| General information | | DisProt: | DP00329 | | Name: | Beta-casein | | Synonym(s): | CASB_BOVIN
Casoparan [cleavage product 1]
Antioxidant peptide [cleavage product 2]
Casohypotensin [cleavage product 3]
| | First appeared in release: | Release 3.0 (02/17/2006) | | UniProt: | P02666 | | UniGene: | Bt.53272 | | SwissProt: | CASB_BOVIN | | TrEMBL: | | | NCBI (GI): | 115660 | | Source organism: | Bos taurus (Bovine) | | Sequence length: | 224 | | Percent disordered: | 100% | | Homologues: | |
| Native sequence |
10 20 30 40 50 60
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MKVLILACLV ALALARELEE LNVPGEIVES LSSSEESITR INKKIEKFQS EEQQQTEDEL - 60
QDKIHPFAQT QSLVYPFPGP IPNSLPQNIP PLTQTPVVVP PFLQPEVMGV SKVKEAMAPK - 120
HKEMPFPKYP VEPFTESQSL TLTDVENLHL PLPLLQSWMH QPHQPLPPTV MFPPQSVLSL - 180
SQSKVLPVPQ KAVPYPQRDM PIQAFLLYQE PVLGPVRGPF PIIV
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| Functional narrative |
Important role in determination of the surface properties of the casein micelles. Casoparan (residues 41 - 45) acts as a macrophage activator, increasing the phagocytic activity of macrophages and peroxide release from macrophages. It also acts as a bradykinin-potentiating peptide. Casohypotensin (residues 129 - 136) acts as a bradykinin-potentiating peptide. Induces hypotension in rats. Acts as a strong competitive inhibitor of endo-oligopeptidase A. Antioxidant peptide (residues 113 - 120) has antioxidant 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 - 25 | | Length: | 25 | | Region sequence: |
MKVLILACLVALALARELEELNVPG | | Modification type: | Fragment
| | PDB: | | | Structural/functional type: | | | Functional classes: | | | Functional subclasses: | | Detection methods:
- Nuclear magnetic resonance (NMR) (278 K; pH: 6; 1H2O/2H2O (90:10) 0.45 ml; beta-CN (1-25) (protein) 6 mg)
- Nuclear magnetic resonance (NMR) (278 K; pH: 6; 2H2O 0.45 ml; beta-CN (1-25) (protein) 6 mg)
| References:
- Wahlgren NM, Leonil J, Dejmek P, Drakenberg T. "Two-dimensional nuclear magnetic resonance study of the beta-casein peptide 1-25: resonance assignments and secondary structure." Biochim Biophys Acta. 1993; 1202(1): 121-8. PubMed: 8373815
| Comments:
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| Region 2 | | Type: | Disordered | | Name: | | | Location: | 1 - 224 | | Length: | 224 | | Region sequence: |
MKVLILACLVALALARELEELNVPGEIVESLSSSEESITRINKKIEKFQSEEQQQTEDEL
QDKIHPFAQTQSLVYPFPGPIPNSLPQNIPPLTQTPVVVPPFLQPEVMGVSKVKEAMAPK
HKEMPFPKYPVEPFTESQSLTLTDVENLHLPLPLLQSWMHQPHQPLPPTVMFPPQSVLSL
SQSKVLPVPQKAVPYPQRDMPIQAFLLYQEPVLGPVRGPFPIIV | | Modification type: | | | PDB: | | | Structural/functional type: | | | Functional classes: | | | Functional subclasses: | | Detection methods:
- Circular dichroism (CD) spectroscopy, far-UV (guanidine-HCl 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 |
- 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.
- Yong YH, Foegeding EA. "Caseins: Utilizing Molecular Chaperone Properties to Control Protein Aggregation in Foods." J Agric Food Chem. 2009. PubMed: 20025277
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| Comments |
For disorder region 2, there is some evidence of secondary structure throughout. This needs to be looked at more carefully because different papers report different areas of secondary structure. Also, since the disorder appears in the cleavage products, separate entries may need to be created for these as well.
Cleavage products will be added after the locations of secondary structure are figured out.
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