[1]	NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS LEU-108; PRO-152 AND LEU-153. DOI=10.1016/0006-291X(87)90318-4; PubMed=3814153 [NCBI, ExPASy, EBI, Israel, Japan] Jimenez-Flores R., Kang Y.C., Richardson T.; "Cloning and sequence analysis of bovine beta-casein cDNA."; Biochem. Biophys. Res. Commun. 142:617-621(1987).
[2]	NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT HIS-82. Baev A.A., Smirnov I.K., Gorodetsky S.I.; "Primary structure of bovine beta-casein cDNA."; Mol. Biol. (Mosk.) 21:214-222(1987).
[3]	NUCLEOTIDE SEQUENCE [MRNA]. PubMed=2833669 [NCBI, ExPASy, EBI, Israel, Japan] Stewart A.F., Bonsing J., Beattie C.W., Shah F., Willis I.M., Mackinlay A.G.; "Complete nucleotide sequences of bovine alpha S2- and beta-casein cDNAs: comparisons with related sequences in other species."; Mol. Biol. Evol. 4:231-241(1987).
[4]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT HIS-82. PubMed=3271384 [NCBI, ExPASy, EBI, Israel, Japan] Bonsing J., Ring J.M., Stewart A.F., Mackinlay A.G.; "Complete nucleotide sequence of the bovine beta-casein gene."; Aust. J. Biol. Sci. 41:527-537(1988).
[5]	NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT A3 GLN-121. TISSUE=Mammary gland; DOI=10.1093/protein/6.7.763; PubMed=8248100 [NCBI, ExPASy, EBI, Israel, Japan] Simons G., van den Heuvel W., Reynen T., Frijters A., Rutten G., Slangen C.J., Groenen M., de Vos W.M., Siezen R.J.; "Overproduction of bovine beta-casein in Escherichia coli and engineering of its main chymosin cleavage site."; Protein Eng. 6:763-770(1993).
[6]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS HIS-82 AND ARG-137. STRAIN=Crossbred X Angus; TISSUE=Liver; NIH - Mammalian Gene Collection (MGC) project; Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
[7]	NUCLEOTIDE SEQUENCE [MRNA] OF 1-101. TISSUE=Mammary epithelium; DOI=10.1016/j.rvsc.2006.02.002; PubMed=16624358 [NCBI, ExPASy, EBI, Israel, Japan] Anaya-Lopez J.L., Contreras-Guzman O.E., Carabez-Trejo A., Baizabal-Aguirre V.M., Lopez-Meza J.E., Valdez-Alarcon J.J., Ochoa-Zarzosa A.; "Invasive potential of bacterial isolates associated with subclinical bovine mastitis."; Res. Vet. Sci. 81:358-361(2006).
[8]	PROTEIN SEQUENCE OF 16-224 (VARIANT A2), AND VARIANT LEU-108. PubMed=4557764 [NCBI, ExPASy, EBI, Israel, Japan] Ribadeau-Dumas B., Brignon G., Grosclaude F., Mercier J.-C.; "Primary structure of bovine beta casein. Complete sequence."; Eur. J. Biochem. 25:505-514(1972).
[9]	PROTEIN SEQUENCE OF 16-224 (VARIANT A2). DOI=10.1016/0014-5793(88)81138-4; PubMed=3278933 [NCBI, ExPASy, EBI, Israel, Japan] Carles C., Huet J.-C., Ribadeau-Dumas B.; "A new strategy for primary structure determination of proteins: application to bovine beta-casein."; FEBS Lett. 229:265-272(1988).
[10]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 18-57, PROTEIN SEQUENCE OF 16-224 (VARIANT H), AND VARIANT D LYS-33. STRAIN=Korean; TISSUE=Milk; PubMed=10690361 [NCBI, ExPASy, EBI, Israel, Japan] Han S.K., Shin Y.C., Byun H.D.; "Biochemical, molecular and physiological characterization of a new beta-casein variant detected in Korean cattle."; Anim. Genet. 31:49-51(2000).
[11]	PROTEIN SEQUENCE OF 41-71; 113-157 AND 180-224, AND VARIANT GLN-132. DOI=10.1002/rcm.1290050410; PubMed=1804413 [NCBI, ExPASy, EBI, Israel, Japan] Jones D.S., Heerma W., van Wassenaar P.D., Haverkamp J.; "Analysis of bovine beta-casein tryptic digest by continuous-flow fast-atom bombardment mass spectrometry."; Rapid Commun. Mass Spectrom. 5:192-195(1991).
[12]	PROTEIN SEQUENCE OF 41-45, AND FUNCTION. DOI=10.1080/09629350400003068; PubMed=15545057 [NCBI, ExPASy, EBI, Israel, Japan] Lebrun I., Cavallaro V., Juliano L., Juliano M.A., de Sousa e Silva M.C.C.; "Effects of 'casoparan', a peptide isolated from casein hydrolysates with mastoparan-like properties."; Mediators Inflamm. 13:263-268(2004).
[13]	PROTEIN SEQUENCE OF 48-63, AND VARIANT E LYS-51. DOI=10.1016/0014-5793(74)80796-9; PubMed=4411121 [NCBI, ExPASy, EBI, Israel, Japan] Grosclaude F., Mahe M.-F., Voglino G.-F.; "The beta E variant and the phosphorylation code of bovine caseins."; FEBS Lett. 45:3-5(1974).
[14]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 58-223. Otaviano A.R., Lima A.L.F., Laureano M.M.M., Albuquerque L.G., Tonhati H., Sena J.A.D.; "Polymorphisms in beta and kappa casein genes in bubaline and bovine."; Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases.
[15]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 58-223. Shahla M.N., Cheema F.R., Naeem M.K., Riazuddin S.; "Polymorphism in the cattle beta casein gene."; Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases.
[16]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 63-208. TISSUE=Mammary gland; Klotz A., Buchberger J., Krause I., Einspanier R.; "Characterization of milk proteins."; Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases.
[17]	NUCLEOTIDE SEQUENCE [MRNA] OF 68-105. DOI=10.1016/0378-1119(84)90013-1; PubMed=6397405 [NCBI, ExPASy, EBI, Israel, Japan] Ivanov V.N., Kershulite D.R., Bayev A.A., Akhundova A.A., Sulimova G.E., Judinkova E.S., Gorodetsky S.I.; "Identification of bacterial clones encoding bovine caseins by direct immunological screening of the cDNA library."; Gene 32:381-388(1984).
[18]	NUCLEOTIDE SEQUENCE [MRNA] OF 68-95. PubMed=3900695 [NCBI, ExPASy, EBI, Israel, Japan] Ivanov V.N., Kershulite D.R., Bayev A.A., Akhundova A.A., Silimova G.E.; "Identification of bacterial clones that encode cow's caseins by direct immunological screening of the cDNA library."; Mol. Biol. (Mosk.) 19:955-963(1985).
[19]	PROTEIN SEQUENCE OF 74-108, VARIANT LEU-108, PHOSPHORYLATION, AND MASS SPECTROMETRY. DOI=10.1016/j.chroma.2007.08.015; PubMed=17720176 [NCBI, ExPASy, EBI, Israel, Japan] Schmelzer C.E.H., Schoeps R., Reynell L., Ulbrich-Hofmann R., Neubert R.H.H., Raith K.; "Peptic digestion of beta-casein: Time course and fate of possible bioactive peptides."; J. Chromatogr. A 1166:108-115(2007).
[20]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 80-143, AND VARIANT LEU-108. Jann O., Ceriotti G., Caroli A., Erhardt G.; "A new variant in exon VII of bovine beta-casein gene (CSN2) and its contribution among European cattle breeds."; J. Anim. Breed. Genet. 119:65-68(2002).
[21]	PROTEIN SEQUENCE OF 113-120, FUNCTION, AND MASS SPECTROMETRY. Gupta A., Mann B., Kumar Bajaj R., Sangwan R.B.; "Studies on antioxidative peptides generated in cheddar cheese."; Submitted (JAN-2008) to UniProtKB.
[22]	PROTEIN SEQUENCE OF 118-124, AND VARIANT A3 GLN-121. PubMed=4997616 [NCBI, ExPASy, EBI, Israel, Japan] Ribadeau-Dumas B., Grosclaude F., Mercier J.-C.; "Localization in the peptide chain of bovine beta casein of the His-Gln substitution differentiating the A2 and A3 genetic variants."; C.R. Hebd. Seances Acad. Sci., D, Sci. Nat. 270:2369-2372(1970).
[23]	PROTEIN SEQUENCE OF 125-195 (VARIANTS A1 AND G). DOI=10.1016/S0958-6946(99)00019-9; AGRICOLA=IND22004684 Dong C., Ng-Kwai-Hang K.F.; "Characterization of a non-electrophoretic genetic variant of beta-casein by peptide mapping and mass spectrometric analysis."; Int. Dairy J. 8:967-972(1998).
[24]	PROTEIN SQUENCE OF 129-136, FUNCTION, AND VARIANT GLN-132. PubMed=7600458 [NCBI, ExPASy, EBI, Israel, Japan] Lebrun I., Lebrun F.L.A.S., Henriques O.B., Carmona A.K., Juliano L., Camargo A.C.M.; "Isolation and characterization of a new bradykinin potentiating octapeptide from gamma-casein."; Can. J. Physiol. Pharmacol. 73:85-91(1995).
[25]	PROTEIN SQUENCE OF 129-136, AND FUNCTION. DOI=10.1023/B:JOPC.0000008724.98339.ff; PubMed=14714726 [NCBI, ExPASy, EBI, Israel, Japan] Perpetuo E.A., Juliano L., Lebrun I.; "Biochemical and pharmacological aspects of two bradykinin-potentiating peptides obtained from tryptic hydrolysis of casein."; J. Protein Chem. 22:601-606(2003).
[26]	PROTEIN SEQUENCE OF 160-171 (VARIANT F). DOI=10.1016/0021-9673(95)00058-U; PubMed=7496485 [NCBI, ExPASy, EBI, Israel, Japan] Visser S., Slangen C.J., Lagerwerf F.M., Van Dongen W.D., Haverkamp J.; "Identification of a new genetic variant of bovine beta-casein using reversed-phase high-performance liquid chromatography and mass spectrometric analysis."; J. Chromatogr. A 711:141-150(1995).
[27]	NUCLEOTIDE SEQUENCE [MRNA] OF 170-184. PubMed=6897774 [NCBI, ExPASy, EBI, Israel, Japan] Willis I.M., Stewart A.F., Caputo A., Thompson A.R., McKinlay A.G.; "Construction and identification by partial nucleotide sequence analysis of bovine casein and beta-lactoglobulin cDNA clones."; DNA 1:375-386(1982).
[28]	PHOSPHORYLATION AT SER-30; SER-32; SER-33; SER-34 AND SER-50, AND MASS SPECTROMETRY. DOI=10.1021/pr050113n; PubMed=16083266 [NCBI, ExPASy, EBI, Israel, Japan] Wu S.L., Kim J., Hancock W.S., Karger B.; "Extended Range Proteomic Analysis (ERPA): a new and sensitive LC-MS platform for high sequence coverage of complex proteins with extensive post-translational modifications-comprehensive analysis of beta-casein and epidermal growth factor receptor (EGFR)."; J. Proteome Res. 4:1155-1170(2005).
[29]	PHOSPHORYLATION AT SER-30; SER-32; SER-33; SER-34 AND SER-50, AND MASS SPECTROMETRY. DOI=10.1074/mcp.M600480-MCP200; PubMed=17510049 [NCBI, ExPASy, EBI, Israel, Japan] Imanishi S.Y., Kochin V., Ferraris S.E., de Thonel A., Pallari H.M., Corthals G.L., Eriksson J.E.; "Reference-facilitated phosphoproteomics: fast and reliable phosphopeptide validation by micro LC-ESI-Q-TOF MS/MS."; Mol. Cell. Proteomics 6:1380-1391(2007).
[30]	VARIANTS A1; B AND C. PubMed=5064450 [NCBI, ExPASy, EBI, Israel, Japan] Grosclaude F., Mahe M.-F., Mercier J.-C., Ribadeau-Dumas B.; "Characterization of genetic variants of alpha-S1 and beta bovine caseins."; Eur. J. Biochem. 26:328-337(1972).

Comments

FUNCTION: Important role in determination of the surface properties of the casein micelles.
FUNCTION: Casoparan acts as a macrophage activator, increasing the phagocytic activity of macrophages and peroxide release from macrophages. It also acts as a bradykinin-potentiating peptide.
FUNCTION: Casohypotensin acts as a bradykinin-potentiating peptide. Induces hypotension in rats. Acts as a strong competitive inhibitor of endo-oligopeptidase A.
FUNCTION: Antioxidant peptide has antioxidant activity.
SUBCELLULAR LOCATION: Secreted.
TISSUE SPECIFICITY: Mammary gland specific. Secreted in milk.
MASS SPECTROMETRY: Mass=872.51; Method=Electrospray; Range=113-120; Source=Ref.21;.
POLYMORPHISM: Leu-152 is present in the variants F and G; Gln-190 and Glu-210 are present in the variant H. The sequence shown is the A2 variant.
SIMILARITY: Belongs to the beta-casein family.
SEQUENCE CAUTION:
- Sequence=ABL74247.1; Type=Frameshift; Positions=65, 71;
WEB RESOURCE: Name=Protein Spotlight; Note=Of buttons, digestion and glue - Issue 16 of November 2001; URL="http://www.expasy.org/spotlight/back_issues/sptlt016.shtml";.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

M15132; AAA30430.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X06359; CAA29658.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M16645; AAA30480.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M55158; AAA30431.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
S67277; AAB29137.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC111172; AAI11173.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY899917; AAW84270.1; ALT_INIT; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY899918; AAW84271.1; ALT_INIT; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF104929; AAD09813.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF104928; AAD09813.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
EF123100; ABL74247.1; ALT_FRAME; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
EF628290; ABR10906.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ296330; CAC37028.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M64756; AAB59254.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY366419; AAR14677.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
K01087; AAA30481.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A59068; A59068.
I45873; KBBOA2.

RefSeq

NP_851351.1; -.

UniGene

Bt.49421

3D structure databases

DisProt

DP00329; -.

ModBase

P02666.

Family and domain databases

InterPro

IPR001588; Casein.
IPR016345; Casein_beta.
Graphical view of domain structure.

Pfam

PF00363; Casein; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF002372; Beta-casein; 1.

PROSITE

PS00306; CASEIN_ALPHA_BETA; 1.

BLOCKS

P02666.

Genome annotation databases

Ensembl

ENSBTAG00000002632; Bos taurus. [Contig view]

GeneID

281099; -.

KEGG

bta:281099; -.

Phylogenomic databases

HOVERGEN

P02666; -.

Other

ProtoNet

P02666.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Antioxidant; Direct protein sequencing; Hypotensive agent; Metalloenzyme inhibitor; Metalloprotease inhibitor; Milk protein; Phosphoprotein; Polymorphism; Secreted; Signal.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 15`	`15`
`CHAIN`	`16 224`	`209`	`Beta-casein.`	`PRO_0000004470`
`PEPTIDE`	`41 45`	`5`	`Casoparan.`	`PRO_0000292031`
`PEPTIDE`	`113 120`	`8`	`Antioxidant peptide.`	`PRO_0000320153`
`PEPTIDE`	`129 136`	`8`	`Casohypotensin.`	`PRO_0000308464`
`MOD_RES`	`30 30`		`Phosphoserine.`
`MOD_RES`	`32 32`		`Phosphoserine.`
`MOD_RES`	`33 33`		`Phosphoserine.`
`MOD_RES`	`34 34`		`Phosphoserine.`
`MOD_RES`	`50 50`		`Phosphoserine; in variant A1, variant A2, variant A3, variant B, variant E, variant F, variant G and variant H.`
`VARIANT`	`33 33`	`1`	`S -> K (in variant D).`
`VARIANT`	`40 40`	`1`	`R -> C (in variant H).`
`VARIANT`	`51 51`	`1`	`E -> K (in variant E).`
`VARIANT`	`52 52`	`1`	`E -> K (in variant C).`
`VARIANT`	`82 82`	`1`	`P -> H (in variants A1, B, C, F and G).`
`VARIANT`	`103 103`	`1`	`L -> I (in variant H).`
`VARIANT`	`108 108`	`1`	`M -> L.`
`VARIANT`	`121 121`	`1`	`H -> Q (in variant A3).`
`VARIANT`	`132 132`	`1`	`E -> Q (in variants A1 and G).`
`VARIANT`	`137 137`	`1`	`S -> R (in variant B).`
`VARIANT`	`152 152`	`1`	`L -> P (in variants A1 and H).`
`VARIANT`	`153 153`	`1`	`P -> L (in variants A1, G and H).`
`VARIANT`	`167 167`	`1`	`P -> L (in variant F).`
`VARIANT`	`190 190`	`1`	`Q -> E (in variants A1 and G).`
`CONFLICT`	`50 50`		`S -> Z (in Ref. 11; AA sequence).`
`CONFLICT`	`69 69`		`Q -> R (in Ref. 14; ABL74247).`
`CONFLICT`	`112 112`		`K -> R (in Ref. 14; ABL74247).`
`CONFLICT`	`208 208`		`Y -> V (in Ref. 16; CAC37028).`
`CONFLICT`	`209 210`		`QE -> EQ (in Ref. 11; AA sequence).`
`CONFLICT`	`210 210`		`E -> Q (in Ref. 1; AAA30430 and 8).`
`CONFLICT`	`212 212`		`V -> A (in Ref. 15; ABR10906).`

Sequence information

Length: 224 AA [This is the length of the unprocessed precursor]

Molecular weight: 25107 Da [This is the MW of the unprocessed precursor]

CRC64: F0BBDD8148A238AE [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKVLILACLV ALALARELEE LNVPGEIVES LSSSEESITR INKKIEKFQS EEQQQTEDEL 

        70         80         90        100        110        120 
QDKIHPFAQT QSLVYPFPGP IPNSLPQNIP PLTQTPVVVP PFLQPEVMGV SKVKEAMAPK 

       130        140        150        160        170        180 
HKEMPFPKYP VEPFTESQSL TLTDVENLHL PLPLLQSWMH QPHQPLPPTV MFPPQSVLSL 

       190        200        210        220 
SQSKVLPVPQ KAVPYPQRDM PIQAFLLYQE PVLGPVRGPF PIIV

P02666 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools