INVA3_ARATH
ID INVA3_ARATH Reviewed; 648 AA.
AC Q43348; Q42567; Q7DLY6; Q94BX0; Q9SI83; Q9SXD2;
DT 16-MAY-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Acid beta-fructofuranosidase 3, vacuolar {ECO:0000303|PubMed:9332372};
DE Short=At beta fruct3 {ECO:0000303|PubMed:9332372};
DE Short=AtBETAFRUCT3 {ECO:0000303|PubMed:9332372};
DE EC=3.2.1.26 {ECO:0000255|PROSITE-ProRule:PRU10067};
DE AltName: Full=Acid invertase 3 {ECO:0000303|PubMed:9332372};
DE Short=AI 3 {ECO:0000303|PubMed:9332372};
DE AltName: Full=Acid sucrose hydrolase 3 {ECO:0000305};
DE AltName: Full=Vacuolar invertase 3 {ECO:0000303|PubMed:14871666};
DE Short=Inv-V3 {ECO:0000303|PubMed:14871666};
DE Short=VAC-INV 3 {ECO:0000303|PubMed:14871666};
DE Short=VI 3 {ECO:0000303|PubMed:14871666};
DE Flags: Precursor;
GN Name=BFRUCT3 {ECO:0000303|PubMed:9332372};
GN Synonyms=BETAFRUCT3 {ECO:0000303|PubMed:9332372};
GN OrderedLocusNames=At1g62660 {ECO:0000312|Araport:AT1G62660};
GN ORFNames=F23N19.3 {ECO:0000312|EMBL:AAF19535.1},
GN T3P18.21 {ECO:0000312|EMBL:AAD43622.1};
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 [GENOMIC DNA / MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia; TISSUE=Root, and Shoot;
RX PubMed=9332372; DOI=10.1016/s0378-1119(97)00268-0;
RA Haouazine-Takvorian N., Tymowska-Lalanne Z., Takvorian A., Tregear J.,
RA Lejeune B., Lecharny A., Kreis M.;
RT "Characterization of two members of the Arabidopsis thaliana gene family,
RT At beta fruct3 and At beta fruct4, coding for vacuolar invertases.";
RL Gene 197:239-251(1997).
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 ACTIVITY REGULATION.
RX PubMed=14871666; DOI=10.1016/j.bbapap.2003.09.017;
RA Rausch T., Greiner S.;
RT "Plant protein inhibitors of invertases.";
RL Biochim. Biophys. Acta 1696:253-261(2004).
RN [6]
RP DEVELOPMENTAL STAGE, AND INDUCTION BY GIBBERELLIN.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=15056893; DOI=10.1271/bbb.68.602;
RA Mitsuhashi W., Sasaki S., Kanazawa A., Yang Y.-Y., Kamiya Y., Toyomasu T.;
RT "Differential expression of acid invertase genes during seed germination in
RT Arabidopsis thaliana.";
RL Biosci. Biotechnol. Biochem. 68:602-608(2004).
RN [7]
RP INDUCTION BY VIRULENT P.SYRINGAE.
RX PubMed=16807755; DOI=10.1007/s00425-006-0303-3;
RA Bonfig K.B., Schreiber U., Gabler A., Roitsch T., Berger S.;
RT "Infection with virulent and avirulent P. syringae strains differentially
RT affects photosynthesis and sink metabolism in Arabidopsis leaves.";
RL Planta 225:1-12(2006).
RN [8]
RP TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=19901034; DOI=10.1074/jbc.m109.054288;
RA Yamada K., Osakabe Y., Mizoi J., Nakashima K., Fujita Y., Shinozaki K.,
RA Yamaguchi-Shinozaki K.;
RT "Functional analysis of an Arabidopsis thaliana abiotic stress-inducible
RT facilitated diffusion transporter for monosaccharides.";
RL J. Biol. Chem. 285:1138-1146(2010).
CC -!- FUNCTION: Possible role in the continued mobilization of sucrose to
CC sink organs. {ECO:0000250|UniProtKB:Q39041}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal non-reducing beta-D-fructofuranoside
CC residues in beta-D-fructofuranosides.; EC=3.2.1.26;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10067};
CC -!- ACTIVITY REGULATION: Inhibited by C/VIF1 and C/VIF2.
CC {ECO:0000269|PubMed:14871666}.
CC -!- PATHWAY: Glycan biosynthesis; sucrose metabolism. {ECO:0000305}.
CC -!- SUBUNIT: May be present in two forms, a 70 kDa monomer and a
CC heterodimer of the 30 kDa and 38 kDa subunits. The ratio of the levels
CC of the two forms within cells appears to be regulated developmentally
CC (By similarity). {ECO:0000250|UniProtKB:P29001}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass type II
CC membrane protein {ECO:0000255}. Vacuole lumen
CC {ECO:0000250|UniProtKB:Q39041}. Note=May be released into the lumen of
CC the vacuole from the tonoplast through a proteolytic processing.
CC {ECO:0000250|UniProtKB:Q39041}.
CC -!- TISSUE SPECIFICITY: Mostly expressed in stems, roots and flowers, and,
CC to a lower extent, in mature leaves. {ECO:0000269|PubMed:19901034,
CC ECO:0000269|PubMed:9332372}.
CC -!- DEVELOPMENTAL STAGE: Expressed during germination et seedling growth.
CC {ECO:0000269|PubMed:15056893}.
CC -!- INDUCTION: Induced by gibberellin (e.g. gibberellic acid GA) that
CC accumulates in seeds after red light treatment (PubMed:15056893).
CC Accumulates rapidly but transiently upon infection with virulent but
CC not with avirulent P.syringae (PubMed:16807755). In whole plants,
CC expression increases after 2 hours of exposure to drought and abscisic
CC acid (ABA), and after 5 hours of exposure to high salinity treatment.
CC At the 5 hour time point, expression under drought and ABA treatment is
CC also higher than that under the high salinity condition
CC (PubMed:19901034). {ECO:0000269|PubMed:15056893,
CC ECO:0000269|PubMed:16807755, ECO:0000269|PubMed:19901034}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 32 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD43622.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAF19535.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; X89454; CAA61624.1; -; mRNA.
DR EMBL; X95537; CAA64781.1; -; mRNA.
DR EMBL; X99111; CAA67560.1; -; Genomic_DNA.
DR EMBL; AC005698; AAD43622.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC007190; AAF19535.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE33991.1; -; Genomic_DNA.
DR EMBL; AY039610; AAK62665.1; -; mRNA.
DR EMBL; AY048269; AAK82531.1; -; mRNA.
DR EMBL; AY062481; AAL32559.1; -; mRNA.
DR EMBL; AY063904; AAL36260.1; -; mRNA.
DR EMBL; AY114066; AAM45114.1; -; mRNA.
DR EMBL; BT000509; AAN18078.1; -; mRNA.
DR PIR; A96652; A96652.
DR PIR; S57951; S57951.
DR PIR; S71268; S71268.
DR RefSeq; NP_564798.1; NM_104943.3.
DR AlphaFoldDB; Q43348; -.
DR SMR; Q43348; -.
DR BioGRID; 27784; 1.
DR IntAct; Q43348; 1.
DR STRING; 3702.AT1G62660.1; -.
DR CAZy; GH32; Glycoside Hydrolase Family 32.
DR PaxDb; Q43348; -.
DR PRIDE; Q43348; -.
DR ProteomicsDB; 248471; -.
DR EnsemblPlants; AT1G62660.1; AT1G62660.1; AT1G62660.
DR GeneID; 842563; -.
DR Gramene; AT1G62660.1; AT1G62660.1; AT1G62660.
DR KEGG; ath:AT1G62660; -.
DR Araport; AT1G62660; -.
DR TAIR; locus:2026177; AT1G62660.
DR eggNOG; KOG0228; Eukaryota.
DR HOGENOM; CLU_001528_6_1_1; -.
DR InParanoid; Q43348; -.
DR OrthoDB; 405663at2759; -.
DR PhylomeDB; Q43348; -.
DR BioCyc; ARA:AT1G62660-MON; -.
DR UniPathway; UPA00238; -.
DR PRO; PR:Q43348; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q43348; baseline and differential.
DR Genevisible; Q43348; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; HDA:TAIR.
DR GO; GO:0000325; C:plant-type vacuole; IDA:UniProtKB.
DR GO; GO:0005775; C:vacuolar lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0004564; F:beta-fructofuranosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0009738; P:abscisic acid-activated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0071370; P:cellular response to gibberellin stimulus; IEP:UniProtKB.
DR GO; GO:0009737; P:response to abscisic acid; IEP:UniProtKB.
DR GO; GO:0009617; P:response to bacterium; IEP:UniProtKB.
DR GO; GO:0009651; P:response to salt stress; IEP:UniProtKB.
DR GO; GO:0009414; P:response to water deprivation; IEP:UniProtKB.
DR GO; GO:0005985; P:sucrose metabolic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 2.115.10.20; -; 1.
DR InterPro; IPR021792; Beta-fructofuranosidase_N.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR001362; Glyco_hydro_32.
DR InterPro; IPR018053; Glyco_hydro_32_AS.
DR InterPro; IPR013189; Glyco_hydro_32_C.
DR InterPro; IPR013148; Glyco_hydro_32_N.
DR InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR Pfam; PF11837; DUF3357; 1.
DR Pfam; PF08244; Glyco_hydro_32C; 1.
DR Pfam; PF00251; Glyco_hydro_32N; 1.
DR SMART; SM00640; Glyco_32; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR SUPFAM; SSF75005; SSF75005; 1.
DR PROSITE; PS00609; GLYCOSYL_HYDROL_F32; 1.
PE 2: Evidence at transcript level;
KW Abscisic acid signaling pathway; Disulfide bond; Glycoprotein; Glycosidase;
KW Hydrolase; Membrane; Reference proteome; Signal-anchor; Transmembrane;
KW Transmembrane helix; Vacuole; Zymogen.
FT PROPEP 1..93
FT /note="Removed in mature form"
FT /evidence="ECO:0000250|UniProtKB:P80065"
FT /id="PRO_0000417017"
FT CHAIN 94..648
FT /note="Acid beta-fructofuranosidase 3, vacuolar"
FT /id="PRO_0000417018"
FT TOPO_DOM 1..35
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 36..56
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 57..648
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..21
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 120
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10067"
FT BINDING 117..120
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q43866"
FT BINDING 136
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q43866"
FT BINDING 144
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q43866"
FT BINDING 179..180
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q43866"
FT BINDING 243..244
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q43866"
FT BINDING 298
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q43866"
FT BINDING 331
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q43866"
FT CARBOHYD 98
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 265
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 347
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 494..542
FT /evidence="ECO:0000250|UniProtKB:Q43866"
FT CONFLICT 1..90
FT /note="MASTEALLPVTSLQDPLSESRSDQIPETRRRRPIKVHLAVYSGLLLIALYVT
FT LIVTHDGSKAEIATESRPRMAGVSEKSNDGVWISSDDG -> IRHE (in Ref. 1;
FT CAA61624)"
FT /evidence="ECO:0000305"
FT CONFLICT 201
FT /note="E -> G (in Ref. 1; CAA61624)"
FT /evidence="ECO:0000305"
FT CONFLICT 285
FT /note="E -> D (in Ref. 1; CAA61624)"
FT /evidence="ECO:0000305"
FT CONFLICT 310
FT /note="L -> V (in Ref. 1; CAA61624)"
FT /evidence="ECO:0000305"
FT CONFLICT 410
FT /note="Q -> K (in Ref. 4; AAK62665/AAN18078)"
FT /evidence="ECO:0000305"
FT CONFLICT 518
FT /note="G -> N (in Ref. 1; CAA61624)"
FT /evidence="ECO:0000305"
FT CONFLICT 622
FT /note="A -> T (in Ref. 1; CAA61624)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 648 AA; 72228 MW; F7569486B91E4011 CRC64;
MASTEALLPV TSLQDPLSES RSDQIPETRR RRPIKVHLAV YSGLLLIALY VTLIVTHDGS
KAEIATESRP RMAGVSEKSN DGVWISSDDG KVEAFPWNNT ILSWQRTAFH FQPEKNWMND
PNGPLFYKGW YHFFYQYNPN AAVWGDIVWG HAVSKDLIHW LYLPIAMVPD QWYDANGVWT
GSATFLDDGS IVMLYTGSTD EFVQVQNLAY PEDPSDPLLL KWVKFSGNPV LVPPPGIGAK
DFRDPTTAWK TSSGKWRITI GSKINRTGIS LIYDTTDFKT YEKHETLLHQ VPNTGMWECV
DFYPVSKTQL NGLDTSVNGP DVKHVIKASM DDTRIDHYAI GTYDDSNATW VPDNPSIDVG
ISTGLRYDYG KYYASKTFYD QNKGRRILWG WIGESDSEAA DVQKGWSSVQ GIPRTVVLDT
RTHKNLVQWP VEEIKSLRLS SKKFDMTIGP GTVVPVDVGS ATQLDIEAEF EIKTDDLKLF
FDDDSVEADN KFSCETNGGS TARGALGPFG FSVLADEGLS EQTPVYFYVT KGKHSKLNTV
FCTDTSRSTL ANDVVKPIYG SFVPVLKGEK LTMRILVDHS IVEGFAQGGR SCITSRVYPT
KAIYGATKLF LFNNAIDATV TASFTVWQMN NAFIHPYSSD DLGVPSST
