HMT13_CAEEL
ID HMT13_CAEEL Reviewed; 604 AA.
AC Q21455;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 3.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Proton myo-inositol cotransporter hmit-1.3 {ECO:0000305};
DE Short=H(+)-myo-inositol cotransporter hmit-1.3 {ECO:0000312|WormBase:M01F1.5};
DE AltName: Full=H(+)-myo-inositol symporter hmit-1.3 {ECO:0000250|UniProtKB:Q96QE2};
GN Name=hmit-1.3 {ECO:0000312|WormBase:M01F1.5};
GN ORFNames=M01F1.5 {ECO:0000312|WormBase:M01F1.5};
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, AND TISSUE SPECIFICITY.
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.
CC {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:0000269|PubMed:21679696};
CC Multi-pass membrane protein {ECO:0000255}. Perikaryon
CC {ECO:0000269|PubMed:21679696}. Note=Localizes to the endfoot region of
CC glial cells where the cilia of sensory neurons are embedded.
CC {ECO:0000269|PubMed:21679696}.
CC -!- TISSUE SPECIFICITY: Expressed in the intestine and sheath glial cells.
CC {ECO:0000269|PubMed:21679696}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. Sugar
CC transporter (TC 2.A.1.1) family. {ECO:0000255,
CC ECO:0000255|RuleBase:RU003346}.
CC -!- CAUTION: In contrast to family members hmit-1.1 and hmit-1.2, it is not
CC induced by hyperosmotic stress. {ECO:0000269|PubMed:21679696}.
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DR EMBL; BX284603; CAA86519.2; -; Genomic_DNA.
DR PIR; T23658; T23658.
DR RefSeq; NP_497725.2; NM_065324.3.
DR AlphaFoldDB; Q21455; -.
DR SMR; Q21455; -.
DR STRING; 6239.M01F1.5.1; -.
DR EPD; Q21455; -.
DR PaxDb; Q21455; -.
DR EnsemblMetazoa; M01F1.5.1; M01F1.5.1; WBGene00010811.
DR EnsemblMetazoa; M01F1.5.2; M01F1.5.2; WBGene00010811.
DR GeneID; 175458; -.
DR KEGG; cel:CELE_M01F1.5; -.
DR UCSC; M01F1.5.1; c. elegans.
DR CTD; 175458; -.
DR WormBase; M01F1.5; CE33672; WBGene00010811; hmit-1.3.
DR eggNOG; KOG0254; Eukaryota.
DR GeneTree; ENSGT00970000196599; -.
DR HOGENOM; CLU_001265_30_5_1; -.
DR InParanoid; Q21455; -.
DR OMA; SNCDFCV; -.
DR OrthoDB; 326501at2759; -.
DR PhylomeDB; Q21455; -.
DR Reactome; R-CEL-429593; Inositol transporters.
DR PRO; PR:Q21455; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00010811; Expressed in material anatomical entity and 4 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:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
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 TIGRFAMs; TIGR00879; SP; 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..604
FT /note="Proton myo-inositol cotransporter hmit-1.3"
FT /id="PRO_0000450213"
FT TOPO_DOM 1..23
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 24..44
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 45..71
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 72..92
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 93..99
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 100..120
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 121
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 122..142
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 143..157
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 158..178
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 179..191
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 192..212
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 213..281
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 282..302
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 303..320
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 321..341
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 342..351
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 352..372
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 373..468
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 469..489
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TOPO_DOM 490..505
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 506..526
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255"
FT TOPO_DOM 527..535
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 536..556
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255"
FT TOPO_DOM 557..604
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 58
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 317
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 374
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 384
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 448
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 452
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 604 AA; 66562 MW; 68C0A3794246F084 CRC64;
MVQVAPVAAG AGSGQTRPSS DPKTGWFVYM LAFSAVIGGF LFGYDTGIVS AAMLYVPNAS
GIKPLDSVWQ EIIVSITPGV AAIGSLCSGP GSDFLGRKKI IIGASVTFTI GAIICAAAWT
KIILLIGRIL LGLAIGFASM IVPIYVSEAS PSHIRGKLVT GFQLMITVGL VIANIIGGAF
SYVDPDQVGW RLMFAFAAVP AIIQFVCFLF LPESPRWLYE HGRTVEAREV LTRIYNGHTE
WVDYEINEIS FSYEEELRAK AEHAGNGPTI IRILKTPHVR KAMIIGSLLQ MFQQLSGINT
VMYYTGNIIR SAGVKDNHTT IWISVGTSAI NFLGTFIPIA LVERVGRRVL LLVSMIGVIL
FLIAMGVSFL LINNDSLRTF DQQNYTLNYN PSVKHAAKCL KYSNCDFCVT DENCGFCESK
VAKKGYCLPF PSDDSSDYSA TGICEFSNLT NNGTDFEWED TYCHTKFTVL PIIIMVFYLL
SFSAGYAPLP WVLNAEFYPL WARSTAVSVS TACNWIFNLI VSLTFLSLSQ AATKYGTFFI
YCGCTMVALV FVFFFVPETK GYSIDEVEML FMTKEERRKA QKVLDESKEG KHRNSVAMSF
DTKF
