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Entry version 172 (23 Feb 2022)
Sequence version 1 (01 Nov 1997)
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Protein

Probable 1,3-beta-glucanosyltransferase GAS3

Gene

GAS3

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

Splits internally a 1,3-beta-glucan molecule and transfers the newly generated reducing end (the donor) to the non-reducing end of another 1,3-beta-glucan molecule (the acceptor) forming a 1,3-beta linkage, resulting in the elongation of 1,3-beta-glucan chains in the cell wall. Involved in cell wall biosynthesis and morphogenesis (By similarity).

By similarity1 Publication

Miscellaneous

Present with 16400 molecules/cell in log phase SD medium.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 describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei961,3-beta-glucan 1; donor substrate; via carbonyl oxygenBy similarity1
Binding sitei1681,3-beta-glucan 1; donor substrateBy similarity1
<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 sitei169Proton donorBy similarity1
Binding sitei1691,3-beta-glucan 2; acceptor substrateBy similarity1
Binding sitei2121,3-beta-glucan 2; acceptor substrate; via carbonyl oxygenBy similarity1
Binding sitei2171,3-beta-glucan 2; acceptor substrateBy similarity1
Active sitei283NucleophileBy similarity1
Binding sitei3151,3-beta-glucan 1; donor substrateBy similarity1

<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 functionTransferase
Biological processCell wall biogenesis/degradation

Protein family/group databases

Carbohydrate-Active enZymes

More...
CAZyi
GH72, Glycoside Hydrolase Family 72

<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:
Probable 1,3-beta-glucanosyltransferase GAS3 (EC:2.4.1.-)
Alternative name(s):
Glycolipid-anchored surface protein 3
<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:GAS3
Ordered Locus Names:YMR215W
ORF Names:YM8261.09
<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 XIII

Organism-specific databases

Saccharomyces Genome Database

More...
SGDi
S000004828, GAS3

Eukaryotic Pathogen, Vector and Host Database Resources

More...
VEuPathDBi
FungiDB:YMR215W

<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

Cell wall, Membrane, Secreted

<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 denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 21Sequence analysisAdd BLAST21
<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_000001047722 – 498Probable 1,3-beta-glucanosyltransferase GAS3Add BLAST477
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section describes a propeptide, which is a part of a protein that is cleaved during maturation or activation. Once cleaved, a propeptide generally has no independent biological function.<p><a href='/help/propep' target='_top'>More...</a></p>PropeptideiPRO_0000010478499 – 524Removed in mature formSequence analysisAdd BLAST26

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi78 ↔ 107By similarity
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi201N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi226 ↔ 369By similarity
Disulfide bondi254 ↔ 286By similarity
Glycosylationi269N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi350N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi385N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi404N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi422N-linked (GlcNAc...) asparagineSequence analysis1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section specifies the position(s) and the type of covalently attached lipid group(s).<p><a href='/help/lipid' target='_top'>More...</a></p>Lipidationi498GPI-anchor amidated glycineSequence analysis1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

The GPI-anchor is attached to the protein in the endoplasmic reticulum and serves to target the protein to the cell surface. There, the glucosamine-inositol phospholipid moiety is cleaved off and the GPI-modified mannoprotein is covalently attached via its lipidless GPI glycan remnant to the 1,6-beta-glucan of the outer cell wall layer.
N-glycosylated.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein

Proteomic databases

MaxQB - The MaxQuant DataBase

More...
MaxQBi
Q03655

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

More...
PaxDbi
Q03655

PRoteomics IDEntifications database

More...
PRIDEi
Q03655

2D gel databases

2-DE database at Universidad Complutense de Madrid

More...
COMPLUYEAST-2DPAGEi
Q03655

<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
35393, 201 interactors

Database of interacting proteins

More...
DIPi
DIP-4410N

Protein interaction database and analysis system

More...
IntActi
Q03655, 3 interactors

Molecular INTeraction database

More...
MINTi
Q03655

STRING: functional protein association networks

More...
STRINGi
4932.YMR215W

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...
RNActi
Q03655, protein

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
Q03655

Database of comparative protein structure models

More...
ModBasei
Search...

<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>Regioni461 – 498DisorderedSequence analysisAdd BLAST38

<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

Belongs to the glycosyl hydrolase 72 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG502QRZZ, Eukaryota

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000176308

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_021855_1_2_1

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q03655

Identification of Orthologs from Complete Genome Data

More...
OMAi
VGVAYQP

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR004886, Glucanosyltransferase
IPR017853, Glycoside_hydrolase_SF

The PANTHER Classification System

More...
PANTHERi
PTHR31468, PTHR31468, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF03198, Glyco_hydro_72, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF51445, SSF51445, 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.

<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 in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

Q03655-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MQLSKSILLA ALAATPSLVN AMLPIHIKNY RFIKPSSATN SESDNEVFFV
60 70 80 90 100
KGVDYQPGGS SGYDADSDTD ILSDPEVCAR DAYAFQQLGV NTVRIYSLNP
110 120 130 140 150
DLNHDKCMTI FNNAGIYAIL DVNSGNYGES LNRADPSGTY DSLYLSRVFK
160 170 180 190 200
FIDAFKNYPN VLGFFSGNEV INDQSDYAKI DPPYIRAVQR DMKQYISKHA
210 220 230 240 250
NRSIPVGYSA ADNTDLRLAT FKYLQCNSLD GNKVNDDLDI SKSDFFGLNT
260 270 280 290 300
YEWCSGTSSW ESSGYDKLNS TFEDAVIPLI FSEYGCNKNT PRTFDEVSEG
310 320 330 340 350
LYGGLKNVFS GGLVYEYTEE ANNYGLVKLD DSGSLTYKDD FVNLESQLKN
360 370 380 390 400
VSLPTTKESE ISSDSIYKCD NSAITNIYSG FGTNNFTLPS QPAEIANMIE
410 420 430 440 450
YGVNGTNTGK ILTDYAVPTT FNYTIKNNKD DTISATISYD KANSLNELDV
460 470 480 490 500
TATTVAKSAS TSQSSSRSLT SSTSPSSSTG SSSSTGSSSA SSSSKSKGVG
510 520
NIVNVSFSQS GYLALFAGLI SALL
Length:524
Mass (Da):56,794
Last modified:November 1, 1997 - v1
<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:i3A2BED0BD3ED8690
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
Z49809 Genomic DNA Translation: CAA89930.1
AY693202 Genomic DNA Translation: AAT93221.1
BK006946 Genomic DNA Translation: DAA10114.1

Protein sequence database of the Protein Information Resource

More...
PIRi
S55097

NCBI Reference Sequences

More...
RefSeqi
NP_013942.1, NM_001182722.1

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
YMR215W_mRNA; YMR215W; YMR215W

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
855255

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
sce:YMR215W

<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
Z49809 Genomic DNA Translation: CAA89930.1
AY693202 Genomic DNA Translation: AAT93221.1
BK006946 Genomic DNA Translation: DAA10114.1
PIRiS55097
RefSeqiNP_013942.1, NM_001182722.1

3D structure databases

SMRiQ03655
ModBaseiSearch...

Protein-protein interaction databases

BioGRIDi35393, 201 interactors
DIPiDIP-4410N
IntActiQ03655, 3 interactors
MINTiQ03655
STRINGi4932.YMR215W

Protein family/group databases

CAZyiGH72, Glycoside Hydrolase Family 72

2D gel databases

COMPLUYEAST-2DPAGEiQ03655

Proteomic databases

MaxQBiQ03655
PaxDbiQ03655
PRIDEiQ03655

Genome annotation databases

EnsemblFungiiYMR215W_mRNA; YMR215W; YMR215W
GeneIDi855255
KEGGisce:YMR215W

Organism-specific databases

SGDiS000004828, GAS3
VEuPathDBiFungiDB:YMR215W

Phylogenomic databases

eggNOGiENOG502QRZZ, Eukaryota
GeneTreeiENSGT00940000176308
HOGENOMiCLU_021855_1_2_1
InParanoidiQ03655
OMAiVGVAYQP

Miscellaneous databases

Protein Ontology

More...
PROi
PR:Q03655
RNActiQ03655, protein

Family and domain databases

InterProiView protein in InterPro
IPR004886, Glucanosyltransferase
IPR017853, Glycoside_hydrolase_SF
PANTHERiPTHR31468, PTHR31468, 1 hit
PfamiView protein in Pfam
PF03198, Glyco_hydro_72, 1 hit
SUPFAMiSSF51445, SSF51445, 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 nameiGAS3_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: Q03655
Secondary accession number(s): D6W040
<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: November 1, 1997
Last sequence update: November 1, 1997
Last modified: February 23, 2022
This is version 172 of the entry and version 1 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

Reference proteome

Documents

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