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P20840 (SAG1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 124. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Alpha-agglutinin
Alternative name(s):
AG-alpha-1
Gene names
Name:SAG1
Synonyms:AGAL1
Ordered Locus Names:YJR004C
ORF Names:J1418
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length650 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Cell surface glycoprotein promoting cell-cell contact to facilitate mating. Saccharomyces 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. Ref.9

Subunit structure

Interacts with AGA2. Ref.11

Subcellular location

Secretedcell wall. Membrane; Lipid-anchorGPI-anchor. Note: Covalently-linked GPI-modified cell wall protein (GPI-CWP). Ref.6 Ref.7 Ref.8 Ref.10

Induction

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

Post-translational modification

N-glycosylated, and O-glycosylated by both PMT1 and PMT2. Ref.5 Ref.6

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.

Sequence similarities

To C.albicans ALS1.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919
Chain20 – 627608Alpha-agglutinin
PRO_0000022265
Propeptide628 – 65023Removed in mature form Potential
PRO_0000022266

Regions

Repeat339 – 378401
Repeat384 – 423402
Region216 – 322107Ig-like fold domain important for alpha-agglutinin activity, contributing to a functional binding site for a-agglutinin
Region339 – 423852 X 40 AA tandem repeats
Compositional bias331 – 35929Ser/Thr-rich

Sites

Site3481Not glycosylated

Amino acid modifications

Lipidation6271GPI-anchor amidated glycine Potential
Glycosylation791N-linked (GlcNAc...) Potential
Glycosylation1091N-linked (GlcNAc...) Potential
Glycosylation1351N-linked (GlcNAc...) Potential
Glycosylation2481N-linked (GlcNAc...) Ref.5
Glycosylation2821O-linked (Man...) Ref.5
Glycosylation2891O-linked (Man...) Ref.5
Glycosylation2991O-linked (Man...) Ref.5
Glycosylation3031O-linked (Man...) Ref.5
Glycosylation3061N-linked (GlcNAc...) Ref.5
Glycosylation3071O-linked (Man...) Ref.5
Glycosylation3081O-linked (Man...) Ref.5
Glycosylation3111O-linked (Man...) Ref.5
Glycosylation3141O-linked (Man...) Ref.5
Glycosylation3151O-linked (Man...) Ref.5
Glycosylation3161O-linked (Man...) Ref.5
Glycosylation3291O-linked (Man...) Ref.5
Glycosylation3311O-linked (Man...) Ref.5
Glycosylation3341O-linked (Man...) Ref.5
Glycosylation3351O-linked (Man...) Ref.5
Glycosylation3381O-linked (Man...) Ref.5
Glycosylation3391O-linked (Man...) Ref.5
Glycosylation3401O-linked (Man...) Ref.5
Glycosylation3411O-linked (Man...) Ref.5
Glycosylation3421O-linked (Man...) Ref.5
Glycosylation3451O-linked (Man...) Ref.5
Glycosylation3461O-linked (Man...) Ref.5
Glycosylation3491O-linked (Man...) Ref.5
Glycosylation3501O-linked (Man...) Ref.5
Glycosylation3641N-linked (GlcNAc...) Potential
Glycosylation4021N-linked (GlcNAc...) Potential
Glycosylation4601N-linked (GlcNAc...) Potential
Glycosylation4851N-linked (GlcNAc...) Potential
Glycosylation5011N-linked (GlcNAc...) Potential
Glycosylation6141N-linked (GlcNAc...) Potential
Disulfide bond97 ↔ 114 Ref.5
Disulfide bond202 ↔ 300 Ref.5

Experimental info

Mutagenesis2111T → I: Little effect on secreted alpha-agglutinin activity.
Mutagenesis2141I → M: No effect on secreted alpha-agglutinin activity. Ref.9
Mutagenesis2151D → A or N: Little or no effect on secreted alpha-agglutinin activity. Ref.9
Mutagenesis2161Y → D: Complete loss of alpha-agglutinin activity. Ref.9
Mutagenesis2161Y → F: No effect on secreted alpha-agglutinin activity. Ref.9
Mutagenesis2161Y → S: Decreases secreted alpha-agglutinin activity by 100-fold. Ref.9
Mutagenesis2161Y → V: Decreases secreted alpha-agglutinin activity by 10-fold. Ref.9
Mutagenesis2171D → A: Little effect on secreted alpha-agglutinin activity. Ref.9
Mutagenesis2171D → N: Decreases secreted alpha-agglutinin activity by 10-fold. Ref.9
Mutagenesis2891T → A: Decreases secreted alpha-agglutinin activity by less than 2-fold. Ref.9
Mutagenesis2901I → M: Decreases secreted alpha-agglutinin activity by less than 2-fold. Ref.9
Mutagenesis2911D → A or N: Decreases secreted alpha-agglutinin activity by 4-fold. Ref.9
Mutagenesis2921H → L or R: Almost complete loss of secreted alpha-agglutinin activity. Ref.9
Mutagenesis2941L → S: Decreases secreted alpha-agglutinin activity by more than 20-fold. Ref.9
Mutagenesis2951E → A or Q: Decreases secreted alpha-agglutinin activity by 2-fold. Ref.9
Mutagenesis2961F → Y: Decreases secreted alpha-agglutinin activity by more than 20-fold. Ref.9
Mutagenesis2981Y → H: Decreases secreted alpha-agglutinin activity by less than 2-fold. Ref.9
Mutagenesis3221Y → A: Decreases secreted alpha-agglutinin activity by 60-fold. Ref.9
Mutagenesis3221Y → C: Almost complete loss of secreted alpha-agglutinin activity by 10-fold. Ref.9
Mutagenesis3221Y → F: Decreases secreted alpha-agglutinin activity by 15-fold. Ref.9
Mutagenesis3231Q → L: Decreases secreted alpha-agglutinin activity by 2-fold. Ref.9
Mutagenesis3241G → A: Little effect on secreted alpha-agglutinin activity. Ref.9
Mutagenesis3251R → G: Little effect on secreted alpha-agglutinin activity. Ref.9
Sequence conflict4491S → P in AAA34417. Ref.1
Sequence conflict5561K → E in AAA34417. Ref.1
Sequence conflict5811V → L in AAA34417. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P20840 [UniParc].

Last modified November 1, 1995. Version 2.
Checksum: 8BBF7A1C44C93C2B

FASTA65070,340
        10         20         30         40         50         60 
MFTFLKIILW LFSLALASAI NINDITFSNL EITPLTANKQ PDQGWTATFD FSIADASSIR 

        70         80         90        100        110        120 
EGDEFTLSMP HVYRIKLLNS SQTATISLAD GTEAFKCYVS QQAAYLYENT TFTCTAQNDL 

       130        140        150        160        170        180 
SSYNTIDGSI TFSLNFSDGG SSYEYELENA KFFKSGPMLV KLGNQMSDVV NFDPAAFTEN 

       190        200        210        220        230        240 
VFHSGRSTGY GSFESYHLGM YCPNGYFLGG TEKIDYDSSN NNVDLDCSSV QVYSSNDFND 

       250        260        270        280        290        300 
WWFPQSYNDT NADVTCFGSN LWITLDEKLY DGEMLWVNAL QSLPANVNTI DHALEFQYTC 

       310        320        330        340        350        360 
LDTIANTTYA TQFSTTREFI VYQGRNLGTA SAKSSFISTT TTDLTSINTS AYSTGSISTV 

       370        380        390        400        410        420 
ETGNRTTSEV ISHVVTTSTK LSPTATTSLT IAQTSIYSTD SNITVGTDIH TTSEVISDVE 

       430        440        450        460        470        480 
TISRETASTV VAAPTSTTGW TGAMNTYISQ FTSSSFATIN STPIISSSAV FETSDASIVN 

       490        500        510        520        530        540 
VHTENITNTA AVPSEEPTFV NATRNSLNSF CSSKQPSSPS SYTSSPLVSS LSVSKTLLST 

       550        560        570        580        590        600 
SFTPSVPTSN TYIKTKNTGY FEHTALTTSS VGLNSFSETA VSSQGTKIDT FLVSSLIAYP 

       610        620        630        640        650 
SSASGSQLSG IQQNFTSTSL MISTYEGKAS IFFSAELGSI IFLLLSYLLF 

« Hide

References

« Hide 'large scale' references
[1]"Purification of the inducible alpha-agglutinin of S. cerevisiae and molecular cloning of the gene."
Hauser K., Tanner W.
FEBS Lett. 255:290-294(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[2]"AG alpha 1 is the structural gene for the Saccharomyces cerevisiae alpha-agglutinin, a cell surface glycoprotein involved in cell-cell interactions during mating."
Lipke P.N., Wojciechowicz D., Kurjan J.
Mol. Cell. Biol. 9:3155-3165(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X."
Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C., Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D., Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J., Heumann K. expand/collapse author list , Hilger F., Hollenberg C.P., Huang M.-E., Jacq C., Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E., Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T., Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R., Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N., To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H., von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.
EMBO J. 15:2031-2049(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[4]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[5]"Structure of Saccharomyces cerevisiae alpha-agglutinin. Evidence for a yeast cell wall protein with multiple immunoglobulin-like domains with atypical disulfides."
Chen M.-H., Shen Z.-M., Bobin S., Kahn P.C., Lipke P.N.
J. Biol. Chem. 270:26168-26177(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL PROTEIN SEQUENCE, GLYCOSYLATION AT ASN-248; SER-282; THR-289; THR-299; THR-303; ASN-306; THR-307; THR-308; THR-311; SER-314; THR-315; THR-316; THR-329; SER-331; SER-334; SER-335; SER-338; THR-339; THR-340; THR-341; THR-342; THR-345; SER-346; THR-349 AND SER-350, ABSENCE OF GLYCOSYLATION AT ASN-348, DISULFIDE BONDS.
[6]"Cell surface anchorage and ligand-binding domains of the Saccharomyces cerevisiae cell adhesion protein alpha-agglutinin, a member of the immunoglobulin superfamily."
Wojciechowicz D., Lu C.F., Kurjan J., Lipke P.N.
Mol. Cell. Biol. 13:2554-2563(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION, GPI-ANCHOR.
[7]"A pathway for cell wall anchorage of Saccharomyces cerevisiae alpha-agglutinin."
Lu C.-F., Kurjan J., Lipke P.N.
Mol. Cell. Biol. 14:4825-4833(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[8]"Glycosyl phosphatidylinositol-dependent cross-linking of alpha-agglutinin and beta 1,6-glucan in the Saccharomyces cerevisiae cell wall."
Lu C.-F., Montijn R.C., Brown J.L., Klis F., Kurjan J., Bussey H., Lipke P.N.
J. Cell Biol. 128:333-340(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: GPI-ANCHOR, CROSS-LINKING TO CELL WALL.
[9]"Identification of a ligand-binding site in an immunoglobulin fold domain of the Saccharomyces cerevisiae adhesion protein alpha-agglutinin."
de Nobel H., Lipke P.N., Kurjan J.
Mol. Biol. Cell 7:143-153(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF ILE-214; ASP-215; TYR-216; ASP-217; THR-289; ILE-290; ASP-291; HIS-292; LEU-294; GLU-295; PHE-296; TYR-298; TYR-322; GLN-323; GLY-324 AND ARG-325.
[10]"Screening for glycosylphosphatidylinositol (GPI)-dependent cell wall proteins in Saccharomyces cerevisiae."
Hamada K., Fukuchi S., Arisawa M., Baba M., Kitada K.
Mol. Gen. Genet. 258:53-59(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[11]"Interaction of alpha-agglutinin and a-agglutinin, Saccharomyces cerevisiae sexual cell adhesion molecules."
Zhao H., Shen Z.M., Kahn P.C., Lipke P.N.
J. Bacteriol. 183:2874-2880(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH AGA2.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X16861 Genomic DNA. Translation: CAA34752.1.
M28164 Genomic DNA. Translation: AAA34417.1.
X87611 Genomic DNA. Translation: CAA60926.1.
Z49504 Genomic DNA. Translation: CAA89526.1.
BK006943 Genomic DNA. Translation: DAA08794.1.
PIRS22835.
RefSeqNP_012537.1. NM_001181661.1.

3D structure databases

ProteinModelPortalP20840.
SMRP20840. Positions 45-263.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid33760. 8 interactions.
DIPDIP-5692N.
MINTMINT-506539.
STRING4932.YJR004C.

Proteomic databases

PaxDbP20840.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYJR004C; YJR004C; YJR004C.
GeneID853460.
KEGGsce:YJR004C.

Organism-specific databases

CYGDYJR004c.
SGDS000003764. SAG1.

Phylogenomic databases

eggNOGNOG12793.
OMAANGSINF.
OrthoDBEOG70KH1Z.

Enzyme and pathway databases

BioCycYEAST:G3O-31650-MONOMER.

Gene expression databases

GenevestigatorP20840.

Family and domain databases

Gene3D2.60.40.1280. 1 hit.
InterProIPR008966. Adhesion_dom.
IPR024672. Agglutinin-like_N.
IPR011252. Fibrogen-bd_dom1.
[Graphical view]
PfamPF11766. Candida_ALS_N. 1 hit.
[Graphical view]
SMARTSM01056. Candida_ALS_N. 1 hit.
[Graphical view]
SUPFAMSSF49401. SSF49401. 1 hit.
ProtoNetSearch...

Other

NextBio974038.

Entry information

Entry nameSAG1_YEAST
AccessionPrimary (citable) accession number: P20840
Secondary accession number(s): D6VWH8
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: November 1, 1995
Last modified: June 11, 2014
This is version 124 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome X

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

Yeast

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