ID   CASK_TRAJA              Reviewed;         171 AA.
AC   Q29137;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 68.
DE   RecName: Full=Kappa-casein;
DE   Flags: Precursor; Fragment;
GN   Name=CSN3; Synonyms=CSN10, CSNK;
OS   Tragulus javanicus (Lesser Malay chevrotain) (Lesser mouse deer).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Tragulina; Tragulidae;
OC   Tragulus.
OX   NCBI_TaxID=9849;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8587130; DOI=10.1007/bf00173165;
RA   Chikuni K., Mori Y., Tabata T., Saito M., Monma M., Kosugiyama M.;
RT   "Molecular phylogeny based on the kappa-casein and cytochrome b sequences
RT   in the mammalian suborder ruminantia.";
RL   J. Mol. Evol. 41:859-866(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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; D14381; BAA03289.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q29137; -.
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; Signal.
FT   SIGNAL          <1..2
FT                   /evidence="ECO:0000255"
FT   CHAIN           3..171
FT                   /note="Kappa-casein"
FT                   /id="PRO_0000004508"
FT   SITE            107..108
FT                   /note="Cleavage; by chymosin/rennin"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         147
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P02668"
FT   MOD_RES         151
FT                   /note="Phosphoserine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P02668"
FT   MOD_RES         168
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P02670"
FT   CARBOHYD        123
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000250|UniProtKB:P02668"
FT   CARBOHYD        133
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000250|UniProtKB:P02668"
FT   CARBOHYD        135
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000250|UniProtKB:P02668"
FT   CARBOHYD        138
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000250|UniProtKB:P02668"
FT   CARBOHYD        144
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000250|UniProtKB:P02668"
FT   CARBOHYD        151
FT                   /note="O-linked (GalNAc...) serine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P02668"
FT   CARBOHYD        167
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000250|UniProtKB:P02668"
FT   NON_TER         1
SQ   SEQUENCE   171 AA;  19106 MW;  3161EE189D4CAA5F CRC64;
     VAQVQYQEQL TGCENDERFF NDKTIKYIPI PYLLNRYPSY GLNYYQQRPP ALINNQFLPF
     SFYAKPMAVR SPAQILQWQV PLNAVSAKPC QAPPTTMARR PRPHLSFMAI PPKKDQDKTD
     TPTINTIVTV EPTTTPTTES IVNTVATLEA SSESIASAPE TTTVQVTSAE V