INVA_SOLLC
ID INVA_SOLLC Reviewed; 636 AA.
AC P29000;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Acid beta-fructofuranosidase;
DE EC=3.2.1.26;
DE AltName: Full=Acid invertase;
DE Short=AI;
DE AltName: Full=Acid sucrose hydrolase;
DE AltName: Full=Vacuolar invertase;
DE Flags: Precursor;
GN Name=TIV1; Synonyms=AIV-1;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND SUBCELLULAR LOCATION.
RC STRAIN=cv. UC82B, and Wild-type;
RX PubMed=8095164; DOI=10.1007/bf00028808;
RA Elliott K.J., Butler W.O., Dickinson C.D., Konno Y., Vedvick T.S.,
RA Fitzmaurice L., Mirkov T.E.;
RT "Isolation and characterization of fruit vacuolar invertase genes from two
RT tomato species and temporal differences in mRNA levels during fruit
RT ripening.";
RL Plant Mol. Biol. 21:515-524(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Klann E.M., Yelle S., Bennett A.B.;
RL Submitted (MAY-1992) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-553.
RC TISSUE=Fruit;
RX PubMed=1304771; DOI=10.1266/jjg.67.491;
RA Ohyama A., Hirai M., Nishimura S.;
RT "A novel cDNA clone for acid invertase in tomato fruit.";
RL Jpn. J. Genet. 67:491-492(1992).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 474-636.
RC STRAIN=cv. Ailsa Craig; TISSUE=Fruit;
RA Davies K.M., Grierson D.;
RL Submitted (JAN-1994) to the EMBL/GenBank/DDBJ databases.
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.
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 {ECO:0000269|PubMed:8095164}.
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 -!- SIMILARITY: Belongs to the glycosyl hydrolase 32 family. {ECO:0000305}.
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DR EMBL; Z12025; CAA78060.1; -; mRNA.
DR EMBL; Z12026; CAA78061.1; -; mRNA.
DR EMBL; Z12027; CAA78062.1; -; Genomic_DNA.
DR EMBL; Z12028; CAA78063.1; -; Genomic_DNA.
DR EMBL; M81081; AAA34132.1; -; mRNA.
DR EMBL; D11350; BAA01954.1; -; mRNA.
DR EMBL; X77264; CAA54480.1; -; mRNA.
DR PIR; S31155; S31155.
DR RefSeq; NP_001234843.2; NM_001247914.2.
DR AlphaFoldDB; P29000; -.
DR SMR; P29000; -.
DR STRING; 4081.Solyc03g083910.2.1; -.
DR CAZy; GH32; Glycoside Hydrolase Family 32.
DR PaxDb; P29000; -.
DR PRIDE; P29000; -.
DR GeneID; 543992; -.
DR KEGG; sly:543992; -.
DR eggNOG; KOG0228; Eukaryota.
DR InParanoid; P29000; -.
DR OrthoDB; 405663at2759; -.
DR BRENDA; 3.2.1.26; 3101.
DR SABIO-RK; P29000; -.
DR UniPathway; UPA00238; -.
DR Proteomes; UP000004994; Unplaced.
DR ExpressionAtlas; P29000; baseline and differential.
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:0005985; P:sucrose metabolic process; IEA:UniProtKB-UniPathway.
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 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Glycosidase; Hydrolase; Membrane;
KW Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix;
KW Vacuole; Zymogen.
FT PROPEP 1..92
FT /note="Removed in mature form"
FT /evidence="ECO:0000250|UniProtKB:P80065"
FT /id="PRO_0000033374"
FT CHAIN 93..636
FT /note="Acid beta-fructofuranosidase"
FT /id="PRO_0000033375"
FT TOPO_DOM 1..31
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 32..52
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 53..636
FT /note="Lumenal"
FT /evidence="ECO:0000305"
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"
FT ACT_SITE 118
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10067"
FT BINDING 115..118
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q43866"
FT BINDING 134
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q43866"
FT BINDING 142
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q43866"
FT BINDING 177..178
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q43866"
FT BINDING 241..242
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q43866"
FT BINDING 297
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q43866"
FT BINDING 330
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q43866"
FT CARBOHYD 144
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 211
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 276
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 608
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 488..536
FT /evidence="ECO:0000250|UniProtKB:Q43866"
FT CONFLICT 542..553
FT /note="SSEAPGVGKQVY -> FAFLSGTINLSL (in Ref. 3; BAA01954)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 636 AA; 70097 MW; 74C46246FA93974B CRC64;
MATQCYDPEN SASRYTLLPD QPDSGHRKSL KIISGIFLSV FLLLSVAFFP ILNNQSPDLQ
IDSRSPAPPS RGVSQGVSDK TFRDVAGASH VSYAWSNAML SWQRTAYHFQ PQKNWMNDPN
GPLYHKGWYH LFYQYNPDSA IWGNITWGHA VSKDLIHWLY LPFAMVPDQW YDINGVWTGS
ATILPDGQIM MLYTGDTDDY VQVQNLAYPA NLSDPLLLDW VKFKGNPVLV PPPGIGVKDF
RDPTTAWTGP QNGQWLLTIG SKIGKTGVAL VYETSNFTSF KLLDGVLHAV PGTGMWECVD
FYPVSTKKTN GLDTSYNGPG VKHVLKASLD DNKQDHYAIG TYDLGKNKWT PDNPELDCGI
GLRLDYGKYY ASKTFYDPKK 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
