPLLL SVIFVPALLQ CIVLPLCPES PRFLLINRNE ENRAKSVLKK LRGNADVTRD
LQEMKEESRQ MMREKKVTIL ELFRSPAYRQ PILSAVVLQL SQQLSGINAV FYYSTSIFEK
AGVQQPVYAT IGSGIVNTAF TVVSLFVVER AGRRTLHLIG LAGMAACAVL MTIALALLEQ
LPWMSYLSIV AIFGFVAFFE VGPGPIPWFI VAELFSQGPR PAAVAVAGFS NWTSNFIVGM
CFQYVEQLCG PYVFIIFTVL LVLFFIFTYF KVPETKGRTF DEIASGFRQG GASQSDKTPE
ELFHPLGADS QV
