| General information | | DisProt: | DP00199 | | Name: | Beta-casein | | Synonym(s): | CASB_HUMAN
| | First appeared in release: | Release 2.0 (02/14/2005) | | UniProt: | P05814 | | UniGene: | Hs.2242 | | SwissProt: | CASB_HUMAN | | TrEMBL: | | | NCBI (GI): | 115661 | | Source organism: | Homo sapiens (Human) | | Sequence length: | 226 | | Percent disordered: | 100% | | Homologues: | |
| Native sequence |
10 20 30 40 50 60
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MKVLILACLV ALALARETIE SLSSSEESIT EYKQKVEKVK HEDQQQGEDE HQDKIYPSFQ - 60
PQPLIYPFVE PIPYGFLPQN ILPLAQPAVV LPVPQPEIME VPKAKDTVYT KGRVMPVLKS - 120
PTIPFFDPQI PKLTDLENLH LPLPLLQPLM QQVPQPIPQT LALPPQPLWS VPQPKVLPIP - 180
QQVVPYPQRA VPVQALLLNQ ELLLNPTHQI YPVTQPLAPV HNPISV
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| Functional narrative |
Human beta-casein is the major protein found in human milk. The protein binds to calcium at its phosphorylated regions, which in turn are highly conserved. The calcium then binds the caseins together and forms micelles, which better enable it to be ingested by infants. It also has an opiod type effects on newborn sleeping patterns. The protein, as a whole, is disordered and is characterized as a random coil protein. This structure can be modified to some extent with an increase of temperature.
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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 - Extended | | Name: | | | Location: | 1 - 226 | | Length: | 226 | | Region sequence: |
MKVLILACLVALALARETIESLSSSEESITEYKQKVEKVKHEDQQQGEDEHQDKIYPSFQ
PQPLIYPFVEPIPYGFLPQNILPLAQPAVVLPVPQPEIMEVPKAKDTVYTKGRVMPVLKS
PTIPFFDPQIPKLTDLENLHLPLPLLQPLMQQVPQPIPQTLALPPQPLWSVPQPKVLPIP
QQVVPYPQRAVPVQALLLNQELLLNPTHQIYPVTQPLAPVHNPISV | | Modification type: | Native
| | PDB: | | | Structural/functional type: | Function arises from the disordered state
| | Functional classes: | Modification site
Molecular recognition scavengers
| | Functional subclasses: | Metal binding
Phosphorylation
| Detection methods:
- X-ray crystallography
- Circular dichroism (CD) spectroscopy, near-UV (298 K; pH: 7; protein (solution) 0.04 %)
- Circular dichroism (CD) spectroscopy, near-UV (283 K; pH: 7; protein (solution) 0.04 %)
- Circular dichroism (CD) spectroscopy, near-UV (277 K; pH: 7; protein (solution) 0.04 %)
| References:
- Holt C, Sawyer L. "Primary and predicted secondary structures of the caseins in relation to their biological functions." Protein Eng. 1988; 2(4): 251-9. PubMed: 3074304
- Toyoda M, Yamauchi K. "Conformation and some properties of -casein-like fraction of human casein." Biochim Biophys Acta. 1972; 263(3): 555-63. PubMed: 4624541
| Comments:
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| References |
- Dev BC, Sood SM, DeWind S, Slattery CW. "Kappa-casein and beta-caseins in human milk micelles: structural studies." Arch Biochem Biophys. 1994; 314(2): 329-36. PubMed: 7979373
- 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.
- Lonnerdal B, Bergstrom S, Andersson Y, Hjalmarsson K, Sundqvist AK, Hernell O. "Cloning and sequencing of a cDNA encoding human milk beta-casein." FEBS Lett. 1990; 269(1): 153-6. PubMed: 2387396
- 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
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