MYCT_HUMAN
ID MYCT_HUMAN Reviewed; 648 AA.
AC Q96QE2; Q17S07;
DT 16-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 3.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Proton myo-inositol cotransporter {ECO:0000305};
DE Short=H(+)-myo-inositol cotransporter {ECO:0000303|PubMed:11500374};
DE Short=Hmit {ECO:0000303|PubMed:11500374};
DE AltName: Full=H(+)-myo-inositol symporter {ECO:0000303|PubMed:11500374};
DE AltName: Full=Solute carrier family 2 member 13;
GN Name=SLC2A13 {ECO:0000312|HGNC:HGNC:15956};
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]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TRANSPORTER ACTIVITY, SUBCELLULAR
RP LOCATION, GLYCOSYLATION, AND TISSUE SPECIFICITY.
RX PubMed=11500374; DOI=10.1093/emboj/20.16.4467;
RA Uldry M., Ibberson M., Horisberger J.-D., Chatton J.-Y., Riederer B.M.,
RA Thorens B.;
RT "Identification of a mammalian H(+)-myo-inositol symporter expressed
RT predominantly in the brain.";
RL EMBO J. 20:4467-4477(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3-648.
RC TISSUE=Brain;
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-640 AND SER-645, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-640 AND SER-645, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [6]
RP INDUCTION.
RX PubMed=21679696; DOI=10.1016/j.bbrc.2011.06.001;
RA Kage-Nakadai E., Uehara T., Mitani S.;
RT "H+/myo-inositol transporter genes, hmit-1.1 and hmit-1.2, have roles in
RT the osmoprotective response in Caenorhabditis elegans.";
RL Biochem. Biophys. Res. Commun. 410:471-477(2011).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-645, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-645, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- FUNCTION: H(+)-myo-inositol cotransporter (PubMed:11500374). Can also
CC transport related stereoisomers (PubMed:11500374).
CC {ECO:0000269|PubMed:11500374}.
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:0000269|PubMed:11500374};
CC -!- INTERACTION:
CC Q96QE2; P78329: CYP4F2; NbExp=3; IntAct=EBI-18082698, EBI-1752413;
CC Q96QE2; Q96CV9: OPTN; NbExp=3; IntAct=EBI-18082698, EBI-748974;
CC Q96QE2; Q04941: PLP2; NbExp=3; IntAct=EBI-18082698, EBI-608347;
CC Q96QE2; Q9NPQ8-4: RIC8A; NbExp=3; IntAct=EBI-18082698, EBI-9091816;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11500374};
CC Multi-pass membrane protein {ECO:0000269|PubMed:11500374}.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in the brain.
CC {ECO:0000269|PubMed:11500374}.
CC -!- INDUCTION: Induced by hyperosmotic stress.
CC {ECO:0000269|PubMed:21679696}.
CC -!- PTM: Glycosylated. {ECO:0000269|PubMed:11500374}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. Sugar
CC transporter (TC 2.A.1.1) family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI17118.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAI17120.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAC51116.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AJ315644; CAC51116.1; ALT_INIT; mRNA.
DR EMBL; BC117117; AAI17118.1; ALT_INIT; mRNA.
DR EMBL; BC117119; AAI17120.1; ALT_INIT; mRNA.
DR CCDS; CCDS8736.2; -.
DR RefSeq; NP_443117.3; NM_052885.3.
DR AlphaFoldDB; Q96QE2; -.
DR SMR; Q96QE2; -.
DR BioGRID; 125286; 12.
DR IntAct; Q96QE2; 5.
DR STRING; 9606.ENSP00000280871; -.
DR TCDB; 2.A.1.1.25; the major facilitator superfamily (mfs).
DR GlyGen; Q96QE2; 4 sites.
DR iPTMnet; Q96QE2; -.
DR PhosphoSitePlus; Q96QE2; -.
DR SwissPalm; Q96QE2; -.
DR BioMuta; SLC2A13; -.
DR DMDM; 294862502; -.
DR EPD; Q96QE2; -.
DR jPOST; Q96QE2; -.
DR MassIVE; Q96QE2; -.
DR MaxQB; Q96QE2; -.
DR PaxDb; Q96QE2; -.
DR PeptideAtlas; Q96QE2; -.
DR PRIDE; Q96QE2; -.
DR ProteomicsDB; 77861; -.
DR Antibodypedia; 1512; 117 antibodies from 22 providers.
DR DNASU; 114134; -.
DR Ensembl; ENST00000280871.9; ENSP00000280871.4; ENSG00000151229.13.
DR GeneID; 114134; -.
DR KEGG; hsa:114134; -.
DR MANE-Select; ENST00000280871.9; ENSP00000280871.4; NM_052885.4; NP_443117.3.
DR UCSC; uc010skm.2; human.
DR CTD; 114134; -.
DR DisGeNET; 114134; -.
DR GeneCards; SLC2A13; -.
DR HGNC; HGNC:15956; SLC2A13.
DR HPA; ENSG00000151229; Tissue enhanced (parathyroid).
DR MIM; 611036; gene.
DR neXtProt; NX_Q96QE2; -.
DR OpenTargets; ENSG00000151229; -.
DR PharmGKB; PA38066; -.
DR VEuPathDB; HostDB:ENSG00000151229; -.
DR eggNOG; KOG0254; Eukaryota.
DR GeneTree; ENSGT00940000155870; -.
DR HOGENOM; CLU_001265_30_5_1; -.
DR InParanoid; Q96QE2; -.
DR OMA; WAITASF; -.
DR OrthoDB; 326501at2759; -.
DR PhylomeDB; Q96QE2; -.
DR TreeFam; TF314916; -.
DR PathwayCommons; Q96QE2; -.
DR Reactome; R-HSA-429593; Inositol transporters.
DR SignaLink; Q96QE2; -.
DR BioGRID-ORCS; 114134; 16 hits in 1089 CRISPR screens.
DR ChiTaRS; SLC2A13; human.
DR GeneWiki; SLC2A13; -.
DR GenomeRNAi; 114134; -.
DR Pharos; Q96QE2; Tbio.
DR PRO; PR:Q96QE2; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q96QE2; protein.
DR Bgee; ENSG00000151229; Expressed in lateral nuclear group of thalamus and 180 other tissues.
DR ExpressionAtlas; Q96QE2; baseline and differential.
DR Genevisible; Q96QE2; HS.
DR GO; GO:0016324; C:apical plasma membrane; IBA:GO_Central.
DR GO; GO:0097450; C:astrocyte end-foot; ISS:ARUK-UCL.
DR GO; GO:0044297; C:cell body; IDA:ARUK-UCL.
DR GO; GO:0071944; C:cell periphery; IDA:ARUK-UCL.
DR GO; GO:0042995; C:cell projection; IDA:ARUK-UCL.
DR GO; GO:0005737; C:cytoplasm; ISS:ARUK-UCL.
DR GO; GO:0030426; C:growth cone; ISS:ARUK-UCL.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISS:ARUK-UCL.
DR GO; GO:0016020; C:membrane; ISS:ARUK-UCL.
DR GO; GO:0031090; C:organelle membrane; ISS:ARUK-UCL.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0051117; F:ATPase binding; IPI:ARUK-UCL.
DR GO; GO:0005365; F:myo-inositol transmembrane transporter activity; ISS:ARUK-UCL.
DR GO; GO:0005366; F:myo-inositol:proton symporter activity; IDA:UniProtKB.
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; IDA:UniProtKB.
DR GO; GO:1902004; P:positive regulation of amyloid-beta formation; IGI:ARUK-UCL.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR GO; GO:0150104; P:transport across blood-brain barrier; NAS:ARUK-UCL.
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..648
FT /note="Proton myo-inositol cotransporter"
FT /id="PRO_0000050456"
FT TOPO_DOM 1..76
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 77..97
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 98..125
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 126..146
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 147..148
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 149..169
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 170..178
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 179..199
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 200..212
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 213..233
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 234..239
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 240..260
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 261..324
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 325..345
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 346..363
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 364..384
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 385..393
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 394..414
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 415..508
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 509..529
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TOPO_DOM 530..549
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 550..570
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255"
FT TOPO_DOM 571..573
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 574..594
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255"
FT TOPO_DOM 595..648
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOD_RES 6
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3UHK1"
FT MOD_RES 47
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3UHK1"
FT MOD_RES 50
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3UHK1"
FT MOD_RES 640
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 645
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT CARBOHYD 433
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 458
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 485
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 648 AA; 70371 MW; 07B951E20A7F46EB CRC64;
MSRKASENVE YTLRSLSSLM GERRRKQPEP DAASAAGECS LLAAAESSTS LQSAGAGGGG
VGDLERAARR QFQQDETPAF VYVVAVFSAL GGFLFGYDTG VVSGAMLLLK RQLSLDALWQ
ELLVSSTVGA AAVSALAGGA LNGVFGRRAA ILLASALFTA GSAVLAAANN KETLLAGRLV
VGLGIGIASM TVPVYIAEVS PPNLRGRLVT INTLFITGGQ FFASVVDGAF SYLQKDGWRY
MLGLAAVPAV IQFFGFLFLP ESPRWLIQKG QTQKARRILS QMRGNQTIDE EYDSIKNNIE
EEEKEVGSAG PVICRMLSYP PTRRALIVGC GLQMFQQLSG INTIMYYSAT ILQMSGVEDD
RLAIWLASVT AFTNFIFTLV GVWLVEKVGR RKLTFGSLAG TTVALIILAL GFVLSAQVSP
RITFKPIAPS GQNATCTRYS YCNECMLDPD CGFCYKMNKS TVIDSSCVPV NKASTNEAAW
GRCENETKFK TEDIFWAYNF CPTPYSWTAL LGLILYLVFF APGMGPMPWT VNSEIYPLWA
RSTGNACSSG INWIFNVLVS LTFLHTAEYL TYYGAFFLYA GFAAVGLLFI YGCLPETKGK
KLEEIESLFD NRLCTCGTSD SDEGRYIEYI RVKGSNYHLS DNDASDVE
