SC5A1_SHEEP
ID SC5A1_SHEEP Reviewed; 664 AA.
AC P53791;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, 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;
GN Name=SLC5A1; Synonyms=SGLT1;
OS Ovis aries (Sheep).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Ovis.
OX NCBI_TaxID=9940;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Jejunal mucosa;
RX PubMed=7492327; DOI=10.1042/bj3120293;
RA Tarpey P., Wood I.S., Shirazi-Beechey S.P., Beechey R.B.;
RT "Amino acid sequence and the cellular location of the Na(+)-dependent D-
RT glucose symporters (SGLT1) in the ovine enterocyte and the parotid acinar
RT cell.";
RL Biochem. J. 312:293-300(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Mammary gland;
RX PubMed=9388688; DOI=10.1042/bst025467s;
RA Shillingford J.M., Wood I.S., Shennan D.B., Shirazi-Beechey S.P.,
RA Beechey R.B.;
RT "Determination of the sequence of a mRNA from lactating sheep mammary gland
RT that encodes a protein identical to the Na(+)-dependent glucose transporter
RT (SGLT1).";
RL Biochem. Soc. Trans. 25:467-467(1997).
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; X82411; CAA57809.1; -; mRNA.
DR EMBL; X82410; CAA57808.1; -; mRNA.
DR EMBL; AJ001026; CAA04483.1; -; mRNA.
DR PIR; S59637; S59637.
DR PIR; S59638; S59638.
DR RefSeq; NP_001009404.1; NM_001009404.1.
DR AlphaFoldDB; P53791; -.
DR SMR; P53791; -.
DR STRING; 9940.ENSOARP00000012821; -.
DR Ensembl; ENSOART00000013008; ENSOARP00000012821; ENSOARG00000011955.
DR Ensembl; ENSOART00020039471; ENSOARP00020032704; ENSOARG00020025159.
DR GeneID; 492300; -.
DR KEGG; oas:492300; -.
DR CTD; 6523; -.
DR eggNOG; KOG2349; Eukaryota.
DR HOGENOM; CLU_018808_9_2_1; -.
DR OMA; AYMTMVT; -.
DR OrthoDB; 243316at2759; -.
DR Proteomes; UP000002356; Chromosome 17.
DR Bgee; ENSOARG00000011955; Expressed in jejunum and 29 other tissues.
DR GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
DR GO; GO:0005769; C:early endosome; IEA:Ensembl.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR GO; GO:0015151; F:alpha-glucoside transmembrane transporter activity; IEA:Ensembl.
DR GO; GO:0055056; F:D-glucose transmembrane transporter activity; IEA:Ensembl.
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:0098708; P:glucose import across plasma membrane; IEA:Ensembl.
DR GO; GO:0001951; P:intestinal D-glucose absorption; ISS:UniProtKB.
DR GO; GO:0035623; P:renal glucose absorption; ISS:UniProtKB.
DR GO; GO:0010035; P:response to inorganic substance; IEA:Ensembl.
DR GO; GO:0098719; P:sodium ion import across plasma membrane; IEA:Ensembl.
DR GO; GO:0035377; P:transepithelial water transport; IEA:Ensembl.
DR GO; GO:0150104; P:transport across blood-brain barrier; IEA:Ensembl.
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 Reference proteome; Sodium; Sodium transport; Sugar transport; Symport;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..664
FT /note="Sodium/glucose cotransporter 1"
FT /id="PRO_0000105371"
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..643
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 644..664
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 CARBOHYD 248
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 255..610
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"
SQ SEQUENCE 664 AA; 73179 MW; 820AC019B5C93987 CRC64;
MDSSTWSPPA TATAEPLQAY ERIRNAADIS VIVIYFVVVM AVGLWAMFST NRGTVGGFFL
AGRSMVWWPI GASLFASNIG SGHFVGLAGT GAAAGIATGG FEWNALILVV LLGWVFVPIY
IKAGVVTMPE YLRKRFGGQR IQVYLSVLSL VLYIFTKISA DIFSGAIFIN LALGLDLYLA
IFILLAITAL YTITGGLAAV IYTDTLQTVI MLLGSFILTG FAFHEVGGYS AFVTKYMNAI
PTVTSYGNTT VKKECYTPRA DSFHIFRDPL KGDLPWPGLI FGLTIISLWY WCTDQVIVQR
CLSAKNMSHV KAGCIMCGYM KLLPMFLMVM PGMISRILFT EKVACTVPSE CEKYCGTKVG
CTNIAYPTLV VELMPNGLRG LMLSVMLASL MSSLTSIFNS ASTLFTMDIY TKIRKKASEK
ELMIAGRLFM LVLIGVSIAW VPIVQSAQSG QLFDYIQSIT SYLGPPIAAV FLLAIFCKRV
NEPGAFWGLI IGFLIGVSRM ITEFAYGTGS CMEPSNCPTI ICGVHYLYFA IILFVITIIV
ILAISLFTKP IADVHLYRLC WSLRNSKEER IDLDAEDEDI QDAREDALEI DTEASEEKKG
CLRQAYDMFC GLDQQKGPKM TKEEEAAMKL KMTDTSEKRL WRMVVNINGI ILLAVAVFCH
AYFA
