INT2_ARATH
ID INT2_ARATH Reviewed; 580 AA.
AC Q9C757;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Probable inositol transporter 2;
GN Name=INT2; OrderedLocusNames=At1g30220; ORFNames=F12P21.2;
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
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, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE
RP SPECIFICITY, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=17951450; DOI=10.1104/pp.107.109033;
RA Schneider S., Schneidereit A., Udvardi P., Hammes U., Gramann M.,
RA Dietrich P., Sauer N.;
RT "Arabidopsis INOSITOL TRANSPORTER2 mediates H+ symport of different
RT inositol epimers and derivatives across the plasma membrane.";
RL Plant Physiol. 145:1395-1407(2007).
RN [7]
RP DOMAIN, MUTAGENESIS OF CYS-399; CYS-402; CYS-410 AND CYS-413, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=20230529; DOI=10.1111/j.1600-0854.2010.01057.x;
RA Dotzauer D., Wolfenstetter S., Eibert D., Schneider S., Dietrich P.,
RA Sauer N.;
RT "Novel PSI domains in plant and animal H+-inositol symporters.";
RL Traffic 11:767-781(2010).
CC -!- FUNCTION: Plasma membrane inositol-proton symporter. Specific for
CC several inositol epimers, such as myoinositol and scylloinositol. D-
CC chiroinositol, mucoinositol, alloinositol and pinitol are also
CC transported with a lower activity. Not active with galactinol and
CC phytate. {ECO:0000269|PubMed:17951450}.
CC -!- ACTIVITY REGULATION: Inhibited by nickel and to a lesser extent by
CC cobalt.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.16 mM for inositol {ECO:0000269|PubMed:17951450,
CC ECO:0000269|PubMed:20230529};
CC pH dependence:
CC Optimum pH is 5.5-7.0. {ECO:0000269|PubMed:17951450,
CC ECO:0000269|PubMed:20230529};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17951450};
CC Multi-pass membrane protein {ECO:0000269|PubMed:17951450}.
CC -!- TISSUE SPECIFICITY: Expressed in the tapetum, but not in pollen grains.
CC Detected in leaf vascular tissue and in roots.
CC {ECO:0000269|PubMed:17951450}.
CC -!- DOMAIN: The PSI domain (383-450) is not involved in the plasma membrane
CC targeting and is dispensable for the transport function, but is
CC required for the inhibition by nickel. {ECO:0000269|PubMed:20230529}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype.
CC {ECO:0000269|PubMed:17951450}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. Sugar
CC transporter (TC 2.A.1.1) family. {ECO:0000305}.
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DR EMBL; AJ973176; CAJ00304.1; -; mRNA.
DR EMBL; AC073506; AAG50560.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE31194.1; -; Genomic_DNA.
DR EMBL; AY074333; AAL67029.1; -; mRNA.
DR EMBL; AY123031; AAM67564.1; -; mRNA.
DR PIR; D86426; D86426.
DR RefSeq; NP_174313.1; NM_102761.4.
DR AlphaFoldDB; Q9C757; -.
DR SMR; Q9C757; -.
DR STRING; 3702.AT1G30220.1; -.
DR TCDB; 2.A.1.1.63; the major facilitator superfamily (mfs).
DR PaxDb; Q9C757; -.
DR PRIDE; Q9C757; -.
DR ProteomicsDB; 248466; -.
DR EnsemblPlants; AT1G30220.1; AT1G30220.1; AT1G30220.
DR GeneID; 839902; -.
DR Gramene; AT1G30220.1; AT1G30220.1; AT1G30220.
DR KEGG; ath:AT1G30220; -.
DR Araport; AT1G30220; -.
DR TAIR; locus:2009832; AT1G30220.
DR eggNOG; KOG0254; Eukaryota.
DR HOGENOM; CLU_001265_30_5_1; -.
DR InParanoid; Q9C757; -.
DR OMA; PECGFCA; -.
DR OrthoDB; 326501at2759; -.
DR PhylomeDB; Q9C757; -.
DR PRO; PR:Q9C757; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9C757; baseline and differential.
DR Genevisible; Q9C757; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR GO; GO:0090406; C:pollen tube; TAS:TAIR.
DR GO; GO:0005366; F:myo-inositol:proton symporter activity; IDA:TAIR.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015798; P:myo-inositol transport; IDA:TAIR.
DR GO; GO:0023052; P:signaling; TAS:TAIR.
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 1: Evidence at protein level;
KW Cell membrane; Membrane; Reference proteome; Symport; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..580
FT /note="Probable inositol transporter 2"
FT /id="PRO_0000259876"
FT TRANSMEM 36..56
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TRANSMEM 71..91
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TRANSMEM 106..126
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TRANSMEM 129..149
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TRANSMEM 156..176
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TRANSMEM 189..209
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TRANSMEM 275..295
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 452..472
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TRANSMEM 490..510
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255"
FT TRANSMEM 521..541
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255"
FT MUTAGEN 399
FT /note="C->A: Strongly decreased nickel inhibition; when
FT associated with A-402, A-410 and A-413."
FT /evidence="ECO:0000269|PubMed:20230529"
FT MUTAGEN 399
FT /note="C->S: No effect on inostol transport or nickel
FT inhibition. No effect on inostol transport or nickel
FT inhibition; when associated with S-410."
FT /evidence="ECO:0000269|PubMed:20230529"
FT MUTAGEN 402
FT /note="C->A: Strongly decreased nickel inhibition; when
FT associated with A-399, A-410 and A-413."
FT /evidence="ECO:0000269|PubMed:20230529"
FT MUTAGEN 410
FT /note="C->A: Strongly decreased nickel inhibition; when
FT associated with A-399, A-402 and A-413."
FT /evidence="ECO:0000269|PubMed:20230529"
FT MUTAGEN 410
FT /note="C->S: No effect on inostol transport or nickel
FT inhibition; when associated with S-399."
FT /evidence="ECO:0000269|PubMed:20230529"
FT MUTAGEN 413
FT /note="C->A: Strongly decreased nickel inhibition; when
FT associated with A-399, A-402 and A-410."
FT /evidence="ECO:0000269|PubMed:20230529"
SQ SEQUENCE 580 AA; 63449 MW; B8E03518F05EED79 CRC64;
MEGGIIHGGA DESAFKECFS LTWKNPYVLR LAFSAGIGGL LFGYDTGVIS GALLYIRDDF
KSVDRNTWLQ EMIVSMAVAG AIVGAAIGGW ANDKLGRRSA ILMADFLFLL GAIIMAAAPN
PSLLVVGRVF VGLGVGMASM TAPLYISEAS PAKIRGALVS TNGFLITGGQ FLSYLINLAF
TDVTGTWRWM LGIAGIPALL QFVLMFTLPE SPRWLYRKGR EEEAKAILRR IYSAEDVEQE
IRALKDSVET EILEEGSSEK INMIKLCKAK TVRRGLIAGV GLQVFQQFVG INTVMYYSPT
IVQLAGFASN RTALLLSLVT AGLNAFGSII SIYFIDRIGR KKLLIISLFG VIISLGILTG
VFYEAATHAP AISSLETQRF NNISCPDYKS AMNTNAWDCM TCLKASSPSC GYCSSPIGKE
HPGACWISDD SVKDLCHNEN RLWYTRGCPS NFGWFALLGL GLYIIFFSPG MGTVPWIVNS
EIYPLRFRGI CGGIAATANW ISNLIVAQSF LSLTEAIGTS WTFLIFGVIS VIALLFVMVC
VPETKGMPME EIEKMLERRS MEFKFWKKKS KLVEKQNQSA