INT1_ARATH
ID INT1_ARATH Reviewed; 509 AA.
AC Q8VZR6; O22848;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Inositol transporter 1;
GN Name=INT1; OrderedLocusNames=At2g43330; ORFNames=T1O24.7;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=16603666; DOI=10.1104/pp.106.077123;
RA Schneider S., Schneidereit A., Konrad K.R., Hajirezaei M.-R., Gramann M.,
RA Hedrich R., Sauer N.;
RT "Arabidopsis INOSITOL TRANSPORTER4 mediates high-affinity H+ symport of
RT myoinositol across the plasma membrane.";
RL Plant Physiol. 141:565-577(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP GENE FAMILY.
RX PubMed=16923188; DOI=10.1186/1471-2148-6-64;
RA Johnson D.A., Hill J.P., Thomas M.A.;
RT "The monosaccharide transporter gene family in land plants is ancient and
RT shows differential subfamily expression and expansion across lineages.";
RL BMC Evol. Biol. 6:64-64(2006).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=18441213; DOI=10.1105/tpc.107.055632;
RA Schneider S., Beyhl D., Hedrich R., Sauer N.;
RT "Functional and physiological characterization of Arabidopsis INOSITOL
RT TRANSPORTER1, a novel tonoplast-localized transporter for myo-inositol.";
RL Plant Cell 20:1073-1087(2008).
RN [7]
RP SUBCELLULAR LOCATION, DOMAIN, AND MUTAGENESIS OF 479-TRP--SER-509;
RP 481-GLU-ARG-482; 500-GLU--SER-509 AND 502-LEU--GLU-504.
RC STRAIN=cv. Columbia;
RX PubMed=22253225; DOI=10.1105/tpc.111.090415;
RA Wolfenstetter S., Wirsching P., Dotzauer D., Schneider S., Sauer N.;
RT "Routes to the tonoplast: the sorting of tonoplast transporters in
RT Arabidopsis mesophyll protoplasts.";
RL Plant Cell 24:215-232(2012).
CC -!- FUNCTION: Vacuolar inositol-proton symporter involved in the release of
CC myo-inositol from vacuoles. Not involved in glucose or fructose
CC transport. {ECO:0000269|PubMed:18441213}.
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:18441213,
CC ECO:0000269|PubMed:22253225}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:18441213, ECO:0000269|PubMed:22253225}.
CC -!- TISSUE SPECIFICITY: Expressed in seedlings, leaves, flowers and pollen
CC grains. Not detected in seeds. {ECO:0000269|PubMed:18441213}.
CC -!- DOMAIN: The C-terminal domain (465-509) is necessary and sufficient for
CC vacuole membrane targeting. The di-Leu motif is required for this
CC sorting. {ECO:0000269|PubMed:22253225}.
CC -!- DISRUPTION PHENOTYPE: Reduced root length at low concentrations of myo-
CC inositol. {ECO:0000269|PubMed:18441213}.
CC -!- MISCELLANEOUS: The sorting of INT1 to the tonoplast is independent of
CC the AP-3 adapter complex but is brefeldin A sensitive.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. Sugar
CC transporter (TC 2.A.1.1) family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB64332.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AJ973175; CAJ00303.1; -; mRNA.
DR EMBL; AC002335; AAB64332.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; AEC10252.1; -; Genomic_DNA.
DR EMBL; AY063901; AAL36257.1; -; mRNA.
DR EMBL; AY096505; AAM20155.1; -; mRNA.
DR PIR; G84864; G84864.
DR RefSeq; NP_850393.1; NM_180062.3.
DR AlphaFoldDB; Q8VZR6; -.
DR SMR; Q8VZR6; -.
DR BioGRID; 4271; 17.
DR IntAct; Q8VZR6; 17.
DR STRING; 3702.AT2G43330.1; -.
DR TCDB; 2.A.1.1.66; the major facilitator superfamily (mfs).
DR PaxDb; Q8VZR6; -.
DR PRIDE; Q8VZR6; -.
DR ProteomicsDB; 248465; -.
DR EnsemblPlants; AT2G43330.1; AT2G43330.1; AT2G43330.
DR GeneID; 818934; -.
DR Gramene; AT2G43330.1; AT2G43330.1; AT2G43330.
DR KEGG; ath:AT2G43330; -.
DR Araport; AT2G43330; -.
DR TAIR; locus:2058193; AT2G43330.
DR eggNOG; KOG0254; Eukaryota.
DR HOGENOM; CLU_001265_30_5_1; -.
DR InParanoid; Q8VZR6; -.
DR OMA; WAITASF; -.
DR OrthoDB; 326501at2759; -.
DR PhylomeDB; Q8VZR6; -.
DR PRO; PR:Q8VZR6; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q8VZR6; baseline and differential.
DR Genevisible; Q8VZR6; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0009705; C:plant-type vacuole membrane; IDA:TAIR.
DR GO; GO:0005366; F:myo-inositol:proton symporter activity; IDA:TAIR.
DR GO; GO:0015798; P:myo-inositol transport; IMP:TAIR.
DR Gene3D; 1.20.1250.20; -; 1.
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; 1.
DR PRINTS; PR00171; SUGRTRNSPORT.
DR SUPFAM; SSF103473; SSF103473; 1.
DR TIGRFAMs; TIGR00879; SP; 1.
DR PROSITE; PS50850; MFS; 1.
DR PROSITE; PS00217; SUGAR_TRANSPORT_2; 1.
PE 1: Evidence at protein level;
KW Membrane; Reference proteome; Symport; Transmembrane; Transmembrane helix;
KW Transport; Vacuole.
FT CHAIN 1..509
FT /note="Inositol transporter 1"
FT /id="PRO_0000259875"
FT TRANSMEM 39..59
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TRANSMEM 74..94
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TRANSMEM 109..129
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TRANSMEM 132..152
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TRANSMEM 159..179
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TRANSMEM 192..212
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TRANSMEM 274..294
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TRANSMEM 315..335
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TRANSMEM 343..363
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TRANSMEM 374..394
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TRANSMEM 423..443
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255"
FT TRANSMEM 444..464
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255"
FT MOTIF 502..503
FT /note="Di-Leu"
FT MUTAGEN 479..509
FT /note="Missing: Leads to endoplasmic reticulum
FT relocalization."
FT /evidence="ECO:0000269|PubMed:22253225"
FT MUTAGEN 481..482
FT /note="ER->AA: No effect on targeting."
FT /evidence="ECO:0000269|PubMed:22253225"
FT MUTAGEN 500..509
FT /note="Missing: Leads to endoplasmic reticulum
FT relocalization."
FT /evidence="ECO:0000269|PubMed:22253225"
FT MUTAGEN 502..504
FT /note="LLE->AAA,SSS: Leads to plasma membrane
FT relocalization."
FT /evidence="ECO:0000269|PubMed:22253225"
SQ SEQUENCE 509 AA; 54813 MW; E51EB0673ECD4E93 CRC64;
MTLTIPNAPG SSGYLDMFPE RRMSYFGNSY ILGLTVTAGI GGLLFGYDTG VISGALLYIK
DDFEVVKQSS FLQETIVSMA LVGAMIGAAA GGWINDYYGR KKATLFADVV FAAGAIVMAA
APDPYVLISG RLLVGLGVGV ASVTAPVYIA EASPSEVRGG LVSTNVLMIT GGQFLSYLVN
SAFTQVPGTW RWMLGVSGVP AVIQFILMLF MPESPRWLFM KNRKAEAIQV LARTYDISRL
EDEIDHLSAA EEEEKQRKRT VGYLDVFRSK ELRLAFLAGA GLQAFQQFTG INTVMYYSPT
IVQMAGFHSN QLALFLSLIV AAMNAAGTVV GIYFIDHCGR KKLALSSLFG VIISLLILSV
SFFKQSETSS DGGLYGWLAV LGLALYIVFF APGMGPVPWT VNSEIYPQQY RGICGGMSAT
VNWISNLIVA QTFLTIAEAA GTGMTFLILA GIAVLAVIFV IVFVPETQGL TFSEVEQIWK
ERAYGNISGW GSSSDSNNME GLLEQGSQS
