ID   CASK_NEMGO              Reviewed;         192 AA.
AC   P50422;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   25-MAY-2022, entry version 74.
DE   RecName: Full=Kappa-casein;
DE   Flags: Precursor;
GN   Name=CSN3; Synonyms=CSN10, CSNK;
OS   Naemorhedus goral (Himalayan goral).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Caprinae; Naemorhedus.
OX   NCBI_TaxID=34871;
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}.
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DR   EMBL; D32179; BAA06884.1; -; Genomic_DNA.
DR   AlphaFoldDB; P50422; -.
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.
DR   PIRSF; PIRSF002374; Casein_kappa; 1.
PE   2: Evidence at transcript level;
KW   Glycoprotein; Milk protein; Phosphoprotein; Secreted; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000250"
FT   CHAIN           22..192
FT                   /note="Kappa-casein"
FT                   /id="PRO_0000004500"
FT   REGION          166..192
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            126..127
FT                   /note="Cleavage; by chymosin/rennin"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         148
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P02668"
FT   MOD_RES         172
FT                   /note="Phosphoserine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P02668"
FT   MOD_RES         189
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P02670"
FT   CARBOHYD        142
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000250|UniProtKB:P02668"
FT   CARBOHYD        152
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000250|UniProtKB:P02668"
FT   CARBOHYD        155
FT                   /note="O-linked (GalNAc...) serine"
FT                   /evidence="ECO:0000250|UniProtKB:P02668"
FT   CARBOHYD        156
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000250|UniProtKB:P02668"
FT   CARBOHYD        159
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000250|UniProtKB:P02668"
FT   CARBOHYD        165
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000250|UniProtKB:P02668"
FT   CARBOHYD        172
FT                   /note="O-linked (GalNAc...) serine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P02668"
FT   CARBOHYD        188
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000250|UniProtKB:P02668"
SQ   SEQUENCE   192 AA;  21485 MW;  D353249986334ED8 CRC64;
     MMKSFFLVVT ILALTLPFLG AQEQNQEQPI CCEKDERFFD DKIAKYIPIQ YVLSRYPSYG
     LNYYQQRPVA LINNQFLPYP YYAKPVAVRS PAQTLQWQVL PNTAPAKSCQ DQPTTMARHP
     HPHLSFMAIP PKKDQDKTEI PTINTIASAE PTVHSTPTTE AIVNTVDNPE ASSESIASAP
     ETNTAQVTST EV