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Protein

Alpha-agglutinin

Gene

SAG1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: 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

GO - Molecular functioni

  • cell adhesion molecule binding Source: SGD

GO - Biological processi

  • agglutination involved in conjugation with cellular fusion Source: SGD

Keywordsi

Biological processCell 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
Proteomesi
  • UP000002311 Componenti: Chromosome X

Organism-specific databases

EuPathDBiFungiDB:YJR004C.
SGDiS000003764. SAG1.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell wall, Membrane, Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi211T → I: Little effect on secreted alpha-agglutinin activity. 1
Mutagenesisi214I → M: No effect on secreted alpha-agglutinin activity. 1 Publication1
Mutagenesisi215D → A or N: Little or no effect on secreted alpha-agglutinin activity. 1 Publication1
Mutagenesisi216Y → D: Complete loss of alpha-agglutinin activity. 1 Publication1
Mutagenesisi216Y → F: No effect on secreted alpha-agglutinin activity. 1 Publication1
Mutagenesisi216Y → S: Decreases secreted alpha-agglutinin activity by 100-fold. 1 Publication1
Mutagenesisi216Y → V: Decreases secreted alpha-agglutinin activity by 10-fold. 1 Publication1
Mutagenesisi217D → A: Little effect on secreted alpha-agglutinin activity. 1 Publication1
Mutagenesisi217D → N: Decreases secreted alpha-agglutinin activity by 10-fold. 1 Publication1
Mutagenesisi289T → A: Decreases secreted alpha-agglutinin activity by less than 2-fold. 1 Publication1
Mutagenesisi290I → M: Decreases secreted alpha-agglutinin activity by less than 2-fold. 1 Publication1
Mutagenesisi291D → A or N: Decreases secreted alpha-agglutinin activity by 4-fold. 1 Publication1
Mutagenesisi292H → L or R: Almost complete loss of secreted alpha-agglutinin activity. 1 Publication1
Mutagenesisi294L → S: Decreases secreted alpha-agglutinin activity by more than 20-fold. 1 Publication1
Mutagenesisi295E → A or Q: Decreases secreted alpha-agglutinin activity by 2-fold. 1 Publication1
Mutagenesisi296F → Y: Decreases secreted alpha-agglutinin activity by more than 20-fold. 1 Publication1
Mutagenesisi298Y → H: Decreases secreted alpha-agglutinin activity by less than 2-fold. 1 Publication1
Mutagenesisi322Y → A: Decreases secreted alpha-agglutinin activity by 60-fold. 1 Publication1
Mutagenesisi322Y → C: Almost complete loss of secreted alpha-agglutinin activity by 10-fold. 1 Publication1
Mutagenesisi322Y → F: Decreases secreted alpha-agglutinin activity by 15-fold. 1 Publication1
Mutagenesisi323Q → L: Decreases secreted alpha-agglutinin activity by 2-fold. 1 Publication1
Mutagenesisi324G → A: Little effect on secreted alpha-agglutinin activity. 1 Publication1
Mutagenesisi325R → G: Little effect on secreted alpha-agglutinin activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 19Add BLAST19
ChainiPRO_000002226520 – 627Alpha-agglutininAdd BLAST608
PropeptideiPRO_0000022266628 – 650Removed in mature formSequence analysisAdd BLAST23

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi79N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi97 ↔ 1141 Publication
Glycosylationi109N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi135N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi202 ↔ 3001 Publication
Glycosylationi248N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi282O-linked (Man...) serine1 Publication1
Glycosylationi289O-linked (Man...) threonine1 Publication1
Glycosylationi299O-linked (Man...) threonine1 Publication1
Glycosylationi303O-linked (Man...) threonine1 Publication1
Glycosylationi306N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi307O-linked (Man...) threonine1 Publication1
Glycosylationi308O-linked (Man...) threonine1 Publication1
Glycosylationi311O-linked (Man...) threonine1 Publication1
Glycosylationi314O-linked (Man...) serine1 Publication1
Glycosylationi315O-linked (Man...) threonine1 Publication1
Glycosylationi316O-linked (Man...) threonine1 Publication1
Glycosylationi329O-linked (Man...) threonine1 Publication1
Glycosylationi331O-linked (Man...) serine1 Publication1
Glycosylationi334O-linked (Man...) serine1 Publication1
Glycosylationi335O-linked (Man...) serine1 Publication1
Glycosylationi338O-linked (Man...) serine1 Publication1
Glycosylationi339O-linked (Man...) threonine1 Publication1
Glycosylationi340O-linked (Man...) threonine1 Publication1
Glycosylationi341O-linked (Man...) threonine1 Publication1
Glycosylationi342O-linked (Man...) threonine1 Publication1
Glycosylationi345O-linked (Man...) threonine1 Publication1
Glycosylationi346O-linked (Man...) serine1 Publication1
Glycosylationi349O-linked (Man...) threonine1 Publication1
Glycosylationi350O-linked (Man...) serine1 Publication1
Glycosylationi364N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi402N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi460N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi485N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi501N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi614N-linked (GlcNAc...) asparagineSequence analysis1
Lipidationi627GPI-anchor amidated glycineSequence analysis1

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.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei348Not glycosylated1 Publication1

Keywords - PTMi

Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein

Proteomic databases

PRIDEiP20840.

Expressioni

Inductioni

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

Interactioni

Subunit structurei

Interacts with AGA2.1 Publication

GO - Molecular functioni

  • cell adhesion molecule binding Source: SGD

Protein-protein interaction databases

BioGridi33760. 35 interactors.
DIPiDIP-5692N.
IntActiP20840. 2 interactors.
MINTiMINT-506539.
STRINGi4932.YJR004C.

Structurei

3D structure databases

ProteinModelPortaliP20840.
SMRiP20840.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati339 – 3781Add BLAST40
Repeati384 – 4232Add BLAST40

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni216 – 322Ig-like fold domain important for alpha-agglutinin activity, contributing to a functional binding site for a-agglutininAdd BLAST107
Regioni339 – 4232 X 40 AA tandem repeatsAdd BLAST85

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi331 – 359Ser/Thr-richAdd BLAST29

Sequence similaritiesi

To C.albicans ALS1.Curated

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

InParanoidiP20840.
KOiK19898.
OMAiANGSINF.
OrthoDBiEOG092C316N.

Family and domain databases

Gene3Di2.60.40.1280. 1 hit.
InterProiView protein in InterPro
IPR008966. Adhesion_dom.
IPR024672. Agglutinin-like_N.
IPR033504. ALS.
IPR011252. Fibrogen-bd_dom1.
PANTHERiPTHR33793. PTHR33793. 1 hit.
PfamiView protein in Pfam
PF11766. Candida_ALS_N. 1 hit.
SMARTiView protein in SMART
SM01056. Candida_ALS_N. 1 hit.
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

« 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)DescriptionActionsGraphical viewLength
Sequence conflicti449S → P in AAA34417 (PubMed:2676603).Curated1
Sequence conflicti556K → E in AAA34417 (PubMed:2676603).Curated1
Sequence conflicti581V → L in AAA34417 (PubMed:2676603).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

Similar proteinsi

Entry informationi

Entry nameiSAG1_YEAST
AccessioniPrimary (citable) accession number: P20840
Secondary accession number(s): D6VWH8
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: November 1, 1995
Last modified: September 27, 2017
This is version 147 of the entry and version 2 of the sequence. See 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