SC5AB_PIG
ID SC5AB_PIG Reviewed; 674 AA.
AC A8I1B9;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 1.
DT 03-AUG-2022, entry version 51.
DE RecName: Full=Sodium/myo-inositol cotransporter 2;
DE Short=Na(+)/myo-inositol cotransporter 2;
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|EMBL:ABV71386.1};
GN Synonyms=SMIT2 {ECO:0000303|Ref.1};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1] {ECO:0000312|EMBL:ABV71386.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Coady M.J., Bissonnette P., Wallendorff B., Lapointe J.-Y.;
RT "The Na+/myo-inositol cotransporters SMIT1 and SMIT2 are not regulated by
RT tonicity in the renal cell line LLC-PK1.";
RL Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases.
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 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q28728}; Multi-
CC pass membrane protein {ECO:0000250|UniProtKB:Q28728}.
CC -!- SIMILARITY: Belongs to the sodium:solute symporter (SSF) (TC 2.A.21)
CC family. {ECO:0000255}.
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DR EMBL; EU152406; ABV71386.1; -; mRNA.
DR RefSeq; NP_001103892.1; NM_001110422.1.
DR AlphaFoldDB; A8I1B9; -.
DR SMR; A8I1B9; -.
DR PRIDE; A8I1B9; -.
DR GeneID; 100126275; -.
DR KEGG; ssc:100126275; -.
DR CTD; 115584; -.
DR InParanoid; A8I1B9; -.
DR OrthoDB; 243316at2759; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0015293; F:symporter activity; IEA:UniProtKB-KW.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0008643; P:carbohydrate transport; IEA:UniProtKB-KW.
DR GO; GO:0006814; P:sodium ion transport; IEA:UniProtKB-KW.
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 2: Evidence at transcript level;
KW Apoptosis; Ion transport; Membrane; Reference proteome; Sodium;
KW Sodium transport; Sugar transport; Symport; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..674
FT /note="Sodium/myo-inositol cotransporter 2"
FT /id="PRO_0000331572"
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..102
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 103..123
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 124..140
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 141..161
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 162..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..374
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 375..397
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 398..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..518
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 519..539
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 540..653
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 654..674
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 674 AA; 73881 MW; 1D8EB7D520C26989 CRC64;
MESSPSSPQP TQSDPLAVFP QRTLEPADIA VLVLYFLFVL AVGLWSTVKT RRDTVKGYFL
AGGDMVWWPV GASLFASNVG SGHFVGLAGS GAAAGLSVTA YEFNGIFSVL MLAWIFLPIY
IAGQVTTMPE YLRKRFGGSR IPITLAVLYL FIYIFTKISV DMYAGAIFIQ QSLHLNLYLA
IVGLLAITAL YTIAGGLAAV IYTDALQTLI MLIGALTLMG YSFAAVGGME GLKEKYFLAL
ASNRSGNSSC GLPREDAFHI FRDPLTSDLP WPGILFGMSI PSLWYWCTDQ VIVQRTLAAK
NLSHAKGGSL MAAYLKVLPL FIMVFPGMVS RVLFPDQVAC ADPEICQKVC SNPAGCSDIA
YPKLVLELLP MGLRGLMMAV MVAALMSSLT SIFNSASTIF TMDLWNHLRP RASERELMIV
GRVFVLLLVL VSILWIPVVQ ASQGGQLFIY IQSISSYLQP PVAVVFIMGC FWKRTNEKGA
FSGLILGLLL GLVRLVLDFI YPQPRCDQPD ERPAVVRDVH YLYFSMILSS VTLVTVSTVS
WCTAPPTQEM VSRLTWFTRH DPIVLKEQVP SATPVPVTVS QNGTPEASST NIQFEIVQEN
TSKTHSCDMT KKQSKVVKTI LWLCGMESKG KEEPPSRADP VIVSLEEIPL VKTLLDINLI
VCISCAIFLW GYFA
