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P20840

- SAG1_YEAST

UniProt

P20840 - SAG1_YEAST

Protein

Alpha-agglutinin

Gene

SAG1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 125 (01 Oct 2014)
      Sequence version 2 (01 Nov 1995)
      Previous versions | rss
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    Functioni

    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.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei348 – 3481Not glycosylated

    GO - Molecular functioni

    1. cell adhesion molecule binding Source: SGD

    GO - Biological processi

    1. agglutination involved in conjugation with cellular fusion Source: SGD

    Keywords - Biological processi

    Cell adhesion

    Enzyme and pathway databases

    BioCyciYEAST:G3O-31650-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Alpha-agglutinin
    Alternative name(s):
    AG-alpha-1
    Gene namesi
    Name:SAG1
    Synonyms:AGAL1
    Ordered Locus Names:YJR004C
    ORF Names:J1418
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome X

    Organism-specific databases

    CYGDiYJR004c.
    SGDiS000003764. SAG1.

    Subcellular locationi

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

    GO - Cellular componenti

    1. anchored component of membrane Source: UniProtKB-KW
    2. extracellular region Source: UniProtKB-KW
    3. fungal-type cell wall Source: SGD

    Keywords - Cellular componenti

    Cell wall, Membrane, Secreted

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi211 – 2111T → I: Little effect on secreted alpha-agglutinin activity.
    Mutagenesisi214 – 2141I → M: No effect on secreted alpha-agglutinin activity. 1 Publication
    Mutagenesisi215 – 2151D → A or N: Little or no effect on secreted alpha-agglutinin activity. 1 Publication
    Mutagenesisi216 – 2161Y → D: Complete loss of alpha-agglutinin activity. 1 Publication
    Mutagenesisi216 – 2161Y → F: No effect on secreted alpha-agglutinin activity. 1 Publication
    Mutagenesisi216 – 2161Y → S: Decreases secreted alpha-agglutinin activity by 100-fold. 1 Publication
    Mutagenesisi216 – 2161Y → V: Decreases secreted alpha-agglutinin activity by 10-fold. 1 Publication
    Mutagenesisi217 – 2171D → A: Little effect on secreted alpha-agglutinin activity. 1 Publication
    Mutagenesisi217 – 2171D → N: Decreases secreted alpha-agglutinin activity by 10-fold. 1 Publication
    Mutagenesisi289 – 2891T → A: Decreases secreted alpha-agglutinin activity by less than 2-fold. 1 Publication
    Mutagenesisi290 – 2901I → M: Decreases secreted alpha-agglutinin activity by less than 2-fold. 1 Publication
    Mutagenesisi291 – 2911D → A or N: Decreases secreted alpha-agglutinin activity by 4-fold. 1 Publication
    Mutagenesisi292 – 2921H → L or R: Almost complete loss of secreted alpha-agglutinin activity. 1 Publication
    Mutagenesisi294 – 2941L → S: Decreases secreted alpha-agglutinin activity by more than 20-fold. 1 Publication
    Mutagenesisi295 – 2951E → A or Q: Decreases secreted alpha-agglutinin activity by 2-fold. 1 Publication
    Mutagenesisi296 – 2961F → Y: Decreases secreted alpha-agglutinin activity by more than 20-fold. 1 Publication
    Mutagenesisi298 – 2981Y → H: Decreases secreted alpha-agglutinin activity by less than 2-fold. 1 Publication
    Mutagenesisi322 – 3221Y → A: Decreases secreted alpha-agglutinin activity by 60-fold. 1 Publication
    Mutagenesisi322 – 3221Y → C: Almost complete loss of secreted alpha-agglutinin activity by 10-fold. 1 Publication
    Mutagenesisi322 – 3221Y → F: Decreases secreted alpha-agglutinin activity by 15-fold. 1 Publication
    Mutagenesisi323 – 3231Q → L: Decreases secreted alpha-agglutinin activity by 2-fold. 1 Publication
    Mutagenesisi324 – 3241G → A: Little effect on secreted alpha-agglutinin activity. 1 Publication
    Mutagenesisi325 – 3251R → G: Little effect on secreted alpha-agglutinin activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1919Add
    BLAST
    Chaini20 – 627608Alpha-agglutininPRO_0000022265Add
    BLAST
    Propeptidei628 – 65023Removed in mature formSequence AnalysisPRO_0000022266Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi79 – 791N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi97 ↔ 1141 Publication
    Glycosylationi109 – 1091N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi135 – 1351N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi202 ↔ 3001 Publication
    Glycosylationi248 – 2481N-linked (GlcNAc...)2 Publications
    Glycosylationi282 – 2821O-linked (Man...)2 Publications
    Glycosylationi289 – 2891O-linked (Man...)2 Publications
    Glycosylationi299 – 2991O-linked (Man...)2 Publications
    Glycosylationi303 – 3031O-linked (Man...)2 Publications
    Glycosylationi306 – 3061N-linked (GlcNAc...)2 Publications
    Glycosylationi307 – 3071O-linked (Man...)2 Publications
    Glycosylationi308 – 3081O-linked (Man...)2 Publications
    Glycosylationi311 – 3111O-linked (Man...)2 Publications
    Glycosylationi314 – 3141O-linked (Man...)2 Publications
    Glycosylationi315 – 3151O-linked (Man...)2 Publications
    Glycosylationi316 – 3161O-linked (Man...)2 Publications
    Glycosylationi329 – 3291O-linked (Man...)2 Publications
    Glycosylationi331 – 3311O-linked (Man...)2 Publications
    Glycosylationi334 – 3341O-linked (Man...)2 Publications
    Glycosylationi335 – 3351O-linked (Man...)2 Publications
    Glycosylationi338 – 3381O-linked (Man...)2 Publications
    Glycosylationi339 – 3391O-linked (Man...)2 Publications
    Glycosylationi340 – 3401O-linked (Man...)2 Publications
    Glycosylationi341 – 3411O-linked (Man...)2 Publications
    Glycosylationi342 – 3421O-linked (Man...)2 Publications
    Glycosylationi345 – 3451O-linked (Man...)2 Publications
    Glycosylationi346 – 3461O-linked (Man...)2 Publications
    Glycosylationi349 – 3491O-linked (Man...)2 Publications
    Glycosylationi350 – 3501O-linked (Man...)2 Publications
    Glycosylationi364 – 3641N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi402 – 4021N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi460 – 4601N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi485 – 4851N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi501 – 5011N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi614 – 6141N-linked (GlcNAc...)Sequence Analysis
    Lipidationi627 – 6271GPI-anchor amidated glycineSequence Analysis

    Post-translational modificationi

    N-glycosylated, and O-glycosylated by both PMT1 and PMT2.2 Publications
    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 - PTMi

    Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein

    Proteomic databases

    PaxDbiP20840.

    Expressioni

    Inductioni

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

    Gene expression databases

    GenevestigatoriP20840.

    Interactioni

    Subunit structurei

    Interacts with AGA2.1 Publication

    Protein-protein interaction databases

    BioGridi33760. 8 interactions.
    DIPiDIP-5692N.
    MINTiMINT-506539.
    STRINGi4932.YJR004C.

    Structurei

    3D structure databases

    ProteinModelPortaliP20840.
    SMRiP20840. Positions 45-263.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati339 – 378401Add
    BLAST
    Repeati384 – 423402Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni216 – 322107Ig-like fold domain important for alpha-agglutinin activity, contributing to a functional binding site for a-agglutininAdd
    BLAST
    Regioni339 – 423852 X 40 AA tandem repeatsAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi331 – 35929Ser/Thr-richAdd
    BLAST

    Sequence similaritiesi

    To C.albicans ALS1.Curated

    Keywords - Domaini

    Repeat, Signal

    Phylogenomic databases

    eggNOGiNOG12793.
    OMAiANGSINF.
    OrthoDBiEOG70KH1Z.

    Family and domain databases

    Gene3Di2.60.40.1280. 1 hit.
    InterProiIPR008966. Adhesion_dom.
    IPR024672. Agglutinin-like_N.
    IPR011252. Fibrogen-bd_dom1.
    [Graphical view]
    PfamiPF11766. Candida_ALS_N. 1 hit.
    [Graphical view]
    SMARTiSM01056. Candida_ALS_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF49401. SSF49401. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P20840-1 [UniParc]FASTAAdd to Basket

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    MFTFLKIILW LFSLALASAI NINDITFSNL EITPLTANKQ PDQGWTATFD    50
    FSIADASSIR EGDEFTLSMP HVYRIKLLNS SQTATISLAD GTEAFKCYVS 100
    QQAAYLYENT TFTCTAQNDL SSYNTIDGSI TFSLNFSDGG SSYEYELENA 150
    KFFKSGPMLV KLGNQMSDVV NFDPAAFTEN VFHSGRSTGY GSFESYHLGM 200
    YCPNGYFLGG TEKIDYDSSN NNVDLDCSSV QVYSSNDFND WWFPQSYNDT 250
    NADVTCFGSN LWITLDEKLY DGEMLWVNAL QSLPANVNTI DHALEFQYTC 300
    LDTIANTTYA TQFSTTREFI VYQGRNLGTA SAKSSFISTT TTDLTSINTS 350
    AYSTGSISTV ETGNRTTSEV ISHVVTTSTK LSPTATTSLT IAQTSIYSTD 400
    SNITVGTDIH TTSEVISDVE TISRETASTV VAAPTSTTGW TGAMNTYISQ 450
    FTSSSFATIN STPIISSSAV FETSDASIVN VHTENITNTA AVPSEEPTFV 500
    NATRNSLNSF CSSKQPSSPS SYTSSPLVSS LSVSKTLLST SFTPSVPTSN 550
    TYIKTKNTGY FEHTALTTSS VGLNSFSETA VSSQGTKIDT FLVSSLIAYP 600
    SSASGSQLSG IQQNFTSTSL MISTYEGKAS IFFSAELGSI IFLLLSYLLF 650
    Length:650
    Mass (Da):70,340
    Last modified:November 1, 1995 - v2
    Checksum:i8BBF7A1C44C93C2B
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti449 – 4491S → P in AAA34417. (PubMed:2676603)Curated
    Sequence conflicti556 – 5561K → E in AAA34417. (PubMed:2676603)Curated
    Sequence conflicti581 – 5811V → L in AAA34417. (PubMed:2676603)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    PIRiS22835.
    RefSeqiNP_012537.1. NM_001181661.1.

    Genome annotation databases

    EnsemblFungiiYJR004C; YJR004C; YJR004C.
    GeneIDi853460.
    KEGGisce:YJR004C.

    Cross-referencesi

    Web resourcesi

    Functional Glycomics Gateway - Glycan Binding

    Alpha-agglutinin

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    PIRi S22835.
    RefSeqi NP_012537.1. NM_001181661.1.

    3D structure databases

    ProteinModelPortali P20840.
    SMRi P20840. Positions 45-263.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 33760. 8 interactions.
    DIPi DIP-5692N.
    MINTi MINT-506539.
    STRINGi 4932.YJR004C.

    Proteomic databases

    PaxDbi P20840.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YJR004C ; YJR004C ; YJR004C .
    GeneIDi 853460.
    KEGGi sce:YJR004C.

    Organism-specific databases

    CYGDi YJR004c.
    SGDi S000003764. SAG1.

    Phylogenomic databases

    eggNOGi NOG12793.
    OMAi ANGSINF.
    OrthoDBi EOG70KH1Z.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-31650-MONOMER.

    Miscellaneous databases

    NextBioi 974038.

    Gene expression databases

    Genevestigatori P20840.

    Family and domain databases

    Gene3Di 2.60.40.1280. 1 hit.
    InterProi IPR008966. Adhesion_dom.
    IPR024672. Agglutinin-like_N.
    IPR011252. Fibrogen-bd_dom1.
    [Graphical view ]
    Pfami PF11766. Candida_ALS_N. 1 hit.
    [Graphical view ]
    SMARTi SM01056. Candida_ALS_N. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49401. SSF49401. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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.
      , 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. 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.

    Entry informationi

    Entry nameiSAG1_YEAST
    AccessioniPrimary (citable) accession number: P20840
    Secondary accession number(s): D6VWH8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1991
    Last sequence update: November 1, 1995
    Last modified: October 1, 2014
    This is version 125 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    2. Yeast chromosome X
      Yeast (Saccharomyces cerevisiae) chromosome X: entries and gene names

    External Data

    Dasty 3