HMT12_CAEEL
ID HMT12_CAEEL Reviewed; 613 AA.
AC Q9XXQ9;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Proton myo-inositol cotransporter hmit-1.2 {ECO:0000305};
DE Short=H(+)-myo-inositol cotransporter hmit-1.2 {ECO:0000312|WormBase:Y51A2D.5};
DE AltName: Full=H(+)-myo-inositol symporter hmit-1.2 {ECO:0000250|UniProtKB:Q96QE2};
GN Name=hmit-1.2 {ECO:0000312|WormBase:Y51A2D.5};
GN ORFNames=Y51A2D.5 {ECO:0000312|WormBase:Y51A2D.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, 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}. Perikaryon
CC {ECO:0000269|PubMed:21679696}. Note=Localizes to the lumenal side of
CC intestinal cells (PubMed:21679696). Localizes to the endfoot region of
CC glial cells where the cilia of sensory neurons are embedded
CC (PubMed:21679696). In the excretory canal cell, localizes to the basal
CC membrane of the distal canal and at the lumenal membrane of the
CC proximal canal (PubMed:21679696). {ECO:0000269|PubMed:21679696}.
CC -!- TISSUE SPECIFICITY: Expressed in the excretory canal cell and in pairs
CC of amphid and sheath glia. {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,
CC ECO:0000255|RuleBase:RU003346}.
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DR EMBL; BX284605; CAA16405.1; -; Genomic_DNA.
DR PIR; T27077; T27077.
DR RefSeq; NP_507624.1; NM_075223.5.
DR AlphaFoldDB; Q9XXQ9; -.
DR SMR; Q9XXQ9; -.
DR STRING; 6239.Y51A2D.5; -.
DR EPD; Q9XXQ9; -.
DR PaxDb; Q9XXQ9; -.
DR PeptideAtlas; Q9XXQ9; -.
DR EnsemblMetazoa; Y51A2D.5.1; Y51A2D.5.1; WBGene00013074.
DR GeneID; 180206; -.
DR KEGG; cel:CELE_Y51A2D.5; -.
DR UCSC; Y51A2D.5; c. elegans.
DR CTD; 180206; -.
DR WormBase; Y51A2D.5; CE19202; WBGene00013074; hmit-1.2.
DR eggNOG; KOG0254; Eukaryota.
DR GeneTree; ENSGT00970000196599; -.
DR HOGENOM; CLU_001265_30_5_1; -.
DR InParanoid; Q9XXQ9; -.
DR OMA; WAITASF; -.
DR OrthoDB; 430696at2759; -.
DR PhylomeDB; Q9XXQ9; -.
DR PRO; PR:Q9XXQ9; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00013074; Expressed in adult organism and 2 other tissues.
DR GO; GO:0016324; C:apical plasma membrane; IDA:WormBase.
DR GO; GO:0009925; C:basal 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..613
FT /note="Proton myo-inositol cotransporter hmit-1.2"
FT /id="PRO_0000450212"
FT TOPO_DOM 1..21
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 22..42
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 43..69
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 70..90
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 91..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..119
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 120..140
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 141..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..189
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 190..210
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 211..279
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 280..300
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 301..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..347
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 348..368
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 369..472
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 473..493
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TOPO_DOM 494..515
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 516..536
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255"
FT TOPO_DOM 537..539
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 540..560
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255"
FT TOPO_DOM 561..613
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 594..613
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 599..613
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 372
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 451
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 456
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 613 AA; 67886 MW; EAD220793DD2B2F1 CRC64;
MVAVEFKVSE SGRPRPEKNP KLGFFVYLLG SAAIIGGFLF GYDTSVVSAA MLYVPEAPGL
KPMGTVWKEV IVSITPGMAA VGAWFSGAGS DRYGRKPIII GSTLIFVCGA VICAVAWTKI
VMLIGRIFLG VGIGFASMVV PVYLGEASPT HVRGTLVSAF AMMISFGQVV ANIMGGVFSY
WEPYTIGWRL MFAFAGIPAL IQFVCFIFLP ETPRWLYENG HTEQAEQVLE KIYGGNTEWI
EYELAEIKTY AEERQKQMEE EKKSGPVIWR ILKTPHVLKA CFIGSMLQAF QQLAGINTIL
YYTADIIRSA GIENYHTIIW ISVILSICNL IGPFAPMFFI EKLGRRKLFL FSCAGVVVSL
VLIGVSFLLV GNDSAPNFDR SAYLLAGNYQ SNGEAESCLM LSNCDSCVTS EHCGFCEDSE
TRTGFCLPVD HNDVTLYSST GLCTNGLDKS NSSFPNATSY VWQKHHCTTS YTILPIVMMG
VYLLTFSCGF TSLPWVLNSE FYPMWARSTC VSISTLSNWV FNLIIALTYL SLTHAITKYG
AFWLYAIFTI IAFIFIYFLV PETTGYSIDE VEMLFMNKRQ RNIAMQARQA KLDAASDKDK
NSSTSLSTET ITM
