INT4_ARATH
ID INT4_ARATH Reviewed; 582 AA.
AC O23492;
DT 14-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Inositol transporter 4;
DE AltName: Full=Myo-inositol-proton symporter INT4;
DE AltName: Full=Protein INOSITOL TRANSPORTER 4;
GN Name=INT4; OrderedLocusNames=At4g16480; ORFNames=dl4265w, FCAALL.375;
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], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES,
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
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=9461215; DOI=10.1038/35140;
RA Bevan M., Bancroft I., Bent E., Love K., Goodman H.M., Dean C.,
RA Bergkamp R., Dirkse W., van Staveren M., Stiekema W., Drost L., Ridley P.,
RA Hudson S.-A., Patel K., Murphy G., Piffanelli P., Wedler H., Wedler E.,
RA Wambutt R., Weitzenegger T., Pohl T., Terryn N., Gielen J., Villarroel R.,
RA De Clercq R., van Montagu M., Lecharny A., Aubourg S., Gy I., Kreis M.,
RA Lao N., Kavanagh T., Hempel S., Kotter P., Entian K.-D., Rieger M.,
RA Schaefer M., Funk B., Mueller-Auer S., Silvey M., James R., Monfort A.,
RA Pons A., Puigdomenech P., Douka A., Voukelatou E., Milioni D.,
RA Hatzopoulos P., Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A.,
RA Moores T., Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S.,
RA Ansorge W., Cooke R., Berger C., Delseny M., Voet M., Volckaert G.,
RA Mewes H.-W., Klosterman S., Schueller C., Chalwatzis N.;
RT "Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of Arabidopsis
RT thaliana.";
RL Nature 391:485-488(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [4]
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 [5]
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 [6]
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 [7]
RP FUNCTION.
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 [8]
RP SUBCELLULAR LOCATION, DOMAIN, AND MUTAGENESIS OF 559-LEU--GLU-561;
RP 559-LEU--ALA-582; 564-PHE-LYS-565 AND 570-ARG--LYS-575.
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: Plasma membrane inositol-proton symporter. Mediates high-
CC affinity myoinositol-proton symport across the plasma membrane. Active
CC with myoinositol, scylloinositol and D-chiroinositol. Low activity with
CC mucoinositol and alloinositol. {ECO:0000269|PubMed:16603666,
CC ECO:0000269|PubMed:17951450}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.24 mM for myo-inositol {ECO:0000269|PubMed:16603666};
CC Note=Determined at three different membrane potentials: -90 mV, -40
CC mV and 0 mV, and at an extracellular pH of 5.5.;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16603666,
CC ECO:0000269|PubMed:22253225}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:16603666, ECO:0000269|PubMed:22253225}.
CC -!- TISSUE SPECIFICITY: Highly expressed in pollen and phloem companion
CC cells. {ECO:0000269|PubMed:16603666}.
CC -!- DOMAIN: The C-terminal domain (546-582) is required for plasma membrane
CC targeting. {ECO:0000269|PubMed:22253225}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. Sugar
CC transporter (TC 2.A.1.1) family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJ973178; CAJ00306.1; -; mRNA.
DR EMBL; Z97341; CAB10424.1; -; Genomic_DNA.
DR EMBL; AL161544; CAB78690.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE83759.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM66112.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM66113.1; -; Genomic_DNA.
DR EMBL; BT004139; AAO42160.1; -; mRNA.
DR EMBL; BT005707; AAO64127.1; -; mRNA.
DR PIR; F71431; F71431.
DR RefSeq; NP_001328028.1; NM_001341102.1.
DR RefSeq; NP_001328029.1; NM_001341103.1.
DR RefSeq; NP_193381.1; NM_117746.4.
DR AlphaFoldDB; O23492; -.
DR SMR; O23492; -.
DR BioGRID; 12639; 3.
DR IntAct; O23492; 3.
DR STRING; 3702.AT4G16480.1; -.
DR TCDB; 2.A.1.1.62; the major facilitator superfamily (mfs).
DR PaxDb; O23492; -.
DR PRIDE; O23492; -.
DR ProteomicsDB; 248468; -.
DR EnsemblPlants; AT4G16480.1; AT4G16480.1; AT4G16480.
DR EnsemblPlants; AT4G16480.2; AT4G16480.2; AT4G16480.
DR EnsemblPlants; AT4G16480.3; AT4G16480.3; AT4G16480.
DR GeneID; 827346; -.
DR Gramene; AT4G16480.1; AT4G16480.1; AT4G16480.
DR Gramene; AT4G16480.2; AT4G16480.2; AT4G16480.
DR Gramene; AT4G16480.3; AT4G16480.3; AT4G16480.
DR KEGG; ath:AT4G16480; -.
DR Araport; AT4G16480; -.
DR TAIR; locus:2130689; AT4G16480.
DR eggNOG; KOG0254; Eukaryota.
DR HOGENOM; CLU_001265_30_5_1; -.
DR InParanoid; O23492; -.
DR OMA; YYMHTLL; -.
DR OrthoDB; 326501at2759; -.
DR PhylomeDB; O23492; -.
DR PRO; PR:O23492; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; O23492; baseline and differential.
DR Genevisible; O23492; 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: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 1: Evidence at protein level;
KW Cell membrane; Membrane; Reference proteome; Symport; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..582
FT /note="Inositol transporter 4"
FT /id="PRO_0000259878"
FT TRANSMEM 35..55
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TRANSMEM 70..90
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TRANSMEM 105..125
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TRANSMEM 128..148
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TRANSMEM 162..182
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TRANSMEM 188..208
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TRANSMEM 290..310
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TRANSMEM 317..337
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TRANSMEM 345..365
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TRANSMEM 456..476
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TRANSMEM 494..514
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255"
FT TRANSMEM 525..545
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255"
FT MUTAGEN 559..582
FT /note="Missing: No effect on targeting."
FT /evidence="ECO:0000269|PubMed:22253225"
FT MUTAGEN 559..561
FT /note="LLE->AAA: No effect on targeting."
FT /evidence="ECO:0000269|PubMed:22253225"
FT MUTAGEN 564..565
FT /note="FK->AA: No effect on targeting."
FT /evidence="ECO:0000269|PubMed:22253225"
FT MUTAGEN 570..575
FT /note="RRREKK->AAAAAA: No effect on targeting."
FT /evidence="ECO:0000269|PubMed:22253225"
SQ SEQUENCE 582 AA; 62892 MW; FA8F8DDCA5D0CBC0 CRC64;
MVEGGIAKAD KTEFTECWRT TWKTPYIMRL ALSAGIGGLL FGYDTGVISG ALLFIKEDFD
EVDKKTWLQS TIVSMAVAGA IVGAAVGGWI NDKFGRRMSI LIADVLFLIG AIVMAFAPAP
WVIIVGRIFV GFGVGMASMT SPLYISEASP ARIRGALVST NGLLITGGQF FSYLINLAFV
HTPGTWRWML GVAGVPAIVQ FVLMLSLPES PRWLYRKDRI AESRAILERI YPADEVEAEM
EALKLSVEAE KADEAIIGDS FSAKLKGAFG NPVVRRGLAA GITVQVAQQF VGINTVMYYS
PSIVQFAGYA SNKTAMALSL ITSGLNALGS IVSMMFVDRY GRRKLMIISM FGIIACLIIL
ATVFSQAAIH APKIDAFESR TFAPNATCSA YAPLAAENAP PSRWNCMKCL RSECGFCASG
VQPYAPGACV VLSDDMKATC SSRGRTFFKD GCPSKFGFLA IVFLGLYIVV YAPGMGTVPW
IVNSEIYPLR YRGLGGGIAA VSNWVSNLIV SESFLSLTHA LGSSGTFLLF AGFSTIGLFF
IWLLVPETKG LQFEEVEKLL EVGFKPSLLR RREKKGKEVD AA
