ID   CASK_CAVPO              Reviewed;         234 AA.
AC   P19442;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1991, sequence version 1.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=Kappa-casein;
DE   Flags: Precursor;
GN   Name=CSN3; Synonyms=CSN10, CSNK;
OS   Cavia porcellus (Guinea pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC   Cavia.
OX   NCBI_TaxID=10141;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Mammary gland;
RX   PubMed=2235497; DOI=10.1093/nar/18.20.6129;
RA   Hall L.;
RT   "Nucleotide sequence of guinea-pig kappa-casein cDNA.";
RL   Nucleic Acids Res. 18:6129-6129(1990).
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; X56020; CAA39497.1; -; mRNA.
DR   PIR; S12092; S12092.
DR   AlphaFoldDB; P19442; -.
DR   STRING; 10141.ENSCPOP00000004384; -.
DR   eggNOG; ENOG502TM2T; Eukaryota.
DR   HOGENOM; CLU_103388_0_0_1; -.
DR   InParanoid; P19442; -.
DR   OMA; HPSFIAI; -.
DR   TreeFam; TF338369; -.
DR   Proteomes; UP000005447; Unassembled WGS sequence.
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; Reference proteome; Repeat;
KW   Secreted; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000250"
FT   CHAIN           22..234
FT                   /note="Kappa-casein"
FT                   /id="PRO_0000004495"
FT   REPEAT          127..153
FT                   /note="1"
FT   REPEAT          154..179
FT                   /note="2"
FT   REPEAT          180..207
FT                   /note="3"
FT   REGION          127..207
FT                   /note="3 X 27 AA tandem repeats"
FT   REGION          143..234
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        143..170
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        217..234
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            118..119
FT                   /note="Cleavage; by chymosin/rennin"
FT   MOD_RES         158
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P02668"
FT   MOD_RES         162
FT                   /note="Phosphoserine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P02668"
FT   CARBOHYD        144
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000250|UniProtKB:P02668"
FT   CARBOHYD        162
FT                   /note="O-linked (GalNAc...) serine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P02668"
SQ   SEQUENCE   234 AA;  25597 MW;  247AB957F49D4659 CRC64;
     MMKSFLLVVN IVALTLPFLA AEVQNQEQPA CCGNDERLFE QKKVLYLLSY PVLNNYLRTA
     PSYYQNRASV PINNPYLCHL YYVPSFVLWA QGQIPKGPVS TDIHQSTMQY HQAKHPSFMA
     ILSKKILGKA TILSTDAIAA PEQTPVSAAQ PTVSAGDTPE VSSQFIDTPD TSVLAEEARE
     SPEDTPEISE FINAPDTAVP SEEPRESAED TPEISSEFIF SPETSTGPAI ASMA