HMT11_CAEEL
ID HMT11_CAEEL Reviewed; 606 AA.
AC Q9XXR3;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Proton myo-inositol cotransporter hmit-1.1 {ECO:0000305};
DE Short=H(+)-myo-inositol cotransporter hmit-1.1 {ECO:0000312|WormBase:Y51A2D.4};
DE AltName: Full=H(+)-myo-inositol symporter hmit-1.1 {ECO:0000250|UniProtKB:Q96QE2};
GN Name=hmit-1.1 {ECO:0000312|WormBase:Y51A2D.4};
GN ORFNames=Y51A2D.4 {ECO:0000312|WormBase:Y51A2D.4};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND 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).
CC -!- FUNCTION: H(+)-myo-inositol cotransporter (By similarity). Probably by
CC promoting the transport of myo-inositol regulates intracellular osmosis
CC in response to hyperosmotic stress (PubMed:21679696).
CC {ECO:0000250|UniProtKB:Q96QE2, ECO:0000269|PubMed:21679696}.
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:0000269|PubMed:21679696};
CC Multi-pass membrane protein {ECO:0000255}. Note=Localizes to the
CC lumenal side of intestinal cells. {ECO:0000269|PubMed:21679696}.
CC -!- TISSUE SPECIFICITY: Expressed in the intestine.
CC {ECO:0000269|PubMed:21679696}.
CC -!- INDUCTION: Induced by hyperosmotic stress.
CC {ECO:0000269|PubMed:21679696}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. Sugar
CC transporter (TC 2.A.1.1) family. {ECO:0000255}.
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DR EMBL; BX284605; CAA16400.1; -; Genomic_DNA.
DR PIR; T27072; T27072.
DR RefSeq; NP_507623.1; NM_075222.4.
DR AlphaFoldDB; Q9XXR3; -.
DR SMR; Q9XXR3; -.
DR IntAct; Q9XXR3; 1.
DR STRING; 6239.Y51A2D.4; -.
DR EPD; Q9XXR3; -.
DR PaxDb; Q9XXR3; -.
DR EnsemblMetazoa; Y51A2D.4.1; Y51A2D.4.1; WBGene00013073.
DR GeneID; 180205; -.
DR KEGG; cel:CELE_Y51A2D.4; -.
DR UCSC; Y51A2D.4; c. elegans.
DR CTD; 180205; -.
DR WormBase; Y51A2D.4; CE19201; WBGene00013073; hmit-1.1.
DR eggNOG; KOG0254; Eukaryota.
DR HOGENOM; CLU_001265_30_5_1; -.
DR InParanoid; Q9XXR3; -.
DR OMA; PECGFCA; -.
DR OrthoDB; 430696at2759; -.
DR PhylomeDB; Q9XXR3; -.
DR PRO; PR:Q9XXR3; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00013073; Expressed in larva and 2 other tissues.
DR GO; GO:0016324; C:apical plasma membrane; IDA:WormBase.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005366; F:myo-inositol:proton symporter activity; IBA:GO_Central.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015798; P:myo-inositol transport; IBA:GO_Central.
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; 1.
DR PROSITE; PS50850; MFS; 1.
DR PROSITE; PS00216; SUGAR_TRANSPORT_1; 1.
DR PROSITE; PS00217; SUGAR_TRANSPORT_2; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Glycoprotein; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..606
FT /note="Proton myo-inositol cotransporter hmit-1.1"
FT /id="PRO_0000450211"
FT TOPO_DOM 1..20
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 21..41
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 42..63
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 64..84
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 85..96
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 97..117
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 118
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 119..139
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 140..152
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 153..173
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 174..188
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 189..209
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 210..278
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 279..299
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 300..317
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 318..338
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 339..345
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 346..366
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 367..464
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 465..485
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TOPO_DOM 486..501
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 502..522
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255"
FT TOPO_DOM 523..531
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 532..552
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255"
FT TOPO_DOM 553..606
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT CARBOHYD 314
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 387
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 445
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 606 AA; 66658 MW; 5A217A21AF87B501 CRC64;
MVAVAAFSSS GQDKPAHTPK LGLFVYILAA ASVIGGFLFG YDTSVVSAAM LYMPDAPGLK
PMDTVWQEVL VSISPGMAAV GSLMSGTSSD YIGRRKVILG ASAIFTIGAL VCAASVNKIM
LLVGRVLLGI AIGFASMIVP VYLGETAPTH VRGMLVAAFA LMISFGQVVA NITGGAFSYI
DPYNVGWRLM FAFAAVPSII QFVCFMFLPE TPRWLYENGF ETETREVLEK VYNGDKEWVE
YEMAEIIAFN EDQAKENEKA HASGPVIWRI LKTPHVLKAC FIGSMLQAFQ QLAGINTILY
YTADIIRSSG ISNNHTTIWI SVLLSLCNFI GPFVPMSLIE KVGRRIIFLF SCGLVVLSLV
FIGVAFLLVN HDSAATLPAN QYGSNFNSSY PDAKGCMAYS NCDYCVTTDA CGFCHDANTK
QGYCLPAGFD NPEVYSSTGS CTNSNGSIAN NFKWEKYYCD TKYTLLPIIA CGVYLLTFSS
GFTSLPWVLN SEFYPMWARS TCVAISTTSN WVFNLIIALT YLSLTQVIGK YGAFWLYAGL
TVIAFIFILF LVPETKGYSI EEVEMLFMNK KQRREAESRR RETVTEVRSR MNSTVSFGQH
NEVHKY
