ID   CASK_BISBO              Reviewed;         136 AA.
AC   P42155;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   25-MAY-2022, entry version 65.
DE   RecName: Full=Kappa-casein;
DE   Flags: Fragment;
GN   Name=CSN3; Synonyms=CSN10, CSNK;
OS   Bison bonasus (European bison).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bison.
OX   NCBI_TaxID=9902;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Bialowieza;
RX   PubMed=7486252; DOI=10.1111/j.1365-2052.1995.tb02669.x;
RA   Burzynska B., Topczewski J.;
RT   "Genotyping of Bison bonasus kappa-casein gene following DNA sequence
RT   amplification.";
RL   Anim. Genet. 26:335-336(1995).
CC   -!- FUNCTION: Kappa-casein stabilizes micelle formation, preventing casein
CC       precipitation in milk.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Mammary gland specific. Secreted in milk.
CC   -!- SIMILARITY: Belongs to the kappa-casein family. {ECO:0000305}.
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DR   EMBL; U10379; AAB60267.1; -; Genomic_DNA.
DR   AlphaFoldDB; P42155; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   InterPro; IPR000117; Casein_kappa.
DR   PANTHER; PTHR11470; PTHR11470; 1.
DR   Pfam; PF00997; Casein_kappa; 1.
PE   2: Evidence at transcript level;
KW   Glycoprotein; Milk protein; Phosphoprotein; Secreted.
FT   CHAIN           <1..136
FT                   /note="Kappa-casein"
FT                   /id="PRO_0000144103"
FT   SITE            72..73
FT                   /note="Cleavage; by chymosin/rennin"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         94
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P02668"
FT   MOD_RES         112
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P02668"
FT   MOD_RES         116
FT                   /note="Phosphoserine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P02668"
FT   MOD_RES         133
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P02670"
FT   CARBOHYD        88
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000250|UniProtKB:P02668"
FT   CARBOHYD        98
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000250|UniProtKB:P02668"
FT   CARBOHYD        99
FT                   /note="O-linked (GalNAc...) serine"
FT                   /evidence="ECO:0000250|UniProtKB:P02668"
FT   CARBOHYD        103
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000250|UniProtKB:P02668"
FT   CARBOHYD        109
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000250|UniProtKB:P02668"
FT   CARBOHYD        116
FT                   /note="O-linked (GalNAc...) serine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P02668"
FT   CARBOHYD        132
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000250|UniProtKB:P02668"
FT   VARIANT         98
FT                   /note="T -> A"
FT   NON_TER         1
SQ   SEQUENCE   136 AA;  14904 MW;  BF9D717DD13C806C CRC64;
     RYPSYGLNYY QQKPVALINN QFLPYPYYAK PAAVRSPAQI LQWQVLSNTV PAKSCQAQPT
     TMARHPHPHL SFMAIPPKKN QDKTEIPTIN TIASGEPTST PTTEAVESTV ATLEASPEVI
     ESPPEINTVQ VTSTAV