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P20840

- SAG1_YEAST

UniProt

P20840 - SAG1_YEAST

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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

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
Complete GO annotation...

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
Complete GO annotation...

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...)1 Publication
Glycosylationi282 – 2821O-linked (Man...)1 Publication
Glycosylationi289 – 2891O-linked (Man...)1 Publication
Glycosylationi299 – 2991O-linked (Man...)1 Publication
Glycosylationi303 – 3031O-linked (Man...)1 Publication
Glycosylationi306 – 3061N-linked (GlcNAc...)1 Publication
Glycosylationi307 – 3071O-linked (Man...)1 Publication
Glycosylationi308 – 3081O-linked (Man...)1 Publication
Glycosylationi311 – 3111O-linked (Man...)1 Publication
Glycosylationi314 – 3141O-linked (Man...)1 Publication
Glycosylationi315 – 3151O-linked (Man...)1 Publication
Glycosylationi316 – 3161O-linked (Man...)1 Publication
Glycosylationi329 – 3291O-linked (Man...)1 Publication
Glycosylationi331 – 3311O-linked (Man...)1 Publication
Glycosylationi334 – 3341O-linked (Man...)1 Publication
Glycosylationi335 – 3351O-linked (Man...)1 Publication
Glycosylationi338 – 3381O-linked (Man...)1 Publication
Glycosylationi339 – 3391O-linked (Man...)1 Publication
Glycosylationi340 – 3401O-linked (Man...)1 Publication
Glycosylationi341 – 3411O-linked (Man...)1 Publication
Glycosylationi342 – 3421O-linked (Man...)1 Publication
Glycosylationi345 – 3451O-linked (Man...)1 Publication
Glycosylationi346 – 3461O-linked (Man...)1 Publication
Glycosylationi349 – 3491O-linked (Man...)1 Publication
Glycosylationi350 – 3501O-linked (Man...)1 Publication
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 19-304.
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.
InParanoidiP20840.
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 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MFTFLKIILW LFSLALASAI NINDITFSNL EITPLTANKQ PDQGWTATFD
60 70 80 90 100
FSIADASSIR EGDEFTLSMP HVYRIKLLNS SQTATISLAD GTEAFKCYVS
110 120 130 140 150
QQAAYLYENT TFTCTAQNDL SSYNTIDGSI TFSLNFSDGG SSYEYELENA
160 170 180 190 200
KFFKSGPMLV KLGNQMSDVV NFDPAAFTEN VFHSGRSTGY GSFESYHLGM
210 220 230 240 250
YCPNGYFLGG TEKIDYDSSN NNVDLDCSSV QVYSSNDFND WWFPQSYNDT
260 270 280 290 300
NADVTCFGSN LWITLDEKLY DGEMLWVNAL QSLPANVNTI DHALEFQYTC
310 320 330 340 350
LDTIANTTYA TQFSTTREFI VYQGRNLGTA SAKSSFISTT TTDLTSINTS
360 370 380 390 400
AYSTGSISTV ETGNRTTSEV ISHVVTTSTK LSPTATTSLT IAQTSIYSTD
410 420 430 440 450
SNITVGTDIH TTSEVISDVE TISRETASTV VAAPTSTTGW TGAMNTYISQ
460 470 480 490 500
FTSSSFATIN STPIISSSAV FETSDASIVN VHTENITNTA AVPSEEPTFV
510 520 530 540 550
NATRNSLNSF CSSKQPSSPS SYTSSPLVSS LSVSKTLLST SFTPSVPTSN
560 570 580 590 600
TYIKTKNTGY FEHTALTTSS VGLNSFSETA VSSQGTKIDT FLVSSLIAYP
610 620 630 640 650
SSASGSQLSG IQQNFTSTSL MISTYEGKAS IFFSAELGSI IFLLLSYLLF
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 19-304.
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.
InParanoidi P20840.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 126 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