| General information | | DisProt: | DP00192 | | Name: | Kappa-casein | | Synonym(s): | CASK_BOVIN
Casoxin-C [cleavage product 1]
Casoxin-6 [cleavage product 2]
Casoxin-A [cleavage product 3]
Casoxin-B [cleavage product 4]
Casoplatelin [cleavage product 5]
| | First appeared in release: | Release 2.1 (03/14/2005) | | UniProt: | P02668 | | UniGene: | Bt.49421 | | SwissProt: | CASK_BOVIN | | TrEMBL: | | | NCBI (GI): | 115667 | | Source organism: | Bos taurus (Bovine) | | Sequence length: | 190 | | Percent disordered: | 96% | | Homologues: | |
| Native sequence |
10 20 30 40 50 60
| | | | | |
MMKSFFLVVT ILALTLPFLG AQEQNQEQPI RCEKDERFFS DKIAKYIPIQ YVLSRYPSYG - 60
LNYYQQKPVA LINNQFLPYP YYAKPAAVRS PAQILQWQVL SNTVPAKSCQ AQPTTMARHP - 120
HPHLSFMAIP PKKNQDKTEI PTINTIASGE PTSTPTTEAV ESTVATLEDS PEVIESPPEI - 180
NTVQVTSTAV
|
| Functional narrative |
Kappa-casein stabilizes micelle formation, preventing casein precipitation in milk. Casoxins A, B and C have opioid antagonist activity. Casoxin C causes biphasic ileal contractions through the binding to the complement C3a receptors. Casoplatelin inhibits platelet aggregation.
|
| 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.
|
| Region 1 | | Type: | Disordered | | Name: | | | Location: | 1 - 182 | | Length: | 182 | | Region sequence: |
MMKSFFLVVTILALTLPFLGAQEQNQEQPIRCEKDERFFSDKIAKYIPIQYVLSRYPSYG
LNYYQQKPVALINNQFLPYPYYAKPAAVRSPAQILQWQVLSNTVPAKSCQAQPTTMARHP
HPHLSFMAIPPKKNQDKTEIPTINTIASGEPTSTPTTEAVESTVATLEDSPEVIESPPEI
NT | | Modification type: | Native
| | PDB: | | | Structural/functional type: | Relationship to function unknown
| | Functional classes: | Molecular assembly
| | Functional subclasses: | Unknown
| Detection methods:
- Raman optical activity
- Stability at thermal extremes
| References:
- Syme CD, Blanch EW, Holt C, Jakes R, Goedert M, Hecht L, Barron LD. "A Raman optical activity study of rheomorphism in caseins, synucleins and tau. New insight into the structure and behaviour of natively unfolded proteins." Eur J Biochem. 2002; 269(1): 148-56. PubMed: 11784308
| Comments:
|
| Region 2 | | Type: | Disordered | | Name: | | | Location: | 125 - 129 | | Length: | 5 | | Region sequence: |
SFMAI | | Modification type: | Fragment
| | PDB: | | | Structural/functional type: | Relationship to function unknown
| | Functional classes: | Unknown
| | Functional subclasses: | Unknown
| Detection methods:
- Circular dichroism (CD) spectroscopy, far-UV (295 K; sodium dodecyl sulfate 0.9 mM)
| References:
- Raap J, Kerling KE, Vreeman HJ, Visser S. "Peptide substrates for chymosin (rennin): conformational studies of kappa-casein and some kappa-casein-related oligopeptides by circular dichroism and secondary structure prediction." Arch Biochem Biophys. 1983; 221(1): 117-24. PubMed: 6402987
| Comments:
|
| Region 3 | | Type: | Disordered | | Name: | | | Location: | 124 - 128 | | Length: | 5 | | Region sequence: |
LSFMA | | Modification type: | Fragment
| | PDB: | | | Structural/functional type: | Relationship to function unknown
| | Functional classes: | Unknown
| | Functional subclasses: | Unknown
| Detection methods:
- Circular dichroism (CD) spectroscopy, far-UV (295 K; sodium dodecyl sulfate 0.9 mM)
| References:
- Raap J, Kerling KE, Vreeman HJ, Visser S. "Peptide substrates for chymosin (rennin): conformational studies of kappa-casein and some kappa-casein-related oligopeptides by circular dichroism and secondary structure prediction." Arch Biochem Biophys. 1983; 221(1): 117-24. PubMed: 6402987
| Comments:
|
| Region 4 | | Type: | Disordered | | Name: | | | Location: | 124 - 129 | | Length: | 6 | | Region sequence: |
LSFMAI | | Modification type: | Fragment
| | PDB: | | | Structural/functional type: | Relationship to function unknown
| | Functional classes: | Unknown
| | Functional subclasses: | Unknown
| Detection methods:
- Circular dichroism (CD) spectroscopy, far-UV (295 K; sodium dodecyl sulfate 0.9 mM)
| References:
- Raap J, Kerling KE, Vreeman HJ, Visser S. "Peptide substrates for chymosin (rennin): conformational studies of kappa-casein and some kappa-casein-related oligopeptides by circular dichroism and secondary structure prediction." Arch Biochem Biophys. 1983; 221(1): 117-24. PubMed: 6402987
| Comments:
|
| Region 5 | | Type: | Disordered | | Name: | | | Location: | 124 - 130 | | Length: | 7 | | Region sequence: |
LSFMAIP | | Modification type: | Fragment
| | PDB: | | | Structural/functional type: | Relationship to function unknown
| | Functional classes: | Unknown
| | Functional subclasses: | Unknown
| Detection methods:
- Circular dichroism (CD) spectroscopy, far-UV (295 K; sodium dodecyl sulfate 0.9 mM)
| References:
- Raap J, Kerling KE, Vreeman HJ, Visser S. "Peptide substrates for chymosin (rennin): conformational studies of kappa-casein and some kappa-casein-related oligopeptides by circular dichroism and secondary structure prediction." Arch Biochem Biophys. 1983; 221(1): 117-24. PubMed: 6402987
| Comments:
|
| 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.
|
| Comments |
Disordered residues lie within the regions for cleavage products 1 - 5, however, there is no experimental evidence to show that these products are disordered.
|
| If you have any comments or wish to provide additional references to this protein or its disordered region(s), please click here to e-mail us. |
Disprot-footer
|
