1. SS-3 is a 33-amino-acid polypeptide. It has 45% α-helical content and relatively weak antifreeze activity (thermal hysteresis of -0.39°C at 10 mg/ml).
2. It contains 11-amino-acid repeat sequences and is structurally homologous to winter flounder AFP (around 60% homology).
AFP011005
General Information
| Protein Name | Ice-structuring protein SS-3 |
| UniProt ID | P04367 |
| Protein Sequence ID in NCBI | AAB36455.1 |
| Species | Myoxocephalus scorpius (Shorthorn sculpin) (Cottus scorpius) |
| Sequence Length | 33 |
| Sequence | |
| Structure | PDB ID: 1y03 |
| Solvent Accessible Surface Area | Total SASA | 2127.15 Ų | Polar SASA | 956.66 Ų | Apolar SASA | 3083.81 Ų |
AFP011005000
| Mutation | Wild Type |
| Sequence |
Thermal Hysteresis
| PMID | 4029130 |
| DOI | 10.1111/j.1432-1033.1985.tb09081.x |
| Protein Name | shorthorn sculpin AFP SS-3 |
| Thermal Hysteresis | Tab.2 Properties of sculpin and flounder AFP, and the cleavage peptides of sculpin AFP. |
Thermal Hysteresis
| PMID | 11940576 |
| DOI | 10.1074/jbc.M200307200 |
| Protein Name | shorthorn sculpin AFP sSS3 |
| Thermal Hysteresis | Tab.1 Polypeptide sequences and Hysteresis. |
Brief description
|
PMID: 4029130
DOI: 10.1111/j.1432-1033.1985.tb09081.x |
|
|
PMID: 11940576
DOI: 10.1074/jbc.M200307200 |
1. Unmodified sSS3 and rSS3 can cause faceting of ice crystals, but have very low thermal hysteresis activity; the acetylated derivative 4Ac-rSS3 can not only cause ice crystal faceting but also has significant thermal hysteresis activity.
2. All type I antifreeze proteins contain a common hydrophobic face, which is required for antifreeze activity, and the N-terminal group plays an important role in its antifreeze activity. |
AFP011005001
| Mutation | 0_1insGS |
| Sequence |
Ice crystal morphology
| PMID | 11940576 |
| DOI | 10.1074/jbc.M200307200 |
| Protein Name | shorthorn sculpin AFP rSS3 |
| Ice crystal morphology | Fig.6.A Ice crystal morphology. Single ice crystals grown in the presence of solutions of (a) rSS3 (18 mg/mL) and (b) 4Ac-rSS3 (16 mg/mL). The long axis of each crystal is ~50 μm. |
Ice crystal morphology
| PMID | 11940576 |
| DOI | 10.1074/jbc.M200307200 |
| Protein Name | shorthorn sculpin AFP 4Ac-rSS3 |
| PTM | Chemical modification: rSS3 was acetylated at the N-terminus and Lys-10, Lys-20, and Lys-21 to yield 4Ac-rSS3. |
| Ice crystal morphology | Fig.6.A Ice crystal morphology. Single ice crystals grown in the presence of solutions of (a) rSS3 (18 mg/mL) and (b) 4Ac-rSS3 (16 mg/mL). The long axis of each crystal is ~50 μm. |
Thermal Hysteresis
| PMID | 11940576 |
| DOI | 10.1074/jbc.M200307200 |
| Protein Name | shorthorn sculpin AFP rSS3 |
| Thermal Hysteresis | Tab.1 Polypeptide sequences and Hysteresis. |
Thermal Hysteresis
| PMID | 11940576 |
| DOI | 10.1074/jbc.M200307200 |
| Protein Name | shorthorn sculpin AFP 4Ac-rSS3 |
| PTM | Chemical modification: rSS3 was acetylated at the N-terminus and Lys-10, Lys-20, and Lys-21 to yield 4Ac-rSS3. |
| Thermal Hysteresis | Tab.1 Polypeptide sequences and Hysteresis. |
Brief description
|
PMID: 11940576
DOI: 10.1074/jbc.M200307200 |
1. Unmodified sSS3 and rSS3 can cause faceting of ice crystals, but have very low thermal hysteresis activity; the acetylated derivative 4Ac-rSS3 can not only cause ice crystal faceting but also has significant thermal hysteresis activity.
2. All type I antifreeze proteins contain a common hydrophobic face, which is required for antifreeze activity, and the N-terminal group plays an important role in its antifreeze activity. |