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Q8C3K6 (SC5A1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 88. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Sodium/glucose cotransporter 1

Short name=Na(+)/glucose cotransporter 1
Alternative name(s):
High affinity sodium-glucose cotransporter
Solute carrier family 5 member 1
Gene names
Name:Slc5a1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length665 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

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.

Post-translational modification

N-glycosylation is not necessary for the cotransporter function By similarity.

Sequence similarities

Belongs to the sodium:solute symporter (SSF) (TC 2.A.21) family. [View classification]

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 665665Sodium/glucose cotransporter 1
PRO_0000105367

Regions

Topological domain1 – 2828Extracellular Potential
Transmembrane29 – 4921Helical; Potential
Topological domain50 – 6415Cytoplasmic Potential
Transmembrane65 – 8521Helical; Potential
Topological domain86 – 10520Extracellular Potential
Transmembrane106 – 12621Helical; Potential
Topological domain127 – 14216Cytoplasmic Potential
Transmembrane143 – 16321Helical; Potential
Topological domain164 – 17815Extracellular Potential
Transmembrane179 – 20123Helical; Potential
Topological domain202 – 2087Cytoplasmic Potential
Transmembrane209 – 22921Helical; Potential
Topological domain230 – 27748Extracellular Potential
Transmembrane278 – 29821Helical; Potential
Topological domain299 – 31315Cytoplasmic Potential
Transmembrane314 – 33421Helical; Potential
Topological domain335 – 38046Extracellular Potential
Transmembrane381 – 40121Helical; Potential
Topological domain402 – 42322Cytoplasmic Potential
Transmembrane424 – 44421Helical; Potential
Topological domain445 – 45511Extracellular Potential
Transmembrane456 – 47621Helical; Potential
Topological domain477 – 4848Cytoplasmic Potential
Transmembrane485 – 50521Helical; Potential
Topological domain506 – 52621Extracellular Potential
Intramembrane527 – 56337Helical; Potential
Topological domain564 – 64481Extracellular Potential
Transmembrane645 – 66521Helical; Potential

Sites

Binding site4571Glucose By similarity
Site431Implicated in sodium coupling By similarity
Site3001Implicated in sodium coupling By similarity
Site4601Involved in sugar-binding/transport and inhibitor binding By similarity

Amino acid modifications

Glycosylation2481N-linked (GlcNAc...) Potential
Disulfide bond255 ↔ 611 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8C3K6 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 70905E30408BE378

FASTA66573,449
        10         20         30         40         50         60 
MDSSTLSPAV TATDAPIPSY ERIRNAADIS VIVIYFVVVM AVGLWAMFST NRGTVGGFFL 

        70         80         90        100        110        120 
AGRSMVWWPI GASLFASNIG SGHFVGLAGT GAAAGIAMGG FEWNALVLVV VLGWIFVPIY 

       130        140        150        160        170        180 
IKAGVVTMPE YLRKRFGGKR IQIYLSVLSL LLYIFTKISA DIFSGAIFIN LALGLDIYLA 

       190        200        210        220        230        240 
IFILLAITAL YTITGGLAAV IYTDTLQTAI MLVGSFILTG FAFNEVGGYE AFMDKYMKAI 

       250        260        270        280        290        300 
PTKVSNGNFT AKEECYTPRA DSFHIFRDPI TGDMPWPGLI FGLAILALWY WCTDQVIVQR 

       310        320        330        340        350        360 
CLSAKNMSHV KADCTLCGYL KLLPMFLMVM PGMISRILYT EKIACVLPEE CQKYCGTPVG 

       370        380        390        400        410        420 
CTNIAYPTLV VELMPNGLRG LMLSVMMASL MSSLTSIFNS ASTLFTMDIY TKIRKKASEK 

       430        440        450        460        470        480 
ELMIAGRLFI LVLIGISIAW VPIVQSAQSG QLFDYIQSIT SYLGPPIAAV FLLAIFCKRV 

       490        500        510        520        530        540 
NEQGAFWGLI LGFLIGISRM ITEFAYGTGS CMEPSNCPKI ICGVHYLYFA IILFVISVIT 

       550        560        570        580        590        600 
ILIISFLTKP IPDVHLYRWC WSLRNSKEER IDLDAGEEED IPEDSKDTIE IDTEAPQKKK 

       610        620        630        640        650        660 
GCFRRAYDLF CGLDQDKGPK MTKEEEEAMK MKMTDTSEKP LWRTVVNING IILLAVAVFC 


HAYFA 

« Hide

References

[1]"The transcriptional landscape of the mammalian genome."
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. expand/collapse author list , 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.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Kidney.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK085602 mRNA. Translation: BAC39483.1.
CCDSCCDS19199.1.
RefSeqNP_062784.3. NM_019810.4.
UniGeneMm.25237.

3D structure databases

ProteinModelPortalQ8C3K6.
SMRQ8C3K6. Positions 26-553.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ8C3K6. 1 interaction.

PTM databases

PhosphoSiteQ8C3K6.

Proteomic databases

MaxQBQ8C3K6.
PaxDbQ8C3K6.
PRIDEQ8C3K6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID20537.
KEGGmmu:20537.

Organism-specific databases

CTD6523.
MGIMGI:107678. Slc5a1.

Phylogenomic databases

eggNOGCOG4146.
HOGENOMHOG000025422.
HOVERGENHBG052859.
InParanoidQ8C3K6.
KOK14158.
PhylomeDBQ8C3K6.

Gene expression databases

GenevestigatorQ8C3K6.

Family and domain databases

InterProIPR001734. Na/solute_symporter.
IPR018212. Na/solute_symporter_CS.
IPR019900. Na/solute_symporter_subgr.
[Graphical view]
PANTHERPTHR11819. PTHR11819. 1 hit.
PfamPF00474. SSF. 1 hit.
[Graphical view]
TIGRFAMsTIGR00813. sss. 1 hit.
PROSITEPS00456. NA_SOLUT_SYMP_1. 1 hit.
PS00457. NA_SOLUT_SYMP_2. 1 hit.
PS50283. NA_SOLUT_SYMP_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio298811.
PROQ8C3K6.
SOURCESearch...

Entry information

Entry nameSC5A1_MOUSE
AccessionPrimary (citable) accession number: Q8C3K6
Entry history
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: March 1, 2003
Last modified: July 9, 2014
This is version 88 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot