ID   CASK_HIPAM              Reviewed;         145 AA.
AC   Q28441;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   11-DEC-2019, entry version 54.
DE   RecName: Full=Kappa-casein;
DE   Flags: Fragment;
GN   Name=CSN3; Synonyms=CSN10, CSNK;
OS   Hippopotamus amphibius (Hippopotamus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Ancodonta;
OC   Hippopotamidae; Hippopotamus.
OX   NCBI_TaxID=9833;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8752004; DOI=10.1093/oxfordjournals.molbev.a025663;
RA   Gatesy J., Hayashi C., Cronin M.A., Arctander P.;
RT   "Evidence from milk casein genes that cetaceans are close relatives of
RT   hippopotamid artiodactyls.";
RL   Mol. Biol. Evol. 13:954-963(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; U53889; AAB08413.1; -; Genomic_DNA.
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..145
FT                   /note="Kappa-casein"
FT                   /id="PRO_0000144111"
FT   MOD_RES         121
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P02668"
FT   MOD_RES         125
FT                   /note="Phosphoserine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P02668"
FT   MOD_RES         142
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P02670"
FT   CARBOHYD        91
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        107
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000250|UniProtKB:P02668"
FT   CARBOHYD        112
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000250|UniProtKB:P02668"
FT   CARBOHYD        118
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000250|UniProtKB:P02668"
FT   CARBOHYD        125
FT                   /note="O-linked (GalNAc...) serine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P02668"
FT   CARBOHYD        141
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000250|UniProtKB:P02668"
FT   NON_TER         1
SQ   SEQUENCE   145 AA;  16274 MW;  874A9EEFD6F80398 CRC64;
     CFNGKTVKYI PVHYVMSRYP KYGLNYYQCR PAALINNQFM PYPYYAKPVA VKPHAQIPQW
     QALPDINPPT VPCRRRPHPS FLAIPPXKDQ NKTVIPIINT IATXEPTLIP TTEPIVNTVV
     TTEASSEFIT STPETTTVQV TSPVV