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P02668 (CASK_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 125. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Kappa-casein

Cleaved into the following 5 chains:

  1. Casoxin-C
  2. Casoxin-6
  3. Casoxin-A
  4. Casoxin-B
  5. Casoplatelin
Gene names
Name:CSN3
Synonyms:CSN10, CSNK
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length190 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subunit structure

Monomer or homomultimer; disulfide-linked. Ref.8

Subcellular location

Secreted.

Tissue specificity

Mammary gland specific. Secreted in milk.

Miscellaneous

The sequence shown is the A variant.

Sequence similarities

Belongs to the kappa-casein family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

itself2EBI-7234047,EBI-7234047
clpBQ9RA633EBI-7234047,EBI-7698530From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2121 Ref.6 Ref.7 Ref.8
Chain22 – 190169Kappa-casein
PRO_0000004483
Peptide46 – 5510Casoxin-C
PRO_0000004484
Peptide54 – 596Casoxin-6 Ref.12
PRO_0000004485
Peptide56 – 627Casoxin-A
PRO_0000004486
Peptide79 – 824Casoxin-B
PRO_0000004487
Peptide127 – 13711Casoplatelin
PRO_0000004488

Sites

Site126 – 1272Cleavage; by chymosin/rennin

Amino acid modifications

Modified residue221Pyrrolidone carboxylic acid
Modified residue1481Phosphoserine Ref.20
Modified residue1701Phosphoserine Ref.20
Modified residue1871Phosphoserine By similarity
Glycosylation1421O-linked (GalNAc...) Ref.19 Ref.20
Glycosylation1521O-linked (GalNAc...) Ref.19 Ref.20
Glycosylation1541O-linked (GalNAc...) Ref.19 Ref.20
Glycosylation1571O-linked (GalNAc...) Ref.19 Ref.20
Glycosylation1631O-linked (GalNAc...) Ref.19 Ref.20
Glycosylation1861O-linked (GalNAc...); partial Ref.19 Ref.20
Disulfide bond32 ↔ 109Alternate; alternate Ref.8
Disulfide bond32Interchain (with C-109); alternate Ref.8
Disulfide bond32Interchain; alternate Ref.8
Disulfide bond109Interchain (with C-32); alternate Ref.8
Disulfide bond109Interchain; alternate Ref.8

Natural variations

Natural variant311R → H in variant F.
Natural variant1181R → C in variant G.
Natural variant1561T → I in variant G and variant H.
Natural variant1571T → I in variant B and variant B2.
Natural variant1691D → A in variant B and variant B2.
Natural variant1741I → T in variant B2.
Natural variant1761S → G in variant E.

Experimental info

Sequence conflict231E → Q AA sequence Ref.7
Sequence conflict261Q → E AA sequence Ref.7
Sequence conflict281Q → E AA sequence Ref.7
Sequence conflict1021N → D AA sequence Ref.6

Sequences

Sequence LengthMass (Da)Tools
P02668 [UniParc].

Last modified April 1, 1988. Version 1.
Checksum: F12D8310C3B93EDA

FASTA19021,269
        10         20         30         40         50         60 
MMKSFFLVVT ILALTLPFLG AQEQNQEQPI RCEKDERFFS DKIAKYIPIQ YVLSRYPSYG 

        70         80         90        100        110        120 
LNYYQQKPVA LINNQFLPYP YYAKPAAVRS PAQILQWQVL SNTVPAKSCQ AQPTTMARHP 

       130        140        150        160        170        180 
HPHLSFMAIP PKKNQDKTEI PTINTIASGE PTSTPTTEAV ESTVATLEDS PEVIESPPEI 

       190 
NTVQVTSTAV 

« Hide

References

« Hide 'large scale' references
[1]"Nucleotide sequences of bovine alpha S1- and kappa-casein cDNAs."
Stewart A.F., Willis I.M., Mackinlay A.G.
Nucleic Acids Res. 12:3895-3907(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (VARIANT A).
[2]"Nucleotide sequence of the cDNA of kappa casein in cows."
Gorodetskii S.I., Kaledin A.S.
Genetika 23:596-604(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (VARIANT B2).
[3]"Isolation and characterization of the bovine kappa-casein gene."
Alexander L.J., Stewart A.F., McKinlay A.G., Kapelinskaya T.V., Tkach T.M., Gorodetsky S.I.
Eur. J. Biochem. 178:395-401(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (VARIANT A).
[4]"Polymorphism in the bovine kappa-casein (CSN3) gene and the 5'-flanking region: sequence analysis of CSN3 A and B alleles."
Robitaille G., Britten M., Morisset J., Petitclerc D.
Anim. Genet. 36:184-185(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (VARIANTS A AND B).
Tissue: Blood.
[5]NIH - Mammalian Gene Collection (MGC) project
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (VARIANT B).
Strain: Hereford.
Tissue: Mammary gland.
[6]"Primary structure of bovine kappa B casein. Complete sequence."
Mercier J.-C., Brignon G., Ribadeau-Dumas B.
Eur. J. Biochem. 35:222-235(1973) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 22-127 (VARIANT B).
[7]"Studies on the primary structure of cow kappa-casein. The primary sequence of cow para-kappa-casein."
Jolles J., Schoentgen F., Alais C., Jolles P.
Chimia 26:645-646(1972)
Cited for: PROTEIN SEQUENCE OF 22-126 (VARIANT A).
[8]"The multimeric structure and disulfide-bonding pattern of bovine kappa-casein."
Rasmussen L.K., Hoejrup P., Petersen T.E.
Eur. J. Biochem. 207:215-222(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 22-38 AND 97-116, INTERCHAIN DISULFIDE BONDS, IDENTIFICATION BY MASS SPECTROMETRY.
[9]"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 31-45.
[10]"Molecular genetic characterization of new bovine kappa-casein alleles CSN3F and CSN3G and genotyping by PCR-RFLP."
Prinzenberg E.M., Hiendleder S., Ikonen T., Erhardt G.
Anim. Genet. 27:347-349(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE OF 31-190 (VARIANTS F AND G).
Strain: Ayrshire and Pinzgauer.
[11]"SSCP analysis at the bovine CSN3 locus discriminates six alleles corresponding to known protein variants (A, B, C, E, F, G) and three new DNA polymorphisms (H, I, A1)."
Prinzenberg E.M., Krause I., Erhardt G.
Anim. Biotechnol. 10:49-62(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 31-190 (VARIANT H).
Strain: Pinzgauer.
[12]"Specificity of hydrolysis of bovine kappa-casein by cell envelope-associated proteinases from Lactococcus lactis strains."
Reid J.R., Coolbear T., Pillidge C.J., Pritchard G.G.
Appl. Environ. Microbiol. 60:801-806(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 54-59.
[13]"Primary structure of cDNA of Bos taurus kappa-casein macropeptide."
Gorodetskii S.I., Kershulyte D.R., Korobko V.G.
Bioorg. Khim. 9:1693-1695(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 92-190 (VARIANT B2).
[14]"Studies on the primary structure of cow kappa-casein. Structural features of para-kappa-casein; N-terminal sequence of kappa-caseinoglycopeptide studied with a sequencer."
Jolles J., Schoentgen F., Alais C., Fiat A.-M., Jolles P.
Helv. Chim. Acta 55:2872-2883(1972) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL PROTEIN SEQUENCE (VARIANT A).
[15]"Kappa-casein from bovine colostrum."
Guerin J., Alais C., Jolles J., Jolles P.
Biochim. Biophys. Acta 351:325-332(1974) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 127-168 AND 187-190.
Tissue: Colostrum.
[16]"Localization of amino-acid substitutions that differenciate bovine kappa-casein variants A and B."
Grosclaude F., Mahe M.-F., Mercier J.-C., Ribadeau-Dumas B.
Ann. Genet. Sel. Anim. 4:515-521(1972)
Cited for: PROTEIN SEQUENCE OF 128-190 (VARIANTS A AND B).
[17]"Genotyping of bovine kappa-casein (kappa-CNA, kappa-CNB, kappa-CNC, kappa-CNE) following DNA sequence amplification and direct sequencing of kappa-CNE PCR product."
Schlieben S., Erhardt G., Senft B.
Anim. Genet. 22:333-342(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE OF 133-190 (VARIANT E).
[18]Woollard J.R., Dentine M.R.
Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE OF 133-190 (VARIANTS A AND B).
[19]"Characterization of O-linked glycosylation motifs in the glycopeptide domain of bovine kappa-casein."
Pisano A., Packer N.H., Redmond J.W., Williams K.L., Gooley A.A.
Glycobiology 4:837-844(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT THR-142; THR-152; THR-154; THR-157; THR-163 AND THR-186.
[20]"Reversed-phase high-performance liquid chromatographic separation of bovine kappa-casein macropeptide and characterization of isolated fractions."
Minkiewicz P., Slangen C.J., Lagerwerf F.M., Haverkamp J., Rollema H.S., Visser S.
J. Chromatogr. A 743:123-135(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT THR-142; THR-152; THR-154; THR-157; THR-163 AND THR-186, PHOSPHORYLATION AT SER-148 AND SER-170.
[21]"Opioid antagonist peptides derived from kappa-casein."
Chiba H., Tani F., Yoshikawa M.
J. Dairy Res. 56:363-366(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: ACTIVITY OF CASOXINS.
[22]"Analogy between fibrinogen and casein. Effect of an undecapeptide isolated from kappa-casein on platelet function."
Jolles P., Levy-Toledano S., Fiat A.-M., Soria C., Gillessen D., Thomaidis A., Dunn F.W., Caen J.P.
Eur. J. Biochem. 158:379-382(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: ACTIVITY OF CASOPLATELIN.
+Additional computationally mapped references.

Web resources

Protein Spotlight

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

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X00565 mRNA. Translation: CAA25231.1.
M36641 mRNA. Translation: AAA30433.1.
X14907, X14908 Genomic DNA. Translation: CAA33034.1.
AY380228 Genomic DNA. Translation: AAQ87922.1.
AY380229 Genomic DNA. Translation: AAQ87923.1.
BC102120 mRNA. Translation: AAI02121.1.
K01085 mRNA. Translation: AAA30482.1.
AF123250 Genomic DNA. Translation: AAD32139.1.
AF123251 Genomic DNA. Translation: AAD32140.1.
AF105260 Genomic DNA. Translation: AAF72097.1.
M38333 mRNA. Translation: AAA30432.1.
AF041482 Genomic DNA. Translation: AAB97519.1.
U84250 Genomic DNA. Translation: AAB47260.1.
U84251 Genomic DNA. Translation: AAB47261.1.
PIRKKBOB. S02076.
RefSeqNP_776719.1. NM_174294.2.
UniGeneBt.49421.

3D structure databases

DisProtDP00192.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid159044. 2 interactions.
IntActP02668. 1 interaction.
MINTMINT-7258912.

Protein family/group databases

Allergome10200. Bos d 12.0101.
167. Bos d 8.
2737. Bos d 12.

PTM databases

UniCarbKBP02668.

Proteomic databases

PaxDbP02668.
PRIDEP02668.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSBTAT00000028685; ENSBTAP00000028685; ENSBTAG00000039787.
GeneID281728.
KEGGbta:281728.

Organism-specific databases

CTD1448.

Phylogenomic databases

eggNOGNOG40632.
GeneTreeENSGT00390000009184.
HOVERGENHBG005246.
InParanoidP02668.
KOK17282.
OrthoDBEOG7MWH09.
TreeFamTF338369.

Family and domain databases

InterProIPR000117. Casein_kappa.
[Graphical view]
PANTHERPTHR11470. PTHR11470. 1 hit.
PfamPF00997. Casein_kappa. 1 hit.
[Graphical view]
PIRSFPIRSF002374. Casein_kappa. 1 hit.
ProtoNetSearch...

Other

NextBio20805648.
PMAP-CutDBP02668.

Entry information

Entry nameCASK_BOVIN
AccessionPrimary (citable) accession number: P02668
Secondary accession number(s): O46566 expand/collapse secondary AC list , Q597F3, Q6U205, Q9N271, Q9TRQ3, Q9TV96, Q9TV97
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: April 1, 1988
Last modified: June 11, 2014
This is version 125 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Protein Spotlight

Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries