INV1_CAPAN
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 03-AUG-2022, entry version 86.
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 CAZy; GH32; Glycoside Hydrolase Family 32.
DR GeneID; 107863437; -.
DR KEGG; cann:107863437; -.
DR UniPathway; UPA00238; -.
DR Proteomes; UP000189700; Genome assembly.
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 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 7..21
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
