ID SC5AB_HUMAN Reviewed; 675 AA.
AC Q8WWX8; B7Z329; Q05BF1; Q6PF02; Q6ZUW3; Q86Y55; Q96PP5;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 27-MAR-2024, entry version 158.
DE RecName: Full=Sodium/myo-inositol cotransporter 2 {ECO:0000305};
DE Short=Na(+)/myo-inositol cotransporter 2;
DE AltName: Full=Sodium-dependent glucose cotransporter;
DE AltName: Full=Sodium/glucose cotransporter KST1;
DE AltName: Full=Sodium/myo-inositol transporter 2;
DE Short=SMIT2;
DE AltName: Full=Solute carrier family 5 member 11;
GN Name=SLC5A11 {ECO:0000312|HGNC:HGNC:23091};
GN Synonyms=KST1 {ECO:0000303|PubMed:12039040},
GN SLGTX {ECO:0000312|EMBL:CAC83728.1}, SMIT2 {ECO:0000303|PubMed:19032932};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAK97784.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY, AND
RP VARIANTS ALA-182; LEU-258 AND ILE-526.
RC TISSUE=Brain {ECO:0000269|PubMed:12039040};
RX PubMed=12039040; DOI=10.1016/s0378-1119(02)00416-x;
RA Roll P., Massacrier A., Pereira S., Robaglia-Schlupp A., Cau P.,
RA Szepetowski P.;
RT "New human sodium/glucose cotransporter gene (KST1): identification,
RT characterization, and mutation analysis in ICCA (infantile convulsions and
RT choreoathetosis) and BFIC (benign familial infantile convulsions)
RT families.";
RL Gene 285:141-148(2002).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAK97053.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT ALA-182.
RA Mount D.B.;
RT "Cloning of the human ortholog of RKST1, a member of the SGLT gene family
RT of sodium-coupled cotransporters.";
RL Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000305, ECO:0000312|EMBL:AAK97053.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Kidney {ECO:0000312|EMBL:CAC83728.1};
RA Bruss M., Bonisch H.;
RT "Cloning and functional characterization of a new human sugar transporter
RT in kidney.";
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000305, ECO:0000312|EMBL:BAC86105.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4 AND 5), AND VARIANT
RP ALA-182.
RC TISSUE=Corpus callosum, and Kidney {ECO:0000312|EMBL:BAC86105.1};
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [6] {ECO:0000305, ECO:0000312|EMBL:AAK97053.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7] {ECO:0000305, ECO:0000312|EMBL:AAH57780.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 6), AND VARIANT
RP ARG-452.
RC TISSUE=Brain, and Hypothalamus {ECO:0000312|EMBL:AAH57780.1};
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP FUNCTION, TRANSPORTER ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY
RP REGULATION.
RX PubMed=19032932; DOI=10.1016/j.abb.2008.11.008;
RA Lin X., Ma L., Fitzgerald R.L., Ostlund R.E. Jr.;
RT "Human sodium/inositol cotransporter 2 (SMIT2) transports inositols but not
RT glucose in L6 cells.";
RL Arch. Biochem. Biophys. 481:197-201(2009).
RN [9] {ECO:0000305}
RP FUNCTION, AND VARIANT ALA-182.
RX PubMed=15172003; DOI=10.1016/j.ymgme.2004.03.007;
RA Groenen P.M.W., Klootwijk R., Schijvenaars M.M.V.A.P., Straatman H.,
RA Mariman E.C.M., Franke B., Steegers-Theunissen R.P.M.;
RT "Spina bifida and genetic factors related to myo-inositol, glucose, and
RT zinc.";
RL Mol. Genet. Metab. 82:154-161(2004).
RN [10] {ECO:0000305}
RP POSSIBLE ROLE IN SLE.
RX PubMed=18069935; DOI=10.1111/j.1399-0039.2007.00975.x;
RA Tsai L.-J., Hsiao S.-H., Tsai L.-M., Lin C.-Y., Tsai J.-J., Liou D.-M.,
RA Lan J.-L.;
RT "The sodium-dependent glucose cotransporter SLC5A11 as an autoimmune
RT modifier gene in SLE.";
RL Tissue Antigens 71:114-126(2008).
CC -!- FUNCTION: Involved in the sodium-dependent cotransport of myo-inositol
CC (MI) with a Na(+):MI stoichiometry of 2:1 (PubMed:15172003,
CC PubMed:19032932). Exclusively responsible for apical MI transport and
CC absorption in intestine (By similarity). Can also transport D-chiro-
CC inositol (DCI) but not L-fucose (PubMed:15172003, PubMed:19032932).
CC Exhibits stereospecific cotransport of both D-glucose and D-xylose (By
CC similarity). May induce apoptosis through the TNF-alpha, PDCD1 pathway
CC (PubMed:15172003, PubMed:18069935). May play a role in the regulation
CC of MI concentration in serum, involving reabsorption in at least the
CC proximal tubule of the kidney (By similarity).
CC {ECO:0000250|UniProtKB:Q28728, ECO:0000250|UniProtKB:Q9Z1F2,
CC ECO:0000269|PubMed:15172003, ECO:0000269|PubMed:18069935,
CC ECO:0000269|PubMed:19032932}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=myo-inositol(out) + 2 Na(+)(out) = myo-inositol(in) + 2
CC Na(+)(in); Xref=Rhea:RHEA:72987, ChEBI:CHEBI:17268,
CC ChEBI:CHEBI:29101; Evidence={ECO:0000269|PubMed:19032932};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1D-chiro-inositol(out) + 2 Na(+)(out) = 1D-chiro-inositol(in)
CC + 2 Na(+)(in); Xref=Rhea:RHEA:73315, ChEBI:CHEBI:27372,
CC ChEBI:CHEBI:29101; Evidence={ECO:0000269|PubMed:19032932};
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:Q28728};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-xylose(out) + 2 Na(+)(out) = D-xylose(in) + 2 Na(+)(in);
CC Xref=Rhea:RHEA:73367, ChEBI:CHEBI:29101, ChEBI:CHEBI:53455;
CC Evidence={ECO:0000250|UniProtKB:Q28728};
CC -!- ACTIVITY REGULATION: MI transport activity inhibited by D-chiro-
CC inositol (DCI), phlorizin (Pz) and sodium (Na(+)) (By similarity).
CC Insulin increases D-chiro-inositol uptake (PubMed:19032932).
CC {ECO:0000250|UniProtKB:Q9Z1F2, ECO:0000269|PubMed:19032932}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=111 uM for D-chiro-inositol {ECO:0000269|PubMed:19032932};
CC KM=158 uM for myo-inositol {ECO:0000269|PubMed:19032932};
CC -!- INTERACTION:
CC Q8WWX8; O00505: KPNA3; NbExp=3; IntAct=EBI-10277669, EBI-358297;
CC Q8WWX8-3; O00505: KPNA3; NbExp=3; IntAct=EBI-12697471, EBI-358297;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305|PubMed:19032932}; Multi-
CC pass membrane protein {ECO:0000255}. Apical cell membrane
CC {ECO:0000250|UniProtKB:Q9Z1F2}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q9Z1F2}. Note=Located on apical membrane of
CC enterocytes (By similarity). Located on membrane of kidney brush border
CC membrane vesicles (BBMVs) and apical membrane of proximal convoluted
CC tubules (By similarity). {ECO:0000250|UniProtKB:Q28728,
CC ECO:0000250|UniProtKB:Q9Z1F2}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1 {ECO:0000269|PubMed:12039040};
CC IsoId=Q8WWX8-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:12039040};
CC IsoId=Q8WWX8-2; Sequence=VSP_052790;
CC Name=3 {ECO:0000269|PubMed:15489334};
CC IsoId=Q8WWX8-3; Sequence=VSP_052789;
CC Name=4;
CC IsoId=Q8WWX8-4; Sequence=VSP_033259;
CC Name=5;
CC IsoId=Q8WWX8-5; Sequence=VSP_045034, VSP_052790;
CC Name=6;
CC IsoId=Q8WWX8-6; Sequence=VSP_052789, VSP_045035, VSP_045036;
CC -!- TISSUE SPECIFICITY: Highest expression in heart, skeletal muscle,
CC kidney, liver and placenta. Weaker expression in brain, colon, spleen,
CC lung and peripheral blood leukocytes. {ECO:0000269|PubMed:12039040}.
CC -!- MISCELLANEOUS: Acts as an autoimmune modifier in systemic lupus
CC erythematosus (SLE) as it is significantly associated with low
CC complement component 4 (C4), anti-Smith antibody, serositis, and
CC alopecia. {ECO:0000269|PubMed:18069935}.
CC -!- SIMILARITY: Belongs to the sodium:solute symporter (SSF) (TC 2.A.21)
CC family. {ECO:0000255}.
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DR EMBL; AY044906; AAK97784.1; -; mRNA.
DR EMBL; AF292385; AAK97053.1; -; mRNA.
DR EMBL; AJ305237; CAC83728.1; -; mRNA.
DR EMBL; AK125267; BAC86105.1; -; mRNA.
DR EMBL; AK295427; BAH12065.1; -; mRNA.
DR EMBL; AC008731; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471145; EAW55781.1; -; Genomic_DNA.
DR EMBL; BC049385; AAH49385.1; -; mRNA.
DR EMBL; BC057780; AAH57780.1; -; mRNA.
DR CCDS; CCDS10625.1; -. [Q8WWX8-1]
DR CCDS; CCDS58437.1; -. [Q8WWX8-2]
DR CCDS; CCDS58438.1; -. [Q8WWX8-5]
DR CCDS; CCDS58439.1; -. [Q8WWX8-3]
DR CCDS; CCDS58440.1; -. [Q8WWX8-6]
DR RefSeq; NP_001245340.1; NM_001258411.2. [Q8WWX8-2]
DR RefSeq; NP_001245341.1; NM_001258412.2. [Q8WWX8-5]
DR RefSeq; NP_001245342.1; NM_001258413.2. [Q8WWX8-3]
DR RefSeq; NP_001245343.1; NM_001258414.1. [Q8WWX8-6]
DR RefSeq; NP_443176.2; NM_052944.4.
DR RefSeq; XP_005255137.1; XM_005255080.2.
DR RefSeq; XP_016878389.1; XM_017022900.1.
DR RefSeq; XP_016878390.1; XM_017022901.1.
DR RefSeq; XP_016878391.1; XM_017022902.1.
DR RefSeq; XP_016878392.1; XM_017022903.1. [Q8WWX8-1]
DR RefSeq; XP_016878394.1; XM_017022905.1.
DR RefSeq; XP_016878395.1; XM_017022906.1.
DR AlphaFoldDB; Q8WWX8; -.
DR SMR; Q8WWX8; -.
DR BioGRID; 125441; 11.
DR IntAct; Q8WWX8; 3.
DR STRING; 9606.ENSP00000289932; -.
DR BindingDB; Q8WWX8; -.
DR ChEMBL; CHEMBL1744524; -.
DR DrugCentral; Q8WWX8; -.
DR GuidetoPHARMACOLOGY; 925; -.
DR TCDB; 2.A.21.3.6; the solute:sodium symporter (sss) family.
DR GlyCosmos; Q8WWX8; 1 site, 1 glycan.
DR GlyGen; Q8WWX8; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q8WWX8; -.
DR PhosphoSitePlus; Q8WWX8; -.
DR BioMuta; SLC5A11; -.
DR DMDM; 74751588; -.
DR MassIVE; Q8WWX8; -.
DR PaxDb; 9606-ENSP00000289932; -.
DR PeptideAtlas; Q8WWX8; -.
DR ProteomicsDB; 58368; -.
DR ProteomicsDB; 6486; -.
DR ProteomicsDB; 74950; -. [Q8WWX8-1]
DR ProteomicsDB; 74951; -. [Q8WWX8-2]
DR ProteomicsDB; 74952; -. [Q8WWX8-3]
DR ProteomicsDB; 74953; -. [Q8WWX8-4]
DR Antibodypedia; 12746; 173 antibodies from 27 providers.
DR DNASU; 115584; -.
DR Ensembl; ENST00000347898.7; ENSP00000289932.3; ENSG00000158865.13. [Q8WWX8-1]
DR Ensembl; ENST00000424767.7; ENSP00000416782.3; ENSG00000158865.13. [Q8WWX8-1]
DR Ensembl; ENST00000565769.5; ENSP00000457179.1; ENSG00000158865.13. [Q8WWX8-3]
DR Ensembl; ENST00000567758.6; ENSP00000454401.1; ENSG00000158865.13. [Q8WWX8-2]
DR Ensembl; ENST00000568579.6; ENSP00000456234.1; ENSG00000158865.13. [Q8WWX8-5]
DR Ensembl; ENST00000569071.2; ENSP00000456376.1; ENSG00000158865.13. [Q8WWX8-6]
DR Ensembl; ENST00000671711.1; ENSP00000500525.1; ENSG00000288216.2. [Q8WWX8-6]
DR Ensembl; ENST00000672306.1; ENSP00000500570.1; ENSG00000288216.2. [Q8WWX8-6]
DR Ensembl; ENST00000672547.1; ENSP00000500395.1; ENSG00000288216.2. [Q8WWX8-2]
DR Ensembl; ENST00000672588.1; ENSP00000499965.1; ENSG00000288216.2. [Q8WWX8-1]
DR Ensembl; ENST00000672672.1; ENSP00000500207.1; ENSG00000288216.2. [Q8WWX8-5]
DR Ensembl; ENST00000672971.1; ENSP00000500955.1; ENSG00000288216.2. [Q8WWX8-5]
DR Ensembl; ENST00000673269.1; ENSP00000500384.1; ENSG00000288216.2. [Q8WWX8-2]
DR Ensembl; ENST00000673441.1; ENSP00000500055.1; ENSG00000288216.2. [Q8WWX8-3]
DR Ensembl; ENST00000710486.1; ENSP00000518306.1; ENSG00000288216.2. [Q8WWX8-1]
DR GeneID; 115584; -.
DR KEGG; hsa:115584; -.
DR MANE-Select; ENST00000424767.7; ENSP00000416782.3; NM_001352248.3; NP_001339177.1.
DR UCSC; uc002dms.5; human. [Q8WWX8-1]
DR AGR; HGNC:23091; -.
DR CTD; 115584; -.
DR DisGeNET; 115584; -.
DR GeneCards; SLC5A11; -.
DR HGNC; HGNC:23091; SLC5A11.
DR HPA; ENSG00000158865; Tissue enriched (brain).
DR MIM; 610238; gene.
DR neXtProt; NX_Q8WWX8; -.
DR OpenTargets; ENSG00000158865; -.
DR PharmGKB; PA134923660; -.
DR VEuPathDB; HostDB:ENSG00000158865; -.
DR eggNOG; KOG2349; Eukaryota.
DR GeneTree; ENSGT00940000157690; -.
DR HOGENOM; CLU_018808_9_2_1; -.
DR InParanoid; Q8WWX8; -.
DR OMA; NWVFVAK; -.
DR OrthoDB; 74094at2759; -.
DR PhylomeDB; Q8WWX8; -.
DR TreeFam; TF352855; -.
DR PathwayCommons; Q8WWX8; -.
DR Reactome; R-HSA-429593; Inositol transporters.
DR SignaLink; Q8WWX8; -.
DR BioGRID-ORCS; 115584; 15 hits in 1143 CRISPR screens.
DR ChiTaRS; SLC5A11; human.
DR GenomeRNAi; 115584; -.
DR Pharos; Q8WWX8; Tchem.
DR PRO; PR:Q8WWX8; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q8WWX8; Protein.
DR Bgee; ENSG00000158865; Expressed in C1 segment of cervical spinal cord and 90 other cell types or tissues.
DR ExpressionAtlas; Q8WWX8; baseline and differential.
DR Genevisible; Q8WWX8; HS.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0005412; F:glucose:sodium symporter activity; IBA:GO_Central.
DR GO; GO:0005365; F:myo-inositol transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0015166; F:polyol transmembrane transporter activity; TAS:Reactome.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0015798; P:myo-inositol transport; IDA:UniProtKB.
DR CDD; cd11490; SLC5sbd_SGLT6; 1.
DR Gene3D; 1.20.1730.10; Sodium/glucose cotransporter; 1.
DR InterPro; IPR038377; Na/Glc_symporter_sf.
DR InterPro; IPR001734; Na/solute_symporter.
DR NCBIfam; TIGR00813; sss; 1.
DR PANTHER; PTHR11819:SF171; SODIUM_MYO-INOSITOL COTRANSPORTER 2; 1.
DR PANTHER; PTHR11819; SOLUTE CARRIER FAMILY 5; 1.
DR Pfam; PF00474; SSF; 1.
DR PROSITE; PS50283; NA_SOLUT_SYMP_3; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Apoptosis; Cell membrane; Ion transport; Membrane;
KW Reference proteome; Sodium; Sodium transport; Sugar transport; Symport;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..675
FT /note="Sodium/myo-inositol cotransporter 2"
FT /id="PRO_0000331568"
FT TOPO_DOM 1..27
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 28..48
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 49..65
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 66..88
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 89..102
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 103..123
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 124..135
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 136..156
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 157..180
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 181..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..272
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 273..293
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 294..308
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 309..329
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 330..375
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 376..396
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 397..418
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 419..439
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 440..446
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 447..467
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 468..479
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 480..500
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 501..521
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 522..542
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 543..654
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 655..675
FT /note="Helical"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..64
FT /note="Missing (in isoform 3 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_052789"
FT VAR_SEQ 45
FT /note="W -> WVGSPSVAQGTRTQWWQSWLTPASTSWAQVILSPRLPDTEEVLSTRN
FT RLSPDTKPLGALILNFQVSRI (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_033259"
FT VAR_SEQ 70..104
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045034"
FT VAR_SEQ 125..159
FT /note="Missing (in isoform 2 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:12039040,
FT ECO:0000303|PubMed:14702039"
FT /id="VSP_052790"
FT VAR_SEQ 223..302
FT /note="FAAVGGMEGLKEKYFLALASNRSENSSCGLPREDAFHIFRDPLTSDLPWPGV
FT LFGMSIPSLWYWCTDQVIVQRTLAAKNL -> DCPADSGCQEPVPCQRRCSDGCIPEGA
FT APLHNGVPWDGQPHPLPRSSGLCRSRDLPEDLQQPLRLFGHRVSQTRAGTPAH (in
FT isoform 6)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_045035"
FT VAR_SEQ 303..394
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_045036"
FT VARIANT 47
FT /note="T -> P (in dbSNP:rs36048966)"
FT /id="VAR_052494"
FT VARIANT 182
FT /note="V -> A (reduces serum myo-inositol concentration;
FT dbSNP:rs11074656)"
FT /evidence="ECO:0000269|PubMed:12039040,
FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15172003,
FT ECO:0000269|Ref.2"
FT /id="VAR_042896"
FT VARIANT 258
FT /note="F -> L (in dbSNP:rs35993597)"
FT /evidence="ECO:0000269|PubMed:12039040"
FT /id="VAR_042897"
FT VARIANT 452
FT /note="Q -> R (in dbSNP:rs17854935)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_042898"
FT VARIANT 526
FT /note="M -> I"
FT /evidence="ECO:0000269|PubMed:12039040"
FT /id="VAR_042899"
FT VARIANT 539
FT /note="V -> M (in dbSNP:rs35038575)"
FT /id="VAR_061877"
FT CONFLICT 41
FT /note="A -> T (in Ref. 2; AAK97053)"
FT /evidence="ECO:0000305"
FT CONFLICT 371
FT /note="T -> P (in Ref. 3; CAC83728)"
FT /evidence="ECO:0000305"
FT CONFLICT 547
FT /note="S -> P (in Ref. 6; BAC86105)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 675 AA; 74036 MW; 44F7BA6D2FE92335 CRC64;
MESGTSSPQP PQLDPLDAFP QKGLEPGDIA VLVLYFLFVL AVGLWSTVKT KRDTVKGYFL
AGGDMVWWPV GASLFASNVG SGHFIGLAGS GAATGISVSA YELNGLFSVL MLAWIFLPIY
IAGQVTTMPE YLRKRFGGIR IPIILAVLYL FIYIFTKISV DMYAGAIFIQ QSLHLDLYLA
IVGLLAITAV YTVAGGLAAV IYTDALQTLI MLIGALTLMG YSFAAVGGME GLKEKYFLAL
ASNRSENSSC GLPREDAFHI FRDPLTSDLP WPGVLFGMSI PSLWYWCTDQ VIVQRTLAAK
NLSHAKGGAL MAAYLKVLPL FIMVFPGMVS RILFPDQVAC ADPEICQKIC SNPSGCSDIA
YPKLVLELLP TGLRGLMMAV MVAALMSSLT SIFNSASTIF TMDLWNHLRP RASEKELMIV
GRVFVLLLVL VSILWIPVVQ ASQGGQLFIY IQSISSYLQP PVAVVFIMGC FWKRTNEKGA
FWGLISGLLL GLVRLVLDFI YVQPRCDQPD ERPVLVKSIH YLYFSMILST VTLITVSTVS
WFTEPPSKEM VSHLTWFTRH DPVVQKEQAP PAAPLSLTLS QNGMPEASSS SSVQFEMVQE
NTSKTHSCDM TPKQSKVVKA ILWLCGIQEK GKEELPARAE AIIVSLEENP LVKTLLDVNL
IFCVSCAIFI WGYFA
//
