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Kappa-casein [Cleaved into: Casoxin-C; Casoxin-6; Casoxin-A; Casoxin-B; Casoplatelin]

 CASK_BOVIN              Reviewed;         190 AA.
P02668; O46566; Q597F3; Q6U205; Q9N271; Q9TRQ3; Q9TV96; Q9TV97;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
01-APR-1988, sequence version 1.
22-NOV-2017, entry version 148.
RecName: Full=Kappa-casein;
Contains:
RecName: Full=Casoxin-C;
Contains:
RecName: Full=Casoxin-6;
Contains:
RecName: Full=Casoxin-A;
Contains:
RecName: Full=Casoxin-B;
Contains:
RecName: Full=Casoplatelin;
Flags: Precursor;
Name=CSN3; Synonyms=CSN10, CSNK;
Bos taurus (Bovine).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Bovinae; Bos.
NCBI_TaxID=9913;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (VARIANT A).
PubMed=6328443; DOI=10.1093/nar/12.9.3895;
Stewart A.F., Willis I.M., Mackinlay A.G.;
"Nucleotide sequences of bovine alpha S1- and kappa-casein cDNAs.";
Nucleic Acids Res. 12:3895-3907(1984).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (VARIANT B2).
PubMed=3582972;
Gorodetskii S.I., Kaledin A.S.;
"Nucleotide sequence of the cDNA of kappa casein in cows.";
Genetika 23:596-604(1987).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (VARIANT A).
PubMed=3208764; DOI=10.1111/j.1432-1033.1988.tb14463.x;
Alexander L.J., Stewart A.F., McKinlay A.G., Kapelinskaya T.V.,
Tkach T.M., Gorodetsky S.I.;
"Isolation and characterization of the bovine kappa-casein gene.";
Eur. J. Biochem. 178:395-401(1988).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (VARIANTS A AND B).
TISSUE=Blood;
PubMed=15771744; DOI=10.1111/j.1365-2052.2005.01260.x;
Robitaille G., Britten M., Morisset J., Petitclerc D.;
"Polymorphism in the bovine kappa-casein (CSN3) gene and the 5'-
flanking region: sequence analysis of CSN3 A and B alleles.";
Anim. Genet. 36:184-185(2005).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (VARIANT B).
STRAIN=Hereford; TISSUE=Mammary gland;
NIH - Mammalian Gene Collection (MGC) project;
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
[6]
PROTEIN SEQUENCE OF 22-127 (VARIANT B).
PubMed=4577852; DOI=10.1111/j.1432-1033.1973.tb02829.x;
Mercier J.-C., Brignon G., Ribadeau-Dumas B.;
"Primary structure of bovine kappa B casein. Complete sequence.";
Eur. J. Biochem. 35:222-235(1973).
[7]
PROTEIN SEQUENCE OF 22-126 (VARIANT A).
Jolles J., Schoentgen F., Alais C., Jolles P.;
"Studies on the primary structure of cow kappa-casein. The primary
sequence of cow para-kappa-casein.";
Chimia 26:645-646(1972).
[8]
PROTEIN SEQUENCE OF 22-38 AND 97-116, PYROGLUTAMATE FORMATION AT
GLN-22, INTERCHAIN DISULFIDE BONDS, AND IDENTIFICATION BY MASS
SPECTROMETRY.
PubMed=1628650; DOI=10.1111/j.1432-1033.1992.tb17040.x;
Rasmussen L.K., Hoejrup P., Petersen T.E.;
"The multimeric structure and disulfide-bonding pattern of bovine
kappa-casein.";
Eur. J. Biochem. 207:215-222(1992).
[9]
NUCLEOTIDE SEQUENCE [MRNA] OF 31-45.
PubMed=6897774; DOI=10.1089/dna.1982.1.375;
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).
[10]
NUCLEOTIDE SEQUENCE OF 31-190 (VARIANTS F AND G).
STRAIN=Ayrshire, and Pinzgauer;
PubMed=8930077;
Prinzenberg E.M., Hiendleder S., Ikonen T., Erhardt G.;
"Molecular genetic characterization of new bovine kappa-casein alleles
CSN3F and CSN3G and genotyping by PCR-RFLP.";
Anim. Genet. 27:347-349(1996).
[11]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 31-190 (VARIANT H).
STRAIN=Pinzgauer;
PubMed=10654430; DOI=10.1080/10495399909525921;
Prinzenberg E.M., Krause I., Erhardt G.;
"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).";
Anim. Biotechnol. 10:49-62(1999).
[12]
PROTEIN SEQUENCE OF 54-59.
PubMed=8161175;
Reid J.R., Coolbear T., Pillidge C.J., Pritchard G.G.;
"Specificity of hydrolysis of bovine kappa-casein by cell envelope-
associated proteinases from Lactococcus lactis strains.";
Appl. Environ. Microbiol. 60:801-806(1994).
[13]
NUCLEOTIDE SEQUENCE [MRNA] OF 92-190 (VARIANT B2).
PubMed=6689612;
Gorodetskii S.I., Kershulyte D.R., Korobko V.G.;
"Primary structure of cDNA of Bos taurus kappa-casein macropeptide.";
Bioorg. Khim. 9:1693-1695(1983).
[14]
PARTIAL PROTEIN SEQUENCE (VARIANT A).
PubMed=4653404; DOI=10.1002/hlca.19720550820;
Jolles J., Schoentgen F., Alais C., Fiat A.-M., Jolles P.;
"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.";
Helv. Chim. Acta 55:2872-2883(1972).
[15]
PROTEIN SEQUENCE OF 127-168 AND 187-190.
TISSUE=Colostrum;
PubMed=4407313;
Guerin J., Alais C., Jolles J., Jolles P.;
"Kappa-casein from bovine colostrum.";
Biochim. Biophys. Acta 351:325-332(1974).
[16]
PROTEIN SEQUENCE OF 128-190 (VARIANTS A AND B).
Grosclaude F., Mahe M.-F., Mercier J.-C., Ribadeau-Dumas B.;
"Localization of amino-acid substitutions that differenciate bovine
kappa-casein variants A and B.";
Ann. Genet. Sel. Anim. 4:515-521(1972).
[17]
NUCLEOTIDE SEQUENCE OF 133-190 (VARIANT E).
PubMed=1683188;
Schlieben S., Erhardt G., Senft B.;
"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.";
Anim. Genet. 22:333-342(1991).
[18]
NUCLEOTIDE SEQUENCE OF 133-190 (VARIANTS A AND B).
Woollard J.R., Dentine M.R.;
Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases.
[19]
GLYCOSYLATION AT THR-142; THR-152; THR-154; THR-157; THR-163 AND
THR-186.
PubMed=7734846; DOI=10.1093/glycob/4.6.837;
Pisano A., Packer N.H., Redmond J.W., Williams K.L., Gooley A.A.;
"Characterization of O-linked glycosylation motifs in the glycopeptide
domain of bovine kappa-casein.";
Glycobiology 4:837-844(1994).
[20]
GLYCOSYLATION AT THR-142; THR-152; THR-154; THR-157; THR-163 AND
THR-186, AND PHOSPHORYLATION AT SER-148 AND SER-170.
PubMed=8817876; DOI=10.1016/0021-9673(96)00122-7;
Minkiewicz P., Slangen C.J., Lagerwerf F.M., Haverkamp J.,
Rollema H.S., Visser S.;
"Reversed-phase high-performance liquid chromatographic separation of
bovine kappa-casein macropeptide and characterization of isolated
fractions.";
J. Chromatogr. A 743:123-135(1996).
[21]
ACTIVITY OF CASOXINS.
PubMed=2760302;
Chiba H., Tani F., Yoshikawa M.;
"Opioid antagonist peptides derived from kappa-casein.";
J. Dairy Res. 56:363-366(1989).
[22]
ACTIVITY OF CASOPLATELIN.
PubMed=3732274; DOI=10.1111/j.1432-1033.1986.tb09764.x;
Jolles P., Levy-Toledano S., Fiat A.-M., Soria C., Gillessen D.,
Thomaidis A., Dunn F.W., Caen J.P.;
"Analogy between fibrinogen and casein. Effect of an undecapeptide
isolated from kappa-casein on platelet function.";
Eur. J. Biochem. 158:379-382(1986).
[23]
GLYCOSYLATION AT THR-142; THR-152; SER-153; THR-154; THR-157; THR-163;
SER-170 AND THR-186, PHOSPHORYLATION AT THR-166 AND SER-170, AND
IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=25456591; DOI=10.1016/j.chroma.2014.10.046;
Huang L.J., Lin J.H., Tsai J.H., Chu Y.Y., Chen Y.W., Chen S.L.,
Chen S.H.;
"Identification of protein O-glycosylation site and corresponding
glycans using liquid chromatography-tandem mass spectrometry via
mapping accurate mass and retention time shift.";
J. Chromatogr. A 1371:136-145(2014).
-!- FUNCTION: Kappa-casein stabilizes micelle formation, preventing
casein precipitation in milk.
-!- FUNCTION: Casoxins A, B and C have opioid antagonist activity.
Casoxin C causes biphasic ileal contractions through the binding
to the complement C3a receptors.
-!- FUNCTION: Casoplatelin inhibits platelet aggregation.
-!- SUBUNIT: Monomer or homomultimer; disulfide-linked.
-!- INTERACTION:
Self; NbExp=2; IntAct=EBI-7234047, EBI-7234047;
Q9RA63:clpB (xeno); NbExp=3; IntAct=EBI-7234047, EBI-7698530;
-!- SUBCELLULAR LOCATION: Secreted.
-!- TISSUE SPECIFICITY: Mammary gland specific. Secreted in milk.
-!- MISCELLANEOUS: The sequence shown is the A variant.
-!- SIMILARITY: Belongs to the kappa-casein family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Protein Spotlight; Note=Of buttons, digestion
and glue - Issue 16 of November 2001;
URL="https://web.expasy.org/spotlight/back_issues/016";
-----------------------------------------------------------------------
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EMBL; X00565; CAA25231.1; -; mRNA.
EMBL; M36641; AAA30433.1; -; mRNA.
EMBL; X14907; CAA33034.1; -; Genomic_DNA.
EMBL; X14908; CAA33034.1; JOINED; Genomic_DNA.
EMBL; AY380228; AAQ87922.1; -; Genomic_DNA.
EMBL; AY380229; AAQ87923.1; -; Genomic_DNA.
EMBL; BC102120; AAI02121.1; -; mRNA.
EMBL; K01085; AAA30482.1; -; mRNA.
EMBL; AF123250; AAD32139.1; -; Genomic_DNA.
EMBL; AF123251; AAD32140.1; -; Genomic_DNA.
EMBL; AF105260; AAF72097.1; -; Genomic_DNA.
EMBL; M38333; AAA30432.1; -; mRNA.
EMBL; AF041482; AAB97519.1; -; Genomic_DNA.
EMBL; U84250; AAB47260.1; -; Genomic_DNA.
EMBL; U84251; AAB47261.1; -; Genomic_DNA.
PIR; S02076; KKBOB.
RefSeq; NP_776719.1; NM_174294.2.
UniGene; Bt.49421; -.
DisProt; DP00192; -.
ProteinModelPortal; P02668; -.
BioGrid; 159044; 2.
IntAct; P02668; 1.
MINT; MINT-7258912; -.
STRING; 9913.ENSBTAP00000028685; -.
Allergome; 10200; Bos d 12.0101.
Allergome; 167; Bos d 8.
Allergome; 2737; Bos d 12.
iPTMnet; P02668; -.
UniCarbKB; P02668; -.
PaxDb; P02668; -.
PeptideAtlas; P02668; -.
PRIDE; P02668; -.
GeneID; 281728; -.
KEGG; bta:281728; -.
CTD; 1448; -.
eggNOG; ENOG410JCVG; Eukaryota.
eggNOG; ENOG4111E7Q; LUCA.
HOVERGEN; HBG005246; -.
InParanoid; P02668; -.
KO; K17282; -.
TreeFam; TF338369; -.
PMAP-CutDB; P02668; -.
Proteomes; UP000009136; Unplaced.
GO; GO:0005615; C:extracellular space; IDA:AgBase.
GO; GO:0005794; C:Golgi apparatus; IDA:AgBase.
GO; GO:0005796; C:Golgi lumen; IDA:AgBase.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0035375; F:zymogen binding; IPI:AgBase.
GO; GO:0007595; P:lactation; IBA:GO_Central.
GO; GO:0051260; P:protein homooligomerization; IDA:AgBase.
GO; GO:0050821; P:protein stabilization; IBA:GO_Central.
GO; GO:1903496; P:response to 11-deoxycorticosterone; IDA:AgBase.
GO; GO:1903494; P:response to dehydroepiandrosterone; IDA:AgBase.
GO; GO:0032355; P:response to estradiol; IDA:AgBase.
GO; GO:0032570; P:response to progesterone; IDA:AgBase.
InterPro; IPR000117; Casein_kappa.
PANTHER; PTHR11470; PTHR11470; 1.
Pfam; PF00997; Casein_kappa; 1.
PIRSF; PIRSF002374; Casein_kappa; 1.
1: Evidence at protein level;
Complete proteome; Direct protein sequencing; Disulfide bond;
Glycoprotein; Milk protein; Phosphoprotein;
Pyrrolidone carboxylic acid; Reference proteome; Secreted; Signal.
SIGNAL 1 21 {ECO:0000269|PubMed:1628650,
ECO:0000269|PubMed:4577852,
ECO:0000269|Ref.7}.
CHAIN 22 190 Kappa-casein.
/FTId=PRO_0000004483.
PEPTIDE 46 55 Casoxin-C.
/FTId=PRO_0000004484.
PEPTIDE 54 59 Casoxin-6.
/FTId=PRO_0000004485.
PEPTIDE 56 62 Casoxin-A.
/FTId=PRO_0000004486.
PEPTIDE 79 82 Casoxin-B.
/FTId=PRO_0000004487.
PEPTIDE 127 137 Casoplatelin.
/FTId=PRO_0000004488.
SITE 126 127 Cleavage; by chymosin/rennin.
MOD_RES 22 22 Pyrrolidone carboxylic acid.
{ECO:0000269|PubMed:1628650}.
MOD_RES 148 148 Phosphoserine.
{ECO:0000269|PubMed:8817876}.
MOD_RES 166 166 Phosphothreonine.
{ECO:0000269|PubMed:25456591}.
MOD_RES 170 170 Phosphoserine; alternate.
{ECO:0000269|PubMed:25456591,
ECO:0000269|PubMed:8817876}.
MOD_RES 187 187 Phosphoserine.
{ECO:0000250|UniProtKB:P02670}.
CARBOHYD 142 142 O-linked (GalNAc...) threonine.
{ECO:0000269|PubMed:25456591,
ECO:0000269|PubMed:7734846,
ECO:0000269|PubMed:8817876}.
CARBOHYD 152 152 O-linked (GalNAc...) threonine.
{ECO:0000269|PubMed:25456591,
ECO:0000269|PubMed:7734846,
ECO:0000269|PubMed:8817876}.
CARBOHYD 153 153 O-linked (GalNAc...) serine.
{ECO:0000269|PubMed:25456591}.
CARBOHYD 154 154 O-linked (GalNAc...) threonine.
{ECO:0000269|PubMed:25456591,
ECO:0000269|PubMed:7734846,
ECO:0000269|PubMed:8817876}.
CARBOHYD 157 157 O-linked (GalNAc...) threonine.
{ECO:0000269|PubMed:25456591,
ECO:0000269|PubMed:7734846,
ECO:0000269|PubMed:8817876}.
CARBOHYD 163 163 O-linked (GalNAc...) threonine.
{ECO:0000269|PubMed:25456591,
ECO:0000269|PubMed:7734846,
ECO:0000269|PubMed:8817876}.
CARBOHYD 170 170 O-linked (GalNAc...) serine; alternate.
{ECO:0000269|PubMed:25456591}.
CARBOHYD 186 186 O-linked (GalNAc...) threonine; partial.
{ECO:0000269|PubMed:25456591,
ECO:0000269|PubMed:7734846,
ECO:0000269|PubMed:8817876}.
DISULFID 32 109
DISULFID 32 32 Interchain (with C-109); in linked form.
DISULFID 109 109 Interchain (with C-32); in linked form.
VARIANT 31 31 R -> H (in variant F).
VARIANT 118 118 R -> C (in variant G).
VARIANT 156 156 T -> I (in variant G and variant H).
VARIANT 157 157 T -> I (in variant B and variant B2).
VARIANT 169 169 D -> A (in variant B and variant B2).
VARIANT 174 174 I -> T (in variant B2).
VARIANT 176 176 S -> G (in variant E).
CONFLICT 23 23 E -> Q (in Ref. 7; AA sequence).
{ECO:0000305}.
CONFLICT 26 26 Q -> E (in Ref. 7; AA sequence).
{ECO:0000305}.
CONFLICT 28 28 Q -> E (in Ref. 7; AA sequence).
{ECO:0000305}.
CONFLICT 102 102 N -> D (in Ref. 6; AA sequence).
{ECO:0000305}.
SEQUENCE 190 AA; 21269 MW; F12D8310C3B93EDA CRC64;
MMKSFFLVVT ILALTLPFLG AQEQNQEQPI RCEKDERFFS DKIAKYIPIQ YVLSRYPSYG
LNYYQQKPVA LINNQFLPYP YYAKPAAVRS PAQILQWQVL SNTVPAKSCQ AQPTTMARHP
HPHLSFMAIP PKKNQDKTEI PTINTIASGE PTSTPTTEAV ESTVATLEDS PEVIESPPEI
NTVQVTSTAV


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