{"results":[{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"P0DYC7","uniProtkbId":"ICEN_ENTPA","entryAudit":{"firstPublicDate":"2026-09-02","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2026-09-02","entryVersion":2,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Entomortierella parvispora","commonName":"Mortierella parvispora","taxonId":205924,"lineage":["Eukaryota","Fungi","Fungi incertae sedis","Mortierellomycota","Mortierellomycotina","Mortierellomycetes","Mortierellales","Mortierellaceae","Entomortierella"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"41811943"}],"value":"Ice-nucleating protein"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"41811943"}],"value":"INpro"}]}},"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"41811943"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"41811943"}],"value":"Fungal ice-nucleating protein (INpro) that catalyzes ice formation at high subzero temperature through a nonmembrane-bound mechanism (PubMed:41811943). Pure water can supercool (stay liquid below 0 degrees Celsius) unless something triggers ice formation. INpros act as that trigger, allowing ice to form at relatively warmer subzero temperatures (like -2 to -5 degrees Celsius instead of -15 degrees Celsius or lower) (PubMed:41811943). Controlled ice formation outside the cell prevents sudden intracellular ice formation which is lethal (Probable). Multimerization enables high fungal ice nucleation activity and the freezing modes that exhibit lower nucleation efficiency (-7.5 degrees Celsius) originate from INpro homotrimers, whereas the more efficient ice-nucleating structures (-6.5 degrees Celsius) correspond to INpro homotetramers. The highest freezing mode -5.6 degrees Celsius can be attributed to the formation of INpro pentamers (PubMed:41811943). Exhibits extraordinary stability and potency, functioning at picomolar concentrations and under extreme conditions, retaining ice nucleation activity at pH 2 and pH 12 (PubMed:41811943)"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"41811943"}],"value":"Multimerizes to form homodimers, homotrimers, homotetramers and homopentamers (PubMed:41811943). Homodimer formation is mediated by stacking of tyrosine ladders between adjacent monomers (PubMed:41811943). The homotrimer, homotetramer and homopentamer formation are likely enabled by electrostatic interactions between the outward-facing positively and negatively charged residues located on opposing ends of the beta-solenoids (PubMed:41811943)"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"41811943"}],"value":"Secreted","id":"SL-0243"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"41811943"}],"value":"Contains 19 imperfect repeats of a consensus octapeptide A-G-Y-G-S-T-L-T (By similarity). Predicted to adopt beta-solenoid folds and multimerize to form extended ice-binding surfaces (PubMed:41811943)"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"41811943"}],"value":"The discovery of cell-free fungal INpros provides tools for innovative freezing applications and reveals biophysical constraints on ice nucleation across life (PubMed:41811943). Their membrane independence and solubility clearly distinguish them from bacterial INpros and could unlock possibilities for bioinspired freezing technologies, from precision cryopreservation to engineered weather modulation (PubMed:41811943). The fungal INpros' ability to remain highly active at low concentrations and under harsh conditions may allow them to retain function if aerosolized (PubMed:41811943)"}],"commentType":"BIOTECHNOLOGY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"41811943"}],"value":"The fungal INpros are encoded by orthologs of the bacterial InaZ gene, which was likely acquired by a fungal ancestor through horizontal gene transfer. Size characterization experiments suggest that fungal INpros are smaller than bacterial INpros and nucleate ice through a fundamentally distinct, nonmembrane-bound mechanism"}],"commentType":"MISCELLANEOUS"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the bacterial ice nucleation protein family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":809,"modifier":"EXACT"}},"description":"Ice-nucleating protein","featureId":"PRO_0000464659"},{"type":"Repeat","location":{"start":{"value":227,"modifier":"EXACT"},"end":{"value":234,"modifier":"EXACT"}},"description":"Ice nucleation 1","evidences":[{"evidenceCode":"ECO:0000255"}]},{"type":"Repeat","location":{"start":{"value":259,"modifier":"EXACT"},"end":{"value":266,"modifier":"EXACT"}},"description":"Ice nucleation 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The CPSase-function is accomplished in 2 steps, by a glutamine-dependent amidotransferase activity (GATase) that binds and cleaves glutamine to produce ammonia, followed by an ammonium-dependent carbamoyl phosphate synthetase, which reacts with the ammonia, hydrogencarbonate and ATP to form carbamoyl phosphate. The endogenously produced carbamoyl phosphate is sequestered and channeled to the ATCase active site. 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The autoendoproteolytic cleavage occurs by a canonical serine protease mechanism, in which the side chain hydroxyl group of the serine supplies its oxygen atom to form the C-terminus of the beta chain, while the remainder of the serine residue undergoes an oxidative deamination to produce ammonia and the pyruvoyl prosthetic group on the alpha chain. During this reaction, the Ser that is part of the protease active site of the proenzyme becomes the pyruvoyl prosthetic group, which constitutes an essential element of the active site of the mature decarboxylase"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03209"}],"value":"Belongs to the phosphatidylserine decarboxylase family. PSD-B subfamily. 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