ID   INV1_CAPAN              Reviewed;         640 AA.
AC   P93761;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   02-SEP-2026, entry version 94.
DE   RecName: Full=Acid beta-fructofuranosidase AIV-18;
DE            EC=3.2.1.26;
DE   AltName: Full=Acid invertase;
DE   AltName: Full=Acid sucrose hydrolase;
DE   Flags: Precursor;
OS   Capsicum annuum (Capsicum pepper).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Capsiceae; Capsicum.
OX   NCBI_TaxID=4072;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Fruit;
RA   Choi D., Lee K.-W., Kim S.;
RT   "Isolation and characterization of acid invertase cDNA clone in Hot pepper
RT   (Capsicum annuum L.) fruits.";
RL   J. Plant Biol. 40:298-303(1997).
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: May be present in two forms, a 70 kDa monomer and a
CC       heterodimer of the 30 kDa and 38 kDa subunits. The ratio of the levels
CC       of the two forms within cells appears to be regulated developmentally
CC       (By similarity). {ECO:0000250|UniProtKB:P29001}.
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   -!- SIMILARITY: Belongs to the glycosyl hydrolase 32 family. {ECO:0000305}.
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DR   EMBL; U87849; AAB48484.1; -; mRNA.
DR   PIR; T09534; T09534.
DR   RefSeq; NP_001311791.1; NM_001324862.1.
DR   AlphaFoldDB; P93761; -.
DR   SMR; P93761; -.
DR   GeneID; 107863437; -.
DR   KEGG; cann:107863437; -.
DR   OrthoDB; 202537at2759; -.
DR   UniPathway; UPA00238; -.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005775; C:vacuolar lumen; ISS:UniProtKB.
DR   GO; GO:0004564; F:beta-fructofuranosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005985; P:sucrose metabolic process; IEA:UniProtKB-UniPathway.
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   2: Evidence at transcript level;
KW   Disulfide bond; Glycoprotein; Glycosidase; Hydrolase; Membrane;
KW   Signal-anchor; Transmembrane; Transmembrane helix; Vacuole.
FT   CHAIN           1..640
FT                   /note="Acid beta-fructofuranosidase AIV-18"
FT                   /id="PRO_0000169866"
FT   PROPEP          1..99
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250|UniProtKB:P80065"
FT                   /id="PRO_0000438788"
FT   TOPO_DOM        1..33
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        34..54
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        55..640
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          62..89
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        62..86
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        126
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10067"
FT   BINDING         123..126
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q43866"
FT   BINDING         142
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q43866"
FT   BINDING         150
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q43866"
FT   BINDING         185..186
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q43866"
FT   BINDING         249..250
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q43866"
FT   BINDING         302
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q43866"
FT   BINDING         335
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q43866"
FT   CARBOHYD        152
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        219
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        491
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        612
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        492..540
FT                   /evidence="ECO:0000250|UniProtKB:Q43866"
SQ   SEQUENCE   640 AA;  70621 MW;  D3C628B7A7E6870B CRC64;
     MAIHPSSYDP ETSTTHYTFL PGQPDSGHRK SIKVVSVILL SSFFLLYLAA FVILNNQPPN
     LQNKSPSASE TLTPATPSRG VSQGVSEKTF KDVSGTSQVS YTWSNAMLNW QRTAYHFQPQ
     KNWMNDPNGP LYHKGWYHLF YQYNPDSAIW GNITWGHAVS TDLIHWLYLP FAMVPDQWYD
     INGVWTGSAT ILPDGLIMML YTGDTDDYVQ VQNLAYPANL SDPLLLDWVK YQGNPVLVPP
     PGIGVKDFRD PTTAWTGPQN GQWLLTIGSK VGKTGIALVY ETSNFKLLDG VLHAVPGTGM
     WECVDFYPVS TLDANGLDTS YNGPGIKHVL KASLDDNKQD HYVIGTYDPV KNKFSPDNPD
     LDCGIGLRLD YGRYYASKTF YDPKKQRRVL WGWIGETDSE SADLQKGWAS VQSIPRTVLF
     DKKTGTHLLQ WPVAEIESLR SGDPKVKEVN LQPGSIELLH VDSAAQFDIE ASFEVDRVTL
     EGIIEADVGY NCSTSGGAAS RGILGPFGVV VIADQTLSEL TPVYFYISRG ADGRAEAHFC
     ADQTRSSEAP GVAKQVYGSS VPVLDGEKHR MRLLVDHSIV ESFAQGGRTV ITSRIYPTKA
     VNGAARLFVF NNATGAIVTA SLKIWSLESA DIRSFPLQKL
//