G1UB63 · CSA1_CANAL
- ProteinCell wall protein 1
- GeneCSA1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids1018 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Heme-binding protein involved in heme-iron utilization. The ability to acquire iron from host tissues is a major virulence factor of pathogenic microorganisms. Required for biofilm formation.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 78 | Fe (UniProtKB | ChEBI) of heme (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: D | ||||||
Binding site | 269 | Fe (UniProtKB | ChEBI) of heme (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: D | ||||||
Binding site | 439 | Fe (UniProtKB | ChEBI) of heme (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: D | ||||||
Binding site | 601 | Fe (UniProtKB | ChEBI) of heme (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: D |
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 | cell surface | |
Cellular Component | cellular bud | |
Cellular Component | extracellular region | |
Cellular Component | fungal-type cell wall | |
Cellular Component | hyphal cell wall | |
Cellular Component | plasma membrane | |
Cellular Component | side of membrane | |
Molecular Function | heme binding | |
Molecular Function | metal ion binding | |
Biological Process | intracellular iron ion homeostasis | |
Biological Process | single-species biofilm formation on inanimate substrate |
Keywords
- Biological process
- Ligand
Names & Taxonomy
Protein names
- Recommended nameCell wall protein 1
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Saccharomycotina > Saccharomycetes > Saccharomycetales > Debaryomycetaceae > Candida/Lodderomyces clade > Candida
Accessions
- Primary accessionG1UB63
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
PTM/Processing
Features
Showing features for signal, chain, disulfide bond, glycosylation, lipidation, propeptide.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-17 | |||||
Sequence: MLPSIVISIVLASFVSA | ||||||
Chain | PRO_0000424777 | 18-989 | Cell wall protein 1 | |||
Sequence: ESSITEAPTTTAEDNPYTIYPSVAKTASINGFADRIYDQLPECAKPCMFQNTGVTPCPYWDTGCLCIMPTFAGAIGSCIAEKCKGQDVVSATSLGTSICSVAGVWDPYWMVPANVQSSLSAAATAVASSSEQPVETSSEPAGSSQSVESSQPAETSSSEPAETSSSEPAETSSETSSEQPASSEPAETSSEESSTITSAPSTPEDNPYTIYPSVAKTASINGFADRIYDQLPECAKPCMFQNTGVTPCPYWDTGCLCIMPTFAGAIGSCIAEKCKGQDVVSATSLGTSICSVAGVWDPYWMVPANVQSSLSAAATAVPSSSEQSVETSSESAESSQSVESSQPAETSSEQPSETSSETSSQQLSSITSAPDSSATSSSSTTSTFIRTASINGFADKLYDQLPECAKPCMFQNTGITPCPYWDAGCLCVMPQFAGAIGSCVADSCKGQDIVSVTSLGTSVCSVAGVNAPYWMLPASVKSSLSVAATAVPTSDSASETASQEPSETSSEQPSETASQQPAETSSEESSTITSAPSTPEDNPYTIYPSVAKTASINGFADRIYDQLPECAKPCMFQNTGVTPCPYWDTGCLCIMPTFAGAIGSCIAEKCKGQDVVSATSLGSSICSVAGVWDPYWMLPANVQSSLNAAATAVATSDSASEVASASESASQVPQETSAASSQSANNSVASAAPSNSSVSAAPSSNSSGVPAAPSNNSSGASVVPSQSANNSSASAAPSNNSSSAISESVAPSSYGNSTIAQPSTSTKSDAASITGPITTDKVITNESGIVFTSTVIITHVSEYCDQTSAAAVQSSACEEQSSAKSEQASASSEQVKVITSVVWCESSIQSIESVKTSAEAAHKTEVIASCASELSSLSSAKSEAMKTVSSLVEVQKSAVAKQTSLAAVQSSAASVQLSAAHAQKSSEAVEVAQTAVAEASKAGDEISTEIVNITKTVSSGKETGVSQATVAANTHS | ||||||
Disulfide bond | 60↔100 | |||||
Sequence: CAKPCMFQNTGVTPCPYWDTGCLCIMPTFAGAIGSCIAEKC | ||||||
Disulfide bond | 64↔95 | |||||
Sequence: CMFQNTGVTPCPYWDTGCLCIMPTFAGAIGSC | ||||||
Disulfide bond | 74↔81 | |||||
Sequence: CPYWDTGC | ||||||
Disulfide bond | 83↔116 | |||||
Sequence: CIMPTFAGAIGSCIAEKCKGQDVVSATSLGTSIC | ||||||
Disulfide bond | 251↔291 | |||||
Sequence: CAKPCMFQNTGVTPCPYWDTGCLCIMPTFAGAIGSCIAEKC | ||||||
Disulfide bond | 255↔286 | |||||
Sequence: CMFQNTGVTPCPYWDTGCLCIMPTFAGAIGSC | ||||||
Disulfide bond | 265↔272 | |||||
Sequence: CPYWDTGC | ||||||
Disulfide bond | 274↔307 | |||||
Sequence: CIMPTFAGAIGSCIAEKCKGQDVVSATSLGTSIC | ||||||
Disulfide bond | 421↔461 | |||||
Sequence: CAKPCMFQNTGITPCPYWDAGCLCVMPQFAGAIGSCVADSC | ||||||
Disulfide bond | 425↔456 | |||||
Sequence: CMFQNTGITPCPYWDAGCLCVMPQFAGAIGSC | ||||||
Disulfide bond | 435↔442 | |||||
Sequence: CPYWDAGC | ||||||
Disulfide bond | 444↔477 | |||||
Sequence: CVMPQFAGAIGSCVADSCKGQDIVSVTSLGTSVC | ||||||
Disulfide bond | 583↔623 | |||||
Sequence: CAKPCMFQNTGVTPCPYWDTGCLCIMPTFAGAIGSCIAEKC | ||||||
Disulfide bond | 587↔618 | |||||
Sequence: CMFQNTGVTPCPYWDTGCLCIMPTFAGAIGSC | ||||||
Disulfide bond | 597↔604 | |||||
Sequence: CPYWDTGC | ||||||
Disulfide bond | 606↔639 | |||||
Sequence: CIMPTFAGAIGSCIAEKCKGQDVVSATSLGSSIC | ||||||
Glycosylation | 698 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 708 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 718 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 729 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 743 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 753 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 769 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 798 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 965 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Lipidation | 989 | GPI-anchor amidated serine | ||||
Sequence: S | ||||||
Propeptide | PRO_0000424778 | 990-1018 | Removed in mature form | |||
Sequence: VAIANMANTKFASTMSLLVASFVFVGLFI |
Post-translational modification
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
PTM databases
Expression
Induction
Preferentially expressed during the mycelial growth phase with only low levels of transcript detected in the yeast form. Induced by iron starvation and ciclopirox. Positively regulated by BCR1 and RIM101, and repressed by TUP1. Expression is also regulated by EFG1, CPH1, HAP43, and SEF1.
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 32-143 | CFEM 1 | ||||
Sequence: NPYTIYPSVAKTASINGFADRIYDQLPECAKPCMFQNTGVTPCPYWDTGCLCIMPTFAGAIGSCIAEKCKGQDVVSATSLGTSICSVAGVWDPYWMVPANVQSSLSAAATAV | ||||||
Region | 147-227 | Disordered | ||||
Sequence: SEQPVETSSEPAGSSQSVESSQPAETSSSEPAETSSSEPAETSSETSSEQPASSEPAETSSEESSTITSAPSTPEDNPYTI | ||||||
Domain | 223-334 | CFEM 2 | ||||
Sequence: NPYTIYPSVAKTASINGFADRIYDQLPECAKPCMFQNTGVTPCPYWDTGCLCIMPTFAGAIGSCIAEKCKGQDVVSATSLGTSICSVAGVWDPYWMVPANVQSSLSAAATAV | ||||||
Region | 338-396 | Disordered | ||||
Sequence: SEQSVETSSESAESSQSVESSQPAETSSEQPSETSSETSSQQLSSITSAPDSSATSSSS | ||||||
Domain | 393-504 | CFEM 3 | ||||
Sequence: SSSSTTSTFIRTASINGFADKLYDQLPECAKPCMFQNTGITPCPYWDAGCLCVMPQFAGAIGSCVADSCKGQDIVSVTSLGTSVCSVAGVNAPYWMLPASVKSSLSVAATAV | ||||||
Region | 507-557 | Disordered | ||||
Sequence: SDSASETASQEPSETSSEQPSETASQQPAETSSEESSTITSAPSTPEDNPY | ||||||
Domain | 555-666 | CFEM 4 | ||||
Sequence: NPYTIYPSVAKTASINGFADRIYDQLPECAKPCMFQNTGVTPCPYWDTGCLCIMPTFAGAIGSCIAEKCKGQDVVSATSLGSSICSVAGVWDPYWMLPANVQSSLNAAATAV | ||||||
Region | 677-785 | Disordered | ||||
Sequence: SASESASQVPQETSAASSQSANNSVASAAPSNSSVSAAPSSNSSGVPAAPSNNSSGASVVPSQSANNSSASAAPSNNSSSAISESVAPSSYGNSTIAQPSTSTKSDAAS |
Domain
The CFEM domain is involved in heme-binding. It contains 8 cysteines and is found in proteins from several pathogenic fungi, including both human and plant pathogens.
Sequence similarities
Belongs to the RBT5 family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length1,018
- Mass (Da)103,515
- Last updated2011-10-19 v1
- ChecksumBA25AF72061A001A
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP017629 EMBL· GenBank· DDBJ | AOW30388.1 EMBL· GenBank· DDBJ | Genomic DNA |