SC5A2_RAT
ID SC5A2_RAT Reviewed; 670 AA.
AC P53792;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Sodium/glucose cotransporter 2;
DE Short=Na(+)/glucose cotransporter 2;
DE AltName: Full=Low affinity sodium-glucose cotransporter;
DE AltName: Full=Solute carrier family 5 member 2;
GN Name=Slc5a2; Synonyms=Sglt2 {ECO:0000303|PubMed:7493971};
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], FUNCTION, TRANSPORTER ACTIVITY, TISSUE
RP SPECIFICITY, DEVELOPMENTAL STAGE, AND GLYCOSYLATION AT ASN-248.
RC STRAIN=Sprague-Dawley; TISSUE=Kidney;
RX PubMed=7493971; DOI=10.1074/jbc.270.49.29365;
RA You G., Lee W.-S., Barros E.J.G., Kanai Y., Huo T.-L., Khawaja S.,
RA Wells R.G., Nigam S.K., Hediger M.A.;
RT "Molecular characteristics of Na(+)-coupled glucose transporters in adult
RT and embryonic rat kidney.";
RL J. Biol. Chem. 270:29365-29371(1995).
CC -!- FUNCTION: Electrogenic Na(+)-coupled sugar simporter that actively
CC transports D-glucose at the plasma membrane, with a Na(+) to sugar
CC coupling ratio of 1:1. Transporter activity is driven by a
CC transmembrane Na(+) electrochemical gradient set by the Na(+)/K(+) pump
CC (PubMed:7493971). Has a primary role in D-glucose reabsorption from
CC glomerular filtrate across the brush border of the early proximal
CC tubules of the kidney (By similarity). {ECO:0000250|UniProtKB:Q923I7,
CC ECO:0000269|PubMed:7493971}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glucose(out) + Na(+)(out) = D-glucose(in) + Na(+)(in);
CC Xref=Rhea:RHEA:70571, ChEBI:CHEBI:4167, ChEBI:CHEBI:29101;
CC Evidence={ECO:0000269|PubMed:7493971};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70572;
CC Evidence={ECO:0000305|PubMed:7493971};
CC -!- SUBUNIT: Forms a heterodimer with PDZK1IP1; this interaction enhances
CC the transporter activity over a hundred-fold.
CC {ECO:0000250|UniProtKB:P31639}.
CC -!- SUBCELLULAR LOCATION: Apical cell membrane
CC {ECO:0000250|UniProtKB:Q923I7}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Kidney, in proximal tubule S1 segments.
CC {ECO:0000269|PubMed:7493971}.
CC -!- DEVELOPMENTAL STAGE: Appears on embryonic day 17 and gradually
CC increases until day 19. Decreases between day 19 and birth.
CC {ECO:0000269|PubMed:7493971}.
CC -!- PTM: Glycosylated at a single site. {ECO:0000305|PubMed:7493971}.
CC -!- SIMILARITY: Belongs to the sodium:solute symporter (SSF) (TC 2.A.21)
CC family. {ECO:0000305}.
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DR EMBL; U29881; AAC52325.1; -; mRNA.
DR RefSeq; NP_072112.2; NM_022590.2.
DR AlphaFoldDB; P53792; -.
DR SMR; P53792; -.
DR STRING; 10116.ENSRNOP00000027265; -.
DR BindingDB; P53792; -.
DR ChEMBL; CHEMBL4316; -.
DR DrugCentral; P53792; -.
DR GuidetoPHARMACOLOGY; 916; -.
DR GlyGen; P53792; 1 site.
DR PaxDb; P53792; -.
DR GeneID; 64522; -.
DR KEGG; rno:64522; -.
DR UCSC; RGD:620217; rat.
DR CTD; 6524; -.
DR RGD; 620217; Slc5a2.
DR eggNOG; KOG2349; Eukaryota.
DR InParanoid; P53792; -.
DR OrthoDB; 243316at2759; -.
DR PhylomeDB; P53792; -.
DR Reactome; R-RNO-189200; Cellular hexose transport.
DR PRO; PR:P53792; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
DR GO; GO:0031526; C:brush border membrane; IDA:RGD.
DR GO; GO:0016021; C:integral component of membrane; IDA: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:0005412; F:glucose:sodium symporter activity; IDA:RGD.
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; IDA:RGD.
DR GO; GO:0035811; P:negative regulation of urine volume; IMP:RGD.
DR GO; GO:0035623; P:renal glucose absorption; ISS:UniProtKB.
DR GO; GO:0036359; P:renal potassium excretion; IMP: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 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 1: Evidence at protein level;
KW Cell membrane; Glycoprotein; Ion transport; Membrane; Reference proteome;
KW Sodium; Sodium transport; Sugar transport; Symport; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..670
FT /note="Sodium/glucose cotransporter 2"
FT /id="PRO_0000105375"
FT TOPO_DOM 1..23
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 24..42
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 43..59
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 60..80
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 81..100
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 101..121
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 122..166
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 167..187
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 188..203
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 204..224
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 225..268
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 269..289
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 290..312
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 313..332
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 333..421
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 422..441
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 442..453
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 454..474
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 475..524
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 525..545
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 546..648
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 649..669
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CARBOHYD 248
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305|PubMed:7493971"
SQ SEQUENCE 670 AA; 72962 MW; 0609562861618BB3 CRC64;
MEGHVEEGSE LGEQKVLIDN PADILVIAAY FLLVIGVGLW SMFRTNRGTV GGYFLAGRSM
VWWPVGASLF ASNIGSGHFV GLAGTGAASG LAVAGFEWNA LFVVLLLGWL FVPVYLTAGV
ITMPQYLRKR FGGRRIRLYL SVLSLFLYIF TKISVDMFSG AVFIQQALGW NIYASVIALL
GITMIYTVTG GLAALMYTDT VQTFVILAGA FILTGYAFHE VGGYSGLFDK YLGAVTSLTV
SKDPAVGNIS STCYQPRPDS YHLLRDPVTG GLPWPALLLG LTIVSGWHWC SDQVIVQRCL
AGKNLTHIKA GCILCGYLKL MPMFLMVMPG MISRILYPDE VACVVPEVCK RVCGTEVGCS
NIAYPRLVVK LMPNGLRGLM LAVMLAALMS SLASIFNSSS TLFTMDIYTR LRPRAGDREL
LLVGRLWVVF IVAVSVAWLP VVQAAQGGQL FDYIQSVSSY LAPPVSAVFV LALFVPRVNE
KGAFWGLIGG LLMGLARLIP EFFFGTGSCV RPSACPAIFC RVHYLYFAII LFFCSGFLTL
AISRCTAPIP QKHLHRLVFS LRHSKEERED LDAEELEGPA PPPVQNGCQE CAMGIEEVQS
PAPGLLRQCL LWFCGMSKSG SGSPPPTTEE VAATTRRLED ISEDPSWARV VNLNALLMMT
VAVFLWGFYA
