ID   INV1_DAUCA              Reviewed;         592 AA.
AC   P26792;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   25-MAY-2022, entry version 103.
DE   RecName: Full=Beta-fructofuranosidase, insoluble isoenzyme 1;
DE            EC=3.2.1.26;
DE   AltName: Full=Cell wall beta-fructosidase 1;
DE   AltName: Full=Invertase 1;
DE   AltName: Full=Sucrose hydrolase 1;
DE   Flags: Precursor;
GN   Name=INV1;
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], AND PARTIAL PROTEIN SEQUENCE.
RC   STRAIN=cv. Queen Anne's Lace;
RX   PubMed=2152110; DOI=10.2307/3869263;
RA   Sturm A., Chrispeels M.J.;
RT   "cDNA cloning of carrot extracellular beta-fructosidase and its expression
RT   in response to wounding and bacterial infection.";
RL   Plant Cell 2:1107-1119(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8220495; DOI=10.1046/j.1365-313x.1993.04030545.x;
RA   Ramloch-Lorenz K., Knudsen S., Sturm A.;
RT   "Molecular characterization of the gene for carrot cell wall beta-
RT   fructosidase.";
RL   Plant J. 4:545-554(1993).
CC   -!- FUNCTION: May play an important role in phloem unloading and in stress
CC       response.
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   -!- SUBCELLULAR LOCATION: Secreted, cell wall. Note=Ionically bound to the
CC       cell wall.
CC   -!- TISSUE SPECIFICITY: In leaves and roots of young plants.
CC   -!- INDUCTION: By wounding and bacterial infection.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 32 family. {ECO:0000305}.
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DR   EMBL; M58362; AAA03516.1; -; mRNA.
DR   EMBL; X69321; CAA49162.1; -; Genomic_DNA.
DR   PIR; JQ0991; JQ0991.
DR   PIR; S61503; S61503.
DR   AlphaFoldDB; P26792; -.
DR   SMR; P26792; -.
DR   CAZy; GH32; Glycoside Hydrolase Family 32.
DR   GlyConnect; 69; 9 N-Linked glycans (3 sites).
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
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   1: Evidence at protein level;
KW   Cell wall; Direct protein sequencing; Glycoprotein; Glycosidase; Hydrolase;
KW   Secreted; Signal; Zymogen.
FT   SIGNAL          1..39
FT                   /evidence="ECO:0000255"
FT   PROPEP          40..48
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000033366"
FT   CHAIN           49..592
FT                   /note="Beta-fructofuranosidase, insoluble isoenzyme 1"
FT                   /id="PRO_0000033367"
FT   ACT_SITE        74
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10067"
FT   CARBOHYD        170
FT                   /note="N-linked (GlcNAc...) (complex) asparagine"
FT                   /id="CAR_000145"
FT   CARBOHYD        195
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        311
FT                   /note="N-linked (GlcNAc...) (complex) asparagine"
FT                   /id="CAR_000146"
FT   CARBOHYD        348
FT                   /note="N-linked (GlcNAc...) (high mannose) asparagine"
FT                   /id="CAR_000147"
FT   CARBOHYD        570
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        133
FT                   /note="R -> W (in Ref. 2; CAA49162)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        487
FT                   /note="A -> V (in Ref. 2; CAA49162)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   592 AA;  66813 MW;  E3DF85355D277D0C CRC64;
     MGVTIRNRNY DHGSLPFLQS LLAILLVTTT TLHINGVEAF HEIHYNLQSV GAENVKQVHR
     TGYHFQPKQN WINDPNGPMY YKGVYHLFYQ YNPKGAVWGN IVWAHSVSTD LINWTPLEPA
     IFPSKPFDKY GCRSGSATIL PGNKPVILYT GIVEGPPKNV QVQNYAIPAN LSDPYLRKWI
     KPDNNPLVVA NNGENATAFR DPTTAWLDKS GHWKMLVGSK RNRRGIAYLY RSKDFIKWTK
     AKHPIHSQAN TGMWECPDFF PVSLKGLNGL DTSVTGESVK HVLKVSLDLT RYEYYTVGTY
     LTDKDRYIPD NTSVDGWAGL RYDYGNFYAS KTFFDPSKNR RILWGWANES DSTAHDVAKG
     WAGIQLIPRT LWLDPSGKQL MQWPIEELET LRGSKVKFSR KQDLSKGILV EVKGITAAQA
     DVEVTFSFKS LAKREPFDPK WLEYDAEKIC SLKGSTVQGG VGPFGLLTLA SEKLEEYTPV
     FFRVFKAQNT HKVLMCSDAT RSSLKEGLYR PSFAGFVDVD LATDKKISLR SLIDNSVVES
     FGAKGKTCIS SRVYPTLAVY ENAHLYVFNN GSETITVENL DAWSMKKPLR MN