P20840 · SAG1_YEAST

Function

function

Cell surface glycoprotein promoting cell-cell contact to facilitate mating. S.cerevisiae A and alpha cells express the complementary cell surface glycoproteins A-agglutinin and alpha-, respectively, which interact with one another to promote cellular aggregation during mating.

Features

Showing features for site.

165050100150200250300350400450500550600650
TypeIDPosition(s)Description
Site348Not glycosylated

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentcell periphery
Cellular Componentextracellular region
Cellular Componentfungal-type cell wall
Cellular Componentfungal-type vacuole
Cellular Componentside of membrane
Molecular Functioncell adhesion molecule binding
Biological Processagglutination involved in conjugation with cellular fusion

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Alpha-agglutinin
  • Alternative names
    • AG-alpha-1

Gene names

    • Name
      SAG1
    • Synonyms
      AGAL1
    • ORF names
      J1418
    • Ordered locus names
      YJR004C

Organism names

Accessions

  • Primary accession
    P20840
  • Secondary accessions
    • D6VWH8

Proteomes

Organism-specific databases

Subcellular Location

Keywords

Phenotypes & Variants

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis211Little effect on secreted alpha-agglutinin activity.
Mutagenesis214No effect on secreted alpha-agglutinin activity.
Mutagenesis215Little or no effect on secreted alpha-agglutinin activity.
Mutagenesis216Complete loss of alpha-agglutinin activity.
Mutagenesis216No effect on secreted alpha-agglutinin activity.
Mutagenesis216Decreases secreted alpha-agglutinin activity by 100-fold.
Mutagenesis216Decreases secreted alpha-agglutinin activity by 10-fold.
Mutagenesis217Little effect on secreted alpha-agglutinin activity.
Mutagenesis217Decreases secreted alpha-agglutinin activity by 10-fold.
Mutagenesis289Decreases secreted alpha-agglutinin activity by less than 2-fold.
Mutagenesis290Decreases secreted alpha-agglutinin activity by less than 2-fold.
Mutagenesis291Decreases secreted alpha-agglutinin activity by 4-fold.
Mutagenesis292Almost complete loss of secreted alpha-agglutinin activity.
Mutagenesis294Decreases secreted alpha-agglutinin activity by more than 20-fold.
Mutagenesis295Decreases secreted alpha-agglutinin activity by 2-fold.
Mutagenesis296Decreases secreted alpha-agglutinin activity by more than 20-fold.
Mutagenesis298Decreases secreted alpha-agglutinin activity by less than 2-fold.
Mutagenesis322Decreases secreted alpha-agglutinin activity by 60-fold.
Mutagenesis322Almost complete loss of secreted alpha-agglutinin activity by 10-fold.
Mutagenesis322Decreases secreted alpha-agglutinin activity by 15-fold.
Mutagenesis323Decreases secreted alpha-agglutinin activity by 2-fold.
Mutagenesis324Little effect on secreted alpha-agglutinin activity.
Mutagenesis325Little effect on secreted alpha-agglutinin activity.

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 18 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

PTM/Processing

Features

Showing features for signal, chain, glycosylation, disulfide bond, lipidation, propeptide.

Type
IDPosition(s)Description
Signal1-19
ChainPRO_000002226520-627Alpha-agglutinin
Glycosylation79N-linked (GlcNAc...) asparagine
Disulfide bond97↔114
Glycosylation109N-linked (GlcNAc...) asparagine
Glycosylation135N-linked (GlcNAc...) asparagine
Disulfide bond202↔300
Glycosylation248N-linked (GlcNAc...) asparagine
Glycosylation282O-linked (Man...) serine
Glycosylation289O-linked (Man...) threonine
Glycosylation299O-linked (Man...) threonine
Glycosylation303O-linked (Man...) threonine
Glycosylation306N-linked (GlcNAc...) asparagine
Glycosylation307O-linked (Man...) threonine
Glycosylation308O-linked (Man...) threonine
Glycosylation311O-linked (Man...) threonine
Glycosylation314O-linked (Man...) serine
Glycosylation315O-linked (Man...) threonine
Glycosylation316O-linked (Man...) threonine
Glycosylation329O-linked (Man...) threonine
Glycosylation331O-linked (Man...) serine
Glycosylation334O-linked (Man...) serine
Glycosylation335O-linked (Man...) serine
Glycosylation338O-linked (Man...) serine
Glycosylation339O-linked (Man...) threonine
Glycosylation340O-linked (Man...) threonine
Glycosylation341O-linked (Man...) threonine
Glycosylation342O-linked (Man...) threonine
Glycosylation345O-linked (Man...) threonine
Glycosylation346O-linked (Man...) serine
Glycosylation349O-linked (Man...) threonine
Glycosylation350O-linked (Man...) serine
Glycosylation364N-linked (GlcNAc...) asparagine
Glycosylation402N-linked (GlcNAc...) asparagine
Glycosylation485N-linked (GlcNAc...) asparagine
Glycosylation501N-linked (GlcNAc...) asparagine
Glycosylation614N-linked (GlcNAc...) asparagine
Lipidation627GPI-anchor amidated glycine
PropeptidePRO_0000022266628-650Removed in mature form

Post-translational modification

N-glycosylated, and O-glycosylated by both PMT1 and PMT2.
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.

Keywords

Proteomic databases

PTM databases

Expression

Induction

By exposition to pheromone (A-factor) secreted by the opposite mating type cells (type A).

Interaction

Subunit

Interacts with AGA2.

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Features

Showing features for region, repeat.

Type
IDPosition(s)Description
Region216-322Ig-like fold domain important for alpha-agglutinin activity, contributing to a functional binding site for a-agglutinin
Repeat339-3781
Region339-4232 X 40 AA tandem repeats
Repeat384-4232

Sequence similarities

To C.albicans ALS1.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    650
  • Mass (Da)
    70,340
  • Last updated
    1995-11-01 v2
  • Checksum
    8BBF7A1C44C93C2B
MFTFLKIILWLFSLALASAININDITFSNLEITPLTANKQPDQGWTATFDFSIADASSIREGDEFTLSMPHVYRIKLLNSSQTATISLADGTEAFKCYVSQQAAYLYENTTFTCTAQNDLSSYNTIDGSITFSLNFSDGGSSYEYELENAKFFKSGPMLVKLGNQMSDVVNFDPAAFTENVFHSGRSTGYGSFESYHLGMYCPNGYFLGGTEKIDYDSSNNNVDLDCSSVQVYSSNDFNDWWFPQSYNDTNADVTCFGSNLWITLDEKLYDGEMLWVNALQSLPANVNTIDHALEFQYTCLDTIANTTYATQFSTTREFIVYQGRNLGTASAKSSFISTTTTDLTSINTSAYSTGSISTVETGNRTTSEVISHVVTTSTKLSPTATTSLTIAQTSIYSTDSNITVGTDIHTTSEVISDVETISRETASTVVAAPTSTTGWTGAMNTYISQFTSSSFATINSTPIISSSAVFETSDASIVNVHTENITNTAAVPSEEPTFVNATRNSLNSFCSSKQPSSPSSYTSSPLVSSLSVSKTLLSTSFTPSVPTSNTYIKTKNTGYFEHTALTTSSVGLNSFSETAVSSQGTKIDTFLVSSLIAYPSSASGSQLSGIQQNFTSTSLMISTYEGKASIFFSAELGSIIFLLLSYLLF

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict449in Ref. 1; AAA34417
Sequence conflict556in Ref. 1; AAA34417
Sequence conflict581in Ref. 1; AAA34417

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
X16861
EMBL· GenBank· DDBJ
CAA34752.1
EMBL· GenBank· DDBJ
Genomic DNA
M28164
EMBL· GenBank· DDBJ
AAA34417.1
EMBL· GenBank· DDBJ
Genomic DNA
X87611
EMBL· GenBank· DDBJ
CAA60926.1
EMBL· GenBank· DDBJ
Genomic DNA
Z49504
EMBL· GenBank· DDBJ
CAA89526.1
EMBL· GenBank· DDBJ
Genomic DNA
BK006943
EMBL· GenBank· DDBJ
DAA08794.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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