RHVI2_ROSHC
ID RHVI2_ROSHC Reviewed; 640 AA.
AC H2DF88;
DT 18-JAN-2017, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2012, sequence version 1.
DT 03-AUG-2022, entry version 31.
DE RecName: Full=Acid beta-fructofuranosidase 2, vacuolar {ECO:0000305};
DE EC=3.2.1.26 {ECO:0000269|PubMed:22505690};
DE AltName: Full=Vacuolar invertase 2 {ECO:0000303|PubMed:22505690};
DE Short=RvVI2 {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:AEY79730.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND LACK OF
RP INDUCTION BY LIGHT.
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 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: Vacuolar invertase. {ECO:0000269|PubMed:22505690}.
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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:27083698}; Multi-
CC pass membrane protein {ECO:0000255}. Vacuole membrane {ECO:0000305};
CC Single-pass membrane protein {ECO:0000305}. Note=After the proteolytic
CC cleavage of the propeptide, the protein should stay anchored to the
CC vacuolar membrane on its vacuolar side. {ECO:0000305|PubMed:27083698}.
CC -!- TISSUE SPECIFICITY: Expressed in buds, stems, roots and leaves.
CC {ECO:0000269|PubMed:22505690}.
CC -!- INDUCTION: Not regulated by light during bud burst.
CC {ECO:0000269|PubMed:22505690}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 32 family. {ECO:0000305}.
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DR EMBL; JN592033; AEY79730.1; -; mRNA.
DR AlphaFoldDB; H2DF88; -.
DR SMR; H2DF88; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005774; C:vacuolar membrane; 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; 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; 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 Disulfide bond; Glycosidase; Hydrolase; Membrane; Transmembrane;
KW Transmembrane helix; Vacuole; Zymogen.
FT PROPEP 1..78
FT /note="Removed in mature form"
FT /evidence="ECO:0000250|UniProtKB:H2DF87"
FT /id="PRO_0000438792"
FT CHAIN 79..640
FT /note="Acid beta-fructofuranosidase 2, vacuolar"
FT /id="PRO_0000438793"
FT TOPO_DOM 1..29
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 30..49
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 50..616
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 617..639
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 640
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 96
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10067"
FT BINDING 93..96
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q43866"
FT BINDING 112
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q43866"
FT BINDING 120
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q43866"
FT BINDING 155..156
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q43866"
FT BINDING 219..220
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q43866"
FT BINDING 274
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q43866"
FT BINDING 307
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q43866"
FT DISULFID 464..512
FT /evidence="ECO:0000250|UniProtKB:Q43866"
SQ SEQUENCE 640 AA; 71647 MW; EA4731B318F46BBA CRC64;
MDTNTTSYTP LPGDPFLSGP PETPRRPLKG FAVIFASVIF LMSLVALIIH QGPQQPPDVM
PDKQDEHHHP QSTTNTMLSW QRTAFHFQPE KNWMNDPNGP MYYKGWYHFF YQYNPRGAVW
GNIVWGHAVS RDLIHWLHLP LAMVADQWYD INGVWTGSAT ILPNDQIVML YTGSTNESVQ
VQCLAYPADH KDPLLTKWVK YSGNPVLVPP PGIGVKDFRD PTTAWYITEG KWRITIGSKV
NKTGISLVYD TKDFIKYEQL DGVLHAVPGT GMWECIDFYP VSKTSDKGLD TSQNGADVKH
VMKASLDDDR NDYYALGSYN EKTGKWVPDN QKIDVGIGIR YDYGKFYASK TFYDQNKQRR
VLWGWIGESD SENADVKKGW ASLQGIPRTV LFDQKTGSNL LQWPVEEIEK LRLNKKNFDK
VQVKAGSVVP LDVGTATQLD IVAEFQLDQK VVESAAETNE EFSCQTSGGA AKRGALGPFG
LLVLADDSLS ERTPVYFYVV KGSGGTVNTY FCADQTRSSV ATDVVKQVSG SYVPVLKGET
LSLRILVDHS IIESFAQGGR TTITTRVYPT QAIYGAARLF LFNNATDTSF TASLQIWQMN
SAFIRPFSPD AASHSSFTPV TVFIKFIVPF GIFLTLYFVR
