MYCT_MOUSE
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 03-AUG-2022, entry version 133.
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 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 IntAct; Q3UHK1; 1.
DR STRING; 10090.ENSMUSP00000104906; -.
DR GlyGen; Q3UHK1; 3 sites.
DR iPTMnet; Q3UHK1; -.
DR PhosphoSitePlus; Q3UHK1; -.
DR SwissPalm; Q3UHK1; -.
DR jPOST; Q3UHK1; -.
DR MaxQB; Q3UHK1; -.
DR PaxDb; Q3UHK1; -.
DR PeptideAtlas; Q3UHK1; -.
DR PRIDE; Q3UHK1; -.
DR ProteomicsDB; 287651; -.
DR Antibodypedia; 1512; 117 antibodies from 22 providers.
DR DNASU; 239606; -.
DR Ensembl; ENSMUST00000109283; ENSMUSP00000104906; ENSMUSG00000036298.
DR GeneID; 239606; -.
DR KEGG; mmu:239606; -.
DR UCSC; uc007xhy.2; mouse.
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; WAITASF; -.
DR OrthoDB; 326501at2759; -.
DR PhylomeDB; Q3UHK1; -.
DR TreeFam; TF314916; -.
DR Reactome; R-MMU-429593; Inositol transporters.
DR BioGRID-ORCS; 239606; 2 hits in 72 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 211 other tissues.
DR Genevisible; Q3UHK1; MM.
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:0005887; C:integral component of plasma membrane; 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: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:0022857; F:transmembrane transporter activity; IBA:GO_Central.
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 Gene3D; 1.20.1250.20; -; 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 Pfam; PF00083; Sugar_tr; 2.
DR PRINTS; PR00171; SUGRTRNSPORT.
DR SUPFAM; SSF103473; SSF103473; 2.
DR TIGRFAMs; TIGR00879; SP; 1.
DR PROSITE; PS50850; MFS; 1.
DR PROSITE; PS00216; SUGAR_TRANSPORT_1; 1.
DR PROSITE; PS00217; SUGAR_TRANSPORT_2; 1.
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
