SC5AB_RAT
ID SC5AB_RAT Reviewed; 673 AA.
AC Q9Z1F2;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 2.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Sodium/myo-inositol cotransporter 2;
DE Short=Na(+)/myo-inositol cotransporter 2;
DE AltName: Full=Sodium-dependent glucose cotransporter;
DE AltName: Full=Sodium/glucose cotransporter KST1;
DE Short=rkST1;
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|RGD:621410};
GN Synonyms=Kst1 {ECO:0000312|RGD:621410},
GN Smit2 {ECO:0000303|PubMed:17932225};
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] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway {ECO:0000269|PubMed:15057822};
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAD10832.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 71-219.
RC TISSUE=Neuron {ECO:0000312|EMBL:AAD10832.1};
RA Poppe R., Gambaryan S., Wiesinger H., Haase W., Karbach U., Koepsell H.;
RL Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000305}
RP FUNCTION, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=17932225; DOI=10.1152/ajpgi.00422.2007;
RA Aouameur R., Da Cal S., Bissonnette P., Coady M.J., Lapointe J.-Y.;
RT "SMIT2 mediates all myo-inositol uptake in apical membranes of rat small
RT intestine.";
RL Am. J. Physiol. 293:G1300-G1307(2007).
CC -!- FUNCTION: Involved in the sodium-dependent cotransport of myo-inositol
CC (MI) with a Na(+):MI stoichiometry of 2:1. Exclusively responsible for
CC apical MI transport and absorption in intestine. Can also transport D-
CC chiro-inositol (DCI) but not L-fructose. Exhibits stereospecific
CC cotransport of both D-glucose and D-xylose. May induce apoptosis
CC through the TNF-alpha, PDCD1 pathway. 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. {ECO:0000250|UniProtKB:Q28728,
CC ECO:0000250|UniProtKB:Q8WWX8, ECO:0000269|PubMed:17932225}.
CC -!- ACTIVITY REGULATION: MI transport activity inhibited by D-chiro-
CC inositol (DCI), phlorizin (Pz) and sodium (Na(+)).
CC {ECO:0000269|PubMed:17932225}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=150 uM for MI (in rat brush border membrane vesicles (BBMv))
CC {ECO:0000269|PubMed:17932225};
CC KM=270 uM for MI (in Xenopus laevis oocytes)
CC {ECO:0000269|PubMed:17932225};
CC KM=146 uM for DCI (in rat BBMv) {ECO:0000269|PubMed:17932225};
CC KM=310 uM for DCI (in Xenopus laevis oocytes)
CC {ECO:0000269|PubMed:17932225};
CC KM=930 uM for glucose (in rat BBMv) {ECO:0000269|PubMed:17932225};
CC KM=35500 uM for glucose (in Xenopus laevis oocytes)
CC {ECO:0000269|PubMed:17932225};
CC KM=15 uM for Pz (in rat BBMv) {ECO:0000269|PubMed:17932225};
CC KM=16 uM for Pz (in Xenopus laevis oocytes)
CC {ECO:0000269|PubMed:17932225};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:17932225}; Multi-
CC pass membrane protein {ECO:0000269|PubMed:17932225}. Apical cell
CC membrane {ECO:0000269|PubMed:17932225}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:17932225}. Note=Located on apical membrane of
CC enterocytes. {ECO:0000269|PubMed:17932225}.
CC -!- TISSUE SPECIFICITY: Expressed in kidney and small intestine.
CC {ECO:0000269|PubMed:17932225}.
CC -!- SIMILARITY: Belongs to the sodium:solute symporter (SSF) (TC 2.A.21)
CC family. {ECO:0000255}.
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DR EMBL; AABR03003549; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03010317; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03003744; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03007524; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; U47673; AAD10832.1; -; mRNA.
DR RefSeq; NP_001093952.2; NM_001100482.2.
DR AlphaFoldDB; Q9Z1F2; -.
DR SMR; Q9Z1F2; -.
DR STRING; 10116.ENSRNOP00000060635; -.
DR PaxDb; Q9Z1F2; -.
DR GeneID; 252854; -.
DR KEGG; rno:252854; -.
DR UCSC; RGD:621410; rat.
DR CTD; 115584; -.
DR RGD; 621410; Slc5a11.
DR eggNOG; KOG2349; Eukaryota.
DR InParanoid; Q9Z1F2; -.
DR PhylomeDB; Q9Z1F2; -.
DR Reactome; R-RNO-429593; Inositol transporters.
DR PRO; PR:Q9Z1F2; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005412; F:glucose:sodium symporter activity; IBA:GO_Central.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0032409; P:regulation of transporter activity; ISO:RGD.
DR Gene3D; 1.20.1730.10; -; 1.
DR InterPro; IPR038377; Na/Glc_symporter_sf.
DR InterPro; IPR001734; Na/solute_symporter.
DR Pfam; PF00474; SSF; 1.
DR TIGRFAMs; TIGR00813; sss; 1.
DR PROSITE; PS50283; NA_SOLUT_SYMP_3; 1.
PE 1: Evidence at protein level;
KW Apoptosis; Cell membrane; Ion transport; Membrane; Reference proteome;
KW Sodium; Sodium transport; Sugar transport; Symport; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..673
FT /note="Sodium/myo-inositol cotransporter 2"
FT /id="PRO_0000331570"
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..56
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 57..77
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 78
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 79..99
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 100..102
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 103..123
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 124..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..652
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 653..673
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CONFLICT 133
FT /note="K -> R (in Ref. 2; AAD10832)"
FT /evidence="ECO:0000305"
FT CONFLICT 142
FT /note="P -> A (in Ref. 2; AAD10832)"
FT /evidence="ECO:0000305"
FT CONFLICT 147..159
FT /note="SIYPSTHSLTILQ -> VLYLFIYIFTKIS (in Ref. 2;
FT AAD10832)"
FT /evidence="ECO:0000305"
FT CONFLICT 166
FT /note="A -> G (in Ref. 2; AAD10832)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 673 AA; 73605 MW; 0C4518CDD80099A7 CRC64;
MESTTSSPQP PPSDALEAFP QKSMEPADIV VLVLYFLFVL AVGLWSTVRT KRDTVKGYFL
AGGDMVWWPV GASLFASNVG SGHFIGLAGS GAAVGISVAA YELNGLFSVL MLAWIFLPIY
IAGQVTTMPE YLKRRFGGSR IPITLASIYP STHSLTILQV DMYAGAIFIQ QSLHLDLYLA
IVGLLAVTAL YTVAGGLAAV IYTDALQTVI MLIGAFILMG YSFAAVGGME GLKDQYFLAL
ASNRSENSSC GLPREDAFHI FRDPLTSDLP WPGILFGMSI PSLWYWCTDQ VIVQRSLAAK
NLSHAKGGSL MAAYLKVLPL FLMVFPGMVS RILFPDQVAC AHPDICQRVC SNPSGCSDIA
YPKLVLELLP TGLRGLMMAV MVAALMSSLT SIFNSASTIF TMDLWHHIRP RASERELMIV
GRVFVLALVL VSILWIPVVQ ASQGGQLFIY IQSISSYLQP PVAVVFIMGC FWKRTNEKGA
FSGLILGLLL GLVRLILDFV YVQPRCDQPD DRPAVVKDVH YLYFSMILSS TTLITVFTVS
WFTETPSKEM VSRLTWFTRH EPVAQKDSVP PENPLSLTIS QNGTTEATGI SIQLESVQEA
TTKAHSDGVS PKQSKVLKAI LWLCGMEKDK EEPPSKVEPV IVSLEENPLV KTLLDVNCIV
CISCAIFLWG YFA
