Q28728 · SC5AB_RABIT
- ProteinSodium/myo-inositol cotransporter 2
- GeneSLC5A11
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids674 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Involved in the sodium-dependent cotransport of myo-inositol (MI) with a Na+:MI stoichiometry of 2:1. Exclusively responsible for apical MI transport and absorption in intestine. Can also transport D-chiro-inositol (DCI) but not L-fucose (PubMed:12133831, PubMed:15181167, PubMed:15613375, PubMed:17932225).
Exhibits stereospecific cotransport of both D-glucose and D-xylose (PubMed:12133831).
May induce apoptosis through the TNF-alpha, PDCD1 pathway (By similarity).
May play a role in the regulation of MI concentration in serum, involving reabsorption in at least the proximal tubule of the kidney (PubMed:17306760).
Exhibits stereospecific cotransport of both D-glucose and D-xylose (PubMed:12133831).
May induce apoptosis through the TNF-alpha, PDCD1 pathway (By similarity).
May play a role in the regulation of MI concentration in serum, involving reabsorption in at least the proximal tubule of the kidney (PubMed:17306760).
Catalytic activity
- myo-inositol(out) + 2 Na+(out) = myo-inositol(in) + 2 Na+(in)myo-inositol (out)CHEBI:17268
+ 2 Na+ (out)CHEBI:29101= myo-inositol (in)CHEBI:17268+ 2 Na+ (in)CHEBI:29101 - 1D-chiro-inositol(out) + 2 Na+(out) = 1D-chiro-inositol(in) + 2 Na+(in)
- D-glucose(out) + 2 Na+(out) = D-glucose(in) + 2 Na+(in)
- D-xylose(out) + 2 Na+(out) = D-xylose(in) + 2 Na+(in)
Activity regulation
MI transport activity stimulated five-fold under 24 hour hypertonic shock conditions. MI inward currents were gradually inhibited as increasing amounts of phlorizin were added to the superfusion medium. When sodium is replaced by potassium, MI uptake is dramatically reduced and in the presence of L-fucose or D-chiro-inositol (DCI), the specific accumulation of tracer amounts of MI is also reduced.
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
120 μM | myoinositol | in Xenopus laevis oocytes | ||||
334 μM | myoinositol | in dog MDCK cells | ||||
13 mM | Na+ | in Xenopus laevis oocytes | ||||
130 μM | D-chiro-inositol | |||||
30 mM | D-glucose |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | apical plasma membrane | |
Cellular Component | plasma membrane | |
Molecular Function | glucose:sodium symporter activity | |
Molecular Function | myo-inositol transmembrane transporter activity | |
Biological Process | apoptotic process | |
Biological Process | myo-inositol transport |
Keywords
- Biological process
- Ligand
Names & Taxonomy
Protein names
- Recommended nameSodium/myo-inositol cotransporter 2
- Short namesNa(+)/myo-inositol cotransporter 2
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Lagomorpha > Leporidae > Oryctolagus
Accessions
- Primary accessionQ28728
- Secondary accessions
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Membrane ; Multi-pass membrane protein
Apical cell membrane ; Multi-pass membrane protein
Note: Located on membrane of kidney brush border membrane vesicles (BBMVs) and apical membrane of proximal convoluted tubules.
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-27 | Extracellular | ||||
Sequence: MESSTSSPQPPLSDPLDPFPQRSLEPG | ||||||
Transmembrane | 28-48 | Helical | ||||
Sequence: DIAVLVLYFLFVLAVGLWSTV | ||||||
Topological domain | 49-56 | Cytoplasmic | ||||
Sequence: KTKRDTVK | ||||||
Transmembrane | 57-77 | Helical | ||||
Sequence: GYFLAGGDMVWWPVGASLFAS | ||||||
Topological domain | 78-102 | Extracellular | ||||
Sequence: NVGSGHFVGLAGSGAATGISVAAYE | ||||||
Transmembrane | 103-123 | Helical | ||||
Sequence: FNGMFSVLMLAWIFLPIYIAG | ||||||
Topological domain | 124-140 | Cytoplasmic | ||||
Sequence: QVTTMPEYLRRRFGGSR | ||||||
Transmembrane | 141-161 | Helical | ||||
Sequence: IAITLAVLYLFIYIFTKISVD | ||||||
Topological domain | 162-180 | Extracellular | ||||
Sequence: MYAGAIFIQQSLHLDLYLS | ||||||
Transmembrane | 181-201 | Helical | ||||
Sequence: VVGLLAVTALYTVAGGLAAVI | ||||||
Topological domain | 202-208 | Cytoplasmic | ||||
Sequence: YTDALQT | ||||||
Transmembrane | 209-229 | Helical | ||||
Sequence: LIMLVGALTLMGYSFAAVGGM | ||||||
Topological domain | 230-272 | Extracellular | ||||
Sequence: EGLQEKYFLALPSNRSENSSCGLPREDAFHLFRDPLTSDLPWP | ||||||
Transmembrane | 273-293 | Helical | ||||
Sequence: GILFGMSIPSLWYWCTDQVIV | ||||||
Topological domain | 294-308 | Cytoplasmic | ||||
Sequence: QRSLAAKNLSHAKGG | ||||||
Transmembrane | 309-329 | Helical | ||||
Sequence: SLMAAYLKVLPLFIMVFPGMV | ||||||
Topological domain | 330-375 | Extracellular | ||||
Sequence: SRILFPDQVACADPETCQRVCNNPSGCSDIAYPKLVLELLPTGLRG | ||||||
Transmembrane | 376-396 | Helical | ||||
Sequence: LMMAVMVAALMSSLTSIFNSA | ||||||
Topological domain | 397-418 | Cytoplasmic | ||||
Sequence: STIFTMDLWNHVRPRASEKELM | ||||||
Transmembrane | 419-439 | Helical | ||||
Sequence: IVGRVFVLLLVLVSVLWIPVV | ||||||
Topological domain | 440-446 | Extracellular | ||||
Sequence: QASQGGQ | ||||||
Transmembrane | 447-467 | Helical | ||||
Sequence: LFVYIQAISSYLQPPVAMVFV | ||||||
Topological domain | 468-479 | Cytoplasmic | ||||
Sequence: LGCFWKRANEKG | ||||||
Transmembrane | 480-500 | Helical | ||||
Sequence: AFWGLVLGLLLGFIRLILDFI | ||||||
Topological domain | 501-521 | Extracellular | ||||
Sequence: YVEPACHQPDERPSVVKNVHY | ||||||
Transmembrane | 522-542 | Helical | ||||
Sequence: LYFSMILSSVTVLTVTVMSLL | ||||||
Topological domain | 543-653 | Cytoplasmic | ||||
Sequence: TEPPSKEMISHLTWFTRRDPVVQKAQVPAATPLPPALSHNGTAEANSASIQLETIQEGASKAHSSDVTPKQSRVVRALLWLCGMEGKSTEQAPRPAEPVLASIEENPVVKT | ||||||
Transmembrane | 654-674 | Helical | ||||
Sequence: LLDVNCLLCICCAFFLWGYFA |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000331571 | 1-674 | Sodium/myo-inositol cotransporter 2 | |||
Sequence: MESSTSSPQPPLSDPLDPFPQRSLEPGDIAVLVLYFLFVLAVGLWSTVKTKRDTVKGYFLAGGDMVWWPVGASLFASNVGSGHFVGLAGSGAATGISVAAYEFNGMFSVLMLAWIFLPIYIAGQVTTMPEYLRRRFGGSRIAITLAVLYLFIYIFTKISVDMYAGAIFIQQSLHLDLYLSVVGLLAVTALYTVAGGLAAVIYTDALQTLIMLVGALTLMGYSFAAVGGMEGLQEKYFLALPSNRSENSSCGLPREDAFHLFRDPLTSDLPWPGILFGMSIPSLWYWCTDQVIVQRSLAAKNLSHAKGGSLMAAYLKVLPLFIMVFPGMVSRILFPDQVACADPETCQRVCNNPSGCSDIAYPKLVLELLPTGLRGLMMAVMVAALMSSLTSIFNSASTIFTMDLWNHVRPRASEKELMIVGRVFVLLLVLVSVLWIPVVQASQGGQLFVYIQAISSYLQPPVAMVFVLGCFWKRANEKGAFWGLVLGLLLGFIRLILDFIYVEPACHQPDERPSVVKNVHYLYFSMILSSVTVLTVTVMSLLTEPPSKEMISHLTWFTRRDPVVQKAQVPAATPLPPALSHNGTAEANSASIQLETIQEGASKAHSSDVTPKQSRVVRALLWLCGMEGKSTEQAPRPAEPVLASIEENPVVKTLLDVNCLLCICCAFFLWGYFA |
Proteomic databases
Expression
Tissue specificity
Expressed in brain, lung and kidney. In the kidney, strongly expressed in the cortex, at the luminal side of proximal convoluted tubules and in BBMVs. Weaker expression observed in the medulla (at protein level).
Interaction
Protein-protein interaction databases
Structure
Sequence
- Sequence statusComplete
- Length674
- Mass (Da)73,599
- Last updated2008-04-29 v2
- Checksum1827A7EC25C1F719
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 164 | in Ref. 1; BAA03753 | ||||
Sequence: A → T |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
D16226 EMBL· GenBank· DDBJ | BAA03753.1 EMBL· GenBank· DDBJ | mRNA | ||
AF506029 EMBL· GenBank· DDBJ | AAP30856.1 EMBL· GenBank· DDBJ | mRNA |