SC5A1_RAT
ID SC5A1_RAT Reviewed; 665 AA.
AC P53790; P97787;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 148.
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;
GN Name=Slc5a1; Synonyms=Sglt1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Kidney;
RX PubMed=8163506; DOI=10.1016/s0021-9258(17)32677-7;
RA Lee W.S., Kanai Y., Wells R.G., Hediger M.A.;
RT "The high affinity Na+/glucose cotransporter. Re-evaluation of function and
RT distribution of expression.";
RL J. Biol. Chem. 269:12032-12039(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Kasahara M., Mori K.;
RL Submitted (MAY-1993) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Jejunum;
RX PubMed=9214758; DOI=10.1271/bbb.61.979;
RA Aoshima H., Yokoyama T., Tanizaki J., Izu H., Yamada M.;
RT "The sugar specificity of Na+/glucose cotransporter from rat jejunum.";
RL Biosci. Biotechnol. Biochem. 61:979-983(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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 -!- DEVELOPMENTAL STAGE: Appears on embryonic day 18 and gradually
CC increases until birth.
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; U03120; AAA19015.1; -; mRNA.
DR EMBL; D16101; BAA03676.1; -; mRNA.
DR EMBL; AB000729; BAA19172.1; -; mRNA.
DR EMBL; BC081827; AAH81827.1; -; mRNA.
DR PIR; A53582; A53582.
DR RefSeq; NP_037165.1; NM_013033.2.
DR AlphaFoldDB; P53790; -.
DR SMR; P53790; -.
DR STRING; 10116.ENSRNOP00000024165; -.
DR BindingDB; P53790; -.
DR ChEMBL; CHEMBL5374; -.
DR DrugCentral; P53790; -.
DR GuidetoPHARMACOLOGY; 915; -.
DR GlyGen; P53790; 1 site.
DR iPTMnet; P53790; -.
DR PhosphoSitePlus; P53790; -.
DR PaxDb; P53790; -.
DR PRIDE; P53790; -.
DR Ensembl; ENSRNOT00000024165; ENSRNOP00000024165; ENSRNOG00000017775.
DR GeneID; 25552; -.
DR KEGG; rno:25552; -.
DR UCSC; RGD:3713; rat.
DR CTD; 6523; -.
DR RGD; 3713; Slc5a1.
DR eggNOG; KOG2349; Eukaryota.
DR GeneTree; ENSGT00940000155844; -.
DR HOGENOM; CLU_018808_9_2_1; -.
DR InParanoid; P53790; -.
DR OMA; TIQATWF; -.
DR OrthoDB; 243316at2759; -.
DR PhylomeDB; P53790; -.
DR Reactome; R-RNO-189200; Cellular hexose transport.
DR Reactome; R-RNO-8981373; Intestinal hexose absorption.
DR PRO; PR:P53790; -.
DR Proteomes; UP000002494; Chromosome 14.
DR Bgee; ENSRNOG00000017775; Expressed in jejunum and 14 other tissues.
DR Genevisible; P53790; RN.
DR GO; GO:0016324; C:apical plasma membrane; IDA:ARUK-UCL.
DR GO; GO:0016323; C:basolateral plasma membrane; TAS:ARUK-UCL.
DR GO; GO:0005903; C:brush border; ISO:RGD.
DR GO; GO:0031526; C:brush border membrane; IDA:ARUK-UCL.
DR GO; GO:0005911; C:cell-cell junction; IDA:RGD.
DR GO; GO:0005769; C:early endosome; ISO:RGD.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0043229; C:intracellular organelle; IDA:ARUK-UCL.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0015151; F:alpha-glucoside transmembrane transporter activity; ISO:RGD.
DR GO; GO:0055056; F:D-glucose transmembrane transporter activity; ISO:RGD.
DR GO; GO:0015371; F:galactose:sodium symporter activity; ISS:UniProtKB.
DR GO; GO:0005355; F:glucose transmembrane transporter activity; ISO:RGD.
DR GO; GO:0005412; F:glucose:sodium symporter activity; IDA:RGD.
DR GO; GO:0005372; F:water transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0000017; P:alpha-glucoside transport; ISO:RGD.
DR GO; GO:0098708; P:glucose import across plasma membrane; ISO:RGD.
DR GO; GO:1904659; P:glucose transmembrane transport; ISO:RGD.
DR GO; GO:0050892; P:intestinal absorption; ISO:RGD.
DR GO; GO:0001951; P:intestinal D-glucose absorption; ISS:UniProtKB.
DR GO; GO:0001656; P:metanephros development; ISO:RGD.
DR GO; GO:0032409; P:regulation of transporter activity; ISO:RGD.
DR GO; GO:0035623; P:renal glucose absorption; ISS:UniProtKB.
DR GO; GO:0010035; P:response to inorganic substance; ISO:RGD.
DR GO; GO:0098719; P:sodium ion import across plasma membrane; ISO:RGD.
DR GO; GO:0006814; P:sodium ion transport; IBA:GO_Central.
DR GO; GO:0035377; P:transepithelial water transport; ISO:RGD.
DR GO; GO:0150104; P:transport across blood-brain barrier; ISO:RGD.
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..665
FT /note="Sodium/glucose cotransporter 1"
FT /id="PRO_0000105370"
FT TOPO_DOM 1..28
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 29..49
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 50..64
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 65..85
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 86..105
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 106..126
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 127..142
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 143..163
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 164..178
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 179..201
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 202..208
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 209..229
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 230..277
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 278..298
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 299..313
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 314..334
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 335..380
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 381..401
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 402..423
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 424..444
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 445..455
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 456..476
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 477..484
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 485..505
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 506..526
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT INTRAMEM 527..563
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 564..644
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 645..665
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 457
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000250"
FT SITE 43
FT /note="Implicated in sodium coupling"
FT /evidence="ECO:0000250"
FT SITE 300
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 588
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8C3K6"
FT CARBOHYD 248
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 255..611
FT /evidence="ECO:0000250"
FT DISULFID 255..511
FT /evidence="ECO:0000250|UniProtKB:P13866"
FT DISULFID 345..351
FT /evidence="ECO:0000250|UniProtKB:P13866"
FT DISULFID 355..361
FT /evidence="ECO:0000250|UniProtKB:P13866"
FT DISULFID 517..522
FT /evidence="ECO:0000250|UniProtKB:P13866"
FT CONFLICT 354
FT /note="Y -> H (in Ref. 3; BAA19172)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 665 AA; 73066 MW; A92038D964BFF061 CRC64;
MDSSTLSPAV TATDAPIQSY ERIRNAADIS VIVIYFVVVM AVGLWAMFST NRGTVGGFFL
AGRSMVWWPI GASLFASNIG SGHFVGLAGT GAAAGIAMGG FEWNALVFVV VLGWLFVPIY
IKAGVVTMPE YLRKRFGGKR IQIYLSVLSL LLYIFTKISA DIFSGAIFIN LALGLDIYLA
IFILLAITAL YTITGGLAAV IYTDTLQTAI MLVGSFILTG FAFREVGGYE AFMDKYMKAI
PTLVSDGNIT VKEECYTPRA DSFHIFRDPI TGDMPWPGLI FGLSILALWY WCTDQVIVQR
CLSAKNMSHV KAGCTLCGYL KLLPMFLMVM PGMISRILYT DKIACVLPSE CKKYCGTPVG
CTNIAYPTLV VELMPNGLRG LMLSVMMASL MSSLTSIFNS ASTLFTMDIY TKIRKGASEK
ELMIAGRLFI LVLIGISIAW VPIVQSAQSG QLFDYIQSIT SYLGPPIAAV FLLAIFCKRV
NEPGAFWGLI LGFLIGISRM ITEFAYGTGS CMEPSNCPKI ICGVHYLYFA IILFAISVVT
VLVISLLTKP IPDVHLYRLC WSLRNSTEER IDLDAGEEEP VEEDPKDTIE IDAEAPQKEK
GCFRKAYDLF CGLDQDKGPK MTKEEEEAMK LKMTDTSEKP LWRTVVNING IILLAVAVFC
HAYFA
