GTR1_CHICK
ID GTR1_CHICK Reviewed; 490 AA.
AC P46896;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Solute carrier family 2, facilitated glucose transporter member 1 {ECO:0000305};
DE AltName: Full=Glucose transporter type 1 {ECO:0000303|PubMed:8589457};
DE Short=GLUT-1 {ECO:0000303|PubMed:8589457};
DE Short=GT1 {ECO:0000303|PubMed:8589457};
GN Name=SLC2A1 {ECO:0000250|UniProtKB:P11166};
GN Synonyms=GLUT1 {ECO:0000303|PubMed:8589457};
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8589457; DOI=10.1091/mbc.6.11.1575;
RA Wagstaff P., Kang H.Y., Mylott D., Robbins P.J., White M.K.;
RT "Characterization of the avian GLUT1 glucose transporter: differential
RT regulation of GLUT1 and GLUT3 in chicken embryo fibroblasts.";
RL Mol. Biol. Cell 6:1575-1589(1995).
RN [2]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH BSG, AND TISSUE
RP SPECIFICITY.
RX PubMed=25957687; DOI=10.1016/j.cell.2015.03.023;
RA Ait-Ali N., Fridlich R., Millet-Puel G., Clerin E., Delalande F.,
RA Jaillard C., Blond F., Perrocheau L., Reichman S., Byrne L.C.,
RA Olivier-Bandini A., Bellalou J., Moyse E., Bouillaud F., Nicol X.,
RA Dalkara D., van Dorsselaer A., Sahel J.A., Leveillard T.;
RT "Rod-derived cone viability factor promotes cone survival by stimulating
RT aerobic glycolysis.";
RL Cell 161:817-832(2015).
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 (PubMed:25957687).
CC {ECO:0000250|UniProtKB:P11166, ECO:0000269|PubMed:25957687}.
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 -!- SUBUNIT: Interacts with isoform 1 of BSG.
CC {ECO:0000269|PubMed:25957687}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:25957687};
CC Multi-pass membrane protein {ECO:0000255}. Photoreceptor inner segment
CC {ECO:0000250|UniProtKB:P17809}.
CC -!- TISSUE SPECIFICITY: Retinal cones (at protein level).
CC {ECO:0000269|PubMed:25957687}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. Sugar
CC transporter (TC 2.A.1.1) family. Glucose transporter subfamily.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; L07300; AAB02037.1; -; mRNA.
DR RefSeq; NP_990540.1; NM_205209.1.
DR AlphaFoldDB; P46896; -.
DR SMR; P46896; -.
DR STRING; 9031.ENSGALP00000007795; -.
DR PaxDb; P46896; -.
DR GeneID; 396130; -.
DR KEGG; gga:396130; -.
DR CTD; 6513; -.
DR VEuPathDB; HostDB:geneid_396130; -.
DR eggNOG; KOG0569; Eukaryota.
DR InParanoid; P46896; -.
DR OrthoDB; 749998at2759; -.
DR PhylomeDB; P46896; -.
DR Reactome; R-GGA-352832; Glucose transport.
DR PRO; PR:P46896; -.
DR Proteomes; UP000000539; 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; IDA: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; IMP:UniProtKB.
DR GO; GO:0065003; P:protein-containing complex assembly; ISS:UniProtKB.
DR GO; GO:0071548; P:response to dexamethasone; IDA:AgBase.
DR GO; GO:0032868; P:response to insulin; IDA:AgBase.
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 1: Evidence at protein level;
KW Cell membrane; Glycoprotein; Membrane; Reference proteome; Sugar transport;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..490
FT /note="Solute carrier family 2, facilitated glucose
FT transporter member 1"
FT /id="PRO_0000050344"
FT TOPO_DOM 1..10
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P11166"
FT TRANSMEM 11..32
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250|UniProtKB:P11166"
FT TOPO_DOM 33..65
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P11166"
FT TRANSMEM 66..86
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250|UniProtKB:P11166"
FT TOPO_DOM 87..89
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P11166"
FT TRANSMEM 90..111
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250|UniProtKB:P11166"
FT TOPO_DOM 112..119
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P11166"
FT TRANSMEM 120..143
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250|UniProtKB:P11166"
FT TOPO_DOM 144..154
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P11166"
FT TRANSMEM 155..175
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250|UniProtKB:P11166"
FT TOPO_DOM 176..184
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P11166"
FT TRANSMEM 185..205
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250|UniProtKB:P11166"
FT TOPO_DOM 206..270
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P11166"
FT TRANSMEM 271..292
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250|UniProtKB:P11166"
FT TOPO_DOM 293..305
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P11166"
FT TRANSMEM 306..327
FT /note="Helical; Name=8"
FT /evidence="ECO:0000250|UniProtKB:P11166"
FT TOPO_DOM 328..333
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P11166"
FT TRANSMEM 334..354
FT /note="Helical; Name=9"
FT /evidence="ECO:0000250|UniProtKB:P11166"
FT TOPO_DOM 355..364
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P11166"
FT TRANSMEM 365..387
FT /note="Helical; Name=10"
FT /evidence="ECO:0000250|UniProtKB:P11166"
FT TOPO_DOM 388..400
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P11166"
FT TRANSMEM 401..421
FT /note="Helical; Name=11"
FT /evidence="ECO:0000250|UniProtKB:P11166"
FT TOPO_DOM 422..428
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P11166"
FT TRANSMEM 429..449
FT /note="Helical; Name=12"
FT /evidence="ECO:0000250|UniProtKB:P11166"
FT TOPO_DOM 450..490
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P11166"
FT REGION 470..490
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 160
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000250|UniProtKB:P11169"
FT BINDING 281..282
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000250|UniProtKB:P11169"
FT BINDING 287
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000250|UniProtKB:P11169"
FT BINDING 316
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000250|UniProtKB:P11169"
FT BINDING 379
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000250|UniProtKB:P11169"
FT BINDING 387
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000250|UniProtKB:P11169"
FT CARBOHYD 44
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 490 AA; 54087 MW; 63BB176812D06104 CRC64;
MESGSKMTAR LMLAVGGAVL GSLQFGYNTG VINRPQKVIE DFYNHTWLYR YEEPISPATL
TTLWSLSVAI FSVGGMIGSF SVGLFVNRFG RRNSMLMSNI LAFLAAVLMG FSKMALSFEM
LILGRFIIGL YSGLTTGFVP MYVGEVSPTA LRGALGTFHQ LGIVLGILIA QVFGLDLIMG
NDSLWPLLLG FIFVPALLQC IILPFAPESP RFLLINRNEE NKAKSVLKKL RGTTDVSSDL
QEMKEESRQM MREKKVTIME LFRSPMYRQP ILIAIVLQLS QQLSGINAVF YYSTSIFEKS
GVEQPVYATI GSGVVNTAFT VVSLFVVERA GRRTLHLIGL AGMAGCAILM TIALTLLDQM
PWMSYLSIVA IFGFVAFFEI GPGPIPWFIV AELFSQGPRP AAFAVAGLSN WTSNFIVGMG
FQYIAQLCGS YVFIIFTVLL VLFFIFTYFK VPETKGRTFD EIAYRFRQGG ASQSDKTPDE
FHSLGADSQV
