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Sodium/glucose cotransporter 1 (Na( )/glucose cotransporter 1) (High affinity sodium-glucose cotransporter) (Solute carrier family 5 member 1)

 SC5A1_MOUSE             Reviewed;         665 AA.
Q8C3K6;
15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
01-MAR-2003, sequence version 1.
20-JUN-2018, entry version 113.
RecName: Full=Sodium/glucose cotransporter 1;
Short=Na(+)/glucose cotransporter 1;
AltName: Full=High affinity sodium-glucose cotransporter;
AltName: Full=Solute carrier family 5 member 1;
Name=Slc5a1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Kidney;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[2]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-585 AND THR-588, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Kidney;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: Actively transports glucose into cells by Na(+)
cotransport with a Na(+) to glucose coupling ratio of 2:1.
Efficient substrate transport in mammalian kidney is provided by
the concerted action of a low affinity high capacity and a high
affinity low capacity Na(+)/glucose cotransporter arranged in
series along kidney proximal tubules.
-!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
-!- PTM: N-glycosylation is not necessary for the cotransporter
function. {ECO:0000250}.
-!- SIMILARITY: Belongs to the sodium:solute symporter (SSF) (TC
2.A.21) family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AK085602; BAC39483.1; -; mRNA.
CCDS; CCDS19199.1; -.
RefSeq; NP_062784.3; NM_019810.4.
UniGene; Mm.25237; -.
ProteinModelPortal; Q8C3K6; -.
IntAct; Q8C3K6; 1.
STRING; 10090.ENSMUSP00000011178; -.
GuidetoPHARMACOLOGY; 915; -.
iPTMnet; Q8C3K6; -.
PhosphoSitePlus; Q8C3K6; -.
MaxQB; Q8C3K6; -.
PaxDb; Q8C3K6; -.
PeptideAtlas; Q8C3K6; -.
PRIDE; Q8C3K6; -.
GeneID; 20537; -.
KEGG; mmu:20537; -.
CTD; 6523; -.
MGI; MGI:107678; Slc5a1.
eggNOG; ENOG410IP49; Eukaryota.
eggNOG; COG4146; LUCA.
HOGENOM; HOG000025422; -.
HOVERGEN; HBG052859; -.
InParanoid; Q8C3K6; -.
KO; K14158; -.
PhylomeDB; Q8C3K6; -.
ChiTaRS; Slc5a1; mouse.
PRO; PR:Q8C3K6; -.
Proteomes; UP000000589; Unplaced.
GO; GO:0016324; C:apical plasma membrane; IDA:MGI.
GO; GO:0005903; C:brush border; IDA:MGI.
GO; GO:0031526; C:brush border membrane; ISO:MGI.
GO; GO:0005911; C:cell-cell junction; ISO:MGI.
GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
GO; GO:0005355; F:glucose transmembrane transporter activity; IMP:MGI.
GO; GO:0005412; F:glucose:sodium symporter activity; ISO:MGI.
GO; GO:1904659; P:glucose transmembrane transport; IMP:MGI.
GO; GO:0050892; P:intestinal absorption; IDA:MGI.
GO; GO:0001951; P:intestinal D-glucose absorption; IBA:GO_Central.
GO; GO:0001656; P:metanephros development; IMP:MGI.
GO; GO:0006814; P:sodium ion transport; IBA:GO_Central.
Gene3D; 1.20.1730.10; -; 1.
InterPro; IPR038377; Na/Glc_symporter_sf.
InterPro; IPR001734; Na/solute_symporter.
InterPro; IPR018212; Na/solute_symporter_CS.
Pfam; PF00474; SSF; 1.
TIGRFAMs; TIGR00813; sss; 1.
PROSITE; PS00456; NA_SOLUT_SYMP_1; 1.
PROSITE; PS00457; NA_SOLUT_SYMP_2; 1.
PROSITE; PS50283; NA_SOLUT_SYMP_3; 1.
1: Evidence at protein level;
Complete proteome; Disulfide bond; Glycoprotein; Ion transport;
Membrane; Phosphoprotein; Reference proteome; Sodium;
Sodium transport; Sugar transport; Symport; Transmembrane;
Transmembrane helix; Transport.
CHAIN 1 665 Sodium/glucose cotransporter 1.
/FTId=PRO_0000105367.
TOPO_DOM 1 28 Extracellular. {ECO:0000255}.
TRANSMEM 29 49 Helical. {ECO:0000255}.
TOPO_DOM 50 64 Cytoplasmic. {ECO:0000255}.
TRANSMEM 65 85 Helical. {ECO:0000255}.
TOPO_DOM 86 105 Extracellular. {ECO:0000255}.
TRANSMEM 106 126 Helical. {ECO:0000255}.
TOPO_DOM 127 142 Cytoplasmic. {ECO:0000255}.
TRANSMEM 143 163 Helical. {ECO:0000255}.
TOPO_DOM 164 178 Extracellular. {ECO:0000255}.
TRANSMEM 179 201 Helical. {ECO:0000255}.
TOPO_DOM 202 208 Cytoplasmic. {ECO:0000255}.
TRANSMEM 209 229 Helical. {ECO:0000255}.
TOPO_DOM 230 277 Extracellular. {ECO:0000255}.
TRANSMEM 278 298 Helical. {ECO:0000255}.
TOPO_DOM 299 313 Cytoplasmic. {ECO:0000255}.
TRANSMEM 314 334 Helical. {ECO:0000255}.
TOPO_DOM 335 380 Extracellular. {ECO:0000255}.
TRANSMEM 381 401 Helical. {ECO:0000255}.
TOPO_DOM 402 423 Cytoplasmic. {ECO:0000255}.
TRANSMEM 424 444 Helical. {ECO:0000255}.
TOPO_DOM 445 455 Extracellular. {ECO:0000255}.
TRANSMEM 456 476 Helical. {ECO:0000255}.
TOPO_DOM 477 484 Cytoplasmic. {ECO:0000255}.
TRANSMEM 485 505 Helical. {ECO:0000255}.
TOPO_DOM 506 526 Extracellular. {ECO:0000255}.
INTRAMEM 527 563 Helical. {ECO:0000255}.
TOPO_DOM 564 644 Extracellular. {ECO:0000255}.
TRANSMEM 645 665 Helical. {ECO:0000255}.
BINDING 457 457 Glucose. {ECO:0000250}.
SITE 43 43 Implicated in sodium coupling.
{ECO:0000250}.
SITE 300 300 Implicated in sodium coupling.
{ECO:0000250}.
SITE 460 460 Involved in sugar-binding/transport and
inhibitor binding. {ECO:0000250}.
MOD_RES 585 585 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 588 588 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
CARBOHYD 248 248 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 255 611 {ECO:0000250}.
SEQUENCE 665 AA; 73449 MW; 70905E30408BE378 CRC64;
MDSSTLSPAV TATDAPIPSY ERIRNAADIS VIVIYFVVVM AVGLWAMFST NRGTVGGFFL
AGRSMVWWPI GASLFASNIG SGHFVGLAGT GAAAGIAMGG FEWNALVLVV VLGWIFVPIY
IKAGVVTMPE YLRKRFGGKR IQIYLSVLSL LLYIFTKISA DIFSGAIFIN LALGLDIYLA
IFILLAITAL YTITGGLAAV IYTDTLQTAI MLVGSFILTG FAFNEVGGYE AFMDKYMKAI
PTKVSNGNFT AKEECYTPRA DSFHIFRDPI TGDMPWPGLI FGLAILALWY WCTDQVIVQR
CLSAKNMSHV KADCTLCGYL KLLPMFLMVM PGMISRILYT EKIACVLPEE CQKYCGTPVG
CTNIAYPTLV VELMPNGLRG LMLSVMMASL MSSLTSIFNS ASTLFTMDIY TKIRKKASEK
ELMIAGRLFI LVLIGISIAW VPIVQSAQSG QLFDYIQSIT SYLGPPIAAV FLLAIFCKRV
NEQGAFWGLI LGFLIGISRM ITEFAYGTGS CMEPSNCPKI ICGVHYLYFA IILFVISVIT
ILIISFLTKP IPDVHLYRWC WSLRNSKEER IDLDAGEEED IPEDSKDTIE IDTEAPQKKK
GCFRRAYDLF CGLDQDKGPK MTKEEEEAMK MKMTDTSEKP LWRTVVNING IILLAVAVFC
HAYFA


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