| General information | | DisProt: | DP00330 | | Name: | Alpha-S1-casein | | Synonym(s): | CASA1_BOVIN
Antioxidant peptide [cleavage product 1]
| | First appeared in release: | Release 1.0 (08/01/2003) | | UniProt: | P02662 | | UniGene: | Bt.59369 | | SwissProt: | CASA1_BOVIN | | TrEMBL: | | | NCBI (GI): | 115646 | | Source organism: | Bos taurus (Bovine) | | Sequence length: | 214 | | Percent disordered: | 100% | | Homologues: | |
| Native sequence |
10 20 30 40 50 60
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MKLLILTCLV AVALARPKHP IKHQGLPQEV LNENLLRFFV APFPEVFGKE KVNELSKDIG - 60
SESTEDQAME DIKQMEAESI SSSEEIVPNS VEQKHIQKED VPSERYLGYL EQLLRLKKYK - 120
VPQLEIVPNS AEERLHSMKE GIHAQQKEPM IGVNQELAYF YPELFRQFYQ LDAYPSGAWY - 180
YVPLGTQYTD APSFSDIPNP IGSENSEKTT MPLW
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| Functional narrative |
Important role in the capacity of milk to transport calcium phosphate. Antioxidant peptide has 2,2-diphenyl-1-picrylhydrazyl (DPPH) radical scavenging activity.
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| Map of ordered and disordered regions |
Note: 'Mouse' over a region to see the start and stop residues. Click on a region to see detailed information.
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| Region 1 | | Type: | Disordered | | Name: | | | Location: | 1 - 214 | | Length: | 214 | | Region sequence: |
MKLLILTCLVAVALARPKHPIKHQGLPQEVLNENLLRFFVAPFPEVFGKEKVNELSKDIG
SESTEDQAMEDIKQMEAESISSSEEIVPNSVEQKHIQKEDVPSERYLGYLEQLLRLKKYK
VPQLEIVPNSAEERLHSMKEGIHAQQKEPMIGVNQELAYFYPELFRQFYQLDAYPSGAWY
YVPLGTQYTDAPSFSDIPNPIGSENSEKTTMPLW | | Modification type: | | | PDB: | | | Structural/functional type: | Relationship to function unknown
| | Functional classes: | Unknown
| | Functional subclasses: | Unknown
| Detection methods:
- Circular dichroism (CD) spectroscopy, far-UV (GuHCl 4.5 M)
| References:
- Creamer LK, Richardson T, Parry DA. "Secondary structure of bovine alpha s1- and beta-casein in solution." Arch Biochem Biophys. 1981; 211(2): 689-96. PubMed: 7305393
| Comments:
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| References |
- Bhattacharyya J, Das KP. "Molecular chaperone-like properties of an unfolded protein, alpha(s)-casein." J Biol Chem. 1999; 274(22): 15505-9. PubMed: 10336443
- Holt C, Sawyer L. "Caseins as Rheomorphic Proteins: Interpretation of Primary and Secondary Structures of the alpha s1-, beta, and kappa caseins." J Chem Soc Faraday Trans. 1993; 89(15): 2683-92.
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| Comments |
Disordered residues lie within the region corresponding to the antioxidant peptide, however, there are no references to confirm that this cleavage product is disordered.
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