ID   CASK_GIRCA              Reviewed;         153 AA.
AC   Q28417; Q95186;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 62.
DE   RecName: Full=Kappa-casein;
DE   Flags: Fragment;
GN   Name=CSN3; Synonyms=CSN10, CSNK;
OS   Giraffa camelopardalis (Giraffe).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Giraffidae;
OC   Giraffa.
OX   NCBI_TaxID=9894;
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).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 32-153.
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; U53886; AAB08411.1; -; Genomic_DNA.
DR   EMBL; U37516; AAC48656.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q28417; -.
DR   PRIDE; Q28417; -.
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..153
FT                   /note="Kappa-casein"
FT                   /id="PRO_0000144110"
FT   SITE            89..90
FT                   /note="Cleavage; by chymosin/rennin"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         133
FT                   /note="Phosphoserine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P02668"
FT   MOD_RES         150
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P02670"
FT   CARBOHYD        105
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000250|UniProtKB:P02668"
FT   CARBOHYD        115
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000250|UniProtKB:P02668"
FT   CARBOHYD        117
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000250|UniProtKB:P02668"
FT   CARBOHYD        120
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000250|UniProtKB:P02668"
FT   CARBOHYD        126
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000250|UniProtKB:P02668"
FT   CARBOHYD        133
FT                   /note="O-linked (GalNAc...) serine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P02668"
FT   CARBOHYD        149
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000250|UniProtKB:P02668"
FT   NON_TER         1
SQ   SEQUENCE   153 AA;  17096 MW;  5530686666BB60FE CRC64;
     FFNDKIVKYI PIQYVLSRYP SYGINYYQHR PVALTNSQFL PYPYYAKPVA VRSPAQILQW
     QVLPNTVPAK SCQAQPTTMA RRPHPRLSFM AIPPKKNQDK TDSPTINTIA TVEPTITPIT
     EAIVNTVAAR EASSEFIASA PETNTVQVTS TVV