SC5A1_PIG
ID SC5A1_PIG Reviewed; 605 AA.
AC P26429;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Sodium/glucose cotransporter 1;
DE Short=Na(+)/glucose cotransporter 1;
DE AltName: Full=High affinity sodium-glucose cotransporter;
DE AltName: Full=Solute carrier family 5 member 1;
DE Flags: Fragment;
GN Name=SLC5A1; Synonyms=SGLT1;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2247068; DOI=10.1128/mcb.10.12.6491-6499.1990;
RA Ohta T., Isselbacher K.J., Rhoads D.B.;
RT "Regulation of glucose transporters in LLC-PK1 cells: effects of D-glucose
RT and monosaccharides.";
RL Mol. Cell. Biol. 10:6491-6499(1990).
CC -!- FUNCTION: Electrogenic Na(+)-coupled sugar simporter that actively
CC transports D-glucose or D-galactose at the plasma membrane, with a
CC Na(+) to sugar coupling ratio of 2:1. Transporter activity is driven by
CC a transmembrane Na(+) electrochemical gradient set by the Na(+)/K(+)
CC pump (By similarity). Has a primary role in the transport of dietary
CC monosaccharides from enterocytes to blood. Responsible for the
CC absorption of D-glucose or D-galactose across the apical brush-border
CC membrane of enterocytes, whereas basolateral exit is provided by GLUT2.
CC Additionally, functions as a D-glucose sensor in enteroendocrine cells,
CC triggering the secretion of the incretins GCG and GIP that control food
CC intake and energy homeostasis (By similarity). Together with SGLT2,
CC functions in reabsorption of D-glucose from glomerular filtrate,
CC playing a nonredundant role in the S3 segment of the proximal tubules
CC (By similarity). Transports D-glucose into endometrial epithelial
CC cells, controlling glycogen synthesis and nutritional support for the
CC embryo as well as the decidual transformation of endometrium prior to
CC conception (By similarity). Acts as a water channel enabling passive
CC water transport in response to the osmotic gradient created upon sugar
CC and Na(+) uptake. Has high water conductivity comparable to aquaporins
CC and therefore is expected to play an important role in transepithelial
CC water permeability, especially in the small intestine.
CC {ECO:0000250|UniProtKB:P13866, ECO:0000250|UniProtKB:Q8C3K6}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glucose(out) + 2 Na(+)(out) = D-glucose(in) + 2 Na(+)(in);
CC Xref=Rhea:RHEA:70495, ChEBI:CHEBI:4167, ChEBI:CHEBI:29101;
CC Evidence={ECO:0000250|UniProtKB:P13866};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70496;
CC Evidence={ECO:0000250|UniProtKB:P13866};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-galactose(out) + 2 Na(+)(out) = D-galactose(in) + 2
CC Na(+)(in); Xref=Rhea:RHEA:70499, ChEBI:CHEBI:4139, ChEBI:CHEBI:29101;
CC Evidence={ECO:0000250|UniProtKB:P13866};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70500;
CC Evidence={ECO:0000250|UniProtKB:P13866};
CC -!- SUBCELLULAR LOCATION: Apical cell membrane
CC {ECO:0000250|UniProtKB:Q8C3K6}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- DOMAIN: The cholesterol-binding site is formed by transmembrane helices
CC TM1, TM7 and TM13. {ECO:0000250|UniProtKB:P13866}.
CC -!- PTM: N-glycosylation is not necessary for the cotransporter function.
CC {ECO:0000250|UniProtKB:P13866}.
CC -!- SIMILARITY: Belongs to the sodium:solute symporter (SSF) (TC 2.A.21)
CC family. {ECO:0000305}.
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DR EMBL; M34044; AAA31122.1; -; mRNA.
DR PIR; A36361; A36361.
DR AlphaFoldDB; P26429; -.
DR SMR; P26429; -.
DR STRING; 9823.ENSSSCP00000010706; -.
DR PaxDb; P26429; -.
DR PeptideAtlas; P26429; -.
DR PRIDE; P26429; -.
DR eggNOG; KOG2349; Eukaryota.
DR InParanoid; P26429; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0015371; F:galactose:sodium symporter activity; ISS:UniProtKB.
DR GO; GO:0005412; F:glucose:sodium symporter activity; ISS:UniProtKB.
DR GO; GO:0005372; F:water transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0001951; P:intestinal D-glucose absorption; ISS:UniProtKB.
DR GO; GO:0035623; P:renal glucose absorption; ISS:UniProtKB.
DR GO; GO:0006814; P:sodium ion transport; IBA:GO_Central.
DR Gene3D; 1.20.1730.10; -; 1.
DR InterPro; IPR038377; Na/Glc_symporter_sf.
DR InterPro; IPR001734; Na/solute_symporter.
DR InterPro; IPR018212; Na/solute_symporter_CS.
DR Pfam; PF00474; SSF; 1.
DR TIGRFAMs; TIGR00813; sss; 1.
DR PROSITE; PS00456; NA_SOLUT_SYMP_1; 1.
DR PROSITE; PS00457; NA_SOLUT_SYMP_2; 1.
DR PROSITE; PS50283; NA_SOLUT_SYMP_3; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Disulfide bond; Glycoprotein; Ion transport; Membrane;
KW Phosphoprotein; Reference proteome; Sodium; Sodium transport;
KW Sugar transport; Symport; Transmembrane; Transmembrane helix; Transport.
FT CHAIN <1..605
FT /note="Sodium/glucose cotransporter 1"
FT /id="PRO_0000105368"
FT TOPO_DOM <1..7
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 8..28
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 29..48
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 49..69
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 70..85
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 86..106
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 107..121
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 122..144
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 145..151
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 152..172
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 173..220
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 221..241
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 242..256
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 257..277
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 278..323
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 324..344
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 345..366
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 367..387
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 388..398
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 399..419
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 420..427
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 428..448
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 449..469
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT INTRAMEM 470..506
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 507..584
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 585..605
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 400
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000250"
FT SITE 243
FT /note="Implicated in sodium coupling"
FT /evidence="ECO:0000250"
FT SITE 460
FT /note="Involved in sugar-binding/transport and inhibitor
FT binding"
FT /evidence="ECO:0000250"
FT MOD_RES 530
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8C3K6"
FT CARBOHYD 191
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 198..551
FT /evidence="ECO:0000250"
FT DISULFID 198..454
FT /evidence="ECO:0000250|UniProtKB:P13866"
FT DISULFID 288..294
FT /evidence="ECO:0000250|UniProtKB:P13866"
FT DISULFID 298..304
FT /evidence="ECO:0000250|UniProtKB:P13866"
FT DISULFID 460..465
FT /evidence="ECO:0000250|UniProtKB:P13866"
FT NON_TER 1
SQ SEQUENCE 605 AA; 66917 MW; 132B6D08E8199F02 CRC64;
FFLAGRSMVW WPVGASLFAS YIGSGHFVGL AGTGAAAGIA TGGFEWNALI WVVVLGWLFV
PIYIKAGVVT MPEYLRKRFG GKRIQVYLSI LSLMLYIFTK ISADIFSGAI FITLALGLDL
YLAIFLLLAI TGLYTITGGL AAVIYTDTLQ TAIMLVGSFI LTGFAFHEVG GYDAFIEKYM
NAIPTVISDG NITIKKECYA PRADSFHIFR DPLKGDLPWP GLTFGLSILA LWYWCTDQVI
VQRCLSAKNM SHVKAGCVMC GYFKLLPMFV IVMPGMISRV LYTEKIACTV PSECEKYCGT
KVGCSNIAYP TLVVELMPNG LRGLMLSVIL ASLMSSLTSI FNSATTLFTM DVYAKIRKRA
SEKELMIAGR LFILVLIGIS IAWVPIVQSA QSGQLFDYIQ SVTSYLGPPI AAVFLLAIFC
KRVNEEGAFW GLVIGCMIGL ARMITEFAYG TGSCVEPSNC PTIICGVHYL YFAIILFVIS
IIIVLVVSLF TKPIPDVHLY RLCWSLRNSK EERIDLDAEE EDIQEAPEET IEIEVPEEKK
GCFRRTYDLF CGLDQQKGPK MTKEEEAAMK LKMTDTSEKP LWRTVVNING IILLTVAVFC
HAYFA
