ID   CASK_RUCDU              Reviewed;         122 AA.
AC   Q95147;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   25-MAY-2022, entry version 63.
DE   RecName: Full=Kappa-casein;
DE   Flags: Fragment;
GN   Name=CSN3; Synonyms=CSN10, CSNK;
OS   Rucervus duvaucelii (Swamp deer) (Cervus duvaucelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Cervidae;
OC   Cervinae; Rucervus.
OX   NCBI_TaxID=43328;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8899730; DOI=10.1006/mpev.1996.0078;
RA   Cronin M.A., Stuart R., Pierson B.J., Patton J.C.;
RT   "K-casein gene phylogeny of higher ruminants (Pecora, Artiodactyla).";
RL   Mol. Phylogenet. Evol. 6:295-311(1996).
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; U37507; AAC48651.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q95147; -.
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..122
FT                   /note="Kappa-casein"
FT                   /id="PRO_0000144105"
FT   REGION          102..122
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            58..59
FT                   /note="Cleavage; by chymosin/rennin"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         98
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P02668"
FT   MOD_RES         102
FT                   /note="Phosphoserine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P02668"
FT   MOD_RES         119
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P02670"
FT   CARBOHYD        84
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000250|UniProtKB:P02668"
FT   CARBOHYD        86
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000250|UniProtKB:P02668"
FT   CARBOHYD        89
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000250|UniProtKB:P02668"
FT   CARBOHYD        95
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000250|UniProtKB:P02668"
FT   CARBOHYD        102
FT                   /note="O-linked (GalNAc...) serine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P02668"
FT   CARBOHYD        118
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000250|UniProtKB:P02668"
FT   NON_TER         1
SQ   SEQUENCE   122 AA;  13209 MW;  CF3C4A337C2AA754 CRC64;
     VALINNQFLP YPYYAKPGAV RSPAQILQWQ VLPNTVSARS CQAQPTTMAR HPHPHLSFMA
     IPPKKNQDKT DIPSINTIAT AESTITPTTE VIVNTVATQE ASSEVIESAP EAKTDQVTST
     VV