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Database: UniProt
Entry: Q8RVW4_SOLLC
LinkDB: Q8RVW4_SOLLC
Original site: Q8RVW4_SOLLC 
ID   Q8RVW4_SOLLC            Unreviewed;       636 AA.
AC   Q8RVW4;
DT   01-JUN-2002, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2002, sequence version 1.
DT   22-FEB-2023, entry version 76.
DE   RecName: Full=beta-fructofuranosidase {ECO:0000256|ARBA:ARBA00012758};
DE            EC=3.2.1.26 {ECO:0000256|ARBA:ARBA00012758};
OS   Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC   Solanum subgen. Lycopersicon.
OX   NCBI_TaxID=4081 {ECO:0000313|EMBL:AAL75450.1};
RN   [1] {ECO:0000313|EMBL:AAL75450.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Mature fruit {ECO:0000313|EMBL:AAL75450.1};
RA   Westphal S., Foetisch K., Haustein D., Vieths S., Scheurer S.;
RT   "Cloning and characterization of beta-fructofuranosidase, a newly
RT   identified glycoprotein as a minor allergen of tomato (Lycopersicon
RT   Esculentum).";
RL   Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004606}; Single-
CC       pass type II membrane protein {ECO:0000256|ARBA:ARBA00004606}. Vacuole
CC       lumen {ECO:0000256|ARBA:ARBA00004410}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 32 family.
CC       {ECO:0000256|ARBA:ARBA00009902, ECO:0000256|RuleBase:RU362110}.
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DR   EMBL; AF465613; AAL75450.1; -; mRNA.
DR   AlphaFoldDB; Q8RVW4; -.
DR   Allergome; 704; Sola l 2.
DR   Allergome; 706; Sola l 2.0102.
DR   CAZy; GH32; Glycoside Hydrolase Family 32.
DR   ExpressionAtlas; Q8RVW4; baseline and differential.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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   CDD; cd18624; GH32_Fruct1-like; 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   PANTHER; PTHR31953:SF84; ACID BETA-FRUCTOFURANOSIDASE; 1.
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   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU362110};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU362110};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Vacuole {ECO:0000256|ARBA:ARBA00022554}.
FT   TRANSMEM        32..52
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          62..100
FT                   /note="Beta-fructofuranosidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF11837"
FT   DOMAIN          108..427
FT                   /note="Glycosyl hydrolase family 32 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00251"
FT   DOMAIN          430..622
FT                   /note="Glycosyl hydrolase family 32 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08244"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..18
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   636 AA;  70073 MW;  B848DBB8ADFB036E CRC64;
     MATQCYDPEN SASRYTLLPD QPDSGHRKSL KIISGIFLSV FLLLSVAFFP ILNNQSPDLQ
     IDSRSPAPPS RGVSQGVSDK TFRDVAGASH VSYAWSNAML SWQRTAYHFQ PQKNWMNDPN
     GPLYHKGWYH LFYQYNPDSA IWGNITWGHA VSKDLIHWLY LPFAMVPDQW YDINGVWTGS
     ATILPDGQII MLYTGDTDDY VQVQNLAYPA NLSDPLLLDW VKFKANPVLV PPPGIGVKDF
     RDPITAWTGP QNGQWLLTIG SKIGKTGVAL VCETSNFTSF KLLDGVLHAV PGTGMWECVD
     FYPVSTKKTN GLDTSYNGPG VKHVLKASLD DNKQDHYAIG TYDLGKNKWT PDNPELDCGI
     GLRLDYGKYY ASKTFYDPKR ERRVLWGWIG ETDSESADLQ KGWASVQSIP RTVLYDKKTG
     THLLQWPVEE IESLRVGDPT VKQVDLQPGS IELLRVDSAA ELDIEASFEV DKVALQGIIE
     ADHVGFSCST SGGAASRGIL GPFGVIVIAD QTLSELTPVY FYISKGADGR AETHFCADQT
     RSSEAPGVGK QVYGSSVPVL DGEKHSMRLL VDHSIVESFA QGGRTVITSR IYPTKAVNGA
     ARLFVFNNAT GASVTASVKI WSLESANIQS FPLQDL
//
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