Q59SF7 · PIR1_CANAL
- ProteinCell wall mannoprotein PIR1
- GenePIR1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids385 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Component of the outer cell wall layer required for stability of the cell wall and specifically for cell wall rigidity.
Features
Showing features for site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 88 | Covalent attachment to cell wall glycan | ||||
Sequence: Q | ||||||
Site | 107 | Covalent attachment to cell wall glycan | ||||
Sequence: Q | ||||||
Site | 125 | Covalent attachment to cell wall glycan | ||||
Sequence: Q | ||||||
Site | 146 | Covalent attachment to cell wall glycan | ||||
Sequence: Q | ||||||
Site | 163 | Covalent attachment to cell wall glycan | ||||
Sequence: Q | ||||||
Site | 183 | Covalent attachment to cell wall glycan | ||||
Sequence: Q | ||||||
Site | 200 | Covalent attachment to cell wall glycan | ||||
Sequence: Q | ||||||
Site | 220 | Covalent attachment to cell wall glycan | ||||
Sequence: Q | ||||||
Site | 243 | Covalent attachment to cell wall glycan | ||||
Sequence: Q |
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 | extracellular region | |
Cellular Component | fungal biofilm matrix | |
Cellular Component | fungal-type cell wall | |
Cellular Component | yeast-form cell wall | |
Molecular Function | structural constituent of cell wall | |
Biological Process | cellular response to temperature stimulus | |
Biological Process | fungal-type cell wall organization |
Keywords
- Biological process
Names & Taxonomy
Protein names
- Recommended nameCell wall mannoprotein PIR1
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Saccharomycotina > Saccharomycetes > Saccharomycetales > Debaryomycetaceae > Candida/Lodderomyces clade > Candida
Accessions
- Primary accessionQ59SF7
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Covalently attached to the cell wall.
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
Increases sensitivity to calcofluor white and Congo red.
PTM/Processing
Features
Showing features for signal, chain, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-18 | |||||
Sequence: MKYSTLVSIAAFISTSLA | ||||||
Chain | PRO_0000428629 | 19-385 | Cell wall mannoprotein PIR1 | |||
Sequence: ATVPDEHYSTLSPSAKIPSGASTDFSGTFGIQVVTVESASALSTDTATSTLTRNDNKKEATPVAQITDGQVQHQTTGGVSAIKQISDGQVQHQTNAAQPIAQISDGQIQHQTTAKATATPVQQINDGQIQHQTTVQPVAQISDGQIQHQTAKATATPVQQIGDGQIQHQTTVQPVAQISDGQIQHQTVKASATPVQQIGDGQIQHQTTAAAATTASAVKQINDGQIQHQTTTAENVAKAQSDGQAIATGSPSSNSTLSDDDDLSSTIPKACSSANNLEMTLHDSVLKDTHERWGAIVANHQFQFDGPIPQAGTIYSAGWSIKDGYLYLGDSNIFYQCLSGDFYNLYDENVAKQCSAVKLSVIEFVNC | ||||||
Glycosylation | 272 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Post-translational modification
Covalently linked to beta-1,3-glucan of the inner cell wall layer via an alkali-sensitive ester linkage between the gamma-carboxyl group of glutamic acids, arising from specific glutamines within the PIR1/2/3 repeats, and hydroxyl groups of glucoses of beta-1,3-glucan chains.
Highly O-glycosylated by PMT1 and contains one N-mannosylated chain.
Keywords
- PTM
PTM databases
Expression
Induction
Expression varies during the cell-cycle with a peak at the beginning of G1. Expression increases in hypoxic and acidic conditions and is down-regulated during the switch from yeast to hyphal growth and under low-iron conditions. The promoter contains E-box consensus sequences (CANNTG) suggesting that PIR1 is directly regulated by EFG1. Expression is also regulated by ACE2, HOG1, and RIM101.
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for repeat, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Repeat | 78-96 | PIR1/2/3 1 | ||||
Sequence: ATPVAQITDGQVQHQTTGG | ||||||
Repeat | 97-115 | PIR1/2/3 2 | ||||
Sequence: VSAIKQISDGQVQHQTNAA | ||||||
Repeat | 116-133 | PIR1/2/3 3 | ||||
Sequence: QPIAQISDGQIQHQTTAK | ||||||
Repeat | 136-153 | PIR1/2/3 4 | ||||
Sequence: ATPVQQINDGQIQHQTTV | ||||||
Repeat | 154-171 | PIR1/2/3 5 | ||||
Sequence: QPVAQISDGQIQHQTAKA | ||||||
Repeat | 173-190 | PIR1/2/3 6 | ||||
Sequence: ATPVQQIGDGQIQHQTTV | ||||||
Repeat | 191-208 | PIR1/2/3 7 | ||||
Sequence: QPVAQISDGQIQHQTVKA | ||||||
Repeat | 210-228 | PIR1/2/3 8 | ||||
Sequence: ATPVQQIGDGQIQHQTTAA | ||||||
Repeat | 233-251 | PIR1/2/3 9 | ||||
Sequence: ASAVKQINDGQIQHQTTTA | ||||||
Region | 257-282 | Disordered | ||||
Sequence: AQSDGQAIATGSPSSNSTLSDDDDLS |
Domain
The PIR1/2/3 repeats are required for covalent linkage to the cell wall.
Sequence similarities
Belongs to the PIR protein family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length385
- Mass (Da)40,621
- Last updated2017-03-15 v2
- Checksum2A24722AFC101884
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP017624 EMBL· GenBank· DDBJ | AOW27875.1 EMBL· GenBank· DDBJ | Genomic DNA |