INV2_YEAST
ID INV2_YEAST Reviewed; 532 AA.
AC P00724; D6VVC4; Q12671;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=Invertase 2;
DE EC=3.2.1.26;
DE AltName: Full=Beta-fructofuranosidase 2;
DE AltName: Full=Saccharase;
DE Flags: Precursor;
GN Name=SUC2; OrderedLocusNames=YIL162W;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6300785; DOI=10.1093/nar/11.6.1943;
RA Taussig R., Carlson M.;
RT "Nucleotide sequence of the yeast SUC2 gene for invertase.";
RL Nucleic Acids Res. 11:1943-1954(1983).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169870;
RA Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D.,
RA Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., Harris D.E.,
RA Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C.,
RA Pearson D., Rajandream M.A., Rice P., Rowley N., Skelton J., Smith V.,
RA Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IX.";
RL Nature 387:84-87(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-67.
RC STRAIN=33;
RX PubMed=1888528;
RA Xie K.W., Feng B., Li Y.Y.;
RT "[The effects of upstream region of SUC2 gene on its expression].";
RL Yi Chuan Xue Bao 18:175-184(1991).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-54.
RX PubMed=6341817; DOI=10.1128/mcb.3.3.439-447.1983;
RA Carlson M., Taussig R., Kustu S., Botstein D.;
RT "The secreted form of invertase in Saccharomyces cerevisiae is synthesized
RT from mRNA encoding a signal sequence.";
RL Mol. Cell. Biol. 3:439-447(1983).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-30.
RX PubMed=6396505; DOI=10.1128/mcb.4.12.2750-2757.1984;
RA Sarokin L., Carlson M.;
RT "Upstream region required for regulated expression of the glucose-
RT repressible SUC2 gene of Saccharomyces cerevisiae.";
RL Mol. Cell. Biol. 4:2750-2757(1984).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-21.
RX PubMed=3537718; DOI=10.1128/mcb.6.7.2382-2391.1986;
RA Kaiser C.A., Botstein D.;
RT "Secretion-defective mutations in the signal sequence for Saccharomyces
RT cerevisiae invertase.";
RL Mol. Cell. Biol. 6:2382-2391(1986).
RN [8]
RP PROTEIN SEQUENCE OF 20-27 AND 38-45, ACTIVE SITE, AND MUTAGENESIS OF
RP ASP-42.
RX PubMed=2113524; DOI=10.1016/s0021-9258(19)38518-7;
RA Reddy V.A., Maley F.;
RT "Identification of an active-site residue in yeast invertase by affinity
RT labeling and site-directed mutagenesis.";
RL J. Biol. Chem. 265:10817-10820(1990).
RN [9]
RP PROTEIN SEQUENCE OF 21-532, AND GLYCOSYLATION AT ASN-23; ASN-64; ASN-97;
RP ASN-111; ASN-118; ASN-165; ASN-266; ASN-275; ASN-356; ASN-369; ASN-384;
RP ASN-398 AND ASN-512.
RX PubMed=3284881; DOI=10.1016/s0021-9258(18)68592-8;
RA Reddy V.A., Johnson R.S., Biemann K., Williams R.S., Ziegler F.D.,
RA Trimble R.B., Maley F.;
RT "Characterization of the glycosylation sites in yeast external invertase.
RT I. N-linked oligosaccharide content of the individual sequons.";
RL J. Biol. Chem. 263:6978-6985(1988).
RN [10]
RP IDENTIFICATION OF ISOFORMS, AND SUBCELLULAR LOCATION.
RX PubMed=7039847; DOI=10.1016/0092-8674(82)90384-1;
RA Carlson M., Botstein D.;
RT "Two differentially regulated mRNAs with different 5' ends encode secreted
RT with intracellular forms of yeast invertase.";
RL Cell 28:145-154(1982).
RN [11]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
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.
CC -!- SUBCELLULAR LOCATION: [Isoform Secreted]: Secreted.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=Secreted;
CC IsoId=P00724-1; Sequence=Displayed;
CC Name=Intracellular;
CC IsoId=P00724-2; Sequence=VSP_019611;
CC -!- PTM: Isoform Secreted is glycosylated. Isoform Intracellular is not
CC glycosylated. {ECO:0000269|PubMed:3284881}.
CC -!- MISCELLANEOUS: Present with 1780 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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}.
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DR EMBL; Z46921; CAA87030.1; -; Genomic_DNA.
DR EMBL; U19781; AAA73474.1; -; Genomic_DNA.
DR EMBL; V01311; CAA24618.1; -; Genomic_DNA.
DR EMBL; K03294; AAA35127.1; -; Genomic_DNA.
DR EMBL; M13627; AAA35129.1; -; Genomic_DNA.
DR EMBL; BK006942; DAA08390.1; -; Genomic_DNA.
DR PIR; A00899; IFBY.
DR RefSeq; NP_012104.1; NM_001179510.1. [P00724-1]
DR PDB; 4EQV; X-ray; 3.40 A; A/B/C/D/E/F/G/H=21-532.
DR PDBsum; 4EQV; -.
DR AlphaFoldDB; P00724; -.
DR SMR; P00724; -.
DR BioGRID; 34830; 91.
DR DIP; DIP-5542N; -.
DR IntAct; P00724; 2.
DR MINT; P00724; -.
DR STRING; 4932.YIL162W; -.
DR CAZy; GH32; Glycoside Hydrolase Family 32.
DR CLAE; SUC32B_YEAST; -.
DR GlyConnect; 303; 10 N-Linked glycans.
DR iPTMnet; P00724; -.
DR COMPLUYEAST-2DPAGE; P00724; -.
DR MaxQB; P00724; -.
DR PaxDb; P00724; -.
DR PRIDE; P00724; -.
DR EnsemblFungi; YIL162W_mRNA; YIL162W; YIL162W. [P00724-1]
DR GeneID; 854644; -.
DR KEGG; sce:YIL162W; -.
DR SGD; S000001424; SUC2.
DR VEuPathDB; FungiDB:YIL162W; -.
DR eggNOG; KOG0228; Eukaryota.
DR HOGENOM; CLU_001528_3_3_1; -.
DR InParanoid; P00724; -.
DR OMA; GTEWRHA; -.
DR BioCyc; YEAST:YIL162W-MON; -.
DR BRENDA; 3.2.1.26; 984.
DR PRO; PR:P00724; -.
DR Proteomes; UP000002311; Chromosome IX.
DR RNAct; P00724; protein.
DR GO; GO:0071944; C:cell periphery; HDA:SGD.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005576; C:extracellular region; IDA:SGD.
DR GO; GO:0000324; C:fungal-type vacuole; HDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0004564; F:beta-fructofuranosidase activity; IDA:SGD.
DR GO; GO:0051670; F:inulinase activity; IDA:SGD.
DR GO; GO:0004575; F:sucrose alpha-glucosidase activity; IBA:GO_Central.
DR GO; GO:0010147; P:fructan catabolic process; IMP:SGD.
DR GO; GO:1902927; P:inulin catabolic process; IDA:SGD.
DR GO; GO:0034484; P:raffinose catabolic process; IMP:SGD.
DR GO; GO:0005987; P:sucrose catabolic process; IDA:SGD.
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 3D-structure; Alternative initiation; Cytoplasm; Direct protein sequencing;
KW Glycoprotein; Glycosidase; Hydrolase; Reference proteome; Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000269|PubMed:2113524"
FT CHAIN 20..532
FT /note="Invertase 2"
FT /id="PRO_0000033399"
FT ACT_SITE 42
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10067,
FT ECO:0000269|PubMed:2113524"
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:0000269|PubMed:3284881"
FT CARBOHYD 64
FT /note="N-linked (GlcNAc...) asparagine; partial"
FT /evidence="ECO:0000269|PubMed:3284881"
FT CARBOHYD 97
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:3284881"
FT CARBOHYD 111
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:3284881"
FT CARBOHYD 118
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:3284881"
FT CARBOHYD 165
FT /note="N-linked (GlcNAc...) asparagine; partial"
FT /evidence="ECO:0000269|PubMed:3284881"
FT CARBOHYD 266
FT /note="N-linked (GlcNAc...) asparagine; partial"
FT /evidence="ECO:0000269|PubMed:3284881"
FT CARBOHYD 275
FT /note="N-linked (GlcNAc...) asparagine; partial"
FT /evidence="ECO:0000269|PubMed:3284881"
FT CARBOHYD 356
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:3284881"
FT CARBOHYD 369
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:3284881"
FT CARBOHYD 384
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:3284881"
FT CARBOHYD 398
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:3284881"
FT CARBOHYD 512
FT /note="N-linked (GlcNAc...) asparagine; partial"
FT /evidence="ECO:0000269|PubMed:3284881"
FT VAR_SEQ 1..20
FT /note="Missing (in isoform Intracellular)"
FT /evidence="ECO:0000305"
FT /id="VSP_019611"
FT MUTAGEN 42
FT /note="D->N: Loss of activity."
FT /evidence="ECO:0000269|PubMed:2113524"
FT CONFLICT 51
FT /note="K -> P (in Ref. 4; AAA73474)"
FT /evidence="ECO:0000305"
FT CONFLICT 409
FT /note="A -> P (in Ref. 9; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 30..32
FT /evidence="ECO:0007829|PDB:4EQV"
FT STRAND 36..49
FT /evidence="ECO:0007829|PDB:4EQV"
FT TURN 50..53
FT /evidence="ECO:0007829|PDB:4EQV"
FT STRAND 54..67
FT /evidence="ECO:0007829|PDB:4EQV"
FT STRAND 73..84
FT /evidence="ECO:0007829|PDB:4EQV"
FT STRAND 86..92
FT /evidence="ECO:0007829|PDB:4EQV"
FT STRAND 100..108
FT /evidence="ECO:0007829|PDB:4EQV"
FT HELIX 123..125
FT /evidence="ECO:0007829|PDB:4EQV"
FT STRAND 127..134
FT /evidence="ECO:0007829|PDB:4EQV"
FT STRAND 139..145
FT /evidence="ECO:0007829|PDB:4EQV"
FT STRAND 147..152
FT /evidence="ECO:0007829|PDB:4EQV"
FT STRAND 170..177
FT /evidence="ECO:0007829|PDB:4EQV"
FT TURN 178..181
FT /evidence="ECO:0007829|PDB:4EQV"
FT STRAND 182..189
FT /evidence="ECO:0007829|PDB:4EQV"
FT HELIX 190..192
FT /evidence="ECO:0007829|PDB:4EQV"
FT STRAND 194..205
FT /evidence="ECO:0007829|PDB:4EQV"
FT STRAND 207..212
FT /evidence="ECO:0007829|PDB:4EQV"
FT STRAND 223..234
FT /evidence="ECO:0007829|PDB:4EQV"
FT STRAND 239..247
FT /evidence="ECO:0007829|PDB:4EQV"
FT STRAND 257..265
FT /evidence="ECO:0007829|PDB:4EQV"
FT STRAND 270..275
FT /evidence="ECO:0007829|PDB:4EQV"
FT STRAND 278..280
FT /evidence="ECO:0007829|PDB:4EQV"
FT STRAND 283..285
FT /evidence="ECO:0007829|PDB:4EQV"
FT STRAND 287..291
FT /evidence="ECO:0007829|PDB:4EQV"
FT TURN 297..299
FT /evidence="ECO:0007829|PDB:4EQV"
FT STRAND 303..309
FT /evidence="ECO:0007829|PDB:4EQV"
FT TURN 311..315
FT /evidence="ECO:0007829|PDB:4EQV"
FT STRAND 316..318
FT /evidence="ECO:0007829|PDB:4EQV"
FT STRAND 320..323
FT /evidence="ECO:0007829|PDB:4EQV"
FT STRAND 329..343
FT /evidence="ECO:0007829|PDB:4EQV"
FT STRAND 345..354
FT /evidence="ECO:0007829|PDB:4EQV"
FT STRAND 374..382
FT /evidence="ECO:0007829|PDB:4EQV"
FT STRAND 387..397
FT /evidence="ECO:0007829|PDB:4EQV"
FT STRAND 410..416
FT /evidence="ECO:0007829|PDB:4EQV"
FT STRAND 418..423
FT /evidence="ECO:0007829|PDB:4EQV"
FT STRAND 425..430
FT /evidence="ECO:0007829|PDB:4EQV"
FT TURN 431..434
FT /evidence="ECO:0007829|PDB:4EQV"
FT STRAND 435..439
FT /evidence="ECO:0007829|PDB:4EQV"
FT HELIX 446..450
FT /evidence="ECO:0007829|PDB:4EQV"
FT STRAND 465..468
FT /evidence="ECO:0007829|PDB:4EQV"
FT STRAND 471..489
FT /evidence="ECO:0007829|PDB:4EQV"
FT TURN 490..493
FT /evidence="ECO:0007829|PDB:4EQV"
FT STRAND 494..499
FT /evidence="ECO:0007829|PDB:4EQV"
FT STRAND 503..505
FT /evidence="ECO:0007829|PDB:4EQV"
FT STRAND 510..517
FT /evidence="ECO:0007829|PDB:4EQV"
FT STRAND 521..530
FT /evidence="ECO:0007829|PDB:4EQV"
SQ SEQUENCE 532 AA; 60639 MW; 7D8AB33E6772B775 CRC64;
MLLQAFLFLL AGFAAKISAS MTNETSDRPL VHFTPNKGWM NDPNGLWYDE KDAKWHLYFQ
YNPNDTVWGT PLFWGHATSD DLTNWEDQPI AIAPKRNDSG AFSGSMVVDY NNTSGFFNDT
IDPRQRCVAI WTYNTPESEE QYISYSLDGG YTFTEYQKNP VLAANSTQFR DPKVFWYEPS
QKWIMTAAKS QDYKIEIYSS DDLKSWKLES AFANEGFLGY QYECPGLIEV PTEQDPSKSY
WVMFISINPG APAGGSFNQY FVGSFNGTHF EAFDNQSRVV DFGKDYYALQ TFFNTDPTYG
SALGIAWASN WEYSAFVPTN PWRSSMSLVR KFSLNTEYQA NPETELINLK AEPILNISNA
GPWSRFATNT TLTKANSYNV DLSNSTGTLE FELVYAVNTT QTISKSVFAD LSLWFKGLED
PEEYLRMGFE VSASSFFLDR GNSKVKFVKE NPYFTNRMSV NNQPFKSEND LSYYKVYGLL
DQNILELYFN DGDVVSTNTY FMTTGNALGS VNMTTGVDNL FYIDKFQVRE VK
