Alpha-agglutinin precursor - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

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P20840 (SAG1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 114. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Alpha-agglutinin

Alternative name(s):
AG-alpha-1

Gene names

Name:	SAG1
Synonyms:	AGAL1
Ordered Locus Names:	YJR004C
ORF Names:	J1418

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›

Protein attributes

Sequence length	650 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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	Secreted › cell wall. Membrane; Lipid-anchor › GPI-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.

Ontologies

Keywords
Biological process	Cell adhesion
Cellular component	Cell wall Membrane Secreted
Domain	Repeat Signal
PTM	Disulfide bond GPI-anchor Glycoprotein Lipoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	agglutination involved in conjugation with cellular fusion Inferred from mutant phenotype PubMed 2673555 Ref.2. Source: SGD
Cellular_component	anchored to membrane Inferred from electronic annotation. Source: UniProtKB-KW extracellular region Inferred from electronic annotation. Source: UniProtKB-KW fungal-type cell wall Inferred from direct assay PubMed 10383953. Source: SGD
Molecular_function	cell adhesion molecule binding Inferred from mutant phenotype PubMed 2673555 Ref.2. Source: SGD
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 19

Chain

20 – 627

608

Alpha-agglutinin

PRO_0000022265

Propeptide

628 – 650

Removed in mature form Potential

PRO_0000022266

Regions

Repeat

339 – 378

Repeat

384 – 423

Region

216 – 322

107

Ig-like fold domain important for alpha-agglutinin activity, contributing to a functional binding site for a-agglutinin

Region

339 – 423

2 X 40 AA tandem repeats

Compositional bias

331 – 359

Ser/Thr-rich

Sites

Site

348

Not glycosylated

Amino acid modifications

Lipidation

627

GPI-anchor amidated glycine Potential

Glycosylation

N-linked (GlcNAc...) Potential

Glycosylation

109

N-linked (GlcNAc...) Potential

Glycosylation

135

N-linked (GlcNAc...) Potential

Glycosylation

248

N-linked (GlcNAc...) Ref.5

Glycosylation

282

O-linked (Man...) Ref.5

Glycosylation

289

O-linked (Man...) Ref.5

Glycosylation

299

O-linked (Man...) Ref.5

Glycosylation

303

O-linked (Man...) Ref.5

Glycosylation

306

N-linked (GlcNAc...) Ref.5

Glycosylation

307

O-linked (Man...) Ref.5

Glycosylation

308

O-linked (Man...) Ref.5

Glycosylation

311

O-linked (Man...) Ref.5

Glycosylation

314

O-linked (Man...) Ref.5

Glycosylation

315

O-linked (Man...) Ref.5

Glycosylation

316

O-linked (Man...) Ref.5

Glycosylation

329

O-linked (Man...) Ref.5

Glycosylation

331

O-linked (Man...) Ref.5

Glycosylation

334

O-linked (Man...) Ref.5

Glycosylation

335

O-linked (Man...) Ref.5

Glycosylation

338

O-linked (Man...) Ref.5

Glycosylation

339

O-linked (Man...) Ref.5

Glycosylation

340

O-linked (Man...) Ref.5

Glycosylation

341

O-linked (Man...) Ref.5

Glycosylation

342

O-linked (Man...) Ref.5

Glycosylation

345

O-linked (Man...) Ref.5

Glycosylation

346

O-linked (Man...) Ref.5

Glycosylation

349

O-linked (Man...) Ref.5

Glycosylation

350

O-linked (Man...) Ref.5

Glycosylation

364

N-linked (GlcNAc...) Potential

Glycosylation

402

N-linked (GlcNAc...) Potential

Glycosylation

460

N-linked (GlcNAc...) Potential

Glycosylation

485

N-linked (GlcNAc...) Potential

Glycosylation

501

N-linked (GlcNAc...) Potential

Glycosylation

614

N-linked (GlcNAc...) Potential

Disulfide bond

Disulfide bond

Experimental info

Mutagenesis

211

T → I: Little effect on secreted alpha-agglutinin activity.

Mutagenesis

214

I → M: No effect on secreted alpha-agglutinin activity. Ref.9

Mutagenesis

215

D → A or N: Little or no effect on secreted alpha-agglutinin activity. Ref.9

Mutagenesis

216

Y → D: Complete loss of alpha-agglutinin activity. Ref.9

Mutagenesis

216

Y → F: No effect on secreted alpha-agglutinin activity. Ref.9

Mutagenesis

216

Y → S: Decreases secreted alpha-agglutinin activity by 100-fold. Ref.9

Mutagenesis

216

Y → V: Decreases secreted alpha-agglutinin activity by 10-fold. Ref.9

Mutagenesis

217

D → A: Little effect on secreted alpha-agglutinin activity. Ref.9

Mutagenesis

217

D → N: Decreases secreted alpha-agglutinin activity by 10-fold. Ref.9

Mutagenesis

289

T → A: Decreases secreted alpha-agglutinin activity by less than 2-fold. Ref.9

Mutagenesis

290

I → M: Decreases secreted alpha-agglutinin activity by less than 2-fold. Ref.9

Mutagenesis

291

D → A or N: Decreases secreted alpha-agglutinin activity by 4-fold. Ref.9

Mutagenesis

292

H → L or R: Almost complete loss of secreted alpha-agglutinin activity. Ref.9

Mutagenesis

294

L → S: Decreases secreted alpha-agglutinin activity by more than 20-fold. Ref.9

Mutagenesis

295

E → A or Q: Decreases secreted alpha-agglutinin activity by 2-fold. Ref.9

Mutagenesis

296

F → Y: Decreases secreted alpha-agglutinin activity by more than 20-fold. Ref.9

Mutagenesis

298

Y → H: Decreases secreted alpha-agglutinin activity by less than 2-fold. Ref.9

Mutagenesis

322

Y → A: Decreases secreted alpha-agglutinin activity by 60-fold. Ref.9

Mutagenesis

322

Y → C: Almost complete loss of secreted alpha-agglutinin activity by 10-fold. Ref.9

Mutagenesis

322

Y → F: Decreases secreted alpha-agglutinin activity by 15-fold. Ref.9

Mutagenesis

323

Q → L: Decreases secreted alpha-agglutinin activity by 2-fold. Ref.9

Mutagenesis

324

G → A: Little effect on secreted alpha-agglutinin activity. Ref.9

Mutagenesis

325

R → G: Little effect on secreted alpha-agglutinin activity. Ref.9

Sequence conflict

449

S → P in AAA34417. Ref.1

Sequence conflict

556

K → E in AAA34417. Ref.1

Sequence conflict

581

V → L in AAA34417. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

P20840 [UniParc].

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

FASTA

650

70,340

        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' referencesShow '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. Karpfinger-Hartl L. EMBO J. 15:2031-2049(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[4]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases 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.

Web resources

Functional Glycomics Gateway - Glycan Binding

Alpha-agglutinin

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.
PIR	S22835.
RefSeq	NP_012537.1. NM_001181661.1.
3D structure databases
ProteinModelPortal	P20840.
SMR	P20840. Positions 45-263.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-5692N.
MINT	MINT-506539.
STRING	4932.YJR004C.
Proteomic databases
PaxDb	P20840.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YJR004C; YJR004C; YJR004C.
GeneID	853460.
KEGG	sce:YJR004C.
Organism-specific databases
CYGD	YJR004c.
SGD	S000003764. SAG1.
Phylogenomic databases
eggNOG	NOG12793.
OMA	ISSEEPT.
OrthoDB	EOG4CJZSK.
Gene expression databases
ArrayExpress	P20840.
Genevestigator	P20840.
GermOnline	YJR004C. Saccharomyces cerevisiae.
Family and domain databases
Gene3D	2.60.40.1280. 1 hit.
InterPro	IPR008966. Adhesion_dom. IPR024672. Agglutinin-like_N. IPR011252. Fibrogen-bd_dom1. [Graphical view]
Pfam	PF11766. Candida_ALS_N. 1 hit. [Graphical view]
SMART	SM01056. Candida_ALS_N. 1 hit. [Graphical view]
SUPFAM	SSF49401. Adhes_bact. 1 hit.
ProtoNet	Search...
Other
NextBio	974038.

Entry information

Entry name

SAG1_YEAST

Accession

Primary (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:	May 1, 2013
This is version 114 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

Yeast

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

Yeast chromosome X

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

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Web resources

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents