CASK_MUNRE
ID CASK_MUNRE Reviewed; 122 AA.
AC Q95199;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 25-MAY-2022, entry version 58.
DE RecName: Full=Kappa-casein;
DE Flags: Fragment;
GN Name=CSN3; Synonyms=CSN10, CSNK;
OS Muntiacus reevesi (Reeves' muntjac) (Cervus reevesi).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Cervidae;
OC Muntiacinae; Muntiacus.
OX NCBI_TaxID=9886;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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; U37509; AAC48657.1; -; Genomic_DNA.
DR AlphaFoldDB; Q95199; -.
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..122
FT /note="Kappa-casein"
FT /id="PRO_0000144114"
FT REGION 43..122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..96
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 58..59
FT /note="Cleavage; by chymosin/rennin"
FT /evidence="ECO:0000250"
FT MOD_RES 98
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P02668"
FT MOD_RES 102
FT /note="Phosphoserine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P02668"
FT MOD_RES 119
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02670"
FT CARBOHYD 74
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250|UniProtKB:P02668"
FT CARBOHYD 76
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 84
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250|UniProtKB:P02668"
FT CARBOHYD 86
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250|UniProtKB:P02668"
FT CARBOHYD 89
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250|UniProtKB:P02668"
FT CARBOHYD 95
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250|UniProtKB:P02668"
FT CARBOHYD 102
FT /note="O-linked (GalNAc...) serine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P02668"
FT CARBOHYD 118
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250|UniProtKB:P02668"
FT NON_TER 1
SQ SEQUENCE 122 AA; 12878 MW; F9D82997264DDEFB CRC64;
VALISNQFLP YPYYAKPGAV RSPAQILQWQ ALPNTVPATS CQAQPATVAR HPHPRLSFMA
IPPKKSQDKT DHPTINTSAT VESTATPTTE AVVDTAATQE ASPEVIASAP EASTDQVTST
VV
