INV1_YEASX
ID INV1_YEASX Reviewed; 532 AA.
AC P10594;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Invertase 1;
DE EC=3.2.1.26;
DE AltName: Full=Beta-fructofuranosidase 1;
DE AltName: Full=Saccharase;
DE Flags: Precursor;
GN Name=SUC1;
OS Saccharomyces cerevisiae (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=4932;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-73.
RX PubMed=2835632; DOI=10.1007/bf00425699;
RA Hohmann S., Gozalbo D.;
RT "Structural analysis of the 5' regions of yeast SUC genes revealed
RT analogous palindromes in SUC, MAL and GAL.";
RL Mol. Gen. Genet. 211:446-454(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Hohmann S.;
RL Submitted (NOV-1988) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP IDENTIFICATION OF ISOFORMS, AND GLYCOSYLATION.
RX PubMed=6765604; DOI=10.1128/mcb.1.5.469-474.1981;
RA Rodriguez L., Lampen J.O., MacKay V.L.;
RT "SUC1 gene of Saccharomyces: a structural gene for the large (glycoprotein)
RT and small (carbohydrate-free) forms of invertase.";
RL Mol. Cell. Biol. 1:469-474(1981).
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: [Isoform Intracellular]: Cytoplasm {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Isoform Secreted]: Secreted.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=Secreted;
CC IsoId=P10594-1; Sequence=Displayed;
CC Name=Intracellular;
CC IsoId=P10594-2; Sequence=VSP_019610;
CC -!- PTM: Isoform Secreted is glycosylated. Isoform Intracellular is not
CC glycosylated. {ECO:0000269|PubMed:6765604}.
CC -!- MISCELLANEOUS: [Isoform Intracellular]: Produced by alternative
CC initiation at Met-21 of isoform Secreted. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 32 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X07570; CAA30457.1; -; Genomic_DNA.
DR PIR; S27372; S27372.
DR AlphaFoldDB; P10594; -.
DR SMR; P10594; -.
DR Allergome; 8263; Sac c Invertase.
DR CAZy; GH32; Glycoside Hydrolase Family 32.
DR CLAE; SUC32A_YEAST; -.
DR PRIDE; P10594; -.
DR SGD; S000029531; SUC1.
DR VEuPathDB; FungiDB:YIL162W; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; 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 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 Alternative initiation; Cytoplasm; Glycoprotein; Glycosidase; Hydrolase;
KW Secreted; Signal.
FT SIGNAL 1..19
FT CHAIN 20..532
FT /note="Invertase 1"
FT /id="PRO_0000033398"
FT ACT_SITE 42
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10067"
FT BINDING 39..42
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 60
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 102..103
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 170..171
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 223
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 311
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CARBOHYD 23
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 64
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 111
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 112
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 118
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 165
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 275
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 356
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 369
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 384
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 398
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 512
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..20
FT /note="Missing (in isoform Intracellular)"
FT /evidence="ECO:0000305"
FT /id="VSP_019610"
SQ SEQUENCE 532 AA; 60570 MW; 3280EF260EA01606 CRC64;
MLLQAFLFLL AGFAAKISAS MTNETSDRPL VHFTPNKGWM NDPNGLWYDA KEGKWHLYFQ
YNPNDTVWGL PLFWGHATSD DLTHWQDEPV AIAPKRKDSG AYSGSMVIDY NNTSGFFNDT
IDPRQRCVAI WTYNTPESEE QYISYSLDGG YTFTEYQKNP VLAANSTQFR DPKVFWYEPS
KKWIMTAAKS QDYKIEIYSS DDLKSWKLES AFANEGFLGY QYECPGLIEV PSEQDPSKSH
WVMFISINPG APAGGSFNQY FVGSFNGHHF EAFDNQSRVV DFGKDYYALQ TFFNTDPTYG
SALGIAWASN WEYSAFVPSN PWRSSMSLVR PFSLNTEYQA NPETELINLK AEPILNISSA
GPWSRFATNT TLTKANSYNV DLSNSTGTLE FELVYAVNTT QTISKSVFAD LSLWFKGLED
PEEYLRMGFE VSASSFFLDR GNSKVKFVKE NPYFTNRMSV NNQPFKSEND LSYYKVYGLL
DQNILELYFN DGDVVSTNTY FMTTGNALGS VNMTTGVDNL FYIDKFQVRE VK
