INVB_DAUCA
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 03-AUG-2022, entry version 101.
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 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 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..40
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 103..117
FT /note="Polar 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
