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2.A.1.1.25
Myoinositol:H+ symporter, HMIT (also transport other inositols including scyllo-, muco- and chiro-, but not allo-inositol) (Aouameur et al., 2007). Expressed in the Golgi of the hippocampus and cortex. May also transport inositoltriphosphate (Di Daniel et al., 2009). Interacts directly with γ-secretase (9.B.47.1.1) to regulate its activity and the production of Abeta production, important in Alzheimer's disease (Teranishi et al. 2015).

Accession Number:Q96QE2
Protein Name:HMIT aka SLC2A13
Length:648
Molecular Weight:70371.00
Species:Homo sapiens [9606]
Number of TMSs:12
Location1 / Topology2 / Orientation3: Membrane1 / Multi-pass membrane protein2
Substrate Myoinositol, H+, Inositol

Cross database links:

Genevestigator: Q96QE2 Q96QE2
eggNOG: prNOG08334 COG0477
HEGENOM: HBG744444 HOG000202868
RefSeq: NP_443117.3   
Entrez Gene ID: 114134   
Pfam: PF00083   
OMIM: 611036  gene
KEGG: hsa:114134    hsa:114134   

Gene Ontology

GO:0016021 C:integral to membrane
GO:0005886 C:plasma membrane
GO:0005366 F:myo-inositol:hydrogen symporter activity
GO:0055085 P:transmembrane transport
GO:0022891 F:substrate-specific transmembrane transporter activity

References (8)

[1] “Identification of a mammalian H(+)-myo-inositol symporter expressed predominantly in the brain.”  Uldry M.et.al.   11500374
[2] “The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).”  The MGC Project Teamet.al.   15489334
[3] “Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.”  Olsen J.V.et.al.   17081983
[4] “Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.”  Gauci S.et.al.   19413330
[5] “Identification of a mammalian H(+)-myo-inositol symporter expressed predominantly in the brain.”  Uldry M.et.al.   11500374
[6] “The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).”  The MGC Project Teamet.al.   15489334
[7] “Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.”  Olsen J.V.et.al.   17081983
[8] “Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.”  Gauci S.et.al.   19413330

External Searches:

  • Search: DB with
  • BLAST ExPASy (Swiss Institute of Bioinformatics (SIB) BLAST)
  • CDD Search (Conserved Domain Database)
  • Search COGs (Clusters of Orthologous Groups of proteins)
  • 2° Structure (Network Protein Sequence Analysis)

Analyze:

Predict TMSs (Predict number of transmembrane segments)
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FASTA formatted sequence
1:	MSRKASENVE YTLRSLSSLM GERRRKQPEP DAASAAGECS LLAAAESSTS LQSAGAGGGG 
61:	VGDLERAARR QFQQDETPAF VYVVAVFSAL GGFLFGYDTG VVSGAMLLLK RQLSLDALWQ 
121:	ELLVSSTVGA AAVSALAGGA LNGVFGRRAA ILLASALFTA GSAVLAAANN KETLLAGRLV 
181:	VGLGIGIASM TVPVYIAEVS PPNLRGRLVT INTLFITGGQ FFASVVDGAF SYLQKDGWRY 
241:	MLGLAAVPAV IQFFGFLFLP ESPRWLIQKG QTQKARRILS QMRGNQTIDE EYDSIKNNIE 
301:	EEEKEVGSAG PVICRMLSYP PTRRALIVGC GLQMFQQLSG INTIMYYSAT ILQMSGVEDD 
361:	RLAIWLASVT AFTNFIFTLV GVWLVEKVGR RKLTFGSLAG TTVALIILAL GFVLSAQVSP 
421:	RITFKPIAPS GQNATCTRYS YCNECMLDPD CGFCYKMNKS TVIDSSCVPV NKASTNEAAW 
481:	GRCENETKFK TEDIFWAYNF CPTPYSWTAL LGLILYLVFF APGMGPMPWT VNSEIYPLWA 
541:	RSTGNACSSG INWIFNVLVS LTFLHTAEYL TYYGAFFLYA GFAAVGLLFI YGCLPETKGK 
601:	KLEEIESLFD NRLCTCGTSD SDEGRYIEYI RVKGSNYHLS DNDASDVE