ID   MYCT_MOUSE              Reviewed;         637 AA.
AC   Q3UHK1;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   20-APR-2010, sequence version 2.
DT   27-MAR-2024, entry version 142.
DE   RecName: Full=Proton myo-inositol cotransporter {ECO:0000305};
DE            Short=H(+)-myo-inositol cotransporter {ECO:0000250|UniProtKB:Q96QE2};
DE            Short=Hmit {ECO:0000250|UniProtKB:Q96QE2};
DE   AltName: Full=H(+)-myo-inositol symporter {ECO:0000250|UniProtKB:Q96QE2};
DE   AltName: Full=Solute carrier family 2 member 13;
GN   Name=Slc2a13 {ECO:0000312|MGI:MGI:2146030};
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6; SER-44; SER-47; SER-629
RP   AND SER-634, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Kidney, Lung, Pancreas, and
RC   Spleen;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: H(+)-myo-inositol cotransporter. Can also transport related
CC       stereoisomers. {ECO:0000250|UniProtKB:Q96QE2}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+)(out) + myo-inositol(out) = H(+)(in) + myo-inositol(in);
CC         Xref=Rhea:RHEA:60364, ChEBI:CHEBI:15378, ChEBI:CHEBI:17268;
CC         Evidence={ECO:0000250|UniProtKB:Q96QE2};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q96QE2};
CC       Multi-pass membrane protein {ECO:0000250|UniProtKB:Q96QE2}.
CC   -!- SIMILARITY: Belongs to the major facilitator superfamily. Sugar
CC       transporter (TC 2.A.1.1) family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAE27856.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AK147341; BAE27856.1; ALT_INIT; mRNA.
DR   CCDS; CCDS27761.2; -.
DR   RefSeq; NP_001028805.2; NM_001033633.3.
DR   AlphaFoldDB; Q3UHK1; -.
DR   SMR; Q3UHK1; -.
DR   BioGRID; 232105; 1.
DR   IntAct; Q3UHK1; 1.
DR   STRING; 10090.ENSMUSP00000104906; -.
DR   GlyCosmos; Q3UHK1; 3 sites, No reported glycans.
DR   GlyGen; Q3UHK1; 3 sites.
DR   iPTMnet; Q3UHK1; -.
DR   PhosphoSitePlus; Q3UHK1; -.
DR   SwissPalm; Q3UHK1; -.
DR   jPOST; Q3UHK1; -.
DR   MaxQB; Q3UHK1; -.
DR   PaxDb; 10090-ENSMUSP00000104906; -.
DR   PeptideAtlas; Q3UHK1; -.
DR   ProteomicsDB; 287651; -.
DR   Pumba; Q3UHK1; -.
DR   Antibodypedia; 1512; 138 antibodies from 22 providers.
DR   DNASU; 239606; -.
DR   Ensembl; ENSMUST00000109283.2; ENSMUSP00000104906.2; ENSMUSG00000036298.11.
DR   GeneID; 239606; -.
DR   KEGG; mmu:239606; -.
DR   UCSC; uc007xhy.2; mouse.
DR   AGR; MGI:2146030; -.
DR   CTD; 114134; -.
DR   MGI; MGI:2146030; Slc2a13.
DR   VEuPathDB; HostDB:ENSMUSG00000036298; -.
DR   eggNOG; KOG0254; Eukaryota.
DR   GeneTree; ENSGT00940000155870; -.
DR   HOGENOM; CLU_001265_30_5_1; -.
DR   InParanoid; Q3UHK1; -.
DR   OMA; ETGWRWM; -.
DR   OrthoDB; 2013244at2759; -.
DR   PhylomeDB; Q3UHK1; -.
DR   TreeFam; TF314916; -.
DR   Reactome; R-MMU-429593; Inositol transporters.
DR   BioGRID-ORCS; 239606; 2 hits in 77 CRISPR screens.
DR   ChiTaRS; Slc2a13; mouse.
DR   PRO; PR:Q3UHK1; -.
DR   Proteomes; UP000000589; Chromosome 15.
DR   RNAct; Q3UHK1; Protein.
DR   Bgee; ENSMUSG00000036298; Expressed in olfactory tubercle and 212 other cell types or tissues.
DR   GO; GO:0016324; C:apical plasma membrane; IBA:GO_Central.
DR   GO; GO:0097450; C:astrocyte end-foot; ISO:MGI.
DR   GO; GO:0044297; C:cell body; ISO:MGI.
DR   GO; GO:0071944; C:cell periphery; ISO:MGI.
DR   GO; GO:0042995; C:cell projection; ISO:MGI.
DR   GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR   GO; GO:0030426; C:growth cone; ISO:MGI.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR   GO; GO:0016020; C:membrane; ISO:MGI.
DR   GO; GO:0031090; C:organelle membrane; IDA:ARUK-UCL.
DR   GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR   GO; GO:0051117; F:ATPase binding; ISO:MGI.
DR   GO; GO:0005365; F:myo-inositol transmembrane transporter activity; ISO:MGI.
DR   GO; GO:0005366; F:myo-inositol:proton symporter activity; ISO:MGI.
DR   GO; GO:0002020; F:protease binding; IPI:ARUK-UCL.
DR   GO; GO:0015798; P:myo-inositol transport; ISO:MGI.
DR   GO; GO:1902004; P:positive regulation of amyloid-beta formation; ISO:MGI.
DR   GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR   CDD; cd17360; MFS_HMIT_like; 1.
DR   Gene3D; 1.20.1250.20; MFS general substrate transporter like domains; 2.
DR   InterPro; IPR020846; MFS_dom.
DR   InterPro; IPR005828; MFS_sugar_transport-like.
DR   InterPro; IPR036259; MFS_trans_sf.
DR   InterPro; IPR003663; Sugar/inositol_transpt.
DR   InterPro; IPR005829; Sugar_transporter_CS.
DR   NCBIfam; TIGR00879; SP; 1.
DR   PANTHER; PTHR48020; PROTON MYO-INOSITOL COTRANSPORTER; 1.
DR   PANTHER; PTHR48020:SF47; PROTON MYO-INOSITOL COTRANSPORTER; 1.
DR   Pfam; PF00083; Sugar_tr; 2.
DR   PRINTS; PR00171; SUGRTRNSPORT.
DR   SUPFAM; SSF103473; MFS general substrate transporter; 2.
DR   PROSITE; PS50850; MFS; 1.
DR   PROSITE; PS00216; SUGAR_TRANSPORT_1; 1.
DR   PROSITE; PS00217; SUGAR_TRANSPORT_2; 1.
DR   Genevisible; Q3UHK1; MM.
PE   1: Evidence at protein level;
KW   Cell membrane; Glycoprotein; Membrane; Phosphoprotein; Reference proteome;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..637
FT                   /note="Proton myo-inositol cotransporter"
FT                   /id="PRO_0000261317"
FT   TOPO_DOM        1..65
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        66..86
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        87..114
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        115..135
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        136..137
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        138..158
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        159..167
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        168..188
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        189..201
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        202..222
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        223..228
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        229..249
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        250..313
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        314..334
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        335..352
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        353..373
FT                   /note="Helical; Name=8"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        374..382
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        383..403
FT                   /note="Helical; Name=9"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        404..497
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        498..518
FT                   /note="Helical; Name=10"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        519..538
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        539..559
FT                   /note="Helical; Name=11"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        560..562
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        563..583
FT                   /note="Helical; Name=12"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        584..637
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          15..38
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         6
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         44
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         47
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         629
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         634
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   CARBOHYD        422
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        447
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        474
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   637 AA;  69062 MW;  CF13253E46E934D2 CRC64;
     MSRKASEDVE YTLRSLSSLM GERRRRQPEP GAPGGERSLL AAESAASLQG AELERAARRQ
     FQRDETPAFV YAAAAFSALG GFLFGYDTGV VSGAMLLLRR QMRLGAMWQE LLVSGAVGAA
     AVAALAGGAL NGALGRRSAI LLASALCTVG SAVLAAAANK ETLLAGRLVV GLGIGIASMT
     VPVYIAEVSP PNLRGRLVTI NTLFITGGQF FASVVDGAFS YLQKDGWRYM LGLAAIPAVI
     QFLGFLFLPE SPRWLIQKGQ TQKARRILSQ MRGNQTIDEE YDSIRNSIEE EEKEATAAGP
     IICRMLSYPP TRRALVVGCG LQMFQQLSGI NTIMYYSATI LQMSGVEDDR LAIWLASITA
     FTNFIFTLVG VWLVEKVGRR KLTFGSLAGT TVALIILALG FLLSAQVSPR VTFRPTTPSD
     QNTTCTGYSY CNECMLDPDC GFCYKINGSA VIDSSCVPVN KASTTEAAWG RCDNETKFKA
     EGAHWAYSFC PTPYSWTALV GLVLYLVFFA PGMGPMPWTV NSEIYPLWAR STGNACSAGI
     NWIFNVLVSL TFLHTAEYLT YYGAFFLYAG FAAVGLLFVY GCLPETKGKK LEEIESLFDH
     RLCSCGAADS DEGRYIEYIR VKGSNYHLSD NDASDVE
//