ID   INVB_DAUCA              Reviewed;         661 AA.
AC   P80065; Q42719; Q42720; Q42721;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   11-JAN-2001, sequence version 2.
DT   02-SEP-2026, entry version 107.
DE   RecName: Full=Beta-fructofuranosidase, soluble isoenzyme I;
DE            EC=3.2.1.26;
DE   AltName: Full=Invertase;
DE   AltName: Full=Saccharase;
DE   AltName: Full=Sucrose hydrolase;
DE   Flags: Precursor;
GN   Name=INV*DC4;
OS   Daucus carota (Wild carrot).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; campanulids; Apiales; Apiaceae; Apioideae; Scandiceae; Daucinae;
OC   Daucus; Daucus sect. Daucus.
OX   NCBI_TaxID=4039;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Nantaise; TISSUE=Flower bud;
RX   PubMed=8016265; DOI=10.1104/pp.104.4.1351;
RA   Unger C., Hardegger M., Lienhard S., Sturm A.;
RT   "cDNA cloning of carrot (Daucus carota) soluble acid beta-
RT   fructofuranosidases and comparison with the cell wall isoenzyme.";
RL   Plant Physiol. 104:1351-1357(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=cv. Nantaise;
RA   Sturm A.;
RL   Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   PROTEIN SEQUENCE OF 116-121; 269-280; 410-437 AND 507-511, SUBCELLULAR
RP   LOCATION, AND SUBUNIT.
RC   STRAIN=cv. Nantaise; TISSUE=Seed;
RX   PubMed=1541302; DOI=10.1111/j.1432-1033.1992.tb16712.x;
RA   Unger C., Hofstenge J., Sturm A.;
RT   "Purification and characterization of a soluble beta-fructofuranosidase
RT   from Daucus carota.";
RL   Eur. J. Biochem. 204:915-921(1992).
CC   -!- FUNCTION: May participate in the regulation of the hexose level in
CC       mature tissues and in the utilization of sucrose stored in vacuoles.
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   -!- SUBUNIT: Monomer (PubMed:1541302). 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:1541302}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass type II
CC       membrane protein {ECO:0000255}. Vacuole {ECO:0000269|PubMed:1541302}.
CC       Vacuole lumen {ECO:0000250|UniProtKB:Q39041}. Note=May be released into
CC       the lumen of the vacuole from the tonoplast through a proteolytic
CC       processing. {ECO:0000250|UniProtKB:Q39041}.
CC   -!- PTM: N-glycosylated; high-mannose and high-xylose complex glycans.
CC   -!- MISCELLANEOUS: There are at least three isozymes of beta-
CC       fructofuranosidase in carrot: one insoluble and two soluble ones.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 32 family. {ECO:0000305}.
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DR   EMBL; X75351; CAA53097.1; -; mRNA.
DR   EMBL; X75352; CAA53098.1; -; mRNA.
DR   EMBL; X75353; CAA53099.1; -; mRNA.
DR   EMBL; Y18707; CAA77267.1; -; Genomic_DNA.
DR   PIR; S37590; S37590.
DR   PIR; S37591; S37591.
DR   PIR; S37592; S37592.
DR   AlphaFoldDB; P80065; -.
DR   SMR; P80065; -.
DR   CAZy; GH32; Glycoside Hydrolase Family 32.
DR   GlyCosmos; P80065; 5 sites, No reported glycans.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005775; C:vacuolar lumen; ISS:UniProtKB.
DR   GO; GO:0005773; C:vacuole; EXP:UniProtKB.
DR   GO; GO:0004564; F:beta-fructofuranosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd18624; GH32_Fruct1-like; 1.
DR   FunFam; 2.115.10.20:FF:000001; Beta-fructofuranosidase, insoluble isoenzyme CWINV1; 1.
DR   FunFam; 2.60.120.560:FF:000002; Beta-fructofuranosidase, insoluble isoenzyme CWINV1; 1.
DR   Gene3D; 2.60.120.560; Exo-inulinase, domain 1; 1.
DR   Gene3D; 2.115.10.20; Glycosyl hydrolase domain, family 43; 1.
DR   InterPro; IPR021792; Beta-fructofuranosidase_N.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR050551; Fructan_Metab_Enzymes.
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   PANTHER; PTHR31953; BETA-FRUCTOFURANOSIDASE, INSOLUBLE ISOENZYME CWINV1-RELATED; 1.
DR   Pfam; PF08244; Glyco_hydro_32C; 1.
DR   Pfam; PF00251; Glyco_hydro_32N; 1.
DR   Pfam; PF11837; INV_N; 1.
DR   SMART; SM00640; Glyco_32; 1.
DR   SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 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; Signal-anchor; Transmembrane; Transmembrane helix;
KW   Vacuole; Zymogen.
FT   PROPEP          1..115
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000269|PubMed:1541302"
FT                   /id="PRO_0000033372"
FT   CHAIN           116..661
FT                   /note="Beta-fructofuranosidase, soluble isoenzyme I"
FT                   /id="PRO_0000033373"
FT   TOPO_DOM        1..44
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        45..65
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        66..661
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305"
FT   REGION          1..40
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          75..117
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        23..37
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        145
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10067"
FT   BINDING         142..145
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q43866"
FT   BINDING         161
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q43866"
FT   BINDING         169
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q43866"
FT   BINDING         204..205
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q43866"
FT   BINDING         268..269
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q43866"
FT   BINDING         323
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q43866"
FT   BINDING         356
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q43866"
FT   CARBOHYD        171
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        238
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        290
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        512
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        633
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        513..561
FT                   /evidence="ECO:0000250|UniProtKB:Q43866"
FT   VARIANT         21
FT                   /note="R -> L (in class 3)"
FT   VARIANT         52
FT                   /note="S -> A (in class 3)"
FT   VARIANT         56
FT                   /note="L -> F (in class 3)"
FT   VARIANT         85
FT                   /note="R -> H (in class 3)"
FT   VARIANT         210
FT                   /note="V -> I (in class 2 and class 3)"
FT   VARIANT         277
FT                   /note="R -> P (in class 2 and class 3)"
FT   VARIANT         334
FT                   /note="G -> V (in class 2)"
FT   VARIANT         418..423
FT                   /note="TDSESA -> SDNEST (in class 2 and class 3)"
FT   VARIANT         468
FT                   /note="D -> N (in class 2 and class 3)"
FT   VARIANT         503
FT                   /note="G -> R (in class 2)"
FT   VARIANT         586
FT                   /note="H -> P (in class 2 and class 3)"
FT   CONFLICT        422
FT                   /note="S -> P (in Ref. 3; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        425
FT                   /note="L -> V (in Ref. 3; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   661 AA;  73864 MW;  ED534C08D61745EA CRC64;
     MDTYHFLPSR DLEHASSYTP RPDSPETRHE PDPDRSKTNR RPIKIVSSVL LSTLILSFVI
     FLLVNPNVQQ VVRKKVSKNS NGEDRNKASK SPEMLGPPSR GVSQGVSEKS FRQATAEPSY
     PWTNDMLSWQ RTSFHFQPQE NWMNDPNGPL FHMGWYHLFY QYNPDSAIWG NITWGHAISR
     DLINWLHLPF AMQPDQWYDI NGVWTGSATV LPDGKIVMLY TGDTDDLVQV QNLAYPANLS
     DPLLLDWIKY PDNPVMFPPP GIGSTDFRDP TTAWIGRDGK WRITIGSKVN KTGISLMYKT
     TDFITYELLD NLLHAVPGTG MWECVDFYPV SVTGSNGLDT SVNGPGVKHV LKSSLDDDRH
     DYYALGTYDP INDKWTPDNP ELDVGIGLRL DYGKYYASKT FYDQDKERRL LWGWIGETDS
     ESADLLKGWA SVQSIPRTVV FDKKTGTNIL QWPVKEVESL RSRSYEIDDV ELKPGSLVPL
     KISSAAQLDI VASFEVDEEA FKGTYEADAS YNCTASEGAA GRGILGPFGI LVLADDPLSE
     LTPVYFYIAK GVDGNAKTYF CADQSRSSTA SDVDKEVYGS DVPVLHGESL SMRLLVDHSI
     VESFAQGGRT VITSRVYPTR AIYSAARVFL FNNATGVSVT ASVKAWQMAS ATLKPFPFDQ
     L
//