Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 153 (02 Jun 2021)
Sequence version 2 (01 Nov 1997)
Previous versions | rss
Add a publicationFeedback
Protein

Alcohol O-acetyltransferase 1

Gene

ATF1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Major alcohol O-acetyltransferase that uses acetyl-CoA to synthesize acetate esters from various alcohols, producing ethyl acetate, isoamyl acetate, isobutyl acetate, butyl acetate, hexyl acetate, heptyl acetate and octyl acetate (PubMed:7764365, PubMed:9758847, PubMed:10653746, PubMed:12937998, PubMed:16845703, PubMed:18597084, PubMed:17891501, PubMed:25306884, PubMed:28160314).

The alcohol acyltransferase activity is promiscuous with regard to alcohol but relatively specific for acetyl-CoA since ATF1 does not use any other acyl-CoAs (C3, C4, C5, C6, C8, C10, C12) (PubMed:28160314).

Acts also as an efficient thioesterase in vitro with specificity towards medium-chain-length acyl-CoAs (PubMed:28160314).

In natural environments, the production of aromatic volatile metabolites promotes dispersal through insect vectors (PubMed:25310977).

10 Publications

Miscellaneous

Present with 1990 molecules/cell in log phase SD medium.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Found to be inhibited by cadmium, copper, zinc and mercurium divalent cations and sulfhydryl reagents (PubMed:7764365). Inhibited by the addition of unsaturated fatty acids to the culture (PubMed:7764365).1 Publication

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=0.19 mM for acetyl-CoA (for acetyltransferase activity)1 Publication
  2. KM=29.8 mM for isoamyl alcohol (for acetyltransferase activity)1 Publication
  3. KM=61 µM for acetyl-CoA (for thioesterase activity)1 Publication
  4. KM=25 µM for butyryl-CoA (for thioesterase activity)1 Publication
  5. KM=12 µM for hexanoyl-CoA (for thioesterase activity)1 Publication
  6. KM=3 µM for octanoyl-CoA (for thioesterase activity)1 Publication

    pH dependencei

    Optimum pH is 8.1 Publication

    Temperature dependencei

    Optimum temperature is 25 degrees Celsius.1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei191Charge relay system1 Publication1
    Active sitei195Charge relay system1 Publication1

    <p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

    GO - Biological processi

    <p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

    Molecular functionAcyltransferase, Hydrolase, Transferase

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    MetaCyc:YOR377W-MONOMER

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    2.3.1.84, 984

    SABIO-RK: Biochemical Reaction Kinetics Database

    More...
    SABIO-RKi
    P40353

    <p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
    Recommended name:
    Alcohol O-acetyltransferase 11 Publication (EC:2.3.1.842 Publications, EC:3.1.2.201 Publication)
    Short name:
    AATase 11 Publication
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
    Name:ATF11 Publication
    Ordered Locus Names:YOR377W
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri559292 [NCBI]
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
    • UP000002311 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome XV

    Organism-specific databases

    Saccharomyces Genome Database

    More...
    SGDi
    S000005904, ATF1

    Eukaryotic Pathogen, Vector and Host Database Resources

    More...
    VEuPathDBi
    FungiDB:YOR377W

    <p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

    Keywords - Cellular componenti

    Endoplasmic reticulum, Lipid droplet, Membrane

    <p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

    <p>This subsection of the 'Pathology and Biotech' section describes the use of a specific protein in the biotechnological industry.<p><a href='/help/biotechnological_use' target='_top'>More...</a></p>Biotechnological usei

    Understanding the biochemistry of the volatile esters is of considerable importance in industrial agriculture, winemaking and brewing. ATF1 could profoundly affect the flavor profiles of wines and distillates deficient in aroma, thereby paving the way for the production of products maintaining a fruitier character for longer periods after bottling (PubMed:10653746, PubMed:16845703, PubMed:18597084, PubMed:25306884, PubMed:28176138). The most important acetate esters from the perspective of fermented foods and beverages are probably ethyl acetate (fruity, solvent aroma), isobutyl acetate (sweet, fruit), isoamyl acetate (banana) and 2-phenylethyl acetate (rose). In addition, the enzymes responsible for ester synthesis are targets for the metabolic engineering of cellular factories intended to produce insect pheromones for use in pest control, but also for the production of fragrances, industrial solvents, fine chemicals, pharmaceuticals and renewable biofuels (PubMed:25281839, PubMed:24609358, PubMed:26205521, PubMed:26801935).10 Publications

    <p>This subsection of the 'Pathology and Biotech' section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

    Reduces levels of isoamyl acetate production during fermentation to about 16% of those produced by the wild-type strain and causes a 40% reduction of ethyl acetate formation (PubMed:12957907).1 Publication

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi191H → A: Only moderately reduces the thioesterase activity. 1 Publication1

    <p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000647201 – 525Alcohol O-acetyltransferase 1Add BLAST525

    Proteomic databases

    MaxQB - The MaxQuant DataBase

    More...
    MaxQBi
    P40353

    PaxDb, a database of protein abundance averages across all three domains of life

    More...
    PaxDbi
    P40353

    PRoteomics IDEntifications database

    More...
    PRIDEi
    P40353

    <p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

    <p>This subsection of the 'Expression' section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

    Expression is repressed both by aeration and by unsaturated fatty acids (PubMed:9055409, PubMed:9675816). Also repressed by heat and ethanol stress (PubMed:14654433). Rapid induction by glucose depends on the cAMP/PKA signaling pathway (PubMed:14654433). Long-term expression requires both carbon and nitrogen sources (PubMed:14654433). The activation of transcription is dependent on RAP1, and the ROX1-TUP1p-SSN6 hypoxic repressor complex is responsible for repression by oxygen (PubMed:10487921). The putative ROX1-binding sequence in the ATF1 promoter is 5'-CCTATTGTTTT-3' and the RAP1-binding sequence is 5'-AACCCAACAAA-3' (PubMed:10487921).4 Publications

    <p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGRID)

    More...
    BioGRIDi
    34759, 38 interactors

    Database of interacting proteins

    More...
    DIPi
    DIP-5494N

    Protein interaction database and analysis system

    More...
    IntActi
    P40353, 2 interactors

    STRING: functional protein association networks

    More...
    STRINGi
    4932.YOR377W

    Miscellaneous databases

    RNAct, Protein-RNA interaction predictions for model organisms.

    More...
    RNActi
    P40353, protein

    <p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni24 – 41Membrane association1 PublicationAdd BLAST18
    Regioni508 – 525Membrane association1 PublicationAdd BLAST18

    <p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

    Segments of the N- and C-terminal domains (residues 24-41 and 508-525, respectively) are predicted to be amphipathic helices and are essential for endoplasmic reticulum and lipid dropplet association (PubMed:25093817).1 Publication

    <p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    ENOG502QTAU, Eukaryota

    Ensembl GeneTree

    More...
    GeneTreei
    ENSGT00940000176620

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    CLU_043707_0_0_1

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    P40353

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    HFISITN

    Family and domain databases

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR010828, Atf2/Sli1-like

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF07247, AATase, 1 hit

    <p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

    P40353-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MNEIDEKNQA PVQQECLKEM IQNGHARRMG SVEDLYVALN RQNLYRNFCT
    60 70 80 90 100
    YGELSDYCTR DQLTLALREI CLKNPTLLHI VLPTRWPNHE NYYRSSEYYS
    110 120 130 140 150
    RPHPVHDYIS VLQELKLSGV VLNEQPEYSA VMKQILEEFK NSKGSYTAKI
    160 170 180 190 200
    FKLTTTLTIP YFGPTGPSWR LICLPEEHTE KWKKFIFVSN HCMSDGRSSI
    210 220 230 240 250
    HFFHDLRDEL NNIKTPPKKL DYIFKYEEDY QLLRKLPEPI EKVIDFRPPY
    260 270 280 290 300
    LFIPKSLLSG FIYNHLRFSS KGVCMRMDDV EKTDDVVTEI INISPTEFQA
    310 320 330 340 350
    IKANIKSNIQ GKCTITPFLH VCWFVSLHKW GKFFKPLNFE WLTDIFIPAD
    360 370 380 390 400
    CRSQLPDDDE MRQMYRYGAN VGFIDFTPWI SEFDMNDNKE NFWPLIEHYH
    410 420 430 440 450
    EVISEALRNK KHLHGLGFNI QGFVQKYVNI DKVMCDRAIG KRRGGTLLSN
    460 470 480 490 500
    VGLFNQLEEP DAKYSICDLA FGQFQGSWHQ AFSLGVCSTN VKGMNIVVAS
    510 520
    TKNVVGSQES LEELCSIYKA LLLGP
    Length:525
    Mass (Da):61,036
    Last modified:November 1, 1997 - v2
    <p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i79D0733CDDC5C629
    GO

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti84T → I in BAA05552 (PubMed:8085822).Curated1
    Sequence conflicti391N → K in BAA05552 (PubMed:8085822).Curated1

    Sequence databases

    Select the link destinations:

    EMBL nucleotide sequence database

    More...
    EMBLi

    GenBank nucleotide sequence database

    More...
    GenBanki

    DNA Data Bank of Japan; a nucleotide sequence database

    More...
    DDBJi
    Links Updated
    D26554 Genomic DNA Translation: BAA05552.1
    Z75285 Genomic DNA Translation: CAA99708.1
    BK006948 Genomic DNA Translation: DAA11136.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    S67289

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_015022.3, NM_001183797.3

    Genome annotation databases

    Ensembl fungal genome annotation project

    More...
    EnsemblFungii
    YOR377W_mRNA; YOR377W; YOR377W

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    854559

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    sce:YOR377W

    <p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

    <p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    D26554 Genomic DNA Translation: BAA05552.1
    Z75285 Genomic DNA Translation: CAA99708.1
    BK006948 Genomic DNA Translation: DAA11136.1
    PIRiS67289
    RefSeqiNP_015022.3, NM_001183797.3

    3D structure databases

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    SWISS-MODEL Interactive Workspace

    More...
    SWISS-MODEL-Workspacei
    Submit a new modelling project...

    Protein-protein interaction databases

    BioGRIDi34759, 38 interactors
    DIPiDIP-5494N
    IntActiP40353, 2 interactors
    STRINGi4932.YOR377W

    Proteomic databases

    MaxQBiP40353
    PaxDbiP40353
    PRIDEiP40353

    Genome annotation databases

    EnsemblFungiiYOR377W_mRNA; YOR377W; YOR377W
    GeneIDi854559
    KEGGisce:YOR377W

    Organism-specific databases

    SGDiS000005904, ATF1
    VEuPathDBiFungiDB:YOR377W

    Phylogenomic databases

    eggNOGiENOG502QTAU, Eukaryota
    GeneTreeiENSGT00940000176620
    HOGENOMiCLU_043707_0_0_1
    InParanoidiP40353
    OMAiHFISITN

    Enzyme and pathway databases

    BioCyciMetaCyc:YOR377W-MONOMER
    BRENDAi2.3.1.84, 984
    SABIO-RKiP40353

    Miscellaneous databases

    Protein Ontology

    More...
    PROi
    PR:P40353
    RNActiP40353, protein

    Family and domain databases

    InterProiView protein in InterPro
    IPR010828, Atf2/Sli1-like
    PfamiView protein in Pfam
    PF07247, AATase, 1 hit

    MobiDB: a database of protein disorder and mobility annotations

    More...
    MobiDBi
    Search...

    <p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

    <p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiATF1_YEAST
    <p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P40353
    Secondary accession number(s): D6W370, Q08901
    <p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1995
    Last sequence update: November 1, 1997
    Last modified: June 2, 2021
    This is version 153 of the entry and version 2 of the sequence. See complete history.
    <p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    <p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

    Keywords - Technical termi

    Direct protein sequencing, Reference proteome

    Documents

    1. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    2. Yeast chromosome XV
      Yeast (Saccharomyces cerevisiae) chromosome XV: entries and gene names
    3. SIMILARITY comments
      Index of protein domains and families
    UniProt is an ELIXIR core data resource
    Main funding by: National Institutes of Health

    We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

    Do not show this banner again