C7F6X3 · IBP_LEUSY
- ProteinIce-binding protein
- GeneAFP
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids261 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Confers freeze tolerance. Binds to the surface of ice crystals and inhibits their growth. Has low thermal hysteresis (TH) activity, which is the ability to lower the freezing point of an aqueous solution below its melting point (PubMed:20067781, PubMed:22303017, PubMed:22426061, PubMed:22622645, PubMed:23203635, PubMed:24699650).
The TH activity of this protein is approximately 0.2 degrees Celsius at 50 uM and 0.3 degrees Celsius at 400 uM (PubMed:24699650).
The TH activity of this protein is approximately 0.2 degrees Celsius at 50 uM and 0.3 degrees Celsius at 400 uM (PubMed:24699650).
Biotechnology
Improves cryopreservation of the human red blood cells (RBCs). Almost 90 % hemolysis damage induced to RBCs by freeze thawing with the slow warming at 22 degrees Celsius is dramatically decreased to less than 16 % when 0.4 or 0.8 mg/ml of this protein is used as a cryoprotectant. The post-thaw cell counts of RBCs frozen in the presence of 0.8 mg/ml of this protein and thawed by slow warming at 22 degrees Celsius is almost the same as that of non-frozen intact RBCs, whereas the recovery of RBCs frozen in its absence is less than 30 %.
Features
Showing features for site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 65 | Ice-binding | ||||
Sequence: T | ||||||
Site | 147 | Ice-binding | ||||
Sequence: S | ||||||
Site | 234 | Ice-binding | ||||
Sequence: A |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | extracellular region | |
Molecular Function | ice binding |
Keywords
- Molecular function
- Biological process
Names & Taxonomy
Protein names
- Recommended nameIce-binding protein
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Basidiomycota > Pucciniomycotina > Microbotryomycetes > Leucosporidiales > Leucosporidium
Accessions
- Primary accessionC7F6X3
Subcellular Location
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 43 | Has 35% thermal hysteresis (TH) activity of that of the wild-type. | ||||
Sequence: S → Y | ||||||
Mutagenesis | 49 | Has 89% thermal hysteresis (TH) activity of that of the wild-type. | ||||
Sequence: A → Y | ||||||
Mutagenesis | 65 | Has 28% thermal hysteresis (TH) activity of that of the wild-type. | ||||
Sequence: T → Y | ||||||
Mutagenesis | 109 | Has 92% thermal hysteresis (TH) activity of that of the wild-type. | ||||
Sequence: T → Y | ||||||
Mutagenesis | 147 | Has 62% thermal hysteresis (TH) activity of that of the wild-type. Loss of TH activity; when associated with Y-234. | ||||
Sequence: S → Y | ||||||
Mutagenesis | 171 | Has 67% thermal hysteresis (TH) activity of that of the wild-type. | ||||
Sequence: S → Y | ||||||
Mutagenesis | 198 | Has 50% thermal hysteresis (TH) activity of that of the wild-type. | ||||
Sequence: T → Y | ||||||
Mutagenesis | 216 | Has 59% thermal hysteresis (TH) activity of that of the wild-type. | ||||
Sequence: T → Y | ||||||
Mutagenesis | 222 | Has 64% thermal hysteresis (TH) activity of that of the wild-type. | ||||
Sequence: S → Y | ||||||
Mutagenesis | 234 | Has 47% thermal hysteresis (TH) activity of that of the wild-type. Loss of TH activity; when associated with Y-147. | ||||
Sequence: A → Y | ||||||
Mutagenesis | 239 | No effect on thermal hysteresis (TH) activity. | ||||
Sequence: T → Y | ||||||
Mutagenesis | 244-261 | Has 13% higher thermal hysteresis (TH) activity compared to the wild-type. Loss of homodimerization. | ||||
Sequence: Missing |
PTM/Processing
Features
Showing features for signal, chain, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-20 | |||||
Sequence: MSLLSIITIGLAGLGGLVNG | ||||||
Chain | PRO_5011088933 | 21-261 | Ice-binding protein | |||
Sequence: QRDLSVELGVASNFAILAKAGISSVPDSAILGDIGVSPAAATYITGFGLTQDSSTTYATSPQVTGLIYAADYSTPTPNYLAAAVANAETAYNQAAGFVDPDFLELGAGELRDQTLVPGLYKWTSSVSVPTDLTFEGNGDATWVFQIAGGLSLADGVAFTLAGGANSTNIAFQVGDDVTVGKGAHFEGVLLAKRFVTLQTGSSLNGRVLSQTEVALQKATVNSPFVPAPEVVQKRSNARQWL | ||||||
Glycosylation | 185 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Post-translational modification
Glycosylated (PubMed:20067781, PubMed:22303017, PubMed:22426061, PubMed:23203635).
Glycosylation is not required for the thermal hysteresis (TH) activity (PubMed:22426061).
Glycosylation may increase stability and secretion of this protein (Probable)
Glycosylation is not required for the thermal hysteresis (TH) activity (PubMed:22426061).
Glycosylation may increase stability and secretion of this protein (Probable)
Keywords
- PTM
PTM databases
Structure
Family & Domains
Sequence similarities
Belongs to the ice-binding protein family.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length261
- Mass (Da)26,807
- Last updated2009-09-22 v1
- ChecksumF114BC33CBC9B469
Mass Spectrometry
Keywords
- Technical term