P22146 · GAS1_YEAST
- Protein1,3-beta-glucanosyltransferase GAS1
- GeneGAS1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids559 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Splits internally a 1,3-beta-glucan molecule and transfers the newly generated reducing end (the donor) to the non-reducing end of another 1,3-beta-glucan molecule (the acceptor) forming a 1,3-beta linkage, resulting in the elongation of 1,3-beta-glucan chains in the cell wall. Involved in cell wall biosynthesis and morphogenesis.
Miscellaneous
Present with 11000 wall-bound molecules/cell in log phase YPD medium.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 92 | (1,3-beta-D-glucosyl)n 1 (UniProtKB | ChEBI); donor substrate | ||||
Sequence: Y | ||||||
Binding site | 119-127 | (1,3-beta-D-glucosyl)n 1 (UniProtKB | ChEBI); donor substrate | ||||
Sequence: AAPATSINR | ||||||
Binding site | 160 | (1,3-beta-D-glucosyl)n 1 (UniProtKB | ChEBI); donor substrate | ||||
Sequence: N | ||||||
Active site | 161 | Proton donor | ||||
Sequence: E | ||||||
Binding site | 161 | (1,3-beta-D-glucosyl)n 2 (UniProtKB | ChEBI); acceptor substrate | ||||
Sequence: E | ||||||
Binding site | 202 | (1,3-beta-D-glucosyl)n 2 (UniProtKB | ChEBI); acceptor substrate | ||||
Sequence: D | ||||||
Binding site | 207 | (1,3-beta-D-glucosyl)n 2 (UniProtKB | ChEBI); acceptor substrate | ||||
Sequence: R | ||||||
Active site | 262 | Nucleophile | ||||
Sequence: E | ||||||
Binding site | 294 | (1,3-beta-D-glucosyl)n 1 (UniProtKB | ChEBI); donor substrate | ||||
Sequence: Y |
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | cellular bud scar | |
Cellular Component | COPII-coated ER to Golgi transport vesicle | |
Cellular Component | extracellular region | |
Cellular Component | fungal-type cell wall | |
Cellular Component | membrane raft | |
Cellular Component | mitochondrion | |
Cellular Component | nuclear periphery | |
Cellular Component | plasma membrane | |
Cellular Component | primary cell septum | |
Cellular Component | side of membrane | |
Molecular Function | 1,3-beta-glucanosyltransferase activity | |
Biological Process | filamentous growth | |
Biological Process | fungal-type cell wall (1->3)-beta-D-glucan biosynthetic process | |
Biological Process | fungal-type cell wall organization | |
Biological Process | heterochromatin formation | |
Biological Process | regulation of response to endoplasmic reticulum stress |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended name1,3-beta-glucanosyltransferase GAS1
- EC number
- Alternative names
Gene names
Organism names
- Strains
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Saccharomycotina > Saccharomycetes > Saccharomycetales > Saccharomycetaceae > Saccharomyces
Accessions
- Primary accessionP22146
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Lipid-anchor, GPI-anchor
Note: Identified as GPI-anchored plasma membrane protein (GPI-PMP) as well as covalently-linked GPI-modified cell wall protein (GPI-CWP) in the outer cell wall layer.
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 74 | Impairs the folding and stability of the protein. | ||||
Sequence: C → S | ||||||
Mutagenesis | 103 | Partially impairs the folding and stability of the protein. | ||||
Sequence: C → S | ||||||
Mutagenesis | 161 | Loss of function. | ||||
Sequence: E → Q | ||||||
Mutagenesis | 262 | Loss of function. | ||||
Sequence: E → Q | ||||||
Mutagenesis | 265 | Partially impairs the folding and stability of the protein. | ||||
Sequence: C → S | ||||||
Mutagenesis | 348 | Impairs the folding and stability of the protein. | ||||
Sequence: C → S |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 4 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for signal, chain, glycosylation, disulfide bond, lipidation, propeptide.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-22 | |||||
Sequence: MLFKSLSKLATAAAFFAGVATA | ||||||
Chain | PRO_0000010473 | 23-528 | 1,3-beta-glucanosyltransferase GAS1 | |||
Sequence: DDVPAIEVVGNKFFYSNNGSQFYIRGVAYQADTANETSGSTVNDPLANYESCSRDIPYLKKLNTNVIRVYAINTTLDHSECMKALNDADIYVIADLAAPATSINRDDPTWTVDLFNSYKTVVDTFANYTNVLGFFAGNEVTNNYTNTDASAFVKAAIRDVRQYISDKNYRKIPVGYSSNDDEDTRVKMTDYFACGDDDVKADFYGINMYEWCGKSDFKTSGYADRTAEFKNLSIPVFFSEYGCNEVTPRLFTEVEALYGSNMTDVWSGGIVYMYFEETNKYGLVSIDGNDVKTLDDFNNYSSEINKISPTSANTKSYSATTSDVACPATGKYWSAATELPPTPNGGLCSCMNAANSCVVSDDVDSDDYETLFNWICNEVDCSGISANGTAGKYGAYSFCTPKEQLSFVMNLYYEKSGGSKSDCSFSGSATLQTATTQASCSSALKEIGSMGTNSASGSVDLGSGTESSTASSNASGSSSKSNSGSSGSSSSSSSSSASSSSSSKKN | ||||||
Glycosylation | 40 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 57 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 74↔103 | |||||
Sequence: CSRDIPYLKKLNTNVIRVYAINTTLDHSEC | ||||||
Glycosylation | 95 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 149 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 165 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 216↔348 | |||||
Sequence: CGDDDVKADFYGINMYEWCGKSDFKTSGYADRTAEFKNLSIPVFFSEYGCNEVTPRLFTEVEALYGSNMTDVWSGGIVYMYFEETNKYGLVSIDGNDVKTLDDFNNYSSEINKISPTSANTKSYSATTSDVAC | ||||||
Disulfide bond | 234↔265 | |||||
Sequence: CGKSDFKTSGYADRTAEFKNLSIPVFFSEYGC | ||||||
Glycosylation | 253 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 283 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 321 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 370↔421 | |||||
Sequence: CSCMNAANSCVVSDDVDSDDYETLFNWICNEVDCSGISANGTAGKYGAYSFC | ||||||
Disulfide bond | 372↔462 | |||||
Sequence: CMNAANSCVVSDDVDSDDYETLFNWICNEVDCSGISANGTAGKYGAYSFCTPKEQLSFVMNLYYEKSGGSKSDCSFSGSATLQTATTQASC | ||||||
Disulfide bond | 379↔445 | |||||
Sequence: CVVSDDVDSDDYETLFNWICNEVDCSGISANGTAGKYGAYSFCTPKEQLSFVMNLYYEKSGGSKSDC | ||||||
Disulfide bond | 398↔403 | |||||
Sequence: CNEVDC | ||||||
Glycosylation | 409 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 495 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Lipidation | 528 | GPI-anchor amidated asparagine | ||||
Sequence: N | ||||||
Propeptide | PRO_0000010474 | 529-559 | Removed in mature form | |||
Sequence: AATNVKANLAQVVFTSIISLSIAAGVGFALV |
Post-translational modification
Extensively N- and O-glycosylated.
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
- PTM
Proteomic databases
PTM databases
Interaction
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P22146 | SIR2 P06700 | 2 | EBI-7327, EBI-17219 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 474-526 | Disordered | ||||
Sequence: TNSASGSVDLGSGTESSTASSNASGSSSKSNSGSSGSSSSSSSSSASSSSSSK |
Sequence similarities
Belongs to the glycosyl hydrolase 72 family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length559
- Mass (Da)59,582
- Last updated1996-02-01 v2
- ChecksumD6E39568DCB4C5AE
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 211 | in Ref. 1; CAA37512 | ||||
Sequence: T → A |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X53424 EMBL· GenBank· DDBJ | CAA37512.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X56399 EMBL· GenBank· DDBJ | CAA39809.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
Z49212 EMBL· GenBank· DDBJ | CAA89140.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BK006946 EMBL· GenBank· DDBJ | DAA10208.1 EMBL· GenBank· DDBJ | Genomic DNA |