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Protein

Kappa-casein

Gene

CSN3

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei126 – 1272Cleavage; by chymosin/rennin

GO - Molecular functioni

  1. identical protein binding Source: IntAct

GO - Biological processi

  1. lactation Source: Ensembl
  2. protein stabilization Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Milk protein

Names & Taxonomyi

Protein namesi
Recommended name:
Kappa-casein
Cleaved into the following 5 chains:
Gene namesi
Name:CSN3
Synonyms:CSN10, CSNK
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
ProteomesiUP000009136 Componenti: Chromosome 6

Subcellular locationi

GO - Cellular componenti

  1. extracellular space Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Protein family/group databases

Allergomei10200. Bos d 12.0101.
167. Bos d 8.
2737. Bos d 12.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 21213 PublicationsAdd
BLAST
Chaini22 – 190169Kappa-caseinPRO_0000004483Add
BLAST
Peptidei46 – 5510Casoxin-CPRO_0000004484
Peptidei54 – 596Casoxin-6PRO_0000004485
Peptidei56 – 627Casoxin-APRO_0000004486
Peptidei79 – 824Casoxin-BPRO_0000004487
Peptidei127 – 13711CasoplatelinPRO_0000004488Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei22 – 221Pyrrolidone carboxylic acid
Disulfide bondi32 ↔ 109
Disulfide bondi32 – 32Interchain (with C-109); in linked form
Disulfide bondi109 – 109Interchain (with C-32); in linked form
Glycosylationi142 – 1421O-linked (GalNAc...)2 Publications
Modified residuei148 – 1481Phosphoserine1 Publication
Glycosylationi152 – 1521O-linked (GalNAc...)2 Publications
Glycosylationi154 – 1541O-linked (GalNAc...)2 Publications
Glycosylationi157 – 1571O-linked (GalNAc...)2 Publications
Glycosylationi163 – 1631O-linked (GalNAc...)2 Publications
Modified residuei170 – 1701Phosphoserine1 Publication
Glycosylationi186 – 1861O-linked (GalNAc...); partial2 Publications
Modified residuei187 – 1871PhosphoserineBy similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein, Pyrrolidone carboxylic acid

Proteomic databases

PaxDbiP02668.
PRIDEiP02668.

PTM databases

UniCarbKBiP02668.

Miscellaneous databases

PMAP-CutDBP02668.

Expressioni

Tissue specificityi

Mammary gland specific. Secreted in milk.

Gene expression databases

ExpressionAtlasiP02668. baseline.

Interactioni

Subunit structurei

Monomer or homomultimer; disulfide-linked.

Binary interactionsi

WithEntry#Exp.IntActNotes
itself2EBI-7234047,EBI-7234047
clpBQ9RA633EBI-7234047,EBI-7698530From a different organism.

Protein-protein interaction databases

BioGridi159044. 2 interactions.
IntActiP02668. 1 interaction.
MINTiMINT-7258912.

Structurei

3D structure databases

DisProtiDP00192.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the kappa-casein family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG40632.
HOVERGENiHBG005246.
InParanoidiP02668.
KOiK17282.
OrthoDBiEOG7MWH09.
TreeFamiTF338369.

Family and domain databases

InterProiIPR000117. Casein_kappa.
[Graphical view]
PANTHERiPTHR11470. PTHR11470. 1 hit.
PfamiPF00997. Casein_kappa. 1 hit.
[Graphical view]
PIRSFiPIRSF002374. Casein_kappa. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P02668-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MMKSFFLVVT ILALTLPFLG AQEQNQEQPI RCEKDERFFS DKIAKYIPIQ
60 70 80 90 100
YVLSRYPSYG LNYYQQKPVA LINNQFLPYP YYAKPAAVRS PAQILQWQVL
110 120 130 140 150
SNTVPAKSCQ AQPTTMARHP HPHLSFMAIP PKKNQDKTEI PTINTIASGE
160 170 180 190
PTSTPTTEAV ESTVATLEDS PEVIESPPEI NTVQVTSTAV
Length:190
Mass (Da):21,269
Last modified:April 1, 1988 - v1
Checksum:iF12D8310C3B93EDA
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti23 – 231E → Q AA sequence (Ref. 7) Curated
Sequence conflicti26 – 261Q → E AA sequence (Ref. 7) Curated
Sequence conflicti28 – 281Q → E AA sequence (Ref. 7) Curated
Sequence conflicti102 – 1021N → D AA sequence (PubMed:4577852).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti31 – 311R → H in variant F.
Natural varianti118 – 1181R → C in variant G.
Natural varianti156 – 1561T → I in variant G and variant H.
Natural varianti157 – 1571T → I in variant B and variant B2.
Natural varianti169 – 1691D → A in variant B and variant B2.
Natural varianti174 – 1741I → T in variant B2.
Natural varianti176 – 1761S → G in variant E.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiS02076. KKBOB.
RefSeqiNP_776719.1. NM_174294.2.
UniGeneiBt.49421.

Genome annotation databases

GeneIDi281728.
KEGGibta:281728.

Cross-referencesi

Web resourcesi

Protein Spotlight

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiS02076. KKBOB.
RefSeqiNP_776719.1. NM_174294.2.
UniGeneiBt.49421.

3D structure databases

DisProtiDP00192.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi159044. 2 interactions.
IntActiP02668. 1 interaction.
MINTiMINT-7258912.

Protein family/group databases

Allergomei10200. Bos d 12.0101.
167. Bos d 8.
2737. Bos d 12.

PTM databases

UniCarbKBiP02668.

Proteomic databases

PaxDbiP02668.
PRIDEiP02668.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi281728.
KEGGibta:281728.

Organism-specific databases

CTDi1448.

Phylogenomic databases

eggNOGiNOG40632.
HOVERGENiHBG005246.
InParanoidiP02668.
KOiK17282.
OrthoDBiEOG7MWH09.
TreeFamiTF338369.

Miscellaneous databases

NextBioi20805648.
PMAP-CutDBP02668.

Gene expression databases

ExpressionAtlasiP02668. baseline.

Family and domain databases

InterProiIPR000117. Casein_kappa.
[Graphical view]
PANTHERiPTHR11470. PTHR11470. 1 hit.
PfamiPF00997. Casein_kappa. 1 hit.
[Graphical view]
PIRSFiPIRSF002374. Casein_kappa. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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(1983) [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(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (VARIANT B2).
  3. 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(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (VARIANTS A AND B).
    Tissue: Blood.
  5. NIH - Mammalian Gene Collection (MGC) project
    Submitted (JUL-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(1972) [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(1971)
    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(1991) [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(1981) [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(1995) [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(1998) [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(1993) [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(1982) [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(1971) [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(1973) [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(1971)
    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(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE OF 133-190 (VARIANT E).
  18. Woollard J.R., Dentine M.R.
    Submitted (JAN-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(1993) [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(1995) [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(1988) [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(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACTIVITY OF CASOPLATELIN.

Entry informationi

Entry nameiCASK_BOVIN
AccessioniPrimary (citable) accession number: P02668
Secondary accession number(s): O46566
, Q597F3, Q6U205, Q9N271, Q9TRQ3, Q9TV96, Q9TV97
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: April 1, 1988
Last modified: March 4, 2015
This is version 130 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

The sequence shown is the A variant.

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Protein Spotlight
    Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.