INVA_VIGRR
ID INVA_VIGRR Reviewed; 649 AA.
AC P29001;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Acid beta-fructofuranosidase {ECO:0000303|Ref.1};
DE EC=3.2.1.26 {ECO:0000255|PROSITE-ProRule:PRU10067};
DE AltName: Full=Acid invertase {ECO:0000303|Ref.1};
DE Short=AI {ECO:0000303|Ref.1};
DE AltName: Full=Acid sucrose hydrolase;
DE AltName: Full=Vacuolar invertase;
DE Contains:
DE RecName: Full=Acid beta-fructofuranosidase 30 kDa subunit {ECO:0000303|Ref.1};
DE Contains:
DE RecName: Full=Acid beta-fructofuranosidase 38 kDa subunit {ECO:0000303|Ref.1};
DE Contains:
DE RecName: Full=Acid beta-fructofuranosidase 70 kDa monomer {ECO:0000303|Ref.1};
DE Flags: Precursor;
GN Name=INVA;
OS Vigna radiata var. radiata (Mung bean) (Phaseolus aureus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Vigna.
OX NCBI_TaxID=3916;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 329-360, SUBUNIT,
RP DEVELOPMENTAL STAGE, AND INDUCTION.
RC TISSUE=Hypocotyl;
RA Arai M., Mori H., Imaseki H.;
RT "Cloning and sequence of cDNAs for an intracellular acid invertase from
RT etiolated hypocotyls of mung bean and expression of the gene during growth
RT of seedlings.";
RL Plant Cell Physiol. 33:245-252(1992).
CC -!- FUNCTION: Possible role in the continued mobilization of sucrose to
CC sink organs. {ECO:0000305|Ref.1}.
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 -!- PATHWAY: Glycan biosynthesis; sucrose metabolism. {ECO:0000305}.
CC -!- SUBUNIT: Present in two forms, a 70 kDa monomer and a heterodimer of
CC the 30 kDa and 38 kDa subunits. The ratio of the levels of the two
CC forms within cells appears to be regulated developmentally.
CC {ECO:0000269|Ref.1}.
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 -!- DEVELOPMENTAL STAGE: Appears after germination and maintained at high
CC levels in rapidly growing tissues. {ECO:0000269|Ref.1}.
CC -!- INDUCTION: Regulation of synthesis appears to be related to the growth
CC of seedlings. {ECO:0000269|Ref.1}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 32 family. {ECO:0000305}.
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DR EMBL; D10265; BAA01107.1; -; mRNA.
DR RefSeq; NP_001304253.1; NM_001317324.1.
DR AlphaFoldDB; P29001; -.
DR SMR; P29001; -.
DR STRING; 3916.P29001; -.
DR CAZy; GH32; Glycoside Hydrolase Family 32.
DR GeneID; 106768621; -.
DR KEGG; vra:106768621; -.
DR SABIO-RK; P29001; -.
DR UniPathway; UPA00238; -.
DR Proteomes; UP000087766; Chromosome 7.
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: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 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Glycoprotein; Glycosidase;
KW Hydrolase; Membrane; Reference proteome; Signal-anchor; Transmembrane;
KW Transmembrane helix; Vacuole; Zymogen.
FT PROPEP 1..101
FT /note="Removed in mature form"
FT /evidence="ECO:0000269|Ref.1"
FT /id="PRO_0000033386"
FT CHAIN 102..649
FT /note="Acid beta-fructofuranosidase 70 kDa monomer"
FT /id="PRO_0000438789"
FT CHAIN 102..328
FT /note="Acid beta-fructofuranosidase 30 kDa subunit"
FT /id="PRO_0000033387"
FT CHAIN 329..649
FT /note="Acid beta-fructofuranosidase 38 kDa subunit"
FT /id="PRO_0000033388"
FT TOPO_DOM 1..22
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 23..43
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 44..649
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT REGION 52..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 130
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10067"
FT BINDING 127..130
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q43866"
FT BINDING 146
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q43866"
FT BINDING 154
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q43866"
FT BINDING 189..190
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q43866"
FT BINDING 253..254
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q43866"
FT BINDING 308
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q43866"
FT BINDING 341
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q43866"
FT CARBOHYD 210
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 275
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 618
FT /note="N-linked (GlcNAc...) (high mannose) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 498..546
FT /evidence="ECO:0000250|UniProtKB:Q43866"
SQ SEQUENCE 649 AA; 72167 MW; 0E0375B8C60017B9 CRC64;
MEHHKPLLPT SSHAAPTSST RKDLLFVLCG LLFLSSLVAY GGYRASGVPH AHLSSPTSNH
QQDHQSPTSL PSSKWYPVSR GVSSGVSEKS SNLLFAGEGG ASEAFPWDNS MLSWQRTSFH
FQPEKNWMND PNGPMYYKGW YHFFYQYNPN GAVWGDIVWG HAVSRDMIHW LHLPLAMVAD
QWYDKQGVWT GSATILPNGE IIMLYTGSTN ESVQVQNLAY PADPSDPLLL DWIKHTGNPV
LVPPPGIGAK DFRDPTTAWL TSEGKWRITI GSKLNKTGIA LVYDTEDFKT YELKEGLLRA
VPGTGMWECV DFFPVSKKNG NGLDTSVNGA EVKHVMKVSL DDDRHDYYAI GTYDDNKVLF
TPDDVKNDVG VGLRYDYGIF YASKTFYDQN KDRRILWGWI GESDSEYADV TKGWASVQSI
PRTVRLDTKT GSNLLQWPVD EVESLRLRSD EFKSLKAKPG SVVSLDIETA TQLDVVAEFE
IDTESLEKTA ESNEEFTCSS SGGAAQRGAL GPFGLLVLAD EGLSEYTPVY FYVIKGRNGN
LRTSFCSDQS RSSQANDVRK QIFGSVVPVL KGEKFSLRML VDHSIVESFA QGGRTCVTSR
VYPTKAIYGA ARLFLFNNAT EATVTASLKV WQMNSAFIRP FPFNPDQKS
