RHVI1_ROSHC
ID RHVI1_ROSHC Reviewed; 588 AA.
AC H2DF87;
DT 18-JAN-2017, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2012, sequence version 1.
DT 03-AUG-2022, entry version 33.
DE RecName: Full=Acid beta-fructofuranosidase 1, vacuolar {ECO:0000305};
DE EC=3.2.1.26 {ECO:0000269|PubMed:22505690};
DE AltName: Full=Vacuolar invertase 1 {ECO:0000303|PubMed:22505690};
DE Short=RvVI1 {ECO:0000303|PubMed:22505690};
DE Flags: Precursor;
OS Rosa hybrid cultivar.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Rosaceae; Rosoideae; Rosoideae incertae sedis;
OC Rosa.
OX NCBI_TaxID=128735 {ECO:0000312|EMBL:AEY79729.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND INDUCTION BY
RP LIGHT AND SUGARS.
RX PubMed=22505690; DOI=10.1093/pcp/pcs051;
RA Rabot A., Henry C., Ben Baaziz K., Mortreau E., Azri W., Lothier J.,
RA Hamama L., Boummaza R., Leduc N., Pelleschi-Travier S., Le Gourrierec J.,
RA Sakr S.;
RT "Insight into the role of sugars in bud burst under light in the rose.";
RL Plant Cell Physiol. 53:1068-1082(2012).
RN [2]
RP INDUCTION BY LIGHT.
RX PubMed=20374536; DOI=10.1111/j.1365-3040.2010.02152.x;
RA Girault T., Abidi F., Sigogne M., Pelleschi-Travier S., Boumaza R.,
RA Sakr S., Leduc N.;
RT "Sugars are under light control during bud burst in Rosa sp.";
RL Plant Cell Environ. 33:1339-1350(2010).
RN [3]
RP TISSUE SPECIFICITY, AND INDUCTION BY GIBBERELLIN; LIGHT AND SUGARS.
RX PubMed=25108242; DOI=10.1093/pcp/pcu106;
RA Rabot A., Portemer V., Peron T., Mortreau E., Leduc N., Hamama L.,
RA Coutos-Thevenot P., Atanassova R., Sakr S., Le Gourrierec J.;
RT "Interplay of sugar, light and gibberellins in expression of Rosa hybrida
RT vacuolar invertase 1 regulation.";
RL Plant Cell Physiol. 55:1734-1748(2014).
RN [4]
RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, SUBUNIT, GLYCOSYLATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND SUBCELLULAR LOCATION.
RX PubMed=27083698; DOI=10.1093/jxb/erw148;
RA Farci D., Collu G., Kirkpatrick J., Esposito F., Piano D.;
RT "RhVI1 is a membrane-anchored vacuolar invertase highly expressed in Rosa
RT hybrida L. petals.";
RL J. Exp. Bot. 67:3303-3312(2016).
CC -!- FUNCTION: Acidic vacuolar invertase involved in light-induced bud burst
CC (PubMed:22505690, PubMed:27083698). {ECO:0000269|PubMed:22505690,
CC ECO:0000269|PubMed:27083698}.
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:0000269|PubMed:22505690};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 4.5. {ECO:0000269|PubMed:27083698};
CC -!- SUBUNIT: Monomer (PubMed:27083698). May be present in two forms, a 70
CC kDa monomer and a heterodimer of the 30 kDa and 38 kDa subunits (By
CC similarity). The ratio of the levels of the two forms within cells
CC appears to be regulated developmentally (By similarity).
CC {ECO:0000250|UniProtKB:P29001, ECO:0000269|PubMed:27083698}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:27083698}; Single-
CC pass type II 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: Expressed in buds, stems, roots and leaves
CC (PubMed:22505690). Expressed in the epidermal cells of young leaves and
CC of primordial leaves (PubMed:25108242). {ECO:0000269|PubMed:22505690,
CC ECO:0000269|PubMed:25108242}.
CC -!- INDUCTION: Strongly up-regulated synergistically by light and sugars
CC during bud burst (PubMed:22505690, PubMed:20374536, PubMed:25108242).
CC Up-regulated synergistically by the combination of light and
CC gibberellin (PubMed:25108242). {ECO:0000269|PubMed:20374536,
CC ECO:0000269|PubMed:22505690, ECO:0000269|PubMed:25108242}.
CC -!- PTM: Glycosylated. {ECO:0000269|PubMed:27083698}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 32 family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=On light, buds and bursts
CC - Issue 224 of April 2020;
CC URL="https://web.expasy.org/spotlight/back_issues/224";
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DR EMBL; JN592032; AEY79729.1; -; mRNA.
DR AlphaFoldDB; H2DF87; -.
DR SMR; H2DF87; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005775; C:vacuolar lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0004564; F:beta-fructofuranosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
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 1: Evidence at protein level;
KW Disulfide bond; Glycoprotein; Glycosidase; Hydrolase; Membrane;
KW Signal-anchor; Transmembrane; Transmembrane helix; Vacuole; Zymogen.
FT PROPEP 1..115
FT /note="Removed in mature form"
FT /evidence="ECO:0000305|PubMed:27083698"
FT /id="PRO_0000438790"
FT CHAIN 116..588
FT /note="Acid beta-fructofuranosidase 1, vacuolar"
FT /id="PRO_0000438791"
FT TOPO_DOM 1..31
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 32..52
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 53..588
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT REGION 57..86
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 133
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10067"
FT BINDING 130..133
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q43866"
FT BINDING 149
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q43866"
FT BINDING 157
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q43866"
FT BINDING 192..193
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q43866"
FT BINDING 256..257
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q43866"
FT BINDING 311
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q43866"
FT BINDING 344
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q43866"
FT CARBOHYD 159
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 226
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 499..545
FT /evidence="ECO:0000250|UniProtKB:Q43866"
SQ SEQUENCE 588 AA; 65375 MW; DD76AC3FC227174D CRC64;
MDTSTSAYAP LPGEDPLFSG HPPASLRRSW KGFAVIFASV LFLLSLVGLI IHQGPQQPPD
VMPDKQDEHH HPQSTTPASE TTASWEPRGK ALGVSAKSNP PVSDELSYNW TNAMFSWQRT
AFHFQPERNW MNDPNGPLFY KGWYHLFYQY NPDSAIWGNI TWGHAVSTDL IHWLYLPIAM
VADQWYDANG VWSGSATLLP DGQIVMLYTG DTVDAVQVVC LAHPANLSDP LLLDWVKYSG
NPVLTPPPGI LTTDFRDPTT AWTGPDGKWR ITIGSKVNTT GISFVYHTED FKTYNMSKGV
LHAVPGTGMW ECIDFYPVAI NGSKGVETSV NNPSVKHVLK ASLDNTKVDH YALGTYFEEN
ETWVPDNPGL DVGIGLRYDY GRYYASKTFY DQNKERRILR GWINETDTES DDLAKGWASV
QTIPRTVLFD NKTGTNLIQW PVEEIEELRL NNTDFSDVLV EAGTVVELDI GTATQLDILV
EFELEPLESS ETVNSSVGCG GGAVDRGTFG PFGILVIADE TLTELTPIYF NLANSTEGDV
ITYFCADERR SSKAPDVFKQ VYGSEVPVLD GEKHFARVLR ALRKEVGR
