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Protein

Invertase 2

Gene

SUC2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

Hydrolysis of terminal non-reducing beta-D-fructofuranoside residues in beta-D-fructofuranosides.PROSITE-ProRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei42 – 421PROSITE-ProRule annotation1 Publication
Binding sitei60 – 601SubstrateBy similarity
Binding sitei223 – 2231SubstrateBy similarity
Binding sitei311 – 3111SubstrateBy similarity

GO - Molecular functioni

  • beta-fructofuranosidase activity Source: SGD
  • inulinase activity Source: SGD
  • sucrose alpha-glucosidase activity Source: GO_Central

GO - Biological processi

  • fructan catabolic process Source: SGD
  • inulin catabolic process Source: SGD
  • raffinose catabolic process Source: SGD
  • sucrose catabolic process Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Enzyme and pathway databases

BioCyciYEAST:YIL162W-MONOMER.

Protein family/group databases

CAZyiGH32. Glycoside Hydrolase Family 32.
mycoCLAPiSUC32B_YEAST.

Names & Taxonomyi

Protein namesi
Recommended name:
Invertase 2 (EC:3.2.1.26)
Alternative name(s):
Beta-fructofuranosidase 2
Saccharase
Gene namesi
Name:SUC2
Ordered Locus Names:YIL162W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome IX

Organism-specific databases

EuPathDBiFungiDB:YIL162W.
SGDiS000001424. SUC2.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: SGD
  • extracellular region Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi42 – 421D → N: Loss of activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 19191 PublicationAdd
BLAST
Chaini20 – 532513Invertase 2PRO_0000033399Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi23 – 231N-linked (GlcNAc...); in isoform Secreted1 Publication
Glycosylationi64 – 641N-linked (GlcNAc...); in isoform Secreted; partial1 Publication
Glycosylationi97 – 971N-linked (GlcNAc...); in isoform Secreted1 Publication
Glycosylationi111 – 1111N-linked (GlcNAc...); in isoform Secreted1 Publication
Glycosylationi118 – 1181N-linked (GlcNAc...); in isoform Secreted1 Publication
Glycosylationi165 – 1651N-linked (GlcNAc...); in isoform Secreted; partial1 Publication
Glycosylationi266 – 2661N-linked (GlcNAc...); in isoform Secreted; partial1 Publication
Glycosylationi275 – 2751N-linked (GlcNAc...); in isoform Secreted; partial1 Publication
Glycosylationi356 – 3561N-linked (GlcNAc...); in isoform Secreted1 Publication
Glycosylationi369 – 3691N-linked (GlcNAc...); in isoform Secreted1 Publication
Glycosylationi384 – 3841N-linked (GlcNAc...); in isoform Secreted1 Publication
Glycosylationi398 – 3981N-linked (GlcNAc...); in isoform Secreted1 Publication
Glycosylationi512 – 5121N-linked (GlcNAc...); in isoform Secreted; partial1 Publication

Post-translational modificationi

Isoform Secreted is glycosylated. Isoform Intracellular is not glycosylated.1 Publication

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiP00724.

2D gel databases

COMPLUYEAST-2DPAGEP00724.

PTM databases

UniCarbKBiP00724.

Interactioni

Protein-protein interaction databases

BioGridi34830. 25 interactions.
DIPiDIP-5542N.
IntActiP00724. 2 interactions.
MINTiMINT-477961.

Structurei

Secondary structure

1
532
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi30 – 323Combined sources
Beta strandi36 – 4914Combined sources
Turni50 – 534Combined sources
Beta strandi54 – 6714Combined sources
Beta strandi73 – 8412Combined sources
Beta strandi86 – 927Combined sources
Beta strandi100 – 1089Combined sources
Helixi123 – 1253Combined sources
Beta strandi127 – 1348Combined sources
Beta strandi139 – 1457Combined sources
Beta strandi147 – 1526Combined sources
Beta strandi170 – 1778Combined sources
Turni178 – 1814Combined sources
Beta strandi182 – 1898Combined sources
Helixi190 – 1923Combined sources
Beta strandi194 – 20512Combined sources
Beta strandi207 – 2126Combined sources
Beta strandi223 – 23412Combined sources
Beta strandi239 – 2479Combined sources
Beta strandi257 – 2659Combined sources
Beta strandi270 – 2756Combined sources
Beta strandi278 – 2803Combined sources
Beta strandi283 – 2853Combined sources
Beta strandi287 – 2915Combined sources
Turni297 – 2993Combined sources
Beta strandi303 – 3097Combined sources
Turni311 – 3155Combined sources
Beta strandi316 – 3183Combined sources
Beta strandi320 – 3234Combined sources
Beta strandi329 – 34315Combined sources
Beta strandi345 – 35410Combined sources
Beta strandi374 – 3829Combined sources
Beta strandi387 – 39711Combined sources
Beta strandi410 – 4167Combined sources
Beta strandi418 – 4236Combined sources
Beta strandi425 – 4306Combined sources
Turni431 – 4344Combined sources
Beta strandi435 – 4395Combined sources
Helixi446 – 4505Combined sources
Beta strandi465 – 4684Combined sources
Beta strandi471 – 48919Combined sources
Turni490 – 4934Combined sources
Beta strandi494 – 4996Combined sources
Beta strandi503 – 5053Combined sources
Beta strandi510 – 5178Combined sources
Beta strandi521 – 53010Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4EQVX-ray3.40A/B/C/D/E/F/G/H21-532[»]
ProteinModelPortaliP00724.
SMRiP00724. Positions 24-532.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni39 – 424Substrate bindingBy similarity
Regioni102 – 1032Substrate bindingBy similarity
Regioni170 – 1712Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the glycosyl hydrolase 32 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

HOGENOMiHOG000181424.
InParanoidiP00724.
KOiK01193.
OMAiQANPETE.
OrthoDBiEOG77M8ZG.

Family and domain databases

Gene3Di2.60.120.560. 1 hit.
InterProiIPR013320. ConA-like_dom.
IPR001362. Glyco_hydro_32.
IPR018053. Glyco_hydro_32_AS.
IPR013189. Glyco_hydro_32_C.
IPR013148. Glyco_hydro_32_N.
IPR023296. Glyco_hydro_beta-prop.
[Graphical view]
PfamiPF08244. Glyco_hydro_32C. 1 hit.
PF00251. Glyco_hydro_32N. 1 hit.
[Graphical view]
SMARTiSM00640. Glyco_32. 1 hit.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 1 hit.
SSF75005. SSF75005. 1 hit.
PROSITEiPS00609. GLYCOSYL_HYDROL_F32. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative initiation. AlignAdd to basket

Isoform Secreted (identifier: P00724-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MLLQAFLFLL AGFAAKISAS MTNETSDRPL VHFTPNKGWM NDPNGLWYDE
60 70 80 90 100
KDAKWHLYFQ YNPNDTVWGT PLFWGHATSD DLTNWEDQPI AIAPKRNDSG
110 120 130 140 150
AFSGSMVVDY NNTSGFFNDT IDPRQRCVAI WTYNTPESEE QYISYSLDGG
160 170 180 190 200
YTFTEYQKNP VLAANSTQFR DPKVFWYEPS QKWIMTAAKS QDYKIEIYSS
210 220 230 240 250
DDLKSWKLES AFANEGFLGY QYECPGLIEV PTEQDPSKSY WVMFISINPG
260 270 280 290 300
APAGGSFNQY FVGSFNGTHF EAFDNQSRVV DFGKDYYALQ TFFNTDPTYG
310 320 330 340 350
SALGIAWASN WEYSAFVPTN PWRSSMSLVR KFSLNTEYQA NPETELINLK
360 370 380 390 400
AEPILNISNA GPWSRFATNT TLTKANSYNV DLSNSTGTLE FELVYAVNTT
410 420 430 440 450
QTISKSVFAD LSLWFKGLED PEEYLRMGFE VSASSFFLDR GNSKVKFVKE
460 470 480 490 500
NPYFTNRMSV NNQPFKSEND LSYYKVYGLL DQNILELYFN DGDVVSTNTY
510 520 530
FMTTGNALGS VNMTTGVDNL FYIDKFQVRE VK
Length:532
Mass (Da):60,639
Last modified:July 21, 1986 - v1
Checksum:i7D8AB33E6772B775
GO
Isoform Intracellular (identifier: P00724-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-20: Missing.

Note: Produced by alternative initiation at Met-21 of isoform Secreted.
Show »
Length:512
Mass (Da):58,545
Checksum:iEC78825171A0E8D2
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti51 – 511K → P in AAA73474 (PubMed:1888528).Curated
Sequence conflicti409 – 4091A → P AA sequence (PubMed:3284881).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 2020Missing in isoform Intracellular. CuratedVSP_019611Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z46921 Genomic DNA. Translation: CAA87030.1.
U19781 Genomic DNA. Translation: AAA73474.1.
V01311 Genomic DNA. Translation: CAA24618.1.
K03294 Genomic DNA. Translation: AAA35127.1.
M13627 Genomic DNA. Translation: AAA35129.1.
BK006942 Genomic DNA. Translation: DAA08390.1.
PIRiA00899. IFBY.
RefSeqiNP_012104.1. NM_001179510.1. [P00724-1]

Genome annotation databases

EnsemblFungiiYIL162W; YIL162W; YIL162W. [P00724-1]
GeneIDi854644.
KEGGisce:YIL162W.

Keywords - Coding sequence diversityi

Alternative initiation

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z46921 Genomic DNA. Translation: CAA87030.1.
U19781 Genomic DNA. Translation: AAA73474.1.
V01311 Genomic DNA. Translation: CAA24618.1.
K03294 Genomic DNA. Translation: AAA35127.1.
M13627 Genomic DNA. Translation: AAA35129.1.
BK006942 Genomic DNA. Translation: DAA08390.1.
PIRiA00899. IFBY.
RefSeqiNP_012104.1. NM_001179510.1. [P00724-1]

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4EQVX-ray3.40A/B/C/D/E/F/G/H21-532[»]
ProteinModelPortaliP00724.
SMRiP00724. Positions 24-532.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34830. 25 interactions.
DIPiDIP-5542N.
IntActiP00724. 2 interactions.
MINTiMINT-477961.

Protein family/group databases

CAZyiGH32. Glycoside Hydrolase Family 32.
mycoCLAPiSUC32B_YEAST.

PTM databases

UniCarbKBiP00724.

2D gel databases

COMPLUYEAST-2DPAGEP00724.

Proteomic databases

MaxQBiP00724.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYIL162W; YIL162W; YIL162W. [P00724-1]
GeneIDi854644.
KEGGisce:YIL162W.

Organism-specific databases

EuPathDBiFungiDB:YIL162W.
SGDiS000001424. SUC2.

Phylogenomic databases

HOGENOMiHOG000181424.
InParanoidiP00724.
KOiK01193.
OMAiQANPETE.
OrthoDBiEOG77M8ZG.

Enzyme and pathway databases

BioCyciYEAST:YIL162W-MONOMER.

Miscellaneous databases

PROiP00724.

Family and domain databases

Gene3Di2.60.120.560. 1 hit.
InterProiIPR013320. ConA-like_dom.
IPR001362. Glyco_hydro_32.
IPR018053. Glyco_hydro_32_AS.
IPR013189. Glyco_hydro_32_C.
IPR013148. Glyco_hydro_32_N.
IPR023296. Glyco_hydro_beta-prop.
[Graphical view]
PfamiPF08244. Glyco_hydro_32C. 1 hit.
PF00251. Glyco_hydro_32N. 1 hit.
[Graphical view]
SMARTiSM00640. Glyco_32. 1 hit.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 1 hit.
SSF75005. SSF75005. 1 hit.
PROSITEiPS00609. GLYCOSYL_HYDROL_F32. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Nucleotide sequence of the yeast SUC2 gene for invertase."
    Taussig R., Carlson M.
    Nucleic Acids Res. 11:1943-1954(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. "[The effects of upstream region of SUC2 gene on its expression]."
    Xie K.W., Feng B., Li Y.Y.
    Yi Chuan Xue Bao 18:175-184(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-67.
    Strain: 33.
  5. "The secreted form of invertase in Saccharomyces cerevisiae is synthesized from mRNA encoding a signal sequence."
    Carlson M., Taussig R., Kustu S., Botstein D.
    Mol. Cell. Biol. 3:439-447(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-54.
  6. "Upstream region required for regulated expression of the glucose-repressible SUC2 gene of Saccharomyces cerevisiae."
    Sarokin L., Carlson M.
    Mol. Cell. Biol. 4:2750-2757(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-30.
  7. "Secretion-defective mutations in the signal sequence for Saccharomyces cerevisiae invertase."
    Kaiser C.A., Botstein D.
    Mol. Cell. Biol. 6:2382-2391(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-21.
  8. "Identification of an active-site residue in yeast invertase by affinity labeling and site-directed mutagenesis."
    Reddy V.A., Maley F.
    J. Biol. Chem. 265:10817-10820(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 20-27 AND 38-45, ACTIVE SITE, MUTAGENESIS OF ASP-42.
  9. "Characterization of the glycosylation sites in yeast external invertase. I. N-linked oligosaccharide content of the individual sequons."
    Reddy V.A., Johnson R.S., Biemann K., Williams R.S., Ziegler F.D., Trimble R.B., Maley F.
    J. Biol. Chem. 263:6978-6985(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 21-532, GLYCOSYLATION AT ASN-23; ASN-64; ASN-97; ASN-111; ASN-118; ASN-165; ASN-266; ASN-275; ASN-356; ASN-369; ASN-384; ASN-398 AND ASN-512.
  10. "Two differentially regulated mRNAs with different 5' ends encode secreted with intracellular forms of yeast invertase."
    Carlson M., Botstein D.
    Cell 28:145-154(1982) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION OF ISOFORMS, SUBCELLULAR LOCATION.
  11. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiINV2_YEAST
AccessioniPrimary (citable) accession number: P00724
Secondary accession number(s): D6VVC4, Q12671
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: July 6, 2016
This is version 146 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 1780 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
  4. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  5. Yeast chromosome IX
    Yeast (Saccharomyces cerevisiae) chromosome IX: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.