Beta-casein precursor - Bos taurus (Bovine)

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P02666 (CASB_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 120. History...

Clusters with 100%, 90%, 50% identity |

Documents (1) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Beta-casein

Gene names

Name:

CSN2

Organism

Bos taurus (Bovine) [Reference proteome]

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length	224 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Important role in determination of the surface properties of the casein micelles. Ref.12 Ref.21 Ref.24 Ref.25 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. Ref.12 Ref.21 Ref.24 Ref.25 Casohypotensin acts as a bradykinin-potentiating peptide. Induces hypotension in rats. Acts as a strong competitive inhibitor of endo-oligopeptidase A. Ref.12 Ref.21 Ref.24 Ref.25 Antioxidant peptide has antioxidant activity. Ref.12 Ref.21 Ref.24 Ref.25
Subcellular location	Secreted.
Tissue specificity	Mammary gland specific. Secreted in milk.
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.
Sequence similarities	Belongs to the beta-casein family.
Mass spectrometry	Molecular mass is 872.51 Da from positions 113 - 120. Determined by ESI. Ref.21
Sequence caution	The sequence AAW84270.1 differs from that shown. Reason: Erroneous initiation. The sequence AAW84271.1 differs from that shown. Reason: Erroneous initiation. The sequence ABL74247.1 differs from that shown. Reason: Frameshift at positions 65 and 71.

Ontologies

Keywords
Cellular component	Secreted
Coding sequence diversity	Polymorphism
Domain	Signal
Molecular function	Antioxidant Hypotensive agent Metalloenzyme inhibitor Metalloprotease inhibitor Milk protein Protease inhibitor
PTM	Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	regulation of blood pressure Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	antioxidant activity Inferred from electronic annotation. Source: UniProtKB-KW metalloendopeptidase inhibitor activity Inferred from electronic annotation. Source: UniProtKB-KW transporter activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
HTRA2	O43464	2	EBI-5260183,EBI-517086	From a different organism.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 15

Ref.8 Ref.9 Ref.10

Chain

16 – 224

209

Beta-casein

PRO_0000004470

Peptide

41 – 45

Casoparan Ref.12

PRO_0000292031

Peptide

113 – 120

Antioxidant peptide Ref.21

PRO_0000320153

Peptide

129 – 136

Casohypotensin Ref.24 Ref.25

PRO_0000308464

Amino acid modifications

Modified residue

Phosphoserine Ref.8 Ref.28 Ref.29

Modified residue

Phosphoserine Ref.8 Ref.28 Ref.29

Modified residue

Phosphoserine Ref.8 Ref.28 Ref.29

Modified residue

Phosphoserine Ref.8 Ref.28 Ref.29

Modified residue

Phosphoserine; in variant A1, variant A2, variant A3, variant B, variant E, variant F, variant G and variant H Ref.28 Ref.29

Natural variations

Natural variant

S → K in variant D. Ref.10

Natural variant

R → C in variant H.

Natural variant

E → K in variant E. Ref.13

Natural variant

E → K in variant C.

Natural variant

P → H in variants A1, B, C, F and G. Ref.4 Ref.6 Ref.21

Natural variant

103

L → I in variant H.

Natural variant

108

M → L. Ref.1 Ref.8 Ref.19 Ref.20

Natural variant

121

H → Q in variant A3. Ref.5 Ref.22

Natural variant

132

E → Q in variants A1 and G. Ref.11 Ref.24

Natural variant

137

S → R in variant B. Ref.6

Natural variant

152

L → P in variants A1 and H. Ref.1

Natural variant

153

P → L in variants A1, G and H. Ref.1

Natural variant

167

P → L in variant F.

Natural variant

190

Q → E in variants A1 and G.

Experimental info

Sequence conflict

S → Z AA sequence Ref.11

Sequence conflict

Q → R in ABL74247. Ref.14

Sequence conflict

112

K → R in ABL74247. Ref.14

Sequence conflict

208

Y → V in CAC37028. Ref.16

Sequence conflict

209 – 210

QE → EQ AA sequence Ref.11

Sequence conflict

210

E → Q in AAA30430. Ref.1

Sequence conflict

210

E → Q no nucleotide entry Ref.8

Sequence conflict

212

V → A in ABR10906. Ref.15

Sequences

Sequence

Length

Mass (Da)

Tools

P02666 [UniParc].

Last modified July 1, 1989. Version 2.
Checksum: F0BBDD8148A238AE
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FASTA

224

25,107

        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

« Hide

References

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

Web resources

Protein Spotlight

Of buttons, digestion and glue - Issue 16 of November 2001

Cross-references

Sequence databases
EMBL GenBank DDBJ	M15132 mRNA. Translation: AAA30430.1. X06359 mRNA. Translation: CAA29658.1. M16645 mRNA. Translation: AAA30480.1. M55158 Genomic DNA. Translation: AAA30431.1. S67277 mRNA. Translation: AAB29137.1. BC111172 mRNA. Translation: AAI11173.1. AY899917 mRNA. Translation: AAW84270.1. Different initiation. AY899918 mRNA. Translation: AAW84271.1. Different initiation. AH007287 Genomic DNA. Translation: AAD09813.1. EF123100 Genomic DNA. Translation: ABL74247.1. Frameshift. EF628290 Genomic DNA. Translation: ABR10906.1. AJ296330 Genomic DNA. Translation: CAC37028.1. M64756 mRNA. Translation: AAB59254.1. AY366419 Genomic DNA. Translation: AAR14677.1. K01087 mRNA. Translation: AAA30481.1.
IPI	IPI00697085.
PIR	A59068. KBBOA2. I45873.
RefSeq	NP_851351.1. NM_181008.2.
UniGene	Bt.53272.
3D structure databases
DisProt	DP00329.
ProteinModelPortal	P02666.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-46257N.
IntAct	P02666. 1 interaction.
STRING	9913.ENSBTAP00000003409.
Protein family/group databases
Allergome	10199. Bos d 11.0101. 167. Bos d 8. 2736. Bos d 11.
Proteomic databases
PaxDb	P02666.
PRIDE	P02666.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSBTAT00000003409; ENSBTAP00000003409; ENSBTAG00000002632.
GeneID	281099.
KEGG	bta:281099.
Organism-specific databases
CTD	1447.
Phylogenomic databases
eggNOG	NOG45871.
GeneTree	ENSGT00390000001890.
HOVERGEN	HBG004973.
InParanoid	P02666.
OMA	VVPYPQR.
OrthoDB	EOG41NTND.
Family and domain databases
InterPro	IPR001588. Casein. IPR016345. Casein_beta. [Graphical view]
PANTHER	PTHR11500. PTHR11500. 1 hit.
Pfam	PF00363. Casein. 1 hit. [Graphical view]
PIRSF	PIRSF002372. Beta-casein. 1 hit.
PROSITE	PS00306. CASEIN_ALPHA_BETA. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	20805172.
PMAP-CutDB	P02666.

Entry information

Entry name

CASB_BOVIN

Accession

Primary (citable) accession number: P02666
Secondary accession number(s): A1YQZ8

Q9TSD5

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	July 1, 1989
Last modified:	May 1, 2013
This is version 120 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Cleaved into the following 3 chains:

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Amino acid modifications

Natural variations

Experimental info

Sequences

References

Web resources

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Family and domain databases

Other

Entry information

Relevant documents