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P00724 (INV2_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 121. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Invertase 2
EC=3.2.1.26
Alternative name(s):
Beta-fructofuranosidase 2
Saccharase
Gene names
Name:SUC2
Ordered Locus Names:YIL162W
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›

Protein attributes

Sequence length532 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

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

Subcellular location

Isoform Intracellular: Cytoplasm Ref.10.

Isoform Secreted: Secreted Ref.10.

Post-translational modification

Isoform Secreted is glycosylated. Isoform Intracellular is not glycosylated. Ref.9

Miscellaneous

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

Sequence similarities

Belongs to the glycosyl hydrolase 32 family.

Alternative products

This entry describes 2 isoforms produced by alternative initiation. [Align] [Select]
Isoform Secreted (identifier: P00724-1)

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.
Isoform Intracellular (identifier: P00724-2)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Ref.8
Chain20 – 532513Invertase 2
PRO_0000033399

Regions

Region39 – 424Substrate binding By similarity
Region102 – 1032Substrate binding By similarity
Region170 – 1712Substrate binding By similarity

Sites

Active site421 Ref.8
Active site421 By similarity
Binding site601Substrate By similarity
Binding site2231Substrate By similarity
Binding site3111Substrate By similarity

Amino acid modifications

Glycosylation231N-linked (GlcNAc...); in isoform Secreted Ref.9
Glycosylation641N-linked (GlcNAc...); in isoform Secreted; partial Ref.9
Glycosylation971N-linked (GlcNAc...); in isoform Secreted Ref.9
Glycosylation1111N-linked (GlcNAc...); in isoform Secreted Ref.9
Glycosylation1181N-linked (GlcNAc...); in isoform Secreted Ref.9
Glycosylation1651N-linked (GlcNAc...); in isoform Secreted; partial Ref.9
Glycosylation2661N-linked (GlcNAc...); in isoform Secreted; partial Ref.9
Glycosylation2751N-linked (GlcNAc...); in isoform Secreted; partial Ref.9
Glycosylation3561N-linked (GlcNAc...); in isoform Secreted Ref.9
Glycosylation3691N-linked (GlcNAc...); in isoform Secreted Ref.9
Glycosylation3841N-linked (GlcNAc...); in isoform Secreted Ref.9
Glycosylation3981N-linked (GlcNAc...); in isoform Secreted Ref.9
Glycosylation5121N-linked (GlcNAc...); in isoform Secreted; partial Ref.9

Natural variations

Alternative sequence1 – 2020Missing in isoform Intracellular.
VSP_019611

Experimental info

Mutagenesis421D → N: Loss of activity. Ref.8
Sequence conflict511K → P in AAA73474. Ref.4
Sequence conflict4091A → P AA sequence Ref.9

Sequences

Sequence LengthMass (Da)Tools
Isoform Secreted [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: 7D8AB33E6772B775

FASTA53260,639
        10         20         30         40         50         60 
MLLQAFLFLL AGFAAKISAS MTNETSDRPL VHFTPNKGWM NDPNGLWYDE KDAKWHLYFQ 

        70         80         90        100        110        120 
YNPNDTVWGT PLFWGHATSD DLTNWEDQPI AIAPKRNDSG AFSGSMVVDY NNTSGFFNDT 

       130        140        150        160        170        180 
IDPRQRCVAI WTYNTPESEE QYISYSLDGG YTFTEYQKNP VLAANSTQFR DPKVFWYEPS 

       190        200        210        220        230        240 
QKWIMTAAKS QDYKIEIYSS DDLKSWKLES AFANEGFLGY QYECPGLIEV PTEQDPSKSY 

       250        260        270        280        290        300 
WVMFISINPG APAGGSFNQY FVGSFNGTHF EAFDNQSRVV DFGKDYYALQ TFFNTDPTYG 

       310        320        330        340        350        360 
SALGIAWASN WEYSAFVPTN PWRSSMSLVR KFSLNTEYQA NPETELINLK AEPILNISNA 

       370        380        390        400        410        420 
GPWSRFATNT TLTKANSYNV DLSNSTGTLE FELVYAVNTT QTISKSVFAD LSLWFKGLED 

       430        440        450        460        470        480 
PEEYLRMGFE VSASSFFLDR GNSKVKFVKE NPYFTNRMSV NNQPFKSEND LSYYKVYGLL 

       490        500        510        520        530 
DQNILELYFN DGDVVSTNTY FMTTGNALGS VNMTTGVDNL FYIDKFQVRE VK

« Hide

Isoform Intracellular [UniParc].

Checksum: EC78825171A0E8D2
Show »

FASTA51258,545

References

« Hide 'large scale' references
[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]"The nucleotide sequence of Saccharomyces cerevisiae chromosome IX."
Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D., Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., Harris D.E., Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C. expand/collapse author list , Pearson D., Rajandream M.A., Rice P., Rowley N., Skelton J., Smith V., Walsh S.V., Whitehead S., Barrell B.G.
Nature 387:84-87(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204511 / S288c / AB972.
[3]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
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 ASP-42, 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]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		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.
PIRIFBY. A00899.
RefSeqNP_012104.1. NM_001179510.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4EQVX-ray3.40A/B/C/D/E/F/G/H21-532[»]
ProteinModelPortalP00724.
SMRP00724. Positions 20-531.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-5542N.
IntActP00724. 2 interactions.
MINTMINT-477961.

Protein family/group databases

CAZyGH32. Glycoside Hydrolase Family 32.
mycoCLAPSUC32B_YEAST.

PTM databases

GlycoSuiteDBP00724.

2D gel databases

COMPLUYEAST-2DPAGEP00724.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYIL162W; YIL162W; YIL162W.
GeneID854644.
KEGGsce:YIL162W.

Organism-specific databases

CYGDYIL162w.
SGDS000001424. SUC2.

Phylogenomic databases

HOGENOMHOG000181424.
KOK01193.
OMANPWRSSM.
OrthoDBEOG4V1B86.

Gene expression databases

ArrayExpressP00724.
GenevestigatorP00724.
GermOnlineYIL162W. Saccharomyces cerevisiae.

Family and domain databases

InterProIPR008985. ConA-like_lec_gl_sf.
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]
PfamPF08244. Glyco_hydro_32C. 1 hit.
PF00251. Glyco_hydro_32N. 1 hit.
[Graphical view]
SMARTSM00640. Glyco_32. 1 hit.
[Graphical view]
SUPFAMSSF49899. ConA_like_lec_gl. 1 hit.
SSF75005. Glyco_hydro_43_beta-prop. 1 hit.
PROSITEPS00609. GLYCOSYL_HYDROL_F32. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio977181.

Entry information

Entry nameINV2_YEAST
AccessionPrimary (citable) accession number: P00724
Secondary accession number(s): D6VVC4, Q12671
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: May 1, 2013
This is version 121 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Yeast chromosome IX

Yeast (Saccharomyces cerevisiae) chromosome IX: entries and gene names

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents