UniProt functional annotation for C7F6X3



	UniProt functional annotation for C7F6X3

UniProt code: C7F6X3.

Organism: Leucosporidium sp. (strain AY30) (Arctic yeast).

Taxonomy: Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina; Microbotryomycetes; Leucosporidiales; Leucosporidium; unclassified Leucosporidium.

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:24699650, PubMed:22303017, PubMed:20067781, PubMed:22426061, PubMed:23203635, PubMed:22622645). 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). {ECO:0000269|PubMed:20067781, ECO:0000269|PubMed:22303017, ECO:0000269|PubMed:22426061, ECO:0000269|PubMed:22622645, ECO:0000269|PubMed:23203635, ECO:0000269|PubMed:24699650}.

Subunit: Homodimer (PubMed:22426061, PubMed:24699650, PubMed:22303017). Dimerization is not required for the thermal hysteresis (TH) activity (PubMed:22303017). {ECO:0000269|PubMed:22303017, ECO:0000269|PubMed:22426061, ECO:0000269|PubMed:24699650}.

Subcellular location: Secreted {ECO:0000269|PubMed:20067781, ECO:0000269|PubMed:22426061, ECO:0000269|PubMed:23203635}.

Ptm: Glycosylated (PubMed:20067781, PubMed:22426061, PubMed:22303017, PubMed:23203635). Glycosylation is not required for the thermal hysteresis (TH) activity (PubMed:22426061). Glycosylation may increase stability and secretion of this protein (Probable). {ECO:0000269|PubMed:20067781, ECO:0000269|PubMed:22303017, ECO:0000269|PubMed:22426061, ECO:0000269|PubMed:23203635, ECO:0000305|PubMed:22303017}.

Mass spectrometry: Mass=25565; Method=MALDI; Note=The measured mass is that of the mature protein.; Evidence={ECO:0000269|PubMed:23203635};

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 %. {ECO:0000269|PubMed:22622645}.

Similarity: Belongs to the ice-binding protein family. {ECO:0000305}.

Annotations taken from UniProtKB at the EBI.


Organism:		Leucosporidium sp. (strain AY30) (Arctic yeast).
Taxonomy:		Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina; Microbotryomycetes; Leucosporidiales; Leucosporidium; unclassified Leucosporidium.



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:24699650, PubMed:22303017, PubMed:20067781, PubMed:22426061, PubMed:23203635, PubMed:22622645). 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). {ECO:0000269\|PubMed:20067781, ECO:0000269\|PubMed:22303017, ECO:0000269\|PubMed:22426061, ECO:0000269\|PubMed:22622645, ECO:0000269\|PubMed:23203635, ECO:0000269\|PubMed:24699650}.


Subunit:		Homodimer (PubMed:22426061, PubMed:24699650, PubMed:22303017). Dimerization is not required for the thermal hysteresis (TH) activity (PubMed:22303017). {ECO:0000269\|PubMed:22303017, ECO:0000269\|PubMed:22426061, ECO:0000269\|PubMed:24699650}.
Subcellular location:		Secreted {ECO:0000269\|PubMed:20067781, ECO:0000269\|PubMed:22426061, ECO:0000269\|PubMed:23203635}.
Ptm:		Glycosylated (PubMed:20067781, PubMed:22426061, PubMed:22303017, PubMed:23203635). Glycosylation is not required for the thermal hysteresis (TH) activity (PubMed:22426061). Glycosylation may increase stability and secretion of this protein (Probable). {ECO:0000269\|PubMed:20067781, ECO:0000269\|PubMed:22303017, ECO:0000269\|PubMed:22426061, ECO:0000269\|PubMed:23203635, ECO:0000305\|PubMed:22303017}.
Mass spectrometry:		Mass=25565; Method=MALDI; Note=The measured mass is that of the mature protein.; Evidence={ECO:0000269\|PubMed:23203635};
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 %. {ECO:0000269\|PubMed:22622645}.
Similarity:		Belongs to the ice-binding protein family. {ECO:0000305}.